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Conserved domains on  [gi|1189438336|ref|NP_001338224|]
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ATP-binding cassette sub-family C member 8 isoform 3 [Homo sapiens]

Protein Classification

ABC transporter C family protein( domain architecture ID 1000085)

ATP-binding cassette transporter C (ABCC) family protein similar to human multidrug resistance-associated protein 1 that mediates export of organic anions and drugs from the cytoplasm

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
MRP_assoc_pro super family cl33195
multi drug resistance-associated protein (MRP); This model describes multi drug ...
224-1600 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


The actual alignment was detected with superfamily member TIGR00957:

Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 838.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLC---------------------EAFDAQVR 275
Cdd:TIGR00957  209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECkktrkqpvsavygkkdpskpkGSSQLDAN 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  276 KDIQGTQGAR-------AIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLgkeNDVFQPKTQFlgvYFVSS 348
Cdd:TIGR00957  289 EEVEALIVKSphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFV---NDPMAPDWQG---YFYTG 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  349 QEFLANAyvlavllflallLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957  363 LLFVCAC------------LQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957  429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  509 LKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957  509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIreeqcaphEPtpqgpaskyQAVEeglpslhssqpsgssppnhpqplrvv 668
Cdd:TIGR00957  589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL--------EP---------DSIE-------------------------- 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  669 nrKRParedcrgltgplqslVPSADGDAdnccVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAA 748
Cdd:TIGR00957  626 --RRT---------------IKPGEGNS----ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  749 LGEMQKVSGAVfwsslpdseigedpsperetatdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACS 828
Cdd:TIGR00957  685 LAEMDKVEGHV--------------------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  829 LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQ--AGILELLRDdkRTVV 906
Cdd:TIGR00957  739 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRI 816
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  907 LVTHKLQYLPHADWIIAMKDGTI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKE---TVT 966
Cdd:TIGR00957  817 LVTHGISYLPQVDVIIVMSGGKIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIEngmLVT 896
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  967 ERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIP-------WracaKYLSSAGILLLSLLVF 1039
Cdd:TIGR00957  897 DVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGqvelsvyW----DYMKAIGLFITFLSIF 972
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1040 SQLLKHMVLVAIDYWLAKWTDSALT-LTPAARNCSLSqectldqtVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVA 1115
Cdd:TIGR00957  973 LFVCNHVSALASNYWLSLWTDDPMVnGTQNNTSLRLS--------VYG-------ALGIlqgFAVFGYSMAVSIGGIQAS 1037
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1197
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1276 IGACVVLIAAVTSISNslHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSL 1355
Cdd:TIGR00957 1198 VGNCIVLFAALFAVIS--RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQ 1269
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 I-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGID 1430
Cdd:TIGR00957 1270 IqetapPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
                         1450
                   ....*....|
gi 1189438336 1591 KdSVFASFVR 1600
Cdd:TIGR00957 1510 R-GIFYSMAK 1518
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
224-1600 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 838.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLC---------------------EAFDAQVR 275
Cdd:TIGR00957  209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECkktrkqpvsavygkkdpskpkGSSQLDAN 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  276 KDIQGTQGAR-------AIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLgkeNDVFQPKTQFlgvYFVSS 348
Cdd:TIGR00957  289 EEVEALIVKSphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFV---NDPMAPDWQG---YFYTG 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  349 QEFLANAyvlavllflallLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957  363 LLFVCAC------------LQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957  429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  509 LKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957  509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIreeqcaphEPtpqgpaskyQAVEeglpslhssqpsgssppnhpqplrvv 668
Cdd:TIGR00957  589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL--------EP---------DSIE-------------------------- 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  669 nrKRParedcrgltgplqslVPSADGDAdnccVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAA 748
Cdd:TIGR00957  626 --RRT---------------IKPGEGNS----ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  749 LGEMQKVSGAVfwsslpdseigedpsperetatdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACS 828
Cdd:TIGR00957  685 LAEMDKVEGHV--------------------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  829 LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQ--AGILELLRDdkRTVV 906
Cdd:TIGR00957  739 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRI 816
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  907 LVTHKLQYLPHADWIIAMKDGTI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKE---TVT 966
Cdd:TIGR00957  817 LVTHGISYLPQVDVIIVMSGGKIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIEngmLVT 896
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  967 ERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIP-------WracaKYLSSAGILLLSLLVF 1039
Cdd:TIGR00957  897 DVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGqvelsvyW----DYMKAIGLFITFLSIF 972
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1040 SQLLKHMVLVAIDYWLAKWTDSALT-LTPAARNCSLSqectldqtVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVA 1115
Cdd:TIGR00957  973 LFVCNHVSALASNYWLSLWTDDPMVnGTQNNTSLRLS--------VYG-------ALGIlqgFAVFGYSMAVSIGGIQAS 1037
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1197
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1276 IGACVVLIAAVTSISNslHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSL 1355
Cdd:TIGR00957 1198 VGNCIVLFAALFAVIS--RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQ 1269
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 I-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGID 1430
Cdd:TIGR00957 1270 IqetapPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
                         1450
                   ....*....|
gi 1189438336 1591 KdSVFASFVR 1600
Cdd:TIGR00957 1510 R-GIFYSMAK 1518
PLN03130 PLN03130
ABC transporter C family member; Provisional
222-1601 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 733.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDiqgtqgarAIW--QALSHAFGRRL 299
Cdd:PLN03130   232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP--------KPWllRALNNSLGGRF 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENDVFQPKTQ--------FLGVYFvssqeflanayvlavllflalllqRT 371
Cdd:PLN03130   304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGVVL------------------------GV 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130   356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 530
Cdd:PLN03130   434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  531 TSLRAFAIYTSISIFMNTAIPIAAVLITFvGHVSFFKeADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130   514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  611 SEFLSsAEirEEQCAPHEPtpqgpaskyqaVEEGLPSlhssqpsgssppnhpqplrvvnrkrparedcrgltgplqslvp 690
Cdd:PLN03130   592 EELLL-AE--ERVLLPNPP-----------LEPGLPA------------------------------------------- 614
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  691 sadgdadnccVQIMGGYFTWTPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslpdsei 769
Cdd:PLN03130   615 ----------ISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----------- 673
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  770 gedpsperetatdlDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 849
Cdd:PLN03130   674 --------------SVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV 739
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:PLN03130   740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMI 817
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  930 QREGTLKD-------FQrsecQLFEHWKTLMNRQDQELEKE---TVTERKATEPPQGLSRAMSSRDGLLQDeeeeeeeaa 999
Cdd:PLN03130   818 KEEGTYEElsnngplFQ----KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKKKSKEG--------- 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1000 eseeddnlSSMLHQRAE-----IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLT--PAARN 1071
Cdd:PLN03130   885 --------KSVLIKQEEretgvVSWKVLERYKNAlGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKThgPLFYN 956
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1072 cslsqectldqTVYAMVftvlcSLGIVLclVTSVTVEW---TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSS 1148
Cdd:PLN03130   957 -----------LIYALL-----SFGQVL--VTLLNSYWlimSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAK 1018
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1149 DCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAET 1228
Cdd:PLN03130  1019 DLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEA 1098
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1229 VEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA---AVTSISNSLHRELSAGLVGLG 1305
Cdd:PLN03130  1099 LNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTasfAVMQNGRAENQAAFASTMGLL 1178
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1306 LTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLK 1380
Cdd:PLN03130  1179 LSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELP 1252
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1381 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFN 1460
Cdd:PLN03130  1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1461 LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENI 1540
Cdd:PLN03130  1333 LDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
                         1370      1380      1390      1400      1410      1420
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1541 LQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PLN03130  1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1364-1603 4.39e-149

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 455.91  E-value: 4.39e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03288     18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03288     98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
Cdd:cd03288    178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1019-1601 4.40e-89

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 302.04  E-value: 4.40e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1019 WRACAKYLSSAGILLLSLLVFSQLLKhmvlVAIDYWLAKWTDSALTLTPAARNcslsqectldqtvYAMVFTVLCSLGIV 1098
Cdd:COG1132      5 RRLLKYLKYKLLLLAILLLLLSALLS----LLLPLLIGRIIDALLADLGELLE-------------LLLLLLLLALLGGV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1099 LCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVI 1178
Cdd:COG1132     68 LRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAKSGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1179 SYV----TPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDttqlPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDS 1254
Cdd:COG1132    148 FSLswrlALILLLILPLLALVLSLLARKSRKLSRRVREALG----ELNARLLESLSGIRVIKAFGAEDRELKRFEEANEE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1255 NNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVK 1334
Cdd:COG1132    224 LRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLTVGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAE 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1335 RIHGLLKTEAESYEGLLAPslipknWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1414
Cdd:COG1132    304 RLFELLDEEPEVEDPPDPL------KDTIGSIEFENVSFSYPGK-KPVLKDISFSIEPGEKVAIVGPSGSGKSTLIKLLL 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1415 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLD 1493
Cdd:COG1132    377 RLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPdATDEEIEEALKLANAHEFIANLPDGYD 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:COG1132    457 TIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVL 536
                          570       580
                   ....*....|....*....|....*...
gi 1189438336 1574 KRGAILEFDKPEKLLsRKDSVFASFVRA 1601
Cdd:COG1132    537 DNGRIVERGTHEELL-AKGGLYARLYQA 563
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
1034-1316 1.43e-43

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 395537 [Multi-domain]  Cd Length: 274  Bit Score: 160.12  E-value: 1.43e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1034 LSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAArncslsqecTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1113
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE---------TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGER 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLA 1193
Cdd:pfam00664   72 LSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1194 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRM 1273
Cdd:pfam00664  152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1189438336 1274 EYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYL 1316
Cdd:pfam00664  232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
727-910 6.06e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 47.75  E-value: 6.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336   727 RGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseigedpsperetatdldirkrgpvayasqkpwLLNATVE 806
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDI 41
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336   807 ENIIFESPFNkqrykmvieacslqpdidilphgdqTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLS 886
Cdd:smart00382   42 LEEVLDQLLL-------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
                           170       180
                    ....*....|....*....|....*...
gi 1189438336   887 DHLMQAGILELL----RDDKRTVVLVTH 910
Cdd:smart00382   97 ALLLLLEELRLLlllkSEKNLTVILTTN 124
 
Name Accession Description Interval E-value
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
224-1600 0e+00

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 838.45  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  224 LLSKGTYWWMNAFIKTAHKKPI---DLRAIGK----LPIAMRALTNYQRLC---------------------EAFDAQVR 275
Cdd:TIGR00957  209 FLSRITFWWITGMAVYGYRQPLeesDLWSLNKedtsEMVVPVLVENWKKECkktrkqpvsavygkkdpskpkGSSQLDAN 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  276 KDIQGTQGAR-------AIWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLgkeNDVFQPKTQFlgvYFVSS 348
Cdd:TIGR00957  289 EEVEALIVKSphkprkpSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFV---NDPMAPDWQG---YFYTG 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  349 QEFLANAyvlavllflallLQRTFLQASYYVAIETGINLRGAIQTKIYNKImhLSTSNLSMGEMTAGQICNLVAIDTNQL 428
Cdd:TIGR00957  363 LLFVCAC------------LQTLILHQYFHICFVSGMRIKTAVMGAVYRKA--LVITNSARKSSTVGEIVNLMSVDAQRF 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  429 MWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKL 508
Cdd:TIGR00957  429 MDLATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKV 508
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  509 LKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVT 588
Cdd:TIGR00957  509 LKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKAFVSLALFNILRF 588
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  589 PLFLLSSVVRSTVKALVSVQKLSEFLSSAEIreeqcaphEPtpqgpaskyQAVEeglpslhssqpsgssppnhpqplrvv 668
Cdd:TIGR00957  589 PLNILPMVISSIVQASVSLKRLRIFLSHEEL--------EP---------DSIE-------------------------- 625
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  669 nrKRParedcrgltgplqslVPSADGDAdnccVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAA 748
Cdd:TIGR00957  626 --RRT---------------IKPGEGNS----ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL 684
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  749 LGEMQKVSGAVfwsslpdseigedpsperetatdldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACS 828
Cdd:TIGR00957  685 LAEMDKVEGHV--------------------------HMKGSVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA 738
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  829 LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQ--AGILELLRDdkRTVV 906
Cdd:TIGR00957  739 LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvIGPEGVLKN--KTRI 816
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  907 LVTHKLQYLPHADWIIAMKDGTI----------QREGTLKDFQRS------ECQLFEHWKTLMNRQDQE-LEKE---TVT 966
Cdd:TIGR00957  817 LVTHGISYLPQVDVIIVMSGGKIsemgsyqellQRDGAFAEFLRTyapdeqQGHLEDSWTALVSGEGKEaKLIEngmLVT 896
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  967 ERKATEPPQGLSRAMSSRDGLLQDEEEEEEEAAESEEDDNLSSMLHQRAEIP-------WracaKYLSSAGILLLSLLVF 1039
Cdd:TIGR00957  897 DVVGKQLQRQLSASSSDSGDQSRHHGSSAELQKAEAKEETWKLMEADKAQTGqvelsvyW----DYMKAIGLFITFLSIF 972
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1040 SQLLKHMVLVAIDYWLAKWTDSALT-LTPAARNCSLSqectldqtVYAmvftvlcSLGI---VLCLVTSVTVEWTGLKVA 1115
Cdd:TIGR00957  973 LFVCNHVSALASNYWLSLWTDDPMVnGTQNNTSLRLS--------VYG-------ALGIlqgFAVFGYSMAVSIGGIQAS 1037
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLL 1117
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:TIGR00957 1118 YFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLEC 1197
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1276 IGACVVLIAAVTSISNslHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSL 1355
Cdd:TIGR00957 1198 VGNCIVLFAALFAVIS--RHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE------APWQ 1269
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 I-----PKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGID 1430
Cdd:TIGR00957 1270 IqetapPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
                         1450
                   ....*....|
gi 1189438336 1591 KdSVFASFVR 1600
Cdd:TIGR00957 1510 R-GIFYSMAK 1518
PLN03130 PLN03130
ABC transporter C family member; Provisional
222-1601 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 733.47  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  222 VNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDiqgtqgarAIW--QALSHAFGRRL 299
Cdd:PLN03130   232 ANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEELKKP--------KPWllRALNNSLGGRF 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  300 VLSSTFRILADLLGFAGPLcifgIVDHLGKENDVFQPKTQ--------FLGVYFvssqeflanayvlavllflalllqRT 371
Cdd:PLN03130   304 WLGGFFKIGNDLSQFVGPL----LLNLLLESMQNGEPAWIgyiyafsiFVGVVL------------------------GV 355
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  372 FLQASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:PLN03130   356 LCEAQYFQNVmRVGFRLRSTLVAAVFRKSLRLT--HEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMV 433
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 530
Cdd:PLN03130   434 LLYQQLGVASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDEL 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  531 TSLRAFAIYTSISIFMNTAIPIAAVLITFvGHVSFFKeADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:PLN03130   514 SWFRKAQLLSAFNSFILNSIPVLVTVVSF-GVFTLLG-GDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRL 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  611 SEFLSsAEirEEQCAPHEPtpqgpaskyqaVEEGLPSlhssqpsgssppnhpqplrvvnrkrparedcrgltgplqslvp 690
Cdd:PLN03130   592 EELLL-AE--ERVLLPNPP-----------LEPGLPA------------------------------------------- 614
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  691 sadgdadnccVQIMGGYFTWTPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslpdsei 769
Cdd:PLN03130   615 ----------ISIKNGYFSWDSKAeRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDA----------- 673
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  770 gedpsperetatdlDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI 849
Cdd:PLN03130   674 --------------SVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV 739
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRddKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:PLN03130   740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELR--GKTRVLVTNQLHFLSQVDRIILVHEGMI 817
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  930 QREGTLKD-------FQrsecQLFEHWKTLMNRQDQELEKE---TVTERKATEPPQGLSRAMSSRDGLLQDeeeeeeeaa 999
Cdd:PLN03130   818 KEEGTYEElsnngplFQ----KLMENAGKMEEYVEENGEEEddqTSSKPVANGNANNLKKDSSSKKKSKEG--------- 884
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1000 eseeddnlSSMLHQRAE-----IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLT--PAARN 1071
Cdd:PLN03130   885 --------KSVLIKQEEretgvVSWKVLERYKNAlGGAWVVMILFLCYVLTEVFRVSSSTWLSEWTDQGTPKThgPLFYN 956
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1072 cslsqectldqTVYAMVftvlcSLGIVLclVTSVTVEW---TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSS 1148
Cdd:PLN03130   957 -----------LIYALL-----SFGQVL--VTLLNSYWlimSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAK 1018
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1149 DCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAET 1228
Cdd:PLN03130  1019 DLGDIDRNVAVFVNMFLGQIFQLLSTFVLIGIVSTISLWAIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEA 1098
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1229 VEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIA---AVTSISNSLHRELSAGLVGLG 1305
Cdd:PLN03130  1099 LNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLETLGGLMIWLTasfAVMQNGRAENQAAFASTMGLL 1178
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1306 LTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLI-----PKNWPDQGKIQIQNLSVRYDSSLK 1380
Cdd:PLN03130  1179 LSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSE------APLVIennrpPPGWPSSGSIKFEDVVLRYRPELP 1252
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1381 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFN 1460
Cdd:PLN03130  1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1461 LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENI 1540
Cdd:PLN03130  1333 LDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
                         1370      1380      1390      1400      1410      1420
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1541 LQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PLN03130  1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMVQS 1473
PLN03232 PLN03232
ABC transporter C family member; Provisional
223-1601 0e+00

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 712.52  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCEAFDAQVRKDiqgtqgARAIWQALSHAFGRRLVLS 302
Cdd:PLN03232   233 SIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEESRRP------KPWLLRALNNSLGGRFWLG 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  303 STFRILADLLGFAGPLcifgIVDHLGKENDVFQPK--------TQFLGVYFvssqeflanayvlavllflalllqRTFLQ 374
Cdd:PLN03232   307 GIFKIGHDLSQFVGPV----ILSHLLQSMQEGDPAwvgyvyafLIFFGVTF------------------------GVLCE 358
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  375 ASYYVAI-ETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:PLN03232   359 SQYFQNVgRVGFRLRSTLVAAIFHKSLRLT--HEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLY 436
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSL 533
Cdd:PLN03232   437 QQLGVASLFGSLILFLLIPLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWF 516
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  534 RAFAIYTSISIFMNTAIPIAAVLITFvgHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEF 613
Cdd:PLN03232   517 RKAQLLSAFNSFILNSIPVVVTLVSF--GVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEEL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  614 LSSaeirEEQCAPHEPtpqgpaskyqaveeglpslhssqpsgssppnhpqplrvvnrkrparedcrgltgPLQSLVPSad 693
Cdd:PLN03232   595 LLS----EERILAQNP------------------------------------------------------PLQPGAPA-- 614
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  694 gdadnccVQIMGGYFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwsslpdseiged 772
Cdd:PLN03232   615 -------ISIKNGYFSWdSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL-------------------- 667
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  773 pSPERETATDLdirkRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLS 852
Cdd:PLN03232   668 -SHAETSSVVI----RGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNIS 742
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  853 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:PLN03232   743 GGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKG--KTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  933 GTLKDFQRSEcQLFEHWKTLMNRQDQELEKETVTERKATEPP--------QGLSRAMSSRDGllqdeeeeeeeaaeseed 1004
Cdd:PLN03232   821 GTFAELSKSG-SLFKKLMENAGKMDATQEVNTNDENILKLGPtvtidvseRNLGSTKQGKRG------------------ 881
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1005 dnlSSMLHQRAE-----IPWRACAKYLSS-AGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltlTPAARNCSLsqec 1078
Cdd:PLN03232   882 ---RSVLVKQEEretgiISWNVLMRYNKAvGGLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQS---TPKSYSPGF---- 951
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 tldqtvYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIP 1158
Cdd:PLN03232   952 ------YIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVA 1025
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1159 STLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:PLN03232  1026 NLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRAY 1105
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 RYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSI---SNSLHRELSAGLVGLGLTYALMVSNY 1315
Cdd:PLN03232  1106 KAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVlrnGNAENQAGFASTMGLLLSYTLNITTL 1185
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1316 LNWMVRNLADMELQLGAVKRIHGLLKTEAEsyegllAPSLIPKN-----WPDQGKIQIQNLSVRYDSSLKPVLKHVNALI 1390
Cdd:PLN03232  1186 LSGVLRQASKAENSLNSVERVGNYIDLPSE------ATAIIENNrpvsgWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFV 1259
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1391 APGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDS 1470
Cdd:PLN03232  1260 SPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA 1339
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1471 TLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFA 1550
Cdd:PLN03232  1340 DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419
                         1370      1380      1390      1400      1410
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1551 DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PLN03232  1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
PTZ00243 PTZ00243
ABC transporter; Provisional
369-1601 0e+00

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 647.99  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  369 QRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDT---NQLMWFfflCPNLWAMPVQI 445
Cdd:PTZ00243   298 QSVCLHRFYYISIRCGLQYRSALNALIFEKCFTISSKSLAQPDMNTGRIINMMSTDVeriNSFMQY---CMYLWSSPMVL 374
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  446 IVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETT 525
Cdd:PTZ00243   375 LLSILLLSRLVGWCALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDK 454
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  526 RRKEMTSLRAFAIYTSISIFMNTAIP---IAAVLITF--VGHvsffkeaDFSPSVAFASLSLFHILVTPLFLLSSVVRST 600
Cdd:PTZ00243   455 RARELRYLRDVQLARVATSFVNNATPtlmIAVVFTVYylLGH-------ELTPEVVFPTIALLGVLRMPFFMIPWVFTTV 527
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  601 VKALVSVQKLSEFLSS-----------AEIREEQcAPHEPT--------------------PQGPASKYQAVEEGLPSLh 649
Cdd:PTZ00243   528 LQFLVSIKRISTFLECdnatcstvqdmEEYWREQ-REHSTAcqlaavlenvdvtafvpvklPRAPKVKTSLLSRALRML- 605
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  650 sSQPSGSSPPNHPQPLRVVNR------KRPAREDCRGLTGPLQSLVPSADGDADnccVQIMGG--YFTWTPDGIptLSNI 721
Cdd:PTZ00243   606 -CCEQCRPTKRHPSPSVVVEDtdygspSSASRHIVEGGTGGGHEATPTSERSAK---TPKMKTddFFELEPKVL--LRDV 679
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  722 TIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfWSslpdseigedpspEREtatdldirkrgpVAYASQKPWLL 801
Cdd:PTZ00243   680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WA-------------ERS------------IAYVPQQAWIM 733
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  802 NATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSAL 881
Cdd:PTZ00243   734 NATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  882 DIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSEcqLFEHWKT-LMNRQDQel 960
Cdd:PTZ00243   814 DAHVGERVVEECFLGALAG--KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATLAAeLKENKDS-- 887
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  961 eKETVTERKATEppqglsraMSSRDGLLQDEEEEEEEAAESEEDDNLSSM------LHQRAE-----IPWRACAKYLSSA 1029
Cdd:PTZ00243   888 -KEGDADAEVAE--------VDAAPGGAVDHEPPVAKQEGNAEGGDGAALdaaagrLMTREEkasgsVPWSTYVAYLRFC 958
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 G-----ILLLSLLVFSQLlkhmVLVAIDYWLAKWTdsaltltpaarncslSQECTLDQTVYAMVFtvlcsLGIVLCLVTS 1104
Cdd:PTZ00243   959 GglhaaGFVLATFAVTEL----VTVSSGVWLSMWS---------------TRSFKLSAATYLYVY-----LGIVLLGTFS 1014
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1105 V----TVEWTGLKV-AKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVIS 1179
Cdd:PTZ00243  1015 VplrfFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTS 1094
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1180 YVTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIAS 1259
Cdd:PTZ00243  1095 ASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCS 1174
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1260 LFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELS--AGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR-- 1335
Cdd:PTZ00243  1175 YLENVANRWLGVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERll 1254
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1336 --IHGL-------LKTE---AESYEGLLA---------PSLIPKNWP---DQGKIQIQNLSVRYDSSLKPVLKHVNALIA 1391
Cdd:PTZ00243  1255 yyTDEVphedmpeLDEEvdaLERRTGMAAdvtgtvviePASPTSAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIA 1334
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1392 PGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDST 1471
Cdd:PTZ00243  1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAE 1414
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1472 LWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFI-MDEATASIDMATENILQKVVMTAFA 1550
Cdd:PTZ00243  1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFIlMDEATANIDPALDRQIQATVMSAFS 1494
                         1290      1300      1310      1320      1330
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1551 DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRA 1601
Cdd:PTZ00243  1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEA 1545
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1364-1603 4.39e-149

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 455.91  E-value: 4.39e-149
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03288     18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03288     98 SIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
Cdd:cd03288    178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVRTDK 257
ABC_6TM_SUR1_D2_like cd18602
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ...
1036-1337 6.25e-145

Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350046 [Multi-domain]  Cd Length: 307  Bit Score: 446.67  E-value: 6.25e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1036 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1115
Cdd:cd18602      3 LVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTNLAGELAGLRAA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:cd18602     83 RRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIV 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:cd18602    163 YYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDY 242
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1276 IGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18602    243 LGAVIVFLAALSSLTAALAGYISPSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERVL 304
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
701-928 1.64e-139

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 428.67  E-value: 1.64e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedPSPERETA 780
Cdd:cd03290      1 VQVTNGYFSWGS-GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN---------KNESEPSF 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  781 TDLDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRIS 860
Cdd:cd03290     71 EATRSRNRYSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:cd03290    151 VARALYQNTNIVFLDDPFSALDIHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
ABC_6TM_SUR1_D1_like cd18591
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ...
301-610 3.53e-137

Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350035 [Multi-domain]  Cd Length: 309  Bit Score: 425.88  E-value: 3.53e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDVFQPKTQFLGVYFVSSQEFLANAYVLAVLLFLALLLQRTFLQASYYVA 380
Cdd:cd18591      1 LGGILKLLGDLLGFVGPLCISGIVDYVEENTYSSSNSTDKLSVSYVTVEEFFSNGYVLAVILFLALLLQATFSQASYHIV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  381 IETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18591     81 IREGIRLKTALQAMIYEKALRLSSWNLSSGSMTIGQITNHMSEDANNIMFFFWLIHYLWAIPLKIIVGLILLYLKLGVSA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 540
Cdd:cd18591    161 LIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVYW 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  541 SISIFMNTAIPIAAVLITFVGHVsFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18591    241 SLMTFLTQASPILVTLVTFGLYP-YLEGEPLTAAKAFSSLALFNQLTVPLFIFPVVIPILINAVVSTRRL 309
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
223-1603 4.98e-126

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 430.49  E-value: 4.98e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  223 NLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRAltnyQRLCEAFDAQVRKDIQGTQGARAIWQALSHAFGRRLVLs 302
Cdd:TIGR01271   10 NFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSA----DNLSERLEREWDRELASAKKNPKLLNALRRCFFWRFVF- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  303 stfriladllgfagplciFGIVDHLGKENDVFQPktQFLGVYFVSSQEFLAN----AYVLAVLLFLALLLQRTFLQASYY 378
Cdd:TIGR01271   85 ------------------YGILLYFGEATKAVQP--LLLGRIIASYDPFNAPereiAYYLALGLCLLFIVRTLLLHPAIF 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  379 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 458
Cdd:TIGR01271  145 GLHHLGMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEV 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAi 538
Cdd:TIGR01271  223 NGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIA- 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  539 ytSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHIL-VTPLFLLSSVVRSTVKALVSVQKLSEFLSSA 617
Cdd:TIGR01271  302 --YLRYFYSSAFFFSGFFVVFLSVVPYALIKGIILRRIFTTISYCIVLrMTVTRQFPGAIQTWYDSLGAITKIQDFLCKE 379
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  618 EireeqcapheptpqgpaskYQAVEEGLPSLHSSQPSGSSPPNhpQPLRVVNRKRPAREDCRGltgplqslvpSADGDAd 697
Cdd:TIGR01271  380 E-------------------YKTLEYNLTTTEVEMVNVTASWD--EGIGELFEKIKQNNKARK----------QPNGDD- 427
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  698 nccvqimGGYFT-WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdseigedpspe 776
Cdd:TIGR01271  428 -------GLFFSnFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG------------------- 481
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  777 retatdlDIRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQR 856
Cdd:TIGR01271  482 -------KIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQR 554
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 936
Cdd:TIGR01271  555 ARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEGVCYFYGTFS 632
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  937 DFQRSE---------CQLFEHWK--------------------------------------------------------- 950
Cdd:TIGR01271  633 ELQAKRpdfsslllgLEAFDNFSaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasa 712
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  951 -------------------------------------------------------------------TLMNRQDQELEKE 963
Cdd:TIGR01271  713 rkfsfvqmgpqkaqattiedavrepserkfslvpedeqgeeslprgnqyhhglqhqaqrrqsvlqlmTHSNRGENRREQL 792
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  964 TVTERKATEPPQG---------LSRAMSSRDGLLQDEEEEEEEAAESEEDDnlssMLHQRAEIPWRACAKYLSSAG---- 1030
Cdd:TIGR01271  793 QTSFRKKSSITQQnelaseldiYSRRLSKDSVYEISEEINEEDLKECFADE----RENVFETTTWNTYLRYITTNRnlvf 868
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVF-SQLLKHMVLVAIDYWLAKWTDSALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLG---IVLCLVTSVT 1106
Cdd:TIGR01271  869 VLIFCLVIFlAEVAASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIITPTSAYYIFYIYVGTAdsvLALGFFRGLP 948
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1107 VEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFL 1186
Cdd:TIGR01271  949 LVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIF 1028
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF----RYEARFQQKLLEYTdsnniASLFL 1262
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFgrqsYFETLFHKALNLHT-----ANWFL 1103
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1263 TAAN-RWLEVRMEYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLLK 1341
Cdd:TIGR01271 1104 YLSTlRWFQMRIDII--FVFFFIAVTFIAIGTNQD-GEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFID 1180
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1342 TEAESYE-------GLLAPSLIPKN------WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS 1408
Cdd:TIGR01271 1181 LPQEEPRpsggggkYQLSTVLVIENphaqkcWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKST 1260
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1409 FSLAFFRMVDTfEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKAL 1488
Cdd:TIGR01271 1261 LLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQF 1339
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1489 PGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSAD 1568
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQ 1419
                         1530      1540      1550
                   ....*....|....*....|....*....|....*
gi 1189438336 1569 LVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
Cdd:TIGR01271 1420 QFLVIEGSSVKQYDSIQKLLNETSLFKQAMSAADR 1454
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1364-1584 4.28e-111

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 350.64  E-value: 4.28e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03244      1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03244     81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03244    161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
701-928 2.66e-102

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 325.58  E-value: 2.66e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFTWTPDGI---PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseigedpsper 777
Cdd:cd03250      1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  778 etatdldirkrGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQ 857
Cdd:cd03250     66 -----------GSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQ 134
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:cd03250    135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNK-TRILVTHQLQLLPHADQIVVLDNGR 204
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1019-1601 4.40e-89

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 302.04  E-value: 4.40e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1019 WRACAKYLSSAGILLLSLLVFSQLLKhmvlVAIDYWLAKWTDSALTLTPAARNcslsqectldqtvYAMVFTVLCSLGIV 1098
Cdd:COG1132      5 RRLLKYLKYKLLLLAILLLLLSALLS----LLLPLLIGRIIDALLADLGELLE-------------LLLLLLLLALLGGV 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1099 LCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVI 1178
Cdd:COG1132     68 LRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAKSGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1179 SYV----TPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDttqlPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDS 1254
Cdd:COG1132    148 FSLswrlALILLLILPLLALVLSLLARKSRKLSRRVREALG----ELNARLLESLSGIRVIKAFGAEDRELKRFEEANEE 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1255 NNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVK 1334
Cdd:COG1132    224 LRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLTVGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAE 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1335 RIHGLLKTEAESYEGLLAPslipknWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1414
Cdd:COG1132    304 RLFELLDEEPEVEDPPDPL------KDTIGSIEFENVSFSYPGK-KPVLKDISFSIEPGEKVAIVGPSGSGKSTLIKLLL 376
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1415 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLD 1493
Cdd:COG1132    377 RLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPdATDEEIEEALKLANAHEFIANLPDGYD 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:COG1132    457 TIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNADRIIVL 536
                          570       580
                   ....*....|....*....|....*...
gi 1189438336 1574 KRGAILEFDKPEKLLsRKDSVFASFVRA 1601
Cdd:COG1132    537 DNGRIVERGTHEELL-AKGGLYARLYQA 563
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
1030-1337 1.30e-87

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 287.48  E-value: 1.30e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSAltltpaarncslsqecTLDQTVYAMVFTVLCSLG-IVLCLVTSVTVE 1108
Cdd:cd18580      1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSP----------------NSSSGYYLGVYAALLVLAsVLLVLLRWLLFV 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1109 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA 1188
Cdd:cd18580     65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1189 LLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRW 1268
Cdd:cd18580    145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1269 LEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18580    225 LGLRLDLLGALLALVVALLAV--LLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERIL 291
ABC_6TM_MRP1_2_3_6_D2_like cd18603
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ...
1036-1337 9.68e-84

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350047 [Multi-domain]  Cd Length: 296  Bit Score: 276.67  E-value: 9.68e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1036 LLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAARNcslsqectlDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVA 1115
Cdd:cd18603      3 LILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTE---------QRDYRLGVYGALGLGQAIFVFLGSLALALGCVRAS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIV 1195
Cdd:cd18603     74 RNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIPLAIL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1196 CYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEY 1275
Cdd:cd18603    154 YFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAVRLEF 233
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1276 IGACVVLIAAVTSIsnsLHRE-LSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18603    234 LGNLIVLFAALFAV---LSRDsLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERIK 293
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
1031-1340 8.29e-81

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 268.18  E-value: 8.29e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQLLkhmvLVAIDYWLAKWT---DSALTLTPAARNcslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTV 1107
Cdd:cd18604      2 ALLLLLFVLSQLL----SVGQSWWLGIWAsayETSSALPPSEVS----------VLYYLGIYALISLLSVLLGTLRYLLF 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1108 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLV 1187
Cdd:cd18604     68 FFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1188 ALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANR 1267
Cdd:cd18604    148 PAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNR 227
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1268 WLEVRMEYIGACVVLIAAVTSISNslhRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIHGLL 1340
Cdd:cd18604    228 WLSVRIDLLGALFSFATAALLVYG---PGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1360-1584 2.63e-78

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 257.34  E-value: 2.63e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1360 WPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL 1439
Cdd:cd03369      1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1440 RSRLSIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEiaqlklvvkalpggldaiITEGGENFSQGQRQLFCLARAFVR 1519
Cdd:cd03369     81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1520 KTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03369    143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
1031-1337 6.00e-75

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 251.68  E-value: 6.00e-75
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQllkhmvlVAIDYWLAKWTDSAltltpaarNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1110
Cdd:cd18605      5 LLSLILMQASR-------NLIDFWLSYWVSHS--------NNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYG 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1190
Cdd:cd18605     70 GLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1191 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLE 1270
Cdd:cd18605    150 PLAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLS 229
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1271 VRMEYIGACVVLIAAVTSI-SNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18605    230 IRLQLLGVLIVTFVALTAVvQHFFGLSIDAGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVR 297
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
301-610 7.73e-73

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 245.09  E-value: 7.73e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  301 LSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfQPKTQ-------FLGVYFVSSqeflanayvlavllflalllqrTFL 373
Cdd:cd18579      1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPD--EPLSEgyllalaLFLVSLLQS----------------------LLL 56
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  374 QASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLY 453
Cdd:cd18579     57 HQYFFLSFRLGMRVRSALSSLIYRKALRLSSS--ARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLY 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  454 YILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSL 533
Cdd:cd18579    135 RLLGWAALAGLGVLLLLIPLQAFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKAL 214
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  534 RAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEadFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18579    215 RKFGYLRALNSFLFFSTPVLVSLATFATYVLLGNP--LTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
1031-1337 1.56e-69

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 235.45  E-value: 1.56e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1031 ILLLSLLVFSQLLKhmvlVAIDYWLAKWTDSALTLTpaarncslsqectldQTVYAMVFTVLCSLGIVLCLVTSVTVEWT 1110
Cdd:cd18606      2 PLLLLLLILSQFAQ----VFTNLWLSFWTEDFFGLS---------------QGFYIGIYAGLGVLQAIFLFLFGLLLAYL 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALL 1190
Cdd:cd18606     63 GIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALP 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1191 PLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASlFLTAAN-RWL 1269
Cdd:cd18606    143 PLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAYGAQDRFIKKNEKLIDNMNRAY-FLTIANqRWL 221
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1270 EVRMEYIGACVVLIAAVTSISNSLHreLSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18606    222 AIRLDLLGSLLVLIVALLCVTRRFS--ISPSSTGLVLSYVLQITQVLSWLVRQFAEVENNMNSVERLL 287
ABC_6TM_MRP5_8_9_D2 cd18599
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ...
1030-1337 2.76e-69

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350043 [Multi-domain]  Cd Length: 313  Bit Score: 235.92  E-value: 2.76e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKW------TDSALTLTPAARNCSLSQECTLD--QTVYAMVFTVLcslgIVLCL 1101
Cdd:cd18599      1 GYVVFLFVLLLFILSVGSTVFSDWWLSYWlkqgsgNTTNNVDNSTVDSGNISDNPDLNfyQLVYGGSILVI----LLLSL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1181
Cdd:cd18599     77 IRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 TPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLF 1261
Cdd:cd18599    157 FPWFLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFL 236
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1262 LTAANRWLEVRMEYIGACVVLIAAVTSIsnSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRIH 1337
Cdd:cd18599    237 FNCAMRWLAVRLDILAVLITLITALLVV--LLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERIL 310
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
1088-1591 7.55e-66

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 225183 [Multi-domain]  Cd Length: 709  Bit Score: 238.28  E-value: 7.55e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1088 VFTVLCSLGIVLCLVTSVTvEWTGLKVAKRLHRSLLNRIILA----PMRFFETTPLGSILNRFSsDCNTIDQHIP-STLE 1162
Cdd:COG2274    196 LAIGLLLAALFEALLRLLR-TYLIAHLGKRLDLELSGRFFRHllrlPLSYFEKRSVGEIISRVR-ELEQIREFLTgSILT 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISYVTPVFLVALLPLAIVC---YFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFR 1239
Cdd:COG2274    274 LIIDLLFALIFLAVMFLYSWKLTLIVLAAIPLNVlitLIFQPLLRRKTRKLIEESAEQQ----SFLVETIKGIETVKALA 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1240 YEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGlvglGLTYALMVSNYLNWM 1319
Cdd:COG2274    350 AEPRFRSQWDNRLAKQVNIGFKTEKLALILNTIKSLLQQLSSVLILWFGAILVLEGELTLG----QLVAFNMLAGYFISP 425
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1320 VRNLADM--ELQL--GAVKRIHGLLKTEAESYEGllapSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQK 1395
Cdd:COG2274    426 ITRLSQLwtDFQQakVALERLGDILDTPPEQEGD----KTLIHLPKLQGEIEFENVSFRYGPDDPPVLEDLSLEIPPGEK 501
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1396 IGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTL 1472
Cdd:COG2274    502 VAIVGRSGSGKSTLLKLLLGLYKPQQGRILLDGVDLNDIDLASLRRQVGYVLQDPFLFSGSIRENIalgNPE--ATDEEI 579
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1473 WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR 1552
Cdd:COG2274    580 IEAAQLAGAHEFIENLPMGYDTPVGEGGANLSGGQRQRLALARALLSKPKILLLDEATSALDPETEAIILQNLLQILQGR 659
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1189438336 1553 TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:COG2274    660 TVIIIAHRLSTIRSADRIIVLDQGKIVEQGSHEELLAQG 698
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1364-1592 2.04e-61

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 209.77  E-value: 2.04e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03254      1 GEIEFENVNFSYDEK-KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLW-EALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03254     80 GVVLQDTFLFSGTIMENIRLGRPNATDEEViEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:cd03254    160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABC_6TM_MRP1_2_3_6_D1_like cd18595
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ...
301-610 1.48e-60

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350039 [Multi-domain]  Cd Length: 290  Bit Score: 209.63  E-value: 1.48e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  301 LSSTFRILADLLGFAGPLcIFGIVDHLGKENDVFQPKTQFLGVYFvssqeFLANayvlavllflalLLQRTFLQASYYVA 380
Cdd:cd18595      1 LAALLKLLSDILLFASPQ-LLKLLINFVEDPDEPLWKGYLYAVLL-----FLVS------------IIQSLLLHQYFHRC 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  381 IETGINLRGAIQTKIYNKIMHLStsNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSA 460
Cdd:cd18595     63 FRLGMRIRTALTSAIYRKALRLS--NSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSV 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  461 LIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYT 540
Cdd:cd18595    141 LAGLGVMILLIPLNAVLARKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  541 SISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18595    221 AVSSFLWTCAPFLVSLATFATYVLSDPDNVLDAEKAFVSLSLFNILRFPLSMLPMVISNLVQASVSLKRL 290
ABC_6TM_MRP4_D2_like cd18601
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ...
1030-1336 5.62e-60

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350045 [Multi-domain]  Cd Length: 314  Bit Score: 209.10  E-value: 5.62e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1030 GILLLSLLVFSQLLKHMVLVAIDYWLAKWTDS-----ALTLTPAARNCSLSQECTLDQTVYAMVFTVLCSLGIVLCLVTS 1104
Cdd:cd18601      1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLeeklnDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1105 VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPV 1184
Cdd:cd18601     81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1185 FLVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIA-SLFLT 1263
Cdd:cd18601    161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAwFLFLA 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1264 aANRWLEVRMEYIgaCVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18601    241 -TSRWLAVRLDAL--CALFVTVVAFGSLFLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1102-1597 1.04e-53

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 198.79  E-value: 1.04e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISY- 1180
Cdd:TIGR02203   73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYy 152
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1181 ---VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQLDDTtqlplLSHFA-ETVEGLTTIRAFRYEARFQQKLLEYTDSNN 1256
Cdd:TIGR02203  153 swqLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQ-----VTTVAeETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1257 IASLFLTAANRWLEVRMEYIG----ACVVLIAAVTSISNSLhrelSAG-LVGLGLTYALMVSNylnwmVRNLAD----ME 1327
Cdd:TIGR02203  228 RLAMKMTSAGSISSPITQLIAslalAVVLFIALFQAQAGSL----TAGdFTAFITAMIALIRP-----LKSLTNvnapMQ 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1328 LQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKS 1407
Cdd:TIGR02203  299 RGLAAAESLFTLLDSPPEKDTGTRAIERA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1408 SFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPeRKCSDSTLWEALEIAQLKLV 1484
Cdd:TIGR02203  373 TLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIaygRT-EQADRAEIERALAAAYAQDF 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1485 VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTI 1564
Cdd:TIGR02203  452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTI 531
                          490       500       510
                   ....*....|....*....|....*....|...
gi 1189438336 1565 LSADLVIVLKRGAILEFDKPEKLLSRkDSVFAS 1597
Cdd:TIGR02203  532 EKADRIVVMDDGRIVERGTHNELLAR-NGLYAQ 563
ABC_6TM_YOR1_D1_like cd18597
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ...
372-610 5.66e-52

Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350041 [Multi-domain]  Cd Length: 293  Bit Score: 184.96  E-value: 5.66e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18597     59 LLNHFFYRSMLTGAQVRAALTKAIYRKSLRLSGK--SRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAL 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 531
Cdd:cd18597    137 LIVNLGPSALVGIGVLILSIPLQGFLMKKLFKLRKKANKITDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELK 216
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  532 SLRAFAIYTSISIFMNTAIPIAAVLITFVghVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18597    217 YVRKLQILRSILTAVAFSLPVLASMLSFI--TYYATGHTLDPANIFSSLALFNVLRMPLMFLPLALSSLADALVALKRI 293
ABC_6TM_VMR1_D1_like cd18596
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
311-608 2.25e-51

Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350040 [Multi-domain]  Cd Length: 309  Bit Score: 183.85  E-value: 2.25e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  311 LLGFAGPLCIFGIVDHLgkENDVFQPKTQ---FLGVYFVSSqefLANAyvlavllflalllqrTFLQASYYVAIETGINL 387
Cdd:cd18596     11 VLSFAPPFFLNRLLRYL--EDPGEDATVRpwvWVLLLFLGP---LLSS---------------LLDQQYLWIGRRLSVRL 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  388 RGAIQTKIYNKIMHL-----------------STSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVI 450
Cdd:cd18596     71 RAILTQLIFEKALRRrdksgssksseskkkdkEEDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIV 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  451 LLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEM 530
Cdd:cd18596    151 FLYRLLGWSALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEEL 230
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  531 TSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18596    231 KWLRKRFLLDLLLSLLWFLIPILVTVVTFATYTLVMGQ-ELTASVAFTSLALFNMLRGPLNVLPELITQLLQAKVSLD 307
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1366-1576 6.68e-51

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 177.19  E-value: 6.68e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03228      1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03228     81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1526 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:cd03228    120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
1113-1591 4.37e-49

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227321 [Multi-domain]  Cd Length: 559  Bit Score: 184.77  E-value: 4.37e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1113 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFLVA 1188
Cdd:COG4988     70 KVRASLRQLVLDKLAKLGPAFIAQKPAGSAATLALEGIEQLEPYYARYLPQMFLSAIVPLLILIAIFFFNWaaalILLIT 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1189 LLPLAIVCYFIQKyfRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQKLleYTDSNNIASL-------- 1260
Cdd:COG4988    150 APLIPLFMILVGL--AAKDASEKQFSALARLS--GHFLDRLRGLETLRAFGRTEATEERI--RKDSEDFRKAtmsvlria 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1261 FLTAAnrwlevRMEYIGACVVLIAAVTSisnsLHRELSAGLVGL--GLTyALMVSNYLNWMVRNL-ADMELQL---GAVK 1334
Cdd:COG4988    224 FLSSA------VLEFFAYLSIALVAVYI----GFRLLGEGDLTLfaGLF-VLILAPEFFQPLRDLgSFFHAAAageAAAD 292
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1335 RIHGLLKTEAESYEGLLAPSLipkNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1414
Cdd:COG4988    293 KLFTLLESPVATPGSGEKAEV---ANEPPIEISLENLSFRYPDG-KPALSDLNLTIKAGQLTALVGASGAGKSTLLNLLL 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1415 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVVkALPGG 1491
Cdd:COG4988    369 GFLAPTQGEIRVNGIDLRDLSPEAWRKQISWVSQNPYLFAGTIRENIllaRPDA--SDEEIIAALDQAGLLEFV-PKPDG 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1492 LDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVI 1571
Cdd:COG4988    446 LDTVIGEGGAGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQALQELAKQKTVLVITHRLEDAADADRIV 525
                          490       500
                   ....*....|....*....|
gi 1189438336 1572 VLKRGAILEFDKPEKLLSRK 1591
Cdd:COG4988    526 VLDNGRLVEQGTHEELSEKQ 545
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
287-954 6.00e-49

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 184.55  E-value: 6.00e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  287 IWQALSHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKE-NDVFQPKTQFLGVYFVSsqeFLANAYVLavllfla 365
Cdd:COG1132      4 LRRLLKYLKYKLLLLAILLLLLSALLSLLLPLLIGRIIDALLADlGELLELLLLLLLLALLG---GVLRALQS------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  366 lllqrtflqasyYVAIETGINLRGAIQTKIYNKIMHLSTSNLsmGEMTAGQICNLVAIDTNQL-MWFFFLCPNLWAMPVQ 444
Cdd:COG1132     74 ------------YLGSRLGQKIVADLRRDLFEKLLRLPLSFF--DKAKSGDLISRLTNDVEAVsNLVSTVLVLVFTSILL 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  445 IIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVET 524
Cdd:COG1132    140 LIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREALGELNARLLESLSGIRVIKAFGAEDRELKRFEE 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  525 TRRKE-MTSLRAFAIYTSISIFMNTAIPIAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:COG1132    220 ANEELrRANLRASRLEALLAPLMLLLSSLGTVLVLALG-GFLVLSGSLTVGALAAFILYLLRLLTPILQLGEVVSLLQRA 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  604 LVSVQKLSEFLSSAEIREEQcaPHEPTPQGPASKYQAVEeglpslhssqpsgssppnhpqplrvvnrkrparedcrgltg 683
Cdd:COG1132    299 SAAAERLFELLDEEPEVEDP--PDPLKDTIGSIEFENVS----------------------------------------- 335
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  684 plqslvpsadgdadnccvqimggyFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSS 763
Cdd:COG1132    336 ------------------------FSY-PGKKPVLKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDG 390
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  764 LPDSEIGEDpsperetatdlDIRKRgpVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQT 842
Cdd:COG1132    391 IDIRDISLD-----------SLRKR--IGIVSQDPLLFSGTIRENIALGRPdATDEEIEEALKLANAHEFIANLPDGYDT 457
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  843 QIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWII 922
Cdd:COG1132    458 IVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALD-TETEALIQDALKKLLKG--RTTLIIAHRLSTIKNADRII 534
                          650       660       670
                   ....*....|....*....|....*....|..
gi 1189438336  923 AMKDGTIQREGTLKDFQRSECQLFEHWKTLMN 954
Cdd:COG1132    535 VLDNGRIVERGTHEELLAKGGLYARLYQAQGG 566
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
1086-1591 3.95e-47

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 179.53  E-value: 3.95e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:PRK10790    68 AAAYVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSAL-AVISYVTPVFLVALL--PLAIVCYFIQKYF------RVASRdLQQLDDTtqlpllshFAETVEGLTTIR 1236
Cdd:PRK10790   148 RSAALIGAMLvAMFSLDWRMALVAIMifPAVLVVMVIYQRYstpivrRVRAY-LADINDG--------FNEVINGMSVIQ 218
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 AFRYEARFQQKLLEYTDSNNIAslfltaanrwlevRMEYIGACVVLIAAVTSISNS--------LHRELSAGLVGLGLTY 1308
Cdd:PRK10790   219 QFRQQARFGERMGEASRSHYMA-------------RMQTLRLDGFLLRPLLSLFSAlilcgllmLFGFSASGTIEVGVLY 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1309 ALMvsNYLNWMVRNLADME-----LQLGAV--KRIHGLLKTEAESYegllAPSLIPKNwpdQGKIQIQNLSVRYDSSlKP 1381
Cdd:PRK10790   286 AFI--SYLGRLNEPLIELTtqqsmLQQAVVagERVFELMDGPRQQY----GNDDRPLQ---SGRIDIDNVSFAYRDD-NL 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1382 VLKHVNALIAPGQKIGICGRTGSGKSSfsLAFFRM----VDTFEGHIIIDGIdiAKLPLHTLRSRLSIILQDPVLFSGTI 1457
Cdd:PRK10790   356 VLQNINLSVPSRGFVALVGHTGSGKST--LASLLMgyypLTEGEIRLDGRPL--SSLSHSVLRQGVAMVQQDPVVLADTF 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1458 RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1537
Cdd:PRK10790   432 LANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGT 511
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1538 ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:PRK10790   512 EQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1366-1597 1.33e-46

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 167.79  E-value: 1.33e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03253      1 IEFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLDPER-KCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1524
Cdd:cd03253     80 VPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1525 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFAS 1597
Cdd:cd03253    160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKG-GLYAE 231
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1364-1603 4.33e-46

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 167.72  E-value: 4.33e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTfEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03289      1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSI 1523
Cdd:cd03289     80 GVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1524 FIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSVFASFVRADK 1603
Cdd:cd03289    160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDR 239
ABC_6TM_MRP5_8_9_D1 cd18592
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ...
372-610 1.07e-45

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350036 [Multi-domain]  Cd Length: 287  Bit Score: 166.97  E-value: 1.07e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  372 FLQASYYVAIETGINLRGAIQTKIYNKIMHLStsnlSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVIL 451
Cdd:cd18592     55 FFSLTWAISYRTGIRLRGAVLGLLYKKILRLR----SLGDKSVGELINIFSNDGQRLFDAAVFGPLVIGGPVVLILGIVY 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMT 531
Cdd:cd18592    131 STYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSIKLIKMYAWEKPFAKKIADIRKEERK 210
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  532 SLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18592    211 ILEKAGYLQSISISLAPIVPVIASVVTFLAHVAL--GNDLTAAQAFTVIAVFNSMRFSLRMLPYAVKALAEAKVALQRI 287
ABC_6TM_MRP7_D1_like cd18598
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ...
305-610 1.27e-45

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350042 [Multi-domain]  Cd Length: 288  Bit Score: 166.57  E-value: 1.27e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  305 FRILADLLGFAGPLCIFGIVDHLgkENDVFQPKTQFL--GVYFVSSqeFLAnayvlavllflalllqrTFLQASY-YVAI 381
Cdd:cd18598      5 LKLLADVLGFAGPLLLNKLVEFL--EDSSEPLSDGYLyaLGLVLSS--LLG-----------------ALLSSHYnFQMN 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  382 ETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQLMWFfflCPNL---WAMPVQIIVGVILLYYILGV 458
Cdd:cd18598     64 KVSLKVRAALVTAVYRKALRVRSS--SLSKFSTGEIVNLMSTDADRIVNF---CPSFhdlWSLPLQIIVALYLLYQQVGV 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  459 SALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAI 538
Cdd:cd18598    139 AFLAGLVFALVLIPINKWIAKRIGALSEKMMKHKDARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELKALKGRKY 218
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  539 YTSISIFMNTAIPIAAVLITFVGHVsfFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18598    219 LDALCVYFWATTPVLISILTFATYV--LMGNTLTAAKVFTSLALFNMLIGPLNAFPWVLNGLVEAWVSLKRL 288
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
371-956 1.27e-44

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 225183 [Multi-domain]  Cd Length: 709  Bit Score: 173.95  E-value: 1.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  371 TFLQaSYYVAIeTGINLRGAIQTKIYNKIMHLSTS---NLSMGEMTAgQICNLVAIdtNQLMWFFFLcpnlwAMPVQII- 446
Cdd:COG2274    211 RLLR-TYLIAH-LGKRLDLELSGRFFRHLLRLPLSyfeKRSVGEIIS-RVRELEQI--REFLTGSIL-----TLIIDLLf 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  447 --VGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVET 524
Cdd:COG2274    281 alIFLAVMFLYSWKLTLIVLAAIPLNVLITLIFQPLLRRKTRKLIEESAEQQSFLVETIKGIETVKALAAEPRFRSQWDN 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  525 TRRKEMTSLRAFAIYTSISIFMNTAIP-IAAVLITFVGhVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:COG2274    361 RLAKQVNIGFKTEKLALILNTIKSLLQqLSSVLILWFG-AILVLEGELTLGQLVAFNMLAGYFISPITRLSQLWTDFQQA 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  604 LVSVQKLSEFLSSA-EIREEQCAPHEPTPQGpasKYQaveeglpslhssqpsgssppnhpqplrvvnrkrparedCRGLT 682
Cdd:COG2274    440 KVALERLGDILDTPpEQEGDKTLIHLPKLQG---EIE--------------------------------------FENVS 478
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  683 gplqslvpsadgdadnccvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS 762
Cdd:COG2274    479 -------------------------FRYGPDDPPVLEDLSLEIPPGEKVAIVGRSGSGKSTLLKLLLGLYKPQQGRILLD 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  763 SLPDSEIGEDpsperetatdlDIRKRgpVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEACSL---QPDIDILPHG 839
Cdd:COG2274    534 GVDLNDIDLA-----------SLRRQ--VGYVLQDPFLFSGSIRENIALGNPEATD--EEIIEAAQLagaHEFIENLPMG 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  840 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRddKRTVVLVTHKLQYLPHAD 919
Cdd:COG2274    599 YDTPVGEGGANLSGGQRQRLALARALLSKPKILLLDEATSALDPETEAIILQN-LLQILQ--GRTVIIIAHRLSTIRSAD 675
                          570       580       590
                   ....*....|....*....|....*....|....*..
gi 1189438336  920 WIIAMKDGTIQREGTLKDFqRSECQLFEHwktLMNRQ 956
Cdd:COG2274    676 RIIVLDQGKIVEQGSHEEL-LAQGGLYAR---LYQQQ 708
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
714-939 9.32e-44

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 161.18  E-value: 9.32e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslpdseigedpsperetatdldIRKRGPVAY 793
Cdd:cd03291     49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK--------------------------IKHSGRISF 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03291    103 SSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  874 LDDPFSALDIHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQ 939
Cdd:cd03291    183 LDSPFGYLDVFTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 246
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
1034-1316 1.43e-43

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 395537 [Multi-domain]  Cd Length: 274  Bit Score: 160.12  E-value: 1.43e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1034 LSLLVFSQLLKHMVLVAIDYWLAKWTDSALTLTPAArncslsqecTLDQTVYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1113
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE---------TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGER 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLA 1193
Cdd:pfam00664   72 LSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1194 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRM 1273
Cdd:pfam00664  152 PLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGIT 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1189438336 1274 EYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYL 1316
Cdd:pfam00664  232 QFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
1114-1592 4.07e-43

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 169.52  E-value: 4.07e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALLPL 1192
Cdd:TIGR00958  232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPrLTMVTLINL 311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1193 AIVcYFIQK----YFRVASRDLQQ-LDDTTQLPLlshfaETVEGLTTIRAF---RYEA-RFQQKLLEYTDSN---NIASL 1260
Cdd:TIGR00958  312 PLV-FLAEKvfgkRYQLLSEELQEaVAKANQVAE-----EALSGMRTVRSFaaeEGEAsRFKEALEETLQLNkrkALAYA 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1261 FLTAANRWLE----VRMEYIGACVVLIAAVTSisnslhrelsAGLVGLgLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:TIGR00958  386 GYLWTTSVLGmliqVLVLYYGGQLVLTGKVSS----------GNLVSF-LLYQEQLGEAVRVLSYVYSGMMQAVGASEKV 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1337 HGLL-KTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFF 1414
Cdd:TIGR00958  455 FEYLdRKPNIPLTGTLAPL------NLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1415 RMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPE-RKCSDSTLWEALEIAQLKLVVKALPGGLD 1493
Cdd:TIGR00958  529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvvMTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR00958  609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVL 686
                          490
                   ....*....|....*....
gi 1189438336 1574 KRGAILEFDKPEKLLSRKD 1592
Cdd:TIGR00958  687 KKGSVVEMGTHKQLMEDQG 705
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1366-1601 7.59e-43

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 156.93  E-value: 7.59e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:cd03249      1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDPVLFSGTIRFNL---DPERkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03249     81 LVSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKdSVFASFVRA 1601
Cdd:cd03249    159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQK-GVYAKLVKA 237
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1366-1591 2.61e-42

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 155.08  E-value: 2.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03251      1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03251     81 VSQDVFLFNDTVAENIaygRPG--ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:cd03251    159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQG 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
708-927 3.07e-41

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 149.84  E-value: 3.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRK 787
Cdd:cd03228      8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE-----------SLRK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQ 867
Cdd:cd03228     77 N--IAYVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLR 113
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 927
Cdd:cd03228    114 DPPILILDEATSALDPETEALILEA-LRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
708-933 7.42e-41

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 150.43  E-value: 7.42e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSperetatdlDIRK 787
Cdd:cd03245     10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL--DPA---------DLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RgpVAYASQKPWLLNATVEENIIFESPF-NKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 866
Cdd:cd03245     79 N--IGYVPQDVTLFYGTLRDNITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03245    157 NDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD--KTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
1116-1592 1.52e-40

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227320 [Multi-domain]  Cd Length: 573  Bit Score: 159.42  E-value: 1.52e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1116 KRLHRSLLNriiLAPMRFFETTPlGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF--------LV 1187
Cdd:COG4987     95 VRLFEKLEP---LSPALLLRYRS-GDLLNRLVADVDALDNLYLRVIAPAVVALVLIAVVTIGLSFFSIPLalllglilLL 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1188 ALLPLAIVCYfiqKYFRVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANR 1267
Cdd:COG4987    171 LLLIIPTLFY---RAGRKFGAHLAQGRAA----LRSQFTDWVQGQAELLIFGAEDAYRTALEATEASWLKAQRKQARFTG 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1268 WLEVRMEYIGACVVLIAAVTSISNSLHRELSAGLVGLGLTYALMVSNYLNWMvRNLADMELQ--LGAVKRIHGLLKTEAE 1345
Cdd:COG4987    244 LSDAILLLIAGLLVIGLLLWMAAQVGAGALAQPGAALALLVIFAALEAFEPL-APGAFQHLGqvIASARRLNDILDQKPE 322
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1346 syegllAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHII 1425
Cdd:COG4987    323 ------VTFPDEQTATTGQALELRNVSFTYPGQQTKALKNFNLTLAQGEKVAILGRSGSGKSTLLQLLAGAWDPQQGSIT 396
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1426 IDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGEN 1502
Cdd:COG4987    397 LNGVEIASLDEQALRETISVLTQRVHLFSGTLRDNLrlaNPD--ASDEELWAALQQVGLEKLLESAPDGLNTWLGEGGRR 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1503 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFD 1582
Cdd:COG4987    475 LSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLALLFEHAEGKTLLMVTHRLRGLERMDRIIVLDNGKIIEEG 554
                          490
                   ....*....|
gi 1189438336 1583 KPEKLLSRKD 1592
Cdd:COG4987    555 THAELLANNG 564
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
1095-1600 3.49e-40

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 160.49  E-value: 3.49e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1095 LGIVLCLVTSVTVEWTGLKVAKRLHRSL--------LNRIILAPMRFFETTPLGSILNRFSSDcNTIDQHIPSTLECLSR 1166
Cdd:TIGR03796  198 LGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTAL 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1167 STLLCV-SALAVISYVTPVFLVALLPLAI---VCYFIQKYFRVASRDLQQldDTTQLpllshFAETVEGLTTIR------ 1236
Cdd:TIGR03796  277 DAVMLVfYALLMLLYDPVLTLIGIAFAAInvlALQLVSRRRVDANRRLQQ--DAGKL-----TGVAISGLQSIEtlkasg 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 ----AFRYEARFQQKLLEytdsnniaslfltaANRWLEVRMEYIGacvVLIAAVTSISNSLHRELSAGLV-------GLG 1305
Cdd:TIGR03796  350 lesdFFSRWAGYQAKLLN--------------AQQELGVLTQILG---VLPTLLTSLNSALILVVGGLRVmegqltiGML 412
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1306 LTY-ALMVS-----NYLNWMVRNLADMElqlGAVKRIHGLLKTEAESYEGLLAP--SLIPKNWPDQGKIQIQNLSVRYDS 1377
Cdd:TIGR03796  413 VAFqSLMSSflepvNNLVGFGGTLQELE---GDLNRLDDVLRNPVDPLLEEPEGsaATSEPPRRLSGYVELRNITFGYSP 489
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1378 SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTI 1457
Cdd:TIGR03796  490 LEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTV 569
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1458 RFNL---DPerKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:TIGR03796  570 RDNLtlwDP--TIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1535 MATEnilqKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1600
Cdd:TIGR03796  648 PETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV-GGAYARLIR 710
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1364-1578 4.96e-40

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 148.12  E-value: 4.96e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFR-------MVDTFEGhiiidgidiAKL 1434
Cdd:cd03245      1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLklLAGLYkptsgsvLLDGTDI---------RQL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 PLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLF 1511
Cdd:cd03245     72 DPADLRRNIGYVPQDVTLFYGTLRDNItlgAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAV 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03245    150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
712-942 1.76e-39

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227321 [Multi-domain]  Cd Length: 559  Bit Score: 155.88  E-value: 1.76e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperetaTDLDIRKRgpV 791
Cdd:COG4988    331 PDGKPALSDLNLTIKAGQLTALVGASGAGKSTLLNLLLGFLAPTQGEIRVNGIDLRDL-----------SPEAWRKQ--I 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFESPF-NKQRYKMVIEACSLQPDIDiLPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:COG4988    398 SWVSQNPYLFAGTIRENILLARPDaSDEEIIAALDQAGLLEFVP-KPDGLDTVIGEGGAGLSGGQAQRLALARALLSPAS 476
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  871 VVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:COG4988    477 LLLLDEPTAHLDAE-TEQIILQALQELAKQ--KTVLVITHRLEDAADADRIVVLDNGRLVEQGTHEELSEKQ 545
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
708-934 3.94e-39

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 146.22  E-value: 3.94e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAAlgemqkvsgavFWsslpdseigeDPSPERETATDLDI 785
Cdd:cd03251      8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLvnLIPR-----------FY----------DVDSGRILIDGHDV 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  786 RK------RGPVAYASQKPWLLNATVEENIIFESPfNKQRyKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQR 856
Cdd:cd03251     67 RDytlaslRRQIGLVSQDVFLFNDTVAENIAYGRP-GATR-EEVEEAaraANAHEFIMELPEGYDTVIGERGVKLSGGQR 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03251    145 QRIAIARALLKDPPILILDEATSALDTE-SERLVQAALERLMKN--RTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1291-1591 8.57e-39

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227590 [Multi-domain]  Cd Length: 497  Bit Score: 152.51  E-value: 8.57e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1291 NSLHRELSAGLVGLGltyalmvSNYLNwMVRNLADMElqlgavkRIHGLLKTEAESYEGLLAPSLIPKnwpDQGKIQIQN 1370
Cdd:COG5265    206 NALLFQLSIPLNFLG-------FSYRE-IRQALTDME-------KMFDLLDVEAEVSDAPDAPPLWPV---RLGAVAFIN 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1371 LSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDP 1450
Cdd:COG5265    268 VSFAYDPR-RPILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSITIDGQDIRDVTQQSLRRAIGIVPQDT 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1451 VLFSGTIRFNLDPER-KCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEA 1529
Cdd:COG5265    347 VLFNDTIAYNIKYGRpDATAEEVGAAAEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVAIARTILKNPPILILDEA 426
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1530 TASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:COG5265    427 TSALDTHTEQAIQAALREVSAGRTTLVIAHRLSTIIDADEIIVLDNGRIVERGTHEELLAAG 488
ABC_6TM_CFTR_D1 cd18594
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
318-610 1.06e-37

Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.


Pssm-ID: 350038 [Multi-domain]  Cd Length: 291  Bit Score: 143.93  E-value: 1.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  318 LCIFGIVDHLGKendVFQPktQFLG---VYFV-SSQEFLANAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQT 393
Cdd:cd18594      2 LGILLFLEESLK---IVQP--LLLGrlvAYFVpDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSS 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  394 KIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPV 473
Cdd:cd18594     77 LIYKKTLKLSSSALS--KITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  474 QYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIYTSISIFMNTAIPIA 553
Cdd:cd18594    155 QAYLGKLFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTL 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  554 AVLITFVGHVsFFKEAdFSPSVAFASLSLFHILVTPL-FLLSSVVRSTVKALVSVQKL 610
Cdd:cd18594    235 VSFATFVPYV-LTGNT-LTARKVFTVISLLNALRMTItRFFPESIQTLSESRVSLKRI 290
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
1168-1573 1.34e-37

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 149.74  E-value: 1.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1168 TLLCVSALAVISYVTPVFLVALLPLAIVcYFIQKYFRVASRDLQQLDDTTQLPllSHFAETVEGLTTIRAFRYEARFQQK 1247
Cdd:TIGR02857  132 PLAILAAVFPQDWISGLILLLTAPLIPI-FMILIGWAAQAAARKQWAALSRLS--GHFLDRLRGLPTLKLFGRAKAQAAA 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1248 LLEYTDSNNIASL------FLTAAnrwlevRMEYIGACVVLIAAVTsISNSL---HRELSAGLVGLGLTYALmvsnYLNw 1318
Cdd:TIGR02857  209 IRRSSEEYRERTMrvlriaFLSSA------VLELFATLSVALVAVY-IGFRLlagDLDLATGLFVLLLAPEF----YLP- 276
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1319 mVRNL-----ADMELQlGAVKRIHGLLkteaeSYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSlKPVLKHVNALIAPG 1393
Cdd:TIGR02857  277 -LRQLgaqyhARADGV-AAAEALFAVL-----DAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPG 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1394 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTL 1472
Cdd:TIGR02857  349 ERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPdASDAEI 428
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1473 WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR 1552
Cdd:TIGR02857  429 REALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR 508
                          410       420
                   ....*....|....*....|.
gi 1189438336 1553 TVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR02857  509 TVLLVTHRLALAALADRIVVL 529
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1366-1590 2.17e-37

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 141.08  E-value: 2.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03252      1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLDPERKCSD-STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIF 1524
Cdd:cd03252     81 VLQENVLFNRSIRDNIALADPGMSmERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1525 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:cd03252    161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE 226
ABC_6TM_MRP4_D1_like cd18593
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ...
376-617 3.06e-37

Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350037 [Multi-domain]  Cd Length: 291  Bit Score: 142.36  E-value: 3.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  376 SYYVAIETGINLRGAIQTKIYNKIMHLSTSnlSMGEMTAGQICNLVAIDTNQL-MWFFFLcPNLWAMPVQIIVGVILLYY 454
Cdd:cd18593     60 YFFGMQRIGMRLRVACSSLIYRKALRLSQA--ALGKTTVGQIVNLLSNDVNRFdQAVLFL-HYLWVAPLQLIAVIYILWF 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  455 ILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLR 534
Cdd:cd18593    137 EIGWSCLAGLAVLLILIPLQSFFGKLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVR 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  535 AFAIYTSisifMNTAIP-IAAVLITFVGHVSFF-KEADFSPSVAFASLSLFHilvtplfllssVVRSTVKALV--SVQKL 610
Cdd:cd18593    217 RTSFLRA----LNMGLFfVSSKLILFLTFLAYIlLGNILTAERVFVTMALYN-----------AVRLTMTLFFpfAIQFG 281

                   ....*..
gi 1189438336  611 SEFLSSA 617
Cdd:cd18593    282 SELSVSI 288
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1102-1591 4.16e-37

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 149.01  E-value: 4.16e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1102 VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV 1181
Cdd:PRK11176    84 ISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 T---PVFLVALLPL-AIVCYFIQKYFRVASRDLQ----QLDDTTQLPLLSHFAETVEGLTTIRAFRYEA---RFQQKLLE 1250
Cdd:PRK11176   164 SwqlSLILIVIAPIvSIAIRVVSKRFRNISKNMQntmgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKvsnRMRQQGMK 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1251 YTDSNN--------IASLFLtaanrwlevrmeyigACVVLIAAVTSISNslhrELSAGlvglglTYALMVSNYLNWM--V 1320
Cdd:PRK11176   244 MVSASSisdpiiqlIASLAL---------------AFVLYAASFPSVMD----TLTAG------TITVVFSSMIALMrpL 298
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1321 RNLADMELQ----LGAVKRIHGLLKTEAESYEGLLAPSlipknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKI 1396
Cdd:PRK11176   299 KSLTNVNAQfqrgMAACQTLFAILDLEQEKDEGKRVIE------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTV 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1397 GICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWE 1474
Cdd:PRK11176   373 ALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIayARTEQYSREQIEE 452
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1475 ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTV 1554
Cdd:PRK11176   453 AARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS 532
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 1189438336 1555 VTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRK 1591
Cdd:PRK11176   533 LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQN 569
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
1121-1591 7.09e-37

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 150.28  E-value: 7.09e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1121 SLLNRIILAPMRFFETTPLGSILNRFSsDCNTIDQHIPSTLeclsRSTLLCVSALAVISYV-----TPVFLVALLPL--- 1192
Cdd:TIGR01193  234 SYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTI----LSLFLDMWILVIVGLFlvrqnMLLFLLSLLSIpvy 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1193 AIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAFRYEA-RFQQ----------KLLEYTDSNNIASLF 1261
Cdd:TIGR01193  309 AVIIILFKRTFNKLNHDAMQ----ANAVLNSSIIEDLNGIETIKSLTSEAeRYSKidsefgdylnKSFKYQKADQGQQAI 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1262 LTAANRWLEVRMEYIGACVVLIAAVTsisnslhrelsaglVGLGLTYALMVSNYLNwMVRNLADMELQLGAVK----RIH 1337
Cdd:TIGR01193  385 KAVTKLILNVVILWTGAYLVMRGKLT--------------LGQLITFNALLSYFLT-PLENIINLQPKLQAARvannRLN 449
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1338 GLLKTEAESYEGLLAPSLIPKNwpdqGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV 1417
Cdd:TIGR01193  450 EVYLVDSEFINKKKRTELNNLN----GDIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFF 524
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1418 DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCSDSTLWEALEIAQLKLVVKALPGGLDAI 1495
Cdd:TIGR01193  525 QARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE 604
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1496 ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATEnilQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:TIGR01193  605 LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVnnLLNLQDKTIIFVAHRLSVAKQSDKIIVL 681
                          490
                   ....*....|....*...
gi 1189438336 1574 KRGAILEFDKPEKLLSRK 1591
Cdd:TIGR01193  682 DHGKIIEQGSHDELLDRN 699
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
714-934 2.95e-36

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 137.74  E-value: 2.95e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEdpsperetatdldIRKRGPVAY 793
Cdd:cd03254     15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR-------------KSLRSMIGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNATVEENIIFESPFNKQryKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:cd03254     82 VLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKeagAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  871 VVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03254    160 ILILDEATSNIDTE-TEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGT 220
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
1093-1600 1.12e-35

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 146.25  E-value: 1.12e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1093 CSLGIVLCLVTSVTVEWT-GLKVAK-------RLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLECL 1164
Cdd:TIGR03797  178 IALALLAAAVGAAAFQLAqSLAVLRletrmdaSLQAAVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRRILSGSTLTT 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYVTP---VFLVALLPLAIVCYFIQKYFRVA-SRDLQQLDDTTQLPLLshfaETVEGLTTIR---- 1236
Cdd:TIGR03797  257 LLSGIFALLNLGLMFYYSWklaLVAVALALVAIAVTLVLGLLQVRkERRLLELSGKISGLTV----QLINGISKLRvaga 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1237 ---AF-RYEARF-QQKLLEYtDSNNIASlFLTAANRWLEVRmeyigACVVLIAAVTSISNSLHreLSAGLVgLGLTYAL- 1310
Cdd:TIGR03797  333 enrAFaRWAKLFsRQRKLEL-SAQRIEN-LLTVFNAVLPVL-----TSAALFAAAISLLGGAG--LSLGSF-LAFNTAFg 402
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1311 MVSNYLNWMVRNLADMELQLGAVKRIHGLLKTEAESYEGLLAPSLIpknwpdQGKIQIQNLSVRYDSSLKPVLKHVNALI 1390
Cdd:TIGR03797  403 SFSGAVTQLSNTLISILAVIPLWERAKPILEALPEVDEAKTDPGKL------SGAIEVDRVTFRYRPDGPLILDDVSLQI 476
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1391 APGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID----IAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdperk 1466
Cdd:TIGR03797  477 EPGEFVAIVGPSGSGKSTL----LRLLLGFETPESGSVFYdgqdLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI----- 547
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1467 CSDSTL-----WEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNIL 1541
Cdd:TIGR03797  548 AGGAPLtldeaWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALD----NRT 623
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1542 QKVVMTAFA--DRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRkDSVFASFVR 1600
Cdd:TIGR03797  624 QAIVSESLErlKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAR-EGLFAQLAR 683
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
712-934 1.18e-33

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 130.35  E-value: 1.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKS---SLLLAalgemqkvsgavFWsslpdseigeDPSPERETATDLDIRK- 787
Cdd:cd03249     14 PD-VPILKGLSLTIPPGKTVALVGSSGCGKStvvSLLER------------FY----------DPTSGEILLDGVDIRDl 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 -----RGPVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRI 859
Cdd:cd03249     71 nlrwlRSQIGLVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRI 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03249    149 AIARALLRNPKILLLDEATSALDAE-SEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
449-934 4.08e-33

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 136.77  E-value: 4.08e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  449 VILLYYILGVSAligaaVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTN----EMLRGIKLLKLYAWENIFRTRVE- 523
Cdd:TIGR02203  147 IVLLYYSWQLTL-----IVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTtvaeETLQGYRVVKLFGGQAYETRRFDa 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  524 ---TTRRKEMTSLRAFAIYTSISIFmntaipIAAVLITFVGHVSFFKEADFSPSVA-FASLSLFHILV-TPLFLLSSVVR 598
Cdd:TIGR02203  222 vsnRNRRLAMKMTSAGSISSPITQL------IASLALAVVLFIALFQAQAGSLTAGdFTAFITAMIALiRPLKSLTNVNA 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  599 STVKALVSVQKLSEFLSSAeireeqcapheptpqgpaskyQAVEEGLpslhssqpsgssppnhpqplRVVNRKRpAREDC 678
Cdd:TIGR02203  296 PMQRGLAAAESLFTLLDSP---------------------PEKDTGT--------------------RAIERAR-GDVEF 333
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  679 RGLTgplqslvpsadgdadnccvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEmqkvs 756
Cdd:TIGR02203  334 RNVT-------------------------FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLvnLIPRFYE----- 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  757 gavfwsslPDS-EIGEDPSPERE-TATDLdirkRGPVAYASQKPWLLNATVEENIIFESP--FNKQRYKMVIEACSLQPD 832
Cdd:TIGR02203  384 --------PDSgQILLDGHDLADyTLASL----RRQVALVSQDVVLFNDTIANNIAYGRTeqADRAEIERALAAAYAQDF 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  833 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKL 912
Cdd:TIGR02203  452 VDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE-SERLVQAALERLMQG--RTTLVIAHRL 528
                          490       500
                   ....*....|....*....|..
gi 1189438336  913 QYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR02203  529 STIEKADRIVVMDDGRIVERGT 550
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
712-924 4.50e-33

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 135.88  E-value: 4.50e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:TIGR02857  332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD-----------SWRDQ--I 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFESPFNKQ-RYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR02857  399 AWVPQHPFLFAGTIAENIRLARPDASDaEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  871 VVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAM 924
Cdd:TIGR02857  479 LLLLDEPTAHLDAETEAEVLEA-LRALAQG--RTVLLVTHRLALAALADRIVVL 529
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
299-590 4.83e-33

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 395537 [Multi-domain]  Cd Length: 274  Bit Score: 129.69  E-value: 4.83e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  299 LVLSSTFRILADLLGFAGPLCIFGIVDHLGKENDvfqPKTQFLGVYFVssqeFLANAYVLAVLlflalllqrtFLQASYY 378
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD---PETQALNVYSL----ALLLLGLAQFI----------LSFLQSY 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  379 VAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGV 458
Cdd:pfam00664   64 LLNHTGERLSRRLRRKLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGW 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  459 S-ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFA 537
Cdd:pfam00664  142 KlTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKA 221
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  538 IYTSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPL 590
Cdd:pfam00664  222 VANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
707-934 1.07e-32

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 127.73  E-value: 1.07e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPdGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVfwsslpdsEIGedpsperetatDLD 784
Cdd:cd03253      7 TFAYDP-GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTIlrLLFRFYDVS--SGSI--------LID-----------GQD 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 IRK------RGPVAYASQKPWLLNATVEENIIFESP--FNKQrykmVIEAC---SLQPDIDILPHGDQTQIGERGINLSG 853
Cdd:cd03253     65 IREvtldslRRAIGVVPQDTVLFNDTIGYNIRYGRPdaTDEE----VIEAAkaaQIHDKIMRFPDGYDTIVGERGLKLSG 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  854 GQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03253    141 GEKQRVAIARAILKNPPILLLDEATSALDTH-TEREIQAALRDVSKG--RTTIVIAHRLSTIVNADKIIVLKDGRIVERG 217

                   .
gi 1189438336  934 T 934
Cdd:cd03253    218 T 218
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1117-1560 1.01e-31

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 132.10  E-value: 1.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1117 RLHRSLLnRIILAPMRFFETtplGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVALLPLAIVC 1196
Cdd:TIGR02868   91 RVYERLA-RQALAGRRRLRR---GDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLA 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1197 YFIQKYF-----RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEV 1271
Cdd:TIGR02868  167 GFVAPLVslraaRAAEQALARLRGE----LAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAA 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1272 RMEYIGACVVLIAAVTSISNSLHRELSAG------LVGLGLTYALMVsnylnwmvrnLADMELQLGAVK----RIHGLLK 1341
Cdd:TIGR02868  243 LTLLAAGLAVLGALWAGGPAVADGRLAPVtlavlvLLPLAAFEAFAA----------LPAAAQQLTRVRaaaeRIVEVLD 312
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1342 TEAESYEGLL-APSLIPKNWPDqgkIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF 1420
Cdd:TIGR02868  313 AAGPVAEGSApAAGAVGLGKPT---LELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1421 EGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEG 1499
Cdd:TIGR02868  389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEG 468
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1500 GENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR 1560
Cdd:TIGR02868  469 GARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
1035-1335 1.28e-31

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 126.18  E-value: 1.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1035 SLLVFSQLLKHMVLVAIDYWLAKWTDSaltltpaarncslSQECTLDQT-VYAMVFTVLCSLGIVLCLVTSVTVEWTGLK 1113
Cdd:cd18559      2 FLLIKLVLCNHVFSGPSNLWLLLWFDD-------------PVNGPQEHGqVYLSVLGALAILQGITVFQYSMAVSIGGIF 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1114 VAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAlLPLA 1193
Cdd:cd18559     69 ASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVG-IPLG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1194 IVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDsNNIASLFLTAANRWLEVRM 1273
Cdd:cd18559    148 LLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRD-NELAYLPSIVYLRALAVRL 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1274 EYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKR 1335
Cdd:cd18559    227 WCVGPCIVLFASFFAY---VSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEV 285
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1363-1601 1.17e-30

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 129.70  E-value: 1.17e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1363 QGKIQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSR 1442
Cdd:PRK13657   332 KGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDPVLFSGTIRFNLDPERK-CSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:PRK13657   411 IAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpeklLSRKDSVFASF 1598
Cdd:PRK13657   491 PILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVEsgsFDE----LVARGGRFAAL 566

                   ...
gi 1189438336 1599 VRA 1601
Cdd:PRK13657   567 LRA 569
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
707-938 5.98e-30

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 224047 [Multi-domain]  Cd Length: 235  Bit Score: 119.67  E-value: 5.98e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWtPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdLDIR 786
Cdd:COG1122     10 SFRY-PGRKAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVD-------GLDTSSEKSL---LELR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 856
Cdd:COG1122     79 QK--VGLVFQNPddQLFGPTVEDEVAF-GLENlglpreeiEERVAEALELVGLEELLDRPPF-----------NLSGGQK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTL 935
Cdd:COG1122    145 QRVAIAGVLAMGPEILLLDEPTAGLDPKGRRELLEL-LKKLKEEGGKTIIIVTHDLELVLeYADRVVVLDDGKILADGDP 223

                   ...
gi 1189438336  936 KDF 938
Cdd:COG1122    224 AEI 226
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
708-928 7.36e-30

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 118.34  E-value: 7.36e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslPDSEIGEDPSPERetatdldirk 787
Cdd:cd03225      7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV---DGKDLTKLSLKEL---------- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RGPVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQ 857
Cdd:cd03225     74 RRKVGLVFQNPddQFFGPTVEEEVAF-GLENlglpeeeiEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQ 141
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 928
Cdd:cd03225    142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLE--LLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDGK 211
ABC_6TM_CFTR_D2 cd18600
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ...
1110-1336 1.48e-29

Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350044 [Multi-domain]  Cd Length: 324  Bit Score: 121.06  E-value: 1.48e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1110 TGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVAL 1189
Cdd:cd18600     97 TLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIGAITVVSILQPYIFLAT 176
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1190 LPLAIVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFR----YEARFQQKLLEYTdsnniASLFL-TA 1264
Cdd:cd18600    177 VPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHT-----ANWFLyLS 251
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1265 ANRWLEVRMEYIgaCVVLIAAVTSISNSLHRElSAGLVGLGLTYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18600    252 TLRWFQMRIEMI--FVIFFTAVTFISIGTTGD-GEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1366-1576 1.92e-29

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 117.19  E-value: 1.92e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS---SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAffrmvdtfeghiiidgiDIAKLPLH----T 1438
Cdd:cd03250      1 ISVEDASFTWDSgeqETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSA-----------------LLGELEKLsgsvS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTIRFN------LDPERkcsdstLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFC 1512
Cdd:cd03250     64 VPGSIAYVSQEPWIQNGTIRENilfgkpFDEER------YEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRIS 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATEN-ILQKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:cd03250    138 LARAVYSDADIYLLDDPLSAVDAHVGRhIFENCILGLLLNnKTRILVTHQLQLLPHADQIVVLDNG 203
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
715-932 2.27e-29

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224059 [Multi-domain]  Cd Length: 226  Bit Score: 117.61  E-value: 2.27e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFWSslpdseiGEDPSPERETATDLDIRKRgpVAY 793
Cdd:COG1136     18 VEALKDVNLEIEAGEFVAIVGPSGSGKSTLL-NLLGGLDKPtSGEVLIN-------GKDLTKLSEKELAKLRRKK--IGF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENIIFESPFNKQRYKMVIEAcslqpDIDILphgDQTQIGERGIN-----LSGGQRQRISVARALYQ 867
Cdd:COG1136     88 VFQNFNLLpDLTVLENVELPLLIAGKSAGRRKRA-----AEELL---EVLGLEDRLLKkkpseLSGGQQQRVAIARALIN 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:COG1136    160 NPKIILADEPTGNLDSKTAKEVLEL-LRELNKERGKTIIMVTHDPELAKYADRVIELKDGKIEEE 223
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
707-942 3.14e-29

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 117.59  E-value: 3.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssLPDseiGEDpspereTATDLDIR 786
Cdd:cd03252      7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV----LVD---GHD------LALADPAW 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRGPVAYASQKPWLLNATVEENIIFESPFNKQRykMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 863
Cdd:cd03252     74 LRRQVGVVLQENVLFNRSIRDNIALADPGMSME--RVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIAR 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:cd03252    152 ALIHNPRILIFDEATSALDYE-SEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAEN 227
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
713-959 3.14e-29

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224041 [Multi-domain]  Cd Length: 248  Bit Score: 118.04  E-value: 3.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldirkrgpVA 792
Cdd:COG1116     14 GGVEVLEDINLSVEKGEFVAILGPSGCGKSTLLRLIAGLEKPTSGEVLLDGRPVTGPGPD------------------IG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQK----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:COG1116     76 YVFQEdallPWL---TVLDNVALglelrgkSKAEARERAKELLELVGLAGFEDKYPH-----------QLSGGMRQRVAI 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAMKD--GTI------- 929
Cdd:COG1116    142 ARALATRPKLLLLDEPFGALDA-LTREELQDELLRLWEETRKTVLLVTHDVDeavYL--ADRVVVLSNrpGRIgeeleid 218
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1189438336  930 ---QREGTLKDFQRSECQLfehWKTLMNRQDQE 959
Cdd:COG1116    219 lprPRIRGDPEFLELREEL---LEELREEHVKK 248
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
379-934 8.28e-29

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 123.23  E-value: 8.28e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  379 VAIETGINLRGAIQTKIYNKIMhlsTSNLSMGEMTAGQICNlvaiDTNQLMWF--------FFLCPnlWaMPVQIIVgVI 450
Cdd:TIGR01842   69 VLVRIGEKLDGALNQPIFAASF---SATLRRGSGDGLQALR----DLDQLRQFltgpglfaFFDAP--W-MPIYLLV-CF 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  451 LLYYILGVSALIGAAVIILLAPV-QYFVATKLSQAQrstlEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRK- 528
Cdd:TIGR01842  138 LLHPWIGILALGGAVVLVGLALLnNRATKKPLKEAT----EASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKy 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  529 ----EMTSLRAFAIYTSISIFMNtaipIAAVLITFVG-HVSFFKEAdfSPSVAFASLSLFHILVTPLFLLSSVVRSTVKA 603
Cdd:TIGR01842  214 lsaqSAASDRAGMLSNLSKYFRI----VLQSLVLGLGaYLAIDGEI--TPGMMIAGSILVGRALAPIDGAIGGWKQFSGA 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  604 LVSVQKLSEFLSSAEIREEQCAPhePTPQGPASKYQAVeeglpslhssqpsgsspPNHPQPLRvvnrkrparedcrgltg 683
Cdd:TIGR01842  288 RQAYKRLNELLANYPSRDPAMPL--PEPEGHLSVENVT-----------------IVPPGGKK----------------- 331
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  684 plqslvpsadgdadnccvqimggyftwtpdgiPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwss 763
Cdd:TIGR01842  332 --------------------------------PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV---- 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  764 lpdseigedpspeRETATDL---DIRKRGP-VAYASQKPWLLNATVEENII-FESPFNKQRykmVIEACSL---QPDIDI 835
Cdd:TIGR01842  376 -------------RLDGADLkqwDRETFGKhIGYLPQDVELFPGTVAENIArFGENADPEK---IIEAAKLagvHELILR 439
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  836 LPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYL 915
Cdd:TIGR01842  440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA--IKALKARGITVVVITHRPSLL 517
                          570
                   ....*....|....*....
gi 1189438336  916 PHADWIIAMKDGTIQREGT 934
Cdd:TIGR01842  518 GCVDKILVLQDGRIARFGE 536
ABC_6TM_ABCC cd18559
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ...
305-610 1.12e-28

Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.


Pssm-ID: 350003 [Multi-domain]  Cd Length: 290  Bit Score: 117.70  E-value: 1.12e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  305 FRILADLLGFAGPLCIFGIVdhlGKENDVFQPKTQ---FLGVYFVS--SQEFLANAYvlavllflalllqrtflqasYYV 379
Cdd:cd18559      5 IKLVLCNHVFSGPSNLWLLL---WFDDPVNGPQEHgqvYLSVLGALaiLQGITVFQY--------------------SMA 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  380 AIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVS 459
Cdd:cd18559     62 VSIGGIFASRAVHLDLYHKALRSPISFFE--RTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPM 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  460 ALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFRTRVETTRRKEMTSLRAFAIY 539
Cdd:cd18559    140 AAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYL 219
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  540 TSISIFMNTAIPIAAVLITFVGHVSFFKEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd18559    220 RALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
712-934 2.01e-28

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 114.90  E-value: 2.01e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:cd03244     14 PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-----------DLRSR--I 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIifeSPFNKQRYKMVIEA---CSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQH 868
Cdd:cd03244     81 SIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQAlerVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  869 ANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03244    158 SKILVLDEATASVDPE-TDALIQKTIREAFKD--CTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
696-934 2.37e-28

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 122.26  E-value: 2.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  696 ADNCCVqimggyftWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ-----KVSGAVFwsslpdseig 770
Cdd:PRK11174   352 AEDLEI--------LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIEL---------- 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  771 edpsperetaTDLDIRK-RGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERG 848
Cdd:PRK11174   414 ----------RELDPESwRKHLSWVGQNPQLPHGTLRDNVLLGNPdASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQA 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKrTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:PRK11174   484 AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQA--LNAASRRQ-TTLMVTHQLEDLAQWDQIWVMQDGQ 560

                   ....*.
gi 1189438336  929 IQREGT 934
Cdd:PRK11174   561 IVQQGD 566
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
1186-1580 5.55e-28

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 120.97  E-value: 5.55e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1186 LVALLPLAIVCYFIQKY-------FRVASRDLQQLDDTTQlpllshfaetvEGLTTIR---AFRYE----ARFQQKLLEY 1251
Cdd:PRK10789   141 LLALLPMPVMAIMIKRYgdqlherFKLAQAAFSSLNDRTQ-----------ESLTSIRmikAFGLEdrqsALFAADAEDT 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1252 TDSN------------------NIASLFLTAANRWLevrmeyigacvVLIAAVTSisnslhRELSAGLVGLGLTYALMVS 1313
Cdd:PRK10789   210 GKKNmrvaridarfdptiyiaiGMANLLAIGGGSWM-----------VVNGSLTL------GQLTSFVMYLGLMIWPMLA 272
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1314 nyLNWMVrNLadMELQLGAVKRIHGLLKTEAESYEGLLApslIPknwPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPG 1393
Cdd:PRK10789   273 --LAWMF-NI--VERGSAAYSRIRAMLAEAPVVKDGSEP---VP---EGRGELDVNIRQFTYPQTDHPALENVNFTLKPG 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1394 QKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLdpERKCSDSTLW 1473
Cdd:PRK10789   342 QMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNI--ALGRPDATQQ 419
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQKVVMTAf 1549
Cdd:PRK10789   420 EIEHVARLASVhddILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEhQILHNLRQWG- 498
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1189438336 1550 ADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:PRK10789   499 EGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1349-1578 6.22e-28

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 113.33  E-value: 6.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1349 GLLAPSLIpknwpdQGKIQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSlaffRMVDTFEGHIIID 1427
Cdd:cd03248      1 GSLAPDHL------KGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVV----ALLENFYQPQGGQ 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1428 GIDIAK-LPLHT---LRSRLSIILQDPVLFSGTIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGEN 1502
Cdd:cd03248     71 VLLDGKpISQYEhkyLHSKVSLVGQEPVLFARSLQDNIAyGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQ 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1503 FSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03248    151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
718-932 6.30e-28

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 113.34  E-value: 6.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwssLPDSEIGEDPSPERetatdldirkrgpvAYASQK 797
Cdd:cd03293     20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV----LVDGEPVTGPGPDR--------------GYVFQQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 ----PWLlnaTVEENIIFesPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:cd03293     82 dallPWL---TVLDNVAL--GLElqgvpkaeaRERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARA 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  865 LYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKLQ---YLphADWIIAM--KDGTIQRE 932
Cdd:cd03293    146 LAVDPDVLLLDEPFSALD-ALTREQLQEELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLsaRPGRIVAE 215
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
716-934 1.92e-27

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 119.43  E-value: 1.92e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpVAYAS 795
Cdd:PRK10789   329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLD-----------SWRSR--LAVVS 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK10789   396 QTPFLFSDTVANNIALGRPdATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  875 DDPFSALDIHlSDHlmqaGILELLRD--DKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10789   476 DDALSAVDGR-TEH----QILHNLRQwgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGN 532
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
713-937 2.54e-27

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 224045 [Multi-domain]  Cd Length: 258  Bit Score: 112.66  E-value: 2.54e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFW-----SSLPDSEIG--------EDPSPERET 779
Cdd:COG1120     13 GGKPILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLdgkdiASLSPKELAkklayvpqSPSAPFGLT 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  780 ATDLDIRKRgpvaYASQKPWLLNATVEENIIFESpfnkqrykmvIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQR 858
Cdd:COG1120     93 VYELVLLGR----YPHLGLFGRPSKEDEEIVEEA----------LELLGL------------EHLADRPVDeLSGGERQR 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:COG1120    147 VLIARALAQETPILLLDEPTSHLDIA---H--QIEVLELLRDlnreKGLTVVMVLHDLNLaARYADHLILLKDGKIVAQG 221

                   ....
gi 1189438336  934 TLKD 937
Cdd:COG1120    222 TPEE 225
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
718-990 3.68e-27

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 113.17  E-value: 3.68e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdseIGEDPSPEREtatdlDIRKRgpVAYASQK 797
Cdd:COG1131     21 LDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILV-------LGYDVVKEPA-----KVRRR--IGYVPQE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARALYQHA 869
Cdd:COG1131     87 PSLYpELTVRENLEFfarlyglSKEEAEERIEELLELFGLEDKANKKVRT-----------LSGGMKQRLSIALALLHDP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFqRSECQLFEH 948
Cdd:COG1131    156 ELLILDEPTSGLDPESRREIWEL-LRELAKEGGVTILLSTHILEEAEElCDRVIILNDGKIIAEGTPEEL-KEKFGGKGV 233
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1189438336  949 WKTLMNRQDQELEKETVTERKATEPPQGLSRAMSSRDGLLQD 990
Cdd:COG1131    234 IELEPERLELAELLEGLKLVKGEEELAEILEALLEEGVKIES 275
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
718-933 4.51e-27

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 109.45  E-value: 4.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsPERETAtdldiRKrgpVAYASQk 797
Cdd:cd03214     15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-----SPKELA-----RK---IAYVPQ- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 pwllnatveeniifespfnkqrykmVIEACSLqpdidilphgdqTQIGERGIN-LSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03214     81 -------------------------ALELLGL------------AHLADRPFNeLSGGERQRVLLARALAQEPPILLLDE 123
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  877 PFSALDIHlsdhlMQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREG 933
Cdd:cd03214    124 PTSHLDIA-----HQIELLELLRRLARergkTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
715-929 5.64e-27

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 110.27  E-value: 5.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKV-SGAVFwsslpdseI-GEDPSPERETATDLDIRKRgpVA 792
Cdd:cd03255     17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLL-NILGGLDRPtSGEVR--------VdGTDISKLSEKELAAFRRRH--IG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNA-TVEENI----IFESPFNKQRYKMVIEACslqpdidilphgDQTQIGERgIN-----LSGGQRQRISVA 862
Cdd:cd03255     86 FVFQSFNLLPDlTALENVelplLLAGVPKKERRERAEELL------------ERVGLGDR-LNhypseLSGGQQQRVAIA 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03255    153 RALANDPKIILADEPTGNLDSETGKEVMEL-LRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
FetA COG4619
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism] ...
714-929 7.91e-27

ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226970 [Multi-domain]  Cd Length: 223  Bit Score: 110.33  E-value: 7.91e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdseigedpspERETATDLDIRK-RGPVA 792
Cdd:COG4619     15 DAKILNNISLSVRAGEFIAITGPSGCGKSTLLKIVASLISPTSGTLLF--------------EGEDVSTLKPEAyRQQVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNATVEENIIFESPFNKQRYKMVIeACSLQPDIDiLPHgdqTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:COG4619     81 YCAQTPALFGDTVEDNLIFPWQIRNRRPDRAA-ALDLLARFA-LPD---SILTKNITELSGGEKQRIALIRNLQFMPKIL 155
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  873 FLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTI 929
Cdd:COG4619    156 LLDEITSALDES-NKRNIEEMIHRYVREQNVAVLWITHdKDQAIRHADKVITLQPGHA 212
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
690-934 9.51e-27

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227320 [Multi-domain]  Cd Length: 573  Bit Score: 117.05  E-value: 9.51e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  690 PSADGDADNCCVQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEI 769
Cdd:COG4987    326 PDEQTATTGQALELRNVSFTYPGQQTKALKNFNLTLAQGEKVAILGRSGSGKSTLLQLLAGAWDPQQGSITLNGVEIASL 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  770 geDPSPERETatdldirkrgpVAYASQKPWLLNATVEENIIFESPfNKQRYKM--VIEACSLQPDIDILPHGDQTQIGER 847
Cdd:COG4987    406 --DEQALRET-----------ISVLTQRVHLFSGTLRDNLRLANP-DASDEELwaALQQVGLEKLLESAPDGLNTWLGEG 471
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  848 GINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDG 927
Cdd:COG4987    472 GRRLSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLAL-LFEHAEG--KTLLMVTHRLRGLERMDRIIVLDNG 548

                   ....*..
gi 1189438336  928 TIQREGT 934
Cdd:COG4987    549 KIIEEGT 555
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
708-933 1.40e-26

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 109.15  E-value: 1.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRK 787
Cdd:cd03259      6 LSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRD-------VTGVPPER 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RGpVAYASQK----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQR 856
Cdd:cd03259     72 RN-IGMVFQDyalfPHL---TVAENIAFglklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQ 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREG 933
Cdd:cd03259    137 QRVALARALAREPSLLLLDEPLSALDAKLREELREE-LKELQRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
718-942 1.77e-26

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 109.51  E-value: 1.77e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETAtDLDIRKRgpVAYASQK 797
Cdd:cd03261     16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-------GEDISGLSEAE-LYRLRRR--MGMLFQS 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNA-TVEENIIFesPFN----------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:cd03261     86 GALFDSlTVFENVAF--PLRehtrlseeeiREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMKKRVALARALA 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:cd03261    153 LDPELLLYDEPTAGLDPIASG-----VIDDLIRSLKKelglTSIMVTHDLDtAFAIADRIAVLYDGKIVAEGTPEELRAS 227

                   .
gi 1189438336  942 E 942
Cdd:cd03261    228 D 228
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
713-922 3.13e-26

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224046 [Multi-domain]  Cd Length: 254  Bit Score: 109.24  E-value: 3.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperetatdldiRKRGPVA 792
Cdd:COG1121     15 GNRPVLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRKR----------------RKRLRIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKP---WLLNATVEE--------NIIFESPFNKQRYKMVIEAcsLQpDIDILPHGDQtQIGErginLSGGQRQRISV 861
Cdd:COG1121     79 YVPQKSsvdRSFPITVKDvvllgrygKKGWFRRLNKKDKEKVDEA--LE-RVGMEDLRDR-QIGE----LSGGQKQRVLL 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWII 922
Cdd:COG1121    151 ARALAQNPDLLLLDEPFTGVDVAGQKEIYD--LLKELRQEGKTVLMVTHDLGLVMaYFDRVI 210
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
713-925 3.90e-26

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 108.00  E-value: 3.90e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeigedpsperetatdldiRKRGPVA 792
Cdd:cd03235     10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------------------KERKRIG 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQK---PWLLNATVEE--------NIIFESPFNKQRYKMVIEACSLqpdIDILPHGDQtQIGErginLSGGQRQRISV 861
Cdd:cd03235     72 YVPQRrsiDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALER---VGLSELADR-QIGE----LSGGQQQRVLL 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHlsdhlMQAGILEL---LRDDKRTVVLVTHKL-QYLPHADWIIAMK 925
Cdd:cd03235    144 ARALVQDPDLLLLDEPFAGVDPK-----TQEDIYELlreLRREGMTILVVTHDLgLVLEYFDRVLLLN 206
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
381-956 4.20e-26

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 116.21  E-value: 4.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  381 IETGINlrGAIQTKIYNKIMHL--------STSNLSMGEMTAGQICNLVAIDT-NQLMWFFFLCPNLWampvqiivgviL 451
Cdd:TIGR03797  203 LETRMD--ASLQAAVWDRLLRLpvsffrqySTGDLASRAMGISQIRRILSGSTlTTLLSGIFALLNLG-----------L 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  452 LYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAWENIFRTRVE 523
Cdd:TIGR03797  270 MFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRvagaenraFARWAKLFSRQRK 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  524 TTRRKEM------TSLRAFAIYTSISIFMNTAIPIAAVLITFVGHVSFFkeadfspsVAFASLSlfhilvtplfllsSVV 597
Cdd:TIGR03797  350 LELSAQRienlltVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFN--------TAFGSFS-------------GAV 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  598 RSTVKALVSVQklseflssaeireeQCAPHeptpqgpaskyqaVEEGLPSLHSsqpsgssppnhpQPLRVVNRKRPARed 677
Cdd:TIGR03797  409 TQLSNTLISIL--------------AVIPL-------------WERAKPILEA------------LPEVDEAKTDPGK-- 447
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  678 crgLTGPLqslvpsadgDADNCCvqimggyFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSG 757
Cdd:TIGR03797  448 ---LSGAI---------EVDRVT-------FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESG 508
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  758 AVFWSslpdseiGEDPSperetatDLDI----RKRGPVAYASQkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPDI 833
Cdd:TIGR03797  509 SVFYD-------GQDLA-------GLDVqavrRQLGVVLQNGR---LMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDI 571
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  834 DILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:TIGR03797  572 RAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSAL-----DNRTQAIVSESLERLKVTRIVIAHRLS 646
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|...
gi 1189438336  914 YLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEhwktLMNRQ 956
Cdd:TIGR03797  647 TIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ----LARRQ 685
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1366-1580 8.03e-26

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 105.86  E-value: 8.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPlHTLRSRLSI 1445
Cdd:cd03247      1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNLdperkcsdstlwealeiaqlklvvkalpggldaiitegGENFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03247     80 LNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1526 MDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:cd03247    122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIM 176
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
708-937 9.30e-26

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 114.35  E-value: 9.30e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsgavfwsslpdSEIGEDPSPERE-TATDLd 784
Cdd:PRK11176   349 FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIanLLTRFYDIDE------------GEILLDGHDLRDyTLASL- 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 irkRGPVAYASQKPWLLNATVEENIIFESpfnKQRY--KMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRI 859
Cdd:PRK11176   416 ---RNQVALVSQNVHLFNDTIANNIAYAR---TEQYsrEQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRI 489
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK11176   490 AIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
708-942 2.35e-25

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 113.68  E-value: 2.35e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKvsGAVFWSSLpDSEIGeDPSPERetatdldi 785
Cdd:TIGR01846  463 FRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLtkLLQRLYTPQH--GQVLVDGV-DLAIA-DPAWLR-------- 530
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  786 RKRGPVAyasQKPWLLNATVEENIIFESPfnKQRYKMVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISVA 862
Cdd:TIGR01846  531 RQMGVVL---QENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFiseLPQGYNTEVGEKGANLSGGQRQRIAIA 605
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:TIGR01846  606 RALVGNPRILIFDEATSALDYE-SEALIMRNMREICRG--RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQ 682
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1366-1601 2.51e-25

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 113.02  E-value: 2.51e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVR-YDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF------------SLaffrMVDTFEGhiiidgidiA 1432
Cdd:PRK11174   350 IEAEDLEILsPDG--KTLAGPLNFTLPAGQRIALVGPSGAGKTSLlnallgflpyqgSL----KINGIEL---------R 414
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1433 KLPLHTLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQ 1509
Cdd:PRK11174   415 ELDPESWRKHLSWVGQNPQLPHGTLRDNVllgNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQ 492
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1510 LFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILE---FDKpek 1586
Cdd:PRK11174   493 RLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQqgdYAE--- 569
                          250
                   ....*....|....*
gi 1189438336 1587 lLSRKDSVFASFVRA 1601
Cdd:PRK11174   570 -LSQAGGLFATLLAH 583
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
712-912 3.94e-25

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 111.68  E-value: 3.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdlDIRKRgpV 791
Cdd:TIGR02868  345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-----------EVRRR--V 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR02868  412 SVCAQDAHLFDTTVRENLRLARPdATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  871 VVFLDDPFSALDIHLSDHLmqagiLELLRD--DKRTVVLVTHKL 912
Cdd:TIGR02868  492 ILLLDEPTEHLDAETADEL-----LEDLLAalSGRTVVLITHHL 530
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1366-1578 9.46e-25

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 102.68  E-value: 9.46e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiAKLPLHTLRsrlsi 1445
Cdd:cd03246      1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTL----------------------ARLILGLLR----- 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ilqdPVlfSGTIRfnLDperkCSDSTLWEALEIAQLklvVKALPGglDAIITEG--GEN-FSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03246     54 ----PT--SGRVR--LD----GADISQWDPNELGDH---VGYLPQ--DDELFSGsiAENiLSGGQRQRLGLARALYGNPR 116
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASIDMATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAI 1578
Cdd:cd03246    117 ILVLDEPNSHLDVEGERaLNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1361-1592 1.61e-24

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 110.30  E-value: 1.61e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1361 PDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSS-FSLAffrmvdTFEGHIIIDGIDIAKLPLH-- 1437
Cdd:PRK11160   334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTlLQLL------TRAWDPQQGEILLNGQPIAdy 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 ---TLRSRLSIILQDPVLFSGTIRFNL---DPErkCSDSTLWEALEIAQL-KLVvkALPGGLDAIITEGGENFSQGQRQL 1510
Cdd:PRK11160   408 seaALRQAISVVSQRVHLFSATLRDNLllaAPN--ASDEALIEVLQQVGLeKLL--EDDKGLNAWLGEGGRQLSGGEQRR 483
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATEN-ILQkVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK11160   484 LGIARALLHDAPLLLLDEPTEGLDAETERqILE-LLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLA 562

                   ...
gi 1189438336 1590 RKD 1592
Cdd:PRK11160   563 QQG 565
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
712-940 1.87e-24

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226164 [Multi-domain]  Cd Length: 258  Bit Score: 104.26  E-value: 1.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPEREtatdlDIRKRgpV 791
Cdd:COG3638     14 PGGHQALKDVNLEINQGEMVAIIGPSGAGKSTLLRSLNGLVDPTSGEIL---FNGVQITKLKGKELR-----KLRRD--I 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLN-ATVEENII---------FESPFN---KQRYKMVIEAcsLQpDIDILPHGDQtqigeRGINLSGGQRQR 858
Cdd:COG3638     84 GMIFQQFNLVPrLSVLENVLlgrlgytstWRSLFGlfsKEDKAQALDA--LE-RVGILDKAYQ-----RASTLSGGQQQR 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDIHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:COG3638    156 VAIARALVQQPKIILADEPVASLDPESAKKVM-----DILKDinqeDGITVIVNLHQVDLaKKYADRIIGLKAGRIVFDG 230

                   ....*..
gi 1189438336  934 TLKDFQR 940
Cdd:COG3638    231 PASELTD 237
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
712-934 2.47e-24

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 226969 [Multi-domain]  Cd Length: 580  Bit Score: 109.67  E-value: 2.47e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpspeRETATDL---DIRKR 788
Cdd:COG4618    346 GQKKPILKGISFALQAGEALGIIGPSGSGKSTLARLLVGIWPPTSGSV-----------------RLDGADLrqwDREQL 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 GP-VAYASQKPWLLNATVEENII-FESpfNKQRYKmVIEACSLQPDIDI---LPHGDQTQIGERGINLSGGQRQRISVAR 863
Cdd:COG4618    409 GRhIGYLPQDVELFDGTIAENIArFGE--EADPEK-VIEAARLAGVHELilrLPQGYDTRIGEGGATLSGGQRQRIALAR 485
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:COG4618    486 ALYGDPFLVVLDEPNSNLDSEGEAALAAA-ILA-AKARGGTVVVIAHRPSALASVDKILVLQDGRIAAFGP 554
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
715-933 3.95e-24

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 102.58  E-value: 3.95e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatDLDIRkRGPVAYA 794
Cdd:cd03257     18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-------GKDLLKLSRR--LRKIR-RKEIQMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWL-LNA--TVEENI-----IFESPFNKQRYKMVI--EACSLQPDIDIL---PHGdqtqigerginLSGGQRQRISV 861
Cdd:cd03257     88 FQDPMSsLNPrmTIGEQIaeplrIHGKLSKKEARKEAVllLLVGVGLPEEVLnryPHE-----------LSGGQRQRVAI 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIAMKDGTIQREG 933
Cdd:cd03257    157 ARALALNPKLLIADEPTSALDVSV-----QAQILDLLKKLQEelglTLLFITHDLgvvAKI--ADRVAVMYAGKIVEEG 228
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
716-934 4.09e-24

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 109.02  E-value: 4.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSperetatdlDIRKRgpVAYAS 795
Cdd:TIGR02204  354 PALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQL--DPA---------ELRAR--MALVP 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIFESPfnKQRYKMVIEAC-SLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:TIGR02204  421 QDPVLFAASVMENIRYGRP--DATDEEVEAAArAAHAHefISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPIL 498
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  873 FLDDPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR02204  499 LLDEATSALDA-ESEQLVQQALETLMKG--RTTLIIAHRLATVLKADRIVVMDQGRIVAQGT 557
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
716-929 9.87e-24

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 99.60  E-value: 9.87e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldiRKRGPVAYAS 795
Cdd:cd03246     16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-------------ELGDHVGYLP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVFLD 875
Cdd:cd03246     83 QDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  876 DPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03246    122 EPNSHLDVEGERALNQA--IAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
714-928 1.55e-23

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 98.47  E-value: 1.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSPERetatdldirkRGPVAY 793
Cdd:cd00267     11 GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---GKDIAKLPLEEL----------RRRIGY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVF 873
Cdd:cd00267     78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGT 928
Cdd:cd00267    104 LDEPTSGLDPASRERLLE--LLRELAEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
714-937 1.66e-23

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 107.90  E-value: 1.66e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdsEIGEDPSPeretATDLDIRK-RGPVA 792
Cdd:TIGR01193  486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSG----------EILLNGFS----LKDIDRHTlRQFIN 551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNATVEENIIFESPFNKQRyKMVIEACSL---QPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHA 869
Cdd:TIGR01193  552 YLPQEPYIFSGSILENLLLGAKENVSQ-DEIWAACEIaeiKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDS 630
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  870 NVVFLDDPFSALDIhlsdhLMQAGILE-LLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:TIGR01193  631 KVLILDESTSNLDT-----ITEKKIVNnLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDE 694
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
712-941 2.65e-23

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 100.45  E-value: 2.65e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSPERetatdldiRKRGpv 791
Cdd:cd03295     11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ--DPVELR--------RKIG-- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 aYASQKPWLL-NATVEENII-------FESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:cd03295     79 -YVIQQIGLFpHMTVEENIAlvpkllkWPKEKIRERADELLALVGLDPAefADRYPH-----------ELSGGQQQRVGV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTLKDFQR 940
Cdd:cd03295    147 ARALAADPPLLLMDEPFGALDPITRDQL-QEEFKRLQQELGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEILR 225

                   .
gi 1189438336  941 S 941
Cdd:cd03295    226 S 226
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1264-1603 6.16e-23

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 226969 [Multi-domain]  Cd Length: 580  Bit Score: 105.44  E-value: 6.16e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1264 AANRWLEVRMEYIGACVV---LIAAVTSISNSLHRELSAGLVGLG--------LTYALMVSNYLnWMVRNLADMELQLG- 1331
Cdd:COG4618    220 LAKRWGRFNAAYLSAQERasdRNGAFGALSRALRMALQSAVLGLGawlvikgeITPGMMIAGSI-LSGRALAPIDLAIAn 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1332 ---------AVKRIHGLLKTEAESYEGLLAPSlipknwPdQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRT 1402
Cdd:COG4618    299 wkqfvaarqSYKRLNELLAELPAAAERMPLPA------P-QGALSVERLTAAPPGQKKPILKGISFALQAGEALGIIGPS 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1403 GSGKSSfsLAffRMVdtfeghiiidgiDIAKLPLH----------------TLRSRLSIILQDPVLFSGTI-----RFNL 1461
Cdd:COG4618    372 GSGKST--LA--RLL------------VGIWPPTSgsvrldgadlrqwdreQLGRHIGYLPQDVELFDGTIaeniaRFGE 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1462 DPerkcSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIL 1541
Cdd:COG4618    436 EA----DPEKVIEAARLAGVHELILRLPQGYDTRIGEGGATLSGGQRQRIALARALYGDPFLVVLDEPNSNLDSEGEAAL 511
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1542 QKVVMTAFAD-RTVVTIAHRVHTILSADLVIVLKRGAILEFDKpekllsrKDSVFASFVRADK 1603
Cdd:COG4618    512 AAAILAAKARgGTVVVIAHRPSALASVDKILVLQDGRIAAFGP-------REEVLAKVLRPPP 567
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
708-933 7.50e-23

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 97.38  E-value: 7.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldIRK 787
Cdd:cd03247      8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA------------LSS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RgpVAYASQKPWLLNATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQ 867
Cdd:cd03247     76 L--ISVLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQ 115
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03247    116 DAPIVLLDEPTVGLDPITERQLLSL-IFEVLKD--KTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
712-939 9.98e-23

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 98.79  E-value: 9.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSPEretatdldIRK-RGP 790
Cdd:cd03256     11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID---GTDINKLKGKA--------LRQlRRQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLN-ATVEENI---------IFESPFN------KQRykmvieACSLQPDIDILPHGDQtqigeRGINLSGG 854
Cdd:cd03256     80 IGMIFQQFNLIErLSVLENVlsgrlgrrsTWRSLFGlfpkeeKQR------ALAALERVGLLDKAYQ-----RADQLSGG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:cd03256    149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDL-LKRINREEGITVIVSLHQVDLaREYADRIVGLKDGRIVFDG 227

                   ....*.
gi 1189438336  934 TLKDFQ 939
Cdd:cd03256    228 PPAELT 233
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
716-934 1.38e-22

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227590 [Multi-domain]  Cd Length: 497  Bit Score: 103.59  E-value: 1.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpspereTATDLDIRK------RG 789
Cdd:COG5265    277 PILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSI-------------------TIDGQDIRDvtqqslRR 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQKPWLLNATVEENIIFESPfnKQRYKMVI---EACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALY 866
Cdd:COG5265    338 AIGIVPQDTVLFNDTIAYNIKYGRP--DATAEEVGaaaEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVAIARTIL 415
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  867 QHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:COG5265    416 KNPPILILDEATSALDTH-TEQAIQAALREVSAG--RTTLVIAHRLSTIIDADEIIVLDNGRIVERGT 480
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
718-879 1.51e-22

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide as in CFTR, or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 95.41  E-value: 1.51e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATdldirkRGPVAYASQK 797
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLD-------GQDLTDDERKSL------RKEIGYVFQD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNA-TVEENIIFESPFnKQRYKMVIEAcslQPDIDI----LPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:pfam00005   68 PQLFPRlTVRENLRLGLLL-KGLSKREKDA---RAEEALeklgLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLL 143

                   ....*..
gi 1189438336  873 FLDDPFS 879
Cdd:pfam00005  144 LLDEPTA 150
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
716-934 6.39e-22

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226963 [Multi-domain]  Cd Length: 252  Bit Score: 96.99  E-value: 6.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdsEIGEDPSpeRETATDLDIRKRgpvayas 795
Cdd:COG4604     15 VVLDDVSLDIPKGGITSIIGPNGAGKSTLLSMMSRLLKKDSGEITIDGL---ELTSTPS--KELAKKLSILKQ------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIF-ESPFNKQR-----YKMVIEAcslqpdIDILphgDQTQIGERGIN-LSGGQRQRISVARALYQH 868
Cdd:COG4604     83 ENHINSRLTVRDLVGFgRFPYSQGRltkedRRIINEA------IEYL---HLEDLSDRYLDeLSGGQRQRAFIAMVLAQD 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  869 ANVVFLDDPFSALDIHLSDHLMQagILELLRDD-KRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGT 934
Cdd:COG4604    154 TDYVLLDEPLNNLDMKHSVQIMK--ILRRLADElGKTIVVVLHDINFAScYSDHIVALKNGKVVKQGS 219
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
718-929 1.13e-21

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 93.62  E-value: 1.13e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtatdlDIRKRgpVAYASQK 797
Cdd:cd03230     16 LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIKKEPE-----EVKRR--IGYLPEE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIifespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03230     82 PSLYeNLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  877 PFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03230    122 PTSGLDPESRREFWE--LLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
MalK COG3839
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
714-946 1.51e-21

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 226359 [Multi-domain]  Cd Length: 338  Bit Score: 97.72  E-value: 1.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEmqkvsgavfwsslPDS-EI---GEDpsperetATDLDIRK 787
Cdd:COG3839     15 SFEVLKDVNLDIEDGEFVVLLGPSGCGKSTLLrmIAGLEE-------------PTSgEIlidGRD-------VTDLPPEK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RGpVAYASQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRI 859
Cdd:COG3839     75 RG-IAMVFQNYALYpHMTVYENIAFglklrgvPKAEIDKRVKEVAKLLGLEHLLNRKPLQ-----------LSGGQRQRV 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTH---KLQYLphADWIIAMKDGTIQREGTLK 936
Cdd:COG3839    143 ALARALVRKPKVFLLDEPLSNLDAKLRVLMRSE-IKKLHERLGTTTIYVTHdqvEAMTL--ADRIVVMNDGRIQQVGTPL 219
                          250
                   ....*....|
gi 1189438336  937 DFQRSECQLF 946
Cdd:COG3839    220 ELYERPANLF 229
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
718-937 3.01e-21

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 224049 [Multi-domain]  Cd Length: 252  Bit Score: 95.02  E-value: 3.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSperetatdldirKRGPVAYASQK 797
Cdd:COG1124     23 LNNVSLEIERGETLGIVGESGSGKSTLARLLAGLEKPSSGSILLDGKPLAPKKRAKA------------FYRPVQMVFQD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWL-LNA--TVEEnIIFESP----FNKQRYKM--VIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARALYQ 867
Cdd:COG1124     91 PYSsLNPrrTVGR-ILSEPLrphgLSKSQQRIaeLLDQVGLPPSFlDRRPH-----------ELSGGQRQRIAIARALIP 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  868 HANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:COG1124    159 EPKLLILDEPTSALDVSV-----QAQILNLLLELKKerglTYLFISHDLALVEHmCDRIAVMDNGQIVEIGPTEE 228
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
716-938 3.15e-21

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224043 [Multi-domain]  Cd Length: 345  Bit Score: 97.04  E-value: 3.15e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpDSEIGEDpsperetATDLDIRKRGpVAYAS 795
Cdd:COG1118     16 GALDDISLDIKSGELVALLGPSGAGKSTLLRIIAGLETPDAGRIRL----NGRVLFD-------VSNLAVRDRK-VGFVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLL-NATVEENIIF---------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARAL 865
Cdd:COG1118     84 QHYALFpHMTVADNIAFglkvrkerpSEAEIRARVEELLRLVQLEGLADRYPA-----------QLSGGQRQRVALARAL 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 938
Cdd:COG1118    153 AVEPKVLLLDEPFGALDAKVRKEL-RRWLRKLHDRLGVTTVFVTHDQEEaLELADRVVVLNQGRIEQVGPPDEV 225
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
712-929 3.37e-21

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 94.07  E-value: 3.37e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvsgavfwsslpDSEIGEDPSPeretATDLDIRK-R 788
Cdd:cd03248     25 PD-TLVLQDVSFTLHPGEVTALVGPSGSGKSTVvaLLENFYQPQ------------GGQVLLDGKP----ISQYEHKYlH 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 GPVAYASQKPWLLNATVEENIIFESPfnKQRYKMVIEACS---LQPDIDILPHGDQTQIGERGINLSGGQRQRISVARAL 865
Cdd:cd03248     88 SKVSLVGQEPVLFARSLQDNIAYGLQ--SCSFECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  866 YQHANVVFLDDPFSALDIHlSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03248    166 IRNPQVLILDEATSALDAE-SEQQVQQALYDWPER--RTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1367-1576 5.38e-21

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 91.15  E-value: 5.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1446
Cdd:cd00267      1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQdpvlfsgtirfnldperkcsdstlwealeiaqlklvvkalpggldaiiteggenFSQGQRQLFCLARAFVRKTSIFIM 1526
Cdd:cd00267     79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1527 DEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTI-LSADLVIVLKRG 1576
Cdd:cd00267    105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAeLAADRVIVLKDG 156
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport ...
713-934 5.80e-21

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism];


Pssm-ID: 226361 [Multi-domain]  Cd Length: 352  Bit Score: 96.20  E-value: 5.80e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEdpsperETATDLDIRKRgPVA 792
Cdd:COG3842     16 GDFTAVDDISLDIKKGEFVTLLGPSGCGKTTLLRMIAGFEQPSSGEIL--------LDG------EDITDVPPEKR-PIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIFEspfNKQRYKMvieacslqPDIDILPHGDQ-------TQIGERGIN-LSGGQRQRISVAR 863
Cdd:COG3842     81 MVFQSYALFpHMTVEENVAFG---LKVRKKL--------KKAEIKARVEEalelvglEGFADRKPHqLSGGQQQRVALAR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGT 934
Cdd:COG3842    150 ALVPEPKVLLLDEPLSALDAKLREQ-MRKELKELQRELGITFVYVTHDQEeALAMSDRIAVMNDGRIEQVGT 220
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
718-934 6.23e-21

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224050 [Multi-domain]  Cd Length: 309  Bit Score: 95.44  E-value: 6.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSperetatDLDIRK-RGPVAYASQ 796
Cdd:COG1125     17 VDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILID-------GEDIS-------DLDPVElRRKIGYVIQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:COG1125     83 QIGLFpHLTVAENIATvpkllgwDKERIKKRADELLDLVGLDPSeyADRYPH-----------ELSGGQQQRVGVARALA 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  867 QHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGT 934
Cdd:COG1125    152 ADPPILLMDEPFGALD-PITRKQLQEEIKELQKELGKTIVFVTHDIDeALKLADRIAVMDAGEIVQYDT 219
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
833-1603 7.09e-21

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 100.10  E-value: 7.09e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  833 IDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL 912
Cdd:PTZ00265   562 VSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRITIIIAHRL 640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  913 QYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVTERKATEPP----QGLSRA-MSSRDGL 987
Cdd:PTZ00265   641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSyiieQGTHDAlMKNKNGI 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  988 -----------------------------------------------LQDEEEEEEEAAESEEDDNLSS----------- 1009
Cdd:PTZ00265   721 yytminnqkvsskkssnndndkdsdmkssaykdsergydpdemngnsKHENESASNKKSCKMSDENASEnnaggklpflr 800
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1010 -MLHQRAEIP------WRACAKYLSSAGILLLSLLVFSQLLKhmvLVAIDYwlAKWTDSALTLTPAARNCSlsqectlDQ 1082
Cdd:PTZ00265   801 nLFKRKPKAPnnlrivYREIFSYKKDVTIIALSILVAGGLYP---VFALLY--AKYVSTLFDFANLEANSN-------KY 868
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVftvlcslgIVLCLVTSVTVE-----WTGLKVAKRLHRSLLNRIILAPMRFFEttplgsilnrfsSDCNT---ID 1154
Cdd:PTZ00265   869 SLYILV--------IAIAMFISETLKnyynnVIGEKVEKTMKRRLFENILYQEISFFD------------QDKHApglLS 928
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1155 QHIPSTLECLSRSTllcVSALAVISYVTPVFLVALLplaivcyfIQKYFrvasrdlqqlddttqLPLLshfAETVEGLTT 1234
Cdd:PTZ00265   929 AHINRDVHLLKTGL---VNNIVIFTHFIVLFLVSMV--------MSFYF---------------CPIV---AAVLTGTYF 979
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1235 I--RAFRYEARF-QQKLLEYTDSNNIASLFL-----------------------TAANRWLEvrmEYIgaCVVLIAAVTS 1288
Cdd:PTZ00265   980 IfmRVFAIRARLtANKDVEKKEINQPGTVFAynsddeifkdpsfliqeafynmnTVIIYGLE---DYF--CNLIEKAIDY 1054
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1289 ISNSLHRE--LSAGLVGLGLTYALMVSNYLNW----MVRN----LADMELQL----------GAVKRIHGLLKTEAESYE 1348
Cdd:PTZ00265  1055 SNKGQKRKtlVNSMLWGFSQSAQLFINSFAYWfgsfLIRRgtilVDDFMKSLftflftgsyaGKLMSLKGDSENAKLSFE 1134
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1349 G----LLAPSLIP---------KNWPD-QGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAF 1413
Cdd:PTZ00265  1135 KyyplIIRKSNIDvrdnggiriKNKNDiKGKIEIMDVNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL 1214
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1414 FRMVD-------------------------------------TFEGHIIIDGIDIAKL-----------------PLHTL 1439
Cdd:PTZ00265  1215 MRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnEFSLTKEGGSGEDSTVfknsgkilldgvdicdyNLKDL 1294
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1440 RSRLSIILQDPVLFSGTIRFNLDPERKcsDSTLWE---ALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARA 1516
Cdd:PTZ00265  1295 RNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDvkrACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL----KRGAILEFDKP-EKLLS 1589
Cdd:PTZ00265  1373 LLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAHGThEELLS 1452
                          970
                   ....*....|....
gi 1189438336 1590 RKDSVFASFVRADK 1603
Cdd:PTZ00265  1453 VQDGVYKKYVKLAK 1466
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
707-988 8.02e-21

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224058 [Multi-domain]  Cd Length: 339  Bit Score: 95.78  E-value: 8.02e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL-LAALGEMQKvSGAVFwssLPDSEIGEDPSPERETAtdldi 785
Cdd:COG1135     11 FGQTGTGTVTALDDVSLEIPKGEIFGIIGYSGAGKSTLLrLINLLERPT-SGSVF---VDGQDLTALSEAELRQL----- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  786 RKRgpVAYASQKPWLLNA-TVEENIIF----ESPFNKQRYKMVIEACSLqpdIDILPHGDQTQIgergiNLSGGQRQRIS 860
Cdd:COG1135     82 RQK--IGMIFQHFNLLSSrTVFENVAFplelAGVPKAEIKQRVAELLEL---VGLSDKADRYPA-----QLSGGQKQRVA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIHLSDHlmqagILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTL 935
Cdd:COG1135    152 IARALANNPKILLCDEATSALDPETTQS-----ILELLKDINRelglTIVLITHEMEVVKRiCDRVAVLDQGRLVEEGTV 226
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  936 KDfqrsecqLFEHWKtlmnrqdQELEKETVTERKATEPPQGLSRAMSSRDGLL 988
Cdd:COG1135    227 SE-------VFANPK-------HAITQEFIGETLEIDLPEELLERLESGDGPL 265
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
714-928 1.93e-20

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 90.32  E-value: 1.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLdirkRGPVAY 793
Cdd:cd03229     12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------GEDLTDLEDELPPL----RRRIGM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigergiNLSGGQRQRISVARALYQHANVV 872
Cdd:cd03229     81 VFQDFALFpHLTVLENIAL--------------------------------------GLSGGQQQRVALARALAMDPDVL 122
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  873 FLDDPFSALDIhlsdhLMQAGILELLRD----DKRTVVLVTHKLQYLPH-ADWIIAMKDGT 928
Cdd:cd03229    123 LLDEPTSALDP-----ITRREVRALLKSlqaqLGITVVLVTHDLDEAARlADRVVVLRDGK 178
MlaF COG1127
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ...
718-942 2.11e-20

ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224052 [Multi-domain]  Cd Length: 263  Bit Score: 92.66  E-value: 2.11e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPERetatdLDIRKRgpVAYASQK 797
Cdd:COG1127     24 LDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEIL---IDGEDIPQLSEEEL-----YEIRKR--MGVLFQQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNA-TVEENIIF--------ESPFNKQRYKMVIEACSLQPDI-DILPhgdqtqiGErginLSGGQRQRISVARALYQ 867
Cdd:COG1127     94 GALFSSlTVFENVAFplrehtklPESLIRELVLMKLELVGLRGAAaDLYP-------SE----LSGGMRKRVALARAIAL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  868 HANVVFLDDPFSALDIHLSdhlmqAGILELLRDDKR----TVVLVTHKLQYL-PHADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:COG1127    163 DPELLFLDEPTSGLDPISA-----GVIDELIRELNDalglTVIMVTHDLDSLlTIADRVAVLADGKVIAEGTPEELLASD 237
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
710-929 2.29e-20

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 90.93  E-value: 2.29e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPsperetATDLdirkRG 789
Cdd:cd03369     16 YAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI---EIDGIDISTIP------LEDL----RS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQKPWLLNATVEENIifeSPFNKQRYKMVIEACSlqpdidilphgdqtqIGERGINLSGGQRQRISVARALYQHA 869
Cdd:cd03369     83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR---------------VSEGGLNLSQGQRQLLCLARALLKRP 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  870 NVVFLDDPFSALDIHlSDHLMQAGILELLRDDkrTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03369    145 RVLVLDEATASIDYA-TDALIQKTIREEFTNS--TILTIAHRLRTIIDYDKILVMDAGEV 201
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
718-934 6.94e-20

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226643 [Multi-domain]  Cd Length: 386  Bit Score: 93.60  E-value: 6.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtATDLDIRKRgPVAYASQK 797
Cdd:COG4175     44 VNDASLDVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTRGEILVD-------GKDIAKLSA-AELRELRRK-KISMVFQS 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 ----PWLlnaTVEENIIF----------ESpfnKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:COG4175    115 fallPHR---TVLENVAFglevqgvpkaER---EERALEALELVGLEGYADKYPN-----------ELSGGMQQRVGLAR 177
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  864 ALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGT 934
Cdd:COG4175    178 ALANDPDILLMDEAFSALD-PLIRTEMQDELLELQAKLKKTIVFITHDLDeALRIGDRIAIMKDGEIVQVGT 248
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1366-1587 7.24e-20

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 90.32  E-value: 7.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHII--------IDGIDIAKLPLH 1437
Cdd:cd03260      1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDegevlldgKDIYDLDVDVLE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 tLRSRLSIILQDPVLFSGTIRFNLD--------PERKCSDSTLWEALEIAQLKLVVKALPGGLDaiiteggenFSQGQRQ 1509
Cdd:cd03260     79 -LRRRVGMVFQKPNPFPGSIYDNVAyglrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQ 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1510 LFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1587
Cdd:cd03260    149 RLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
703-933 7.41e-20

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226641 [Multi-domain]  Cd Length: 534  Bit Score: 95.42  E-value: 7.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  703 IMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGeMQKVSGAVFWSslpdseiGEDPSPERETATd 782
Cdd:COG4172    288 IKGGFLRRTVDHLRAVDGISLTLRRGQTLGLVGESGSGKSTLGLALLR-LIPSQGEIRFD-------GQDIDGLSRKEM- 358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  783 LDIRKRGPVA----YASQKPWLlnaTVEEnIIFE-------SPFNKQRYKMVIEA---CSLQPDI-DILPHgdqtqiger 847
Cdd:COG4172    359 RPLRRRMQVVfqdpYGSLSPRM---TVGQ-IIEEglrvhepKLSAAERDQRVIEAleeVGLDPATrNRYPH--------- 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  848 giNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKRtvvlvTHKLQYL--PH-------- 917
Cdd:COG4172    426 --EFSGGQRQRIAIARALILKPELILLDEPTSALDRSV-----QAQVLDLLRDLQQ-----KHGLSYLfiSHdlavvral 493
                          250
                   ....*....|....*.
gi 1189438336  918 ADWIIAMKDGTIQREG 933
Cdd:COG4172    494 CHRVIVMRDGKIVEQG 509
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
718-913 9.74e-20

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 89.93  E-value: 9.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFWSSLPDSEIGEDPsperetatdLDIRKRgpVA 792
Cdd:cd03260     16 LKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDV---------LELRRR--VG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNATVEENI-----IFESPFNKQRYKMVIEACS---LQPDIDILPHGDQtqigerginLSGGQRQRISVARA 864
Cdd:cd03260     85 MVFQKPNPFPGSIYDNVayglrLHGIKLKEELDERVEEALRkaaLWDEVKDRLHALG---------LSGGQQQRLCLARA 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1189438336  865 LYQHANVVFLDDPFSALDIHlSDHLMQAGILELlrDDKRTVVLVTHKLQ 913
Cdd:cd03260    156 LANEPEVLLLDEPTSALDPI-STAKIEELIAEL--KKEYTIVIVTHNMQ 201
ThiQ COG3840
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];
722-938 1.10e-19

ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];


Pssm-ID: 226360 [Multi-domain]  Cd Length: 231  Bit Score: 89.72  E-value: 1.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  722 TIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERetatdldirkrgPVAYASQKPWLL 801
Cdd:COG3840     19 DLTVPAGEIVAILGPSGAGKSTLLNLIAGFETPASGEI---LINGVDHTASPPAER------------PVSMLFQENNLF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  802 -NATVEENIIF-ESPFNK----QRYKMVIEACS--LQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHANVVF 873
Cdd:COG3840     84 aHLTVAQNIGLgLSPGLKlnaeQREKVEAAAAQvgLAGFLKRLPG-----------ELSGGQRQRVALARCLVREQPILL 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  874 LDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:COG3840    153 LDEPFSALDPALRAE-MLALVSQLCDERKMTLLMVTHHPEDAARiADRVVFLDNGRIAAQGSTQEL 217
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1367-1576 2.55e-19

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 87.91  E-value: 2.55e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSII 1446
Cdd:cd03225      1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQDP--VLFSGTIR----FNLdPERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRK 1520
Cdd:cd03225     81 FQNPddQFFGPTVEeevaFGL-ENLGLPEEEIEERVEEA-LELV------GLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1521 TSIFIMDEATASIDMATENILQKVVmTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03225    153 PDILLLDEPTAGLDPAGRRELLELL-KKLKAEgkTIIIVTHDLDLLLElADRVIVLEDG 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
703-934 2.71e-19

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 93.41  E-value: 2.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  703 IMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATD 782
Cdd:COG1123    292 SRKGLFVRERGEVKAVDDVSFDLREGETLGLVGESGSGKSTLARILAGLLPPSSGSIIFD-------GQDLDLTGGELRR 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  783 LDIRKRgPV---AYASQKPWLlnaTVEENI----IFESPFNKQRYKMVI----EACSLQPDI-DILPHGdqtqigergin 850
Cdd:COG1123    365 LRRRIQ-MVfqdPYSSLNPRM---TVGDILaeplRIHGGGSGAERRARVaellELVGLPPEFlDRYPHE----------- 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKL---QYLphADWIIA 923
Cdd:COG1123    430 LSGGQRQRVAIARALALEPKLLILDEPVSALDV-----SVQAQVLNLLKDLQEelglTYLFISHDLavvRYI--ADRVAV 502
                          250
                   ....*....|.
gi 1189438336  924 MKDGTIQREGT 934
Cdd:COG1123    503 MYDGRIVEEGP 513
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
708-947 4.66e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 89.04  E-value: 4.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperETATDL-DIR 786
Cdd:PRK13648    15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQA------------ITDDNFeKLR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRGPVAYASQKPWLLNATVEENIIFESPFNKQRY-KMVIEACSLQPDIDILPHGD-QTQigergiNLSGGQRQRISVARA 864
Cdd:PRK13648    83 KHIGIVFQNPDNQFVGSIVKYDVAFGLENHAVPYdEMHRRVSEALKQVDMLERADyEPN------ALSGGQKQRVAIAGV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQ 944
Cdd:PRK13648   157 LALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEE 235

                   ...
gi 1189438336  945 LFE 947
Cdd:PRK13648   236 LTR 238
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
701-937 5.27e-19

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226967 [Multi-domain]  Cd Length: 268  Bit Score: 88.81  E-value: 5.27e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFT-----WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsp 775
Cdd:COG4608      7 VKNLKKYFPvgkgfGKKRYVKAVDGVSFSIKEGETLGLVGESGCGKSTLGRLILGLEEPTSGEILFE-------GKD--- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  776 eretATDLDIRKRgpvayasqkpwllnatveeniifespfnKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGG 854
Cdd:COG4608     77 ----ITKLSKEER----------------------------RERVLELLEKVGLPEEfLYRYPH-----------ELSGG 113
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:COG4608    114 QRQRIGIARALALNPKLIVADEPVSALDV-----SVQAQILNLLKDLQEelglTYLFISHDLSVVRYiSDRIAVMYLGKI 188

                   ....*...
gi 1189438336  930 QREGTLKD 937
Cdd:COG4608    189 VEIGPTEE 196
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
712-936 6.95e-19

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 92.86  E-value: 6.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDgIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgEDPSPEREtatdldirkrgpV 791
Cdd:TIGR00958  492 PD-VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQ------------V 557
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHAN 870
Cdd:TIGR00958  558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMaAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  871 VVFLDDPFSALDIHlSDHLMQagilELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLK 936
Cdd:TIGR00958  638 VLILDEATSALDAE-CEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHK 698
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
701-934 1.43e-18

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 91.93  E-value: 1.43e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALgeMQKVSGAVFWSSLPDSEIgedpSPERE 778
Cdd:TIGR03796  478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIakLVAGL--YQPWSGEILFDGIPREEI----PREVL 551
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  779 TATdldirkrgpVAYASQKPWLLNATVEENIIFESPFNKQryKMVIEAC---SLQPDIDILPHGDQTQIGERGINLSGGQ 855
Cdd:TIGR03796  552 ANS---------VAMVDQDIFLFEGTVRDNLTLWDPTIPD--ADLVRACkdaAIHDVITSRPGGYDAELAEGGANLSGGQ 620
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  856 RQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR03796  621 RQRLEIARALVRNPSILILDEATSALDP-----ETEKIIDDNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGT 694
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
713-924 1.70e-18

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 86.31  E-value: 1.70e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpSPERetatdldirKRGPVA 792
Cdd:PRK10247    18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL----KPEI---------YRQQVS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQ----PDidilphgdqtQIGERGIN-LSGGQRQRISVARALYQ 867
Cdd:PRK10247    85 YCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLErfalPD----------TILTKNIAeLSGGEKQRISLIRNLQF 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  868 HANVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:PRK10247   155 MPKVLLLDEITSALDES-NKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
715-937 2.00e-18

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 90.71  E-value: 2.00e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALG----EMQKVSGAVFWSslpdseiGEDPS--PEREtatdlDIRKR 788
Cdd:COG1123     22 VPAVRDVSFEVEPGEILGIVGESGSGKSTLALALMGllpeGGRITSGEVILD-------GRDLLglSERE-----MRKLR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 GP-VAYASQKPW-LLN-ATVEENIIFESPF------NKQRYKMVIEACSL----QPD-IDILPHgdqtqigergiNLSGG 854
Cdd:COG1123     90 GKrIAMIFQDPMtSLNpVMTIGDQIREALRlhgkgsRAEARKRAVELLEQvglpDPErRDRYPH-----------QLSGG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQ---YLphADWIIAMKDG 927
Cdd:COG1123    159 MRQRVMIAMALALKPKLLIADEPTTALDVTT-----QAQILDLLKDLQRelgmAVLFITHDLGvvaEL--ADRVVVMYKG 231
                          250
                   ....*....|
gi 1189438336  928 TIQREGTLKD 937
Cdd:COG1123    232 EIVETGPTEE 241
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
707-934 2.01e-18

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 91.04  E-value: 2.01e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEdpsperetaTDLdir 786
Cdd:PRK11160   345 SFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---------AAL--- 412
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 kRGPVAYASQKPWLLNATVEENIIFESP-FNKQRYKMVIEACSLQPDIDIlPHGDQTQIGERGINLSGGQRQRISVARAL 865
Cdd:PRK11160   413 -RQAISVVSQRVHLFSATLRDNLLLAAPnASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARAL 490
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHlmqagILELLRD---DKrTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11160   491 LHDAPLLLLDEPTEGLDAETERQ-----ILELLAEhaqNK-TVLMITHRLTGLEQFDRICVMDNGQIIEQGT 556
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1366-1592 3.36e-18

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 224047 [Multi-domain]  Cd Length: 235  Bit Score: 85.39  E-value: 3.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR-MVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:COG1122      4 IEAENLSFRYPGR-KAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGlLKPTSGEVLVDGLDTSSEKSLLELRQKVG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDPV--LFSGTIRFNL---------DPERKcsDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCL 1513
Cdd:COG1122     83 LVFQNPDdqLFGPTVEDEVafglenlglPREEI--EERVAEALELVGLEELLDRPPFNL-----------SGGQKQRVAI 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTIL-SADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:COG1122    150 AGVLAMGPEILLLDEPTAGLDPKGRRELLELLKKLKEEGgkTIIIVTHDLELVLeYADRVVVLDDGKILADGDPAEIFND 229

                   ..
gi 1189438336 1591 KD 1592
Cdd:COG1122    230 AE 231
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
713-933 4.20e-18

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 84.61  E-value: 4.20e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwsslpdseIGEdpsperETATDLDIRKRGp 790
Cdd:cd03301     11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLrmIAGLEEPT--SGRIY--------IGG------RDVTDLPPKDRD- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLL-NATVEENIIFESPFNKQRyKMVIE------ACSLQpdIDILPHGDQTQigerginLSGGQRQRISVAR 863
Cdd:cd03301     74 IAMVFQNYALYpHMTVYDNIAFGLKLRKVP-KDEIDervrevAELLQ--IEHLLDRKPKQ-------LSGGQRQRVALGR 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 933
Cdd:cd03301    144 AIVREPKVFLMDEPLSNLDAKLRVQ-MRAELKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
713-937 4.54e-18

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 84.98  E-value: 4.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIgedpsperetaTDLDIRKRgPVA 792
Cdd:cd03300     11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIL---LDGKDI-----------TNLPPHKR-PVN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIF-----ESPFNKQRYKmVIEACSLqpdIDILPHGDqtqigeRGIN-LSGGQRQRISVARAL 865
Cdd:cd03300     76 TVFQNYALFpHLTVFENIAFglrlkKLPKAEIKER-VAEALDL---VQLEGYAN------RKPSqLSGGQQQRVAIARAL 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHlMQagiLELLRDDKR---TVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03300    146 VNEPKVLLLDEPLGALDLKLRKD-MQ---LELKRLQKElgiTFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEE 217
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1366-1590 5.16e-18

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 86.21  E-value: 5.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-------------VDTFEGHIIIdgidia 1432
Cdd:COG1131      5 IEVRNLTKKYGGD-KTALDGVSFEVEPGEIFGLLGPNGAGKTTL----LKIlagllkptsgeilVLGYDVVKEP------ 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1433 klplHTLRSRLSIILQDPVLFSG-TIRFNLD-------PERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfS 1504
Cdd:COG1131     74 ----AKVRRRIGYVPQEPSLYPElTVRENLEffarlygLSKEEAEERIEELLELFGLEDKANKKVRTL-----------S 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1505 QGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRGAILEF 1581
Cdd:COG1131    139 GGMKQRLSIALALLHDPELLILDEPTSGLDPESRREIWELLRELAKEggVTILLSTHILEEAEElCDRVIILNDGKIIAE 218

                   ....*....
gi 1189438336 1582 DKPEKLLSR 1590
Cdd:COG1131    219 GTPEELKEK 227
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
713-934 9.97e-18

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 84.31  E-value: 9.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVA 792
Cdd:cd03296     13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG-------GED-------ATDVPVQERN-VG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:cd03296     78 FVFQHYALFrHMTVFDNVAFglrvkprsERPPEaeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVA 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03296    147 LARALAVEPKVLLLDEPFGALDAKVRKEL-RRWLRRLHDELHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGT 220
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
707-938 1.11e-17

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 223521 [Multi-domain]  Cd Length: 316  Bit Score: 85.70  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQK-----VSGAVFW-----SSLPDSEIgedpspe 776
Cdd:COG0444     10 SFPTDAGVVKAVDGVSFELKKGEILGIVGESGSGKSVLAKAIMGLLPKpnariVGGEILFdgkdlLSLSEKEL------- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  777 retatdLDIRKRGpVAYASQKPwlLNA-----TVEENII------FESPFNKQRYKMVIEACS---LQPDIDIL---PHg 839
Cdd:COG0444     83 ------RKIRGKE-IAMIFQDP--MTSlnpvmTIGDQIAevlrlhGKGLSKKEAKERAIELLElvgIPDPERRLksyPH- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  840 dqtqigergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKL--- 912
Cdd:COG0444    153 ----------ELSGGMRQRVMIAMALALNPKLLIADEPTTALDV-----TVQAQILDLLKELQRekgtALILITHDLgvv 217
                          250       260
                   ....*....|....*....|....*..
gi 1189438336  913 -QYlphADWIIAMKDGTIQREGTLKDF 938
Cdd:COG0444    218 aEI---ADRVAVMYAGRIVEEGPVEEI 241
ABC_FtsE_transporter cd03292
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic ...
712-910 1.50e-17

ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 83.23  E-value: 1.50e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLDIRKRGpV 791
Cdd:cd03292     11 PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-------GQDVSDLRGRAIPYLRRKIG-V 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKpWLLNATVEENIIF------ESPFN-KQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARA 864
Cdd:cd03292     83 VFQDFR-LLPDRNVYENVAFalevtgVPPREiRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARA 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1189438336  865 LYQHANVVFLDDPFSALDihlSDHlmQAGILELLRD-DKR--TVVLVTH 910
Cdd:cd03292    151 IVNSPTILIADEPTGNLD---PDT--TWEIMNLLKKiNKAgtTVVVATH 194
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
714-942 1.70e-17

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 87.57  E-value: 1.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAalGEMQKVSGAVFWsslpDSEIGEDPSPERetATDLDIRkrgpV 791
Cdd:COG1129     20 GVKALDGVSLTVRPGEVHALLGENGAGKSTLMkiLS--GVYPPDSGEILI----DGKPVAFSSPRD--ALAAGIA----T 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYasQKPWLL-NATVEENIIFESPFNKQ-----RYKMVIEAC----SLQPDIDIlphgdQTQIGergiNLSGGQRQRISV 861
Cdd:COG1129     88 VH--QELSLVpNLSVAENIFLGREPTRRfglidRKAMRRRARellaRLGLDIDP-----DTLVG----DLSIAQRQMVEI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQylpH----ADWIIAMKDGTIQREG-TLK 936
Cdd:COG1129    157 ARALSFDARVLILDEPTAALTVKETERLFD--LIRRLKAQGVAIIYISHRLD---EvfeiADRITVLRDGRVVGTRpTAA 231

                   ....*.
gi 1189438336  937 DFQRSE 942
Cdd:COG1129    232 ETSEDE 237
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
728-933 1.94e-17

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 82.73  E-value: 1.94e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  728 GQLTMIVGQVGCGKSSLL--LAAL-----GEMqKVSGAVfwssLPDSEIGEDPSPERetatdldiRKrgpVAYASQKPWL 800
Cdd:cd03297     23 EEVTGIFGASGAGKSTLLrcIAGLekpdgGTI-VLNGTV----LFDSRKKINLPPQQ--------RK---IGLVFQQYAL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  801 L-NATVEENIIFESPFNKQRYKMVIEAcslqpdiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPF 878
Cdd:cd03297     87 FpHLNVRENLAFGLKRKRNREDRISVD-------ELLDLLGLDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPF 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  879 SALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL---QYLphADWIIAMKDGTIQREG 933
Cdd:cd03297    160 SALDRALRLQLLPE-LKQIKKNLNIPVIFVTHDLseaEYL--ADRIVVMEDGRLQYIG 214
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
718-968 1.96e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 84.06  E-value: 1.96e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFW--SSLPDSEIgeDPSperetatdlDIRKRgp 790
Cdd:PRK14243    26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFhgKNLYAPDV--DPV---------EVRRR-- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNATVEENIIFESPFNKQRYKM--VIEACSLQPdidILPHGDQTQIGERGINLSGGQRQRISVARALYQH 868
Cdd:PRK14243    93 IGMVFQKPNPFPKSIYDNIAYGARINGYKGDMdeLVERSLRQA---ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  869 ANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHKLQYLPHADWIIAM----KDGTIQREGTLKDFQRSE 942
Cdd:PRK14243   170 PEVILMDEPCSAL-----DPISTLRIEELMHELKEqyTIIIVTHNMQQAARVSDMTAFfnveLTEGGGRYGYLVEFDRTE 244
                          250       260
                   ....*....|....*....|....*.
gi 1189438336  943 cqlfehwkTLMNRQDQELEKETVTER 968
Cdd:PRK14243   245 --------KIFNSPQQQATRDYVSGR 262
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1350-1590 2.00e-17

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226641 [Multi-domain]  Cd Length: 534  Bit Score: 87.72  E-value: 2.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1350 LLA--PSLIPKNWPDQGK--IQIQNLSVRYD---SSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRM 1416
Cdd:COG4172    257 LLAaePSGDPPPLPEDAPvlLEVEDLRVWFPikgGFLRRTVDHLRAVdgisltLRRGQTLGLVGESGSGKSTLGLALLRL 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1417 VDT-----FEGHIIIDGIDIAKLPLhtlRSRLSIILQDPvlFSgtirfNLDPeRKCSDSTLWEALEIAQLKL-------- 1483
Cdd:COG4172    337 IPSqgeirFDGQDIDGLSRKEMRPL---RRRMQVVFQDP--YG-----SLSP-RMTVGQIIEEGLRVHEPKLsaaerdqr 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1484 VVKALPG-GLD-AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAteniLQKVVMTAFADR------TVV 1555
Cdd:COG4172    406 VIEALEEvGLDpATRNRYPHEFSGGQRQRIAIARALILKPELILLDEPTSALDRS----VQAQVLDLLRDLqqkhglSYL 481
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1189438336 1556 TIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:COG4172    482 FISHDLAVVRAlCHRVIVMRDGKIVEQGPTEAVFAN 517
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
718-942 2.37e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 84.30  E-value: 2.37e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGEDPSPERETATDL-DIRKRgpVAYASQ 796
Cdd:PRK13634    23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV--------TIGERVITAGKKNKKLkPLRKK--VGIVFQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALY 866
Cdd:PRK13634    93 FPehQLFEETVEKDICF-GPMNfgvseedaKQKAREMIELVGLPEEL----------LARSPFELSGGQMRRVAIAGVLA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKD-FQRS 941
Cdd:PRK13634   162 MEPEVLVLDEPTAGLDPKGRKEMMEM-FYKLHKEKGLTTVLVTHSMedaaRY---ADQIVVMHKGTVFLQGTPREiFADP 237

                   .
gi 1189438336  942 E 942
Cdd:PRK13634   238 D 238
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
718-934 2.63e-17

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 83.52  E-value: 2.63e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGED-------------PSPEretatdlD 784
Cdd:PRK11231    18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlarrlallpqhhLTPE-------G 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 IRKRGPVAYAsQKPWL-----LnatveeniifeSPFNKQRYKMVIEacslqpdidilphgdQTQIGE----RGINLSGGQ 855
Cdd:PRK11231    91 ITVRELVAYG-RSPWLslwgrL-----------SAEDNARVNQAME---------------QTRINHladrRLTDLSGGQ 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  856 RQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11231   144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELM--RLMRELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGT 221
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1383-1531 5.23e-17

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide as in CFTR, or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 79.61  E-value: 5.23e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL 1461
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1462 DPERKC---SDSTLWEALEIAQLKLvvkALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:pfam00005   81 RLGLLLkglSKREKDARAEEALEKL---GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1366-1577 5.52e-17

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 81.61  E-value: 5.52e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHI--IIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03290      1 VQVTNGYFSWGSGL-ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwSNKNESEPSFEATRSRNRY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIIL--QDPVLFSGTIRFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03290     80 SVAYaaQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1522 SIFIMDEATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVHTILSADLVIVLKRGA 1577
Cdd:cd03290    160 NIVFLDDPFSALDIhLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
718-958 5.90e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 82.75  E-value: 5.90e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemQKVSGAVFWSSLPDSEI---GEdpSPERETATDLDIRK-RGPVAY 793
Cdd:PRK09984    20 LHAVDLNIHHGEMVALLGPSGSGKSTLL-------RHLSGLITGDKSAGSHIellGR--TVQREGRLARDIRKsRANTGY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNA-TVEENIIF----ESPFNKQRYKMVIEAcSLQPDIDILphgdqTQIG------ERGINLSGGQRQRISVA 862
Cdd:PRK09984    91 IFQQFNLVNRlSVLENVLIgalgSTPFWRTCFSWFTRE-QKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIA 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLSDHLMqagilELLRD----DKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09984   165 RALMQQAKVILADEPIASLDPESARIVM-----DTLRDinqnDGITVVVTLHQVDYaLRYCERIVALRQGHVFYDGSSQQ 239
                          250       260
                   ....*....|....*....|.
gi 1189438336  938 FQRSEcqlFEHWKTLMNRQDQ 958
Cdd:PRK09984   240 FDNER---FDHLYRSINRVEE 257
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1358-1573 9.68e-17

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 86.62  E-value: 9.68e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1358 KNWPDQGKIQIQNLSVRYDSSLK-PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK-LP 1435
Cdd:PTZ00265   375 KKLKDIKKIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdIN 454
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLRSRLSIILQDPVLFSGTIRFN----------------------------LDPERKC--------------SDSTLW 1473
Cdd:PTZ00265   455 LKWWRSKIGVVSQDPLLFSNSIKNNikyslyslkdlealsnyynedgndsqenKNKRNSCrakcagdlndmsntTDSNEL 534
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 -------------EALEIAQLKLV---VKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT 1537
Cdd:PTZ00265   535 iemrknyqtikdsEVVDVSKKVLIhdfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1189438336 1538 ENILQKVV--MTAFADRTVVTIAHRVHTILSADLVIVL 1573
Cdd:PTZ00265   615 EYLVQKTInnLKGNENRITIIIAHRLSTIRYANTIFVL 652
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1366-1589 2.36e-16

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 224045 [Multi-domain]  Cd Length: 258  Bit Score: 80.69  E-value: 2.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:COG1120      3 LEVENLSFGYGG--KPILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASLSPKELAKKLAY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNL---------DPERKCSDSTLWEALE-IAQLKLVVKAlpgglDAIITEGgenfSQGQRQLFCLAR 1515
Cdd:COG1120     81 VPQSPSAPFGLTVYELvllgryphlGLFGRPSKEDEEIVEEaLELLGLEHLA-----DRPVDEL----SGGERQRVLIAR 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATE----NILQKVVMTafADRTVVTIAHRV-HTILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG1120    152 ALAQETPILLLDEPTSHLDIAHQievlELLRDLNRE--KGLTVVMVLHDLnLAARYADHLILLKDGKIVAQGTPEEVLT 228
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
716-934 2.48e-16

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 84.24  E-value: 2.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaALgeMQKVSgavfwsslpdseigeDPSPERETATDLDIRK------RG 789
Cdd:PRK13657   349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI--NL--LQRVF---------------DPQSGRILIDGTDIRTvtraslRR 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQKPWLLNATVEENIIFESPfNKQRYKMVIEACSLQPD--IDILPHGDQTQIGERGINLSGGQRQRISVARALYQ 867
Cdd:PRK13657   410 NIAVVFQDAGLFNRSIEDNIRVGRP-DATDEEMRAAAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLK 488
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13657   489 DPPILILDEATSALDVETEAKVKAA--LDELMKG-RTTFIIAHRLSTVRNADRILVFDNGRVVESGS 552
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
725-933 2.72e-16

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 79.46  E-value: 2.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  725 IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERetatdldirkrgPVAYASQKPWLL-NA 803
Cdd:cd03298     21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV---LINGVDVTAAPPADR------------PVSMLFQENNLFaHL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  804 TVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPhgdqtqiGErginLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:cd03298     86 TVEQNVglglspgLKLTAEDRQAIEVALARVGLAGLEKRLP-------GE----LSGGERQRVALARVLVRDKPVLLLDE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  877 PFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03298    155 PFAALDPALRAE-MLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
707-937 3.13e-16

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 79.55  E-value: 3.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPERETAtdldiR 786
Cdd:cd03258     10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVL---VDGTDLTLLSGKELRKA-----R 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRgpVAYASQKPWLLNA-TVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQR 858
Cdd:cd03258     82 RR--IGMIFQHFNLLSSrTVFENVALpleiagvPKAEIEERVLELLELVGLEDKADAYPA-----------QLSGGQKQR 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03258    149 VGIARALANNPKVLLCDEATSALDPETTQ-----SILALLRDINRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223

                   ....
gi 1189438336  934 TLKD 937
Cdd:cd03258    224 TVEE 227
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
714-929 3.20e-16

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 77.85  E-value: 3.20e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEdpspERETATDLDIRKRGpVAY 793
Cdd:cd03216     12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------GK----EVSFASPRDARRAG-IAM 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03216     80 VYQ------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03216    106 LDEPTAALTPAEVERLFK--VIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
712-937 3.41e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 80.51  E-value: 3.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSperetaTDLDIRKRGPV 791
Cdd:PRK13639    12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIKYDKK------SLLEVRKTVGI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK13639    83 VFQNPDDQLFAPTVEEDVAF-GPLNlglskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAG 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13639   151 ILAMKPEIIVLDEPTSGLDPMGASQIMK--LLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKE 223
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
718-931 4.28e-16

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 84.01  E-value: 4.28e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAVFWSSLPD-SEIGEDpsperetatDLDIRKRGPVAYASQ 796
Cdd:PRK10535    24 LKGISLDIYAGEMVAIVGASGSGKSTLM-NILGCLDKPTSGTYRVAGQDvATLDAD---------ALAQLRREHFGFIFQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KPWLL-NATVEENIifESPF---------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:PRK10535    94 RYHLLsHLTAAQNV--EVPAvyaglerkqRLLRAQELLQRLGLEDRVEYQPS-----------QLSGGQQQRVSIARALM 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQR 931
Cdd:PRK10535   161 NGGQVILADEPTGALDSHSGEEVM--AILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
712-937 4.49e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 80.28  E-value: 4.49e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperetatdLDIRKRGpv 791
Cdd:PRK13636    16 SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-----------------IDYSRKG-- 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 ayasqkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPhgdQTQIGER--------GIN---------LSGG 854
Cdd:PRK13636    77 --------LMKLRESVGMVFQDPDNQLFSASVYQDVSFGAVNLKLP---EDEVRKRvdnalkrtGIEhlkdkpthcLSFG 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK13636   146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKL-LVEMQKELGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224

                   ....
gi 1189438336  934 TLKD 937
Cdd:PRK13636   225 NPKE 228
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1366-1581 4.80e-16

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 79.09  E-value: 4.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD------TFEGHIIIDGIDIAKLPLh 1437
Cdd:cd03257      2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsgsiIFDGKDLLKLSRRLRKIR- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 tlRSRLSIILQDPvlFSgtirfNLDPERKCSDStLWEALEI--------AQLKLVVKALPG-GLDAII-----TEggenF 1503
Cdd:cd03257     81 --RKEIQMVFQDP--MS-----SLNPRMTIGEQ-IAEPLRIhgklskkeARKEAVLLLLVGvGLPEEVlnrypHE----L 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE-NILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03257    147 SGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaQILD--LLKKLQEElglTLLFITHDLGVVAKiADRVAVMYAGKI 224

                   ...
gi 1189438336 1579 LEF 1581
Cdd:cd03257    225 VEE 227
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
711-910 5.38e-16

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 77.19  E-value: 5.38e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMqkvsgavfWSsLPDSEIGedpSPERETatdldirkrgp 790
Cdd:cd03223     10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF-RALAGL--------WP-WGSGRIG---MPEGED----------- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilPHGDqtqigergiNLSGGQRQRISVARALYQHAN 870
Cdd:cd03223     66 LLFLPQRPYLPLGTLREQLIY-------------------------PWDD---------VLSGGEQQRLAFARLLLHKPK 111
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1189438336  871 VVFLDDPFSALDIHLSDHLMQagileLLRDDKRTVVLVTH 910
Cdd:cd03223    112 FVFLDEATSALDEESEDRLYQ-----LLKELGITVISVGH 146
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
718-929 6.57e-16

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 79.34  E-value: 6.57e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGemQKVSGAVFWSSLPDSEIGEDpsperetaTDLDIRKrgpvayAS 795
Cdd:PRK11247    28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLrlLAGLE--TPSAGELLAGTAPLAEARED--------TRLMFQD------AR 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWllnATVEENIIFESPFN-KQRYKMVIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK11247    92 LLPW---KKVIDNVGLGLKGQwRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPGLLLL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  875 DDPFSALDIhLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 929
Cdd:PRK11247   158 DEPLGALDA-LTRIEMQDLIESLWQQHGFTVLLVTHDVsEAVAMADRVLLIEEGKI 212
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
720-934 8.42e-16

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 79.22  E-value: 8.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpspereTATDL-DIRKRgPVAYASQKP 798
Cdd:cd03294     42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAM---------SRKELrELRRK-KISMVFQSF 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  799 WLL-NATVEENIIF------ESPFNKQRYKM-VIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHAN 870
Cdd:cd03294    112 ALLpHRTVLENVAFglevqgVPRAEREERAAeALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPD 180
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  871 VVFLDDPFSALDiHLSDHLMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:cd03294    181 ILLMDEAFSALD-PLIRREMQDELLRLQAELQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGT 244
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
733-934 1.16e-15

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 79.85  E-value: 1.16e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  733 IVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPsPEREtatdldirkrgPVAYASQKPWLL-NATVEENIIF 811
Cdd:TIGR01187    1 LLGPSGCGKTTLLRLLAGFEQPDSGSIM---LDGEDVTNVP-PHLR-----------HINMVFQSYALFpHMTVEENVAF 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  812 ESPFNK----QRYKMVIEACSLqpdidilphgdqTQIGERG----INLSGGQRQRISVARALYQHANVVFLDDPFSALDI 883
Cdd:TIGR01187   66 GLKMRKvpraEIKPRVLEALRL------------VQLEEFAdrkpHQLSGGQQQRVALARALVFKPKILLLDEPLSALDK 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  884 HLSDhLMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:TIGR01187  134 KLRD-QMQLELKTIQEQLGITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGT 184
cbiO PRK13640
energy-coupling factor transporter ATPase;
708-934 1.17e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 79.07  E-value: 1.17e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllAALgemqkVSGAVFWSSLPDSEIGEDpSPERETATDLDIRK 787
Cdd:PRK13640    13 FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTI--SKL-----INGLLLPDDNPNSKITVD-GITLTAKTVWDIRE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RGPVAYASQKPWLLNATVEENIIFESPfNKQ--RYKMVIEACSLQPDIDILPHGDQTQIgergiNLSGGQRQRISVARAL 865
Cdd:PRK13640    85 KVGIVFQNPDNQFVGATVGDDVAFGLE-NRAvpRPEMIKIVRDVLADVGMLDYIDSEPA-----NLSGGQKQRVAIAGIL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13640   159 AVEPKIIILDESTSMLDPAGKEQILKL-IRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
701-934 1.52e-15

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 82.77  E-value: 1.52e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFTW-TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKS---SLLL---------------AALGEMQK------- 754
Cdd:PTZ00265  1166 IEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKStvmSLLMrfydlkndhhivfknEHTNDMTNeqdyqgd 1245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  755 ------VSGAVFWSSLPDSEIGEDPSPERETAT---------DLDIRK-RGPVAYASQKPWLLNATVEENIIF-ESPFNK 817
Cdd:PTZ00265  1246 eeqnvgMKNVNEFSLTKEGGSGEDSTVFKNSGKilldgvdicDYNLKDlRNLFSIVSQEPMLFNMSIYENIKFgKEDATR 1325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  818 QRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlSDHLMQAGILEL 897
Cdd:PTZ00265  1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDI 1404
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1189438336  898 LRDDKRTVVLVTHKLQYLPHADWIIAM----KDGT-IQREGT 934
Cdd:PTZ00265  1405 KDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGT 1446
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
706-932 1.61e-15

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 78.31  E-value: 1.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  706 GYFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgeDPSPERETATDLD- 784
Cdd:TIGR02769   15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQL--DRKQRRAFRRDVQl 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 IRKRGPVAYASQKP--WLLNATVEENIIFESPFNKQRYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISV 861
Cdd:TIGR02769   93 VFQDSPSAVNPRMTvrQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDaDKLPR-----------QLSGGQLQRINI 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 932
Cdd:TIGR02769  162 ARALAVKPKLIVLDEAVSNLDMVL-----QAVILELLRKLQQafgtAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
720-942 1.63e-15

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 78.49  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSpeRETAtdldiRKRGPVAYasqkpw 799
Cdd:PRK10253    25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW---LDGEHIQHYAS--KEVA-----RRIGLLAQ------ 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 llNATVEENIIFESPFNKQRYKMvieacslQP--------DIDILPHGDQ----TQIGERGIN-LSGGQRQRISVARALY 866
Cdd:PRK10253    89 --NATTPGDITVQELVARGRYPH-------QPlftrwrkeDEEAVTKAMQatgiTHLADQSVDtLSGGQRQRAWIAMVLA 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  867 QHANVVFLDDPFSALDIhlsDHlmQAGILELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:PRK10253   160 QETAIMLLDEPTTWLDI---SH--QIDLLELLSELNRekgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA 234

                   .
gi 1189438336  942 E 942
Cdd:PRK10253   235 E 235
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
720-941 1.63e-15

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 81.86  E-value: 1.63e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLlaalGEMQKVSGAVFWSSLPDseiGEDPSpereTATDLDIRKrgPVAYASQKPW 799
Cdd:TIGR01192  353 DVSFEAKAGQTVAIVGPTGAGKTTLI----NLLQRVYDPTVGQILID---GIDIN----TVTRESLRK--SIATVFQDAG 419
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 LLNATVEENIIF--ESPFNKQRYKMViEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDP 877
Cdd:TIGR01192  420 LFNRSIRENIRLgrEGATDEEVYEAA-KAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEA 498
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  878 FSALDIHLSDHLMQAgiLELLRDDkRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:TIGR01192  499 TSALDVETEARVKNA--IDALRKN-RTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK 559
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1362-1592 1.81e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 78.49  E-value: 1.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1362 DQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS 1441
Cdd:PRK13632     4 KSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDP-VLFSGT-----IRFNLdpERKCSDSTLWEALeIAQLKLVVkalpgGLDAIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK13632    84 KIGIIFQNPdNQFIGAtveddIAFGL--ENKKVPPKKMKDI-IDDLAKKV-----GMEDYLDKEPQNLSGGQKQRVAIAS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1516 AFVRKTSIFIMDEATASID-MATENILQKVV-MTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13632   156 VLALNPEIIIFDESTSMLDpKGKREIKKIMVdLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
714-913 1.94e-15

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226905 [Multi-domain]  Cd Length: 259  Bit Score: 77.87  E-value: 1.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDpsperetatdldirkRGPVAy 793
Cdd:COG4525     17 PRSALEDVSLTIASGELVVVLGPSGCGKTTLLNLIAGFVTPSRGSIQLNGRRIEGPGAE---------------RGVVF- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 asQK----PWLlnaTVEENIIFESPF----NKQRYKMVIEACSLQPdidiLPHGDQTQIGErginLSGGQRQRISVARAL 865
Cdd:COG4525     81 --QNeallPWL---NVIDNVAFGLQLrgieKAQRREIAHQMLALVG----LEGAEHKYIWQ----LSGGMRQRVGIARAL 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:COG4525    148 AVEPQLLLLDEPFGALDALTREQ-MQELLLDLWQETGKQVLLITHDIE 194
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1366-1590 2.09e-15

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 224049 [Multi-domain]  Cd Length: 252  Bit Score: 77.69  E-value: 2.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS--SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-TFEGHIIIDGIDIAKLPLHTLRSR 1442
Cdd:COG1124      4 LSVRNLSIVYGGgkFAFHALNNVSLEIERGETLGIVGESGSGKSTLARLLAGLEKpSSGSILLDGKPLAPKKRAKAFYRP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDPvlfSGTirfnLDPERKCSDStLWEALEIAQL----KLVVKAL------PGGLDAIITEggenFSQGQRQLFC 1512
Cdd:COG1124     84 VQMVFQDP---YSS----LNPRRTVGRI-LSEPLRPHGLsksqQRIAELLdqvglpPSFLDRRPHE----LSGGQRQRIA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATE----NILQKVVmtafADR--TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPE 1585
Cdd:COG1124    152 IARALIPEPKLLILDEPTSALDVSVQaqilNLLLELK----KERglTYLFISHDLALVEHmCDRIAVMDNGQIVEIGPTE 227

                   ....*
gi 1189438336 1586 KLLSR 1590
Cdd:COG1124    228 ELLSH 232
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
711-937 2.61e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 78.59  E-value: 2.61e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSsLPDSEIGEDPSPERETATDL----- 783
Cdd:PRK13651    16 LPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIehLNAL--LLPDTGTIEWI-FKDEKNKKKTKEKEKVLEKLviqkt 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  784 ---------DIRKRGPVAYASQKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLqpDIDILPHGDqtqige 846
Cdd:PRK13651    93 rfkkikkikEIRRRVGVVFQFAEYQLFEQTIEKDIIF-GPVSmgvskeeaKKRAAKYIELVGL--DESYLQRSP------ 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  847 rgINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMK 925
Cdd:PRK13651   164 --FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILE--IFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFK 239
                          250
                   ....*....|....*.
gi 1189438336  926 DGTIQREG----TLKD 937
Cdd:PRK13651   240 DGKIIKDGdtydILSD 255
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
714-938 2.79e-15

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 76.70  E-value: 2.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED----PSPEREtatdldirKRG 789
Cdd:cd03224     12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFD-------GRDitglPPHERA--------RAG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 pVAYASQKPWLL-NATVEENIIF-ESPFNKQRYKMVIE-ACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARALY 866
Cdd:cd03224     77 -IGYVPEGRRIFpELTVEENLLLgAYARRRAKRKARLErVYELFPRL-------KERRKQLAGTLSGGEQQMLAIARALM 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDF 938
Cdd:cd03224    149 SRPKLLLLDEPSEGLAPKIVEEIFEA--IRELRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAEL 219
cbiO PRK13644
energy-coupling factor transporter ATPase;
712-934 5.01e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 77.33  E-value: 5.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeigeDPSPEREtatdldIRKRGPV 791
Cdd:PRK13644    12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG----DFSKLQG------IRKLVGI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFeSPFNkqrykmvieACslQPDIDILPHGDQTqIGERGI---------NLSGGQRQRISVA 862
Cdd:PRK13644    82 VFQNPETQFVGRTVEEDLAF-GPEN---------LC--LPPIEIRKRVDRA-LAEIGLekyrhrspkTLSGGQGQCVALA 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13644   149 GILTMEPECLIFDEVTSMLDPDSGIAVLER--IKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
713-924 8.79e-15

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 226620 [Multi-domain]  Cd Length: 213  Bit Score: 74.87  E-value: 8.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ---KVSGAVFwssLPDSEIGEDPSPEREtatdldirkrg 789
Cdd:COG4136     13 PGSCLLANVNFTIAKGEIVTLMGPSGCGKSTLLSWMIGALAgqfSCTGELW---LNEQRLDMLPAAQRQ----------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 pVAYASQKPWLL-NATVEENIIFESPFN---KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARAL 865
Cdd:COG4136     79 -IGILFQDALLFpHLSVGQNLLFALPATlkgNARRNAANAALE-RSGLDGAFHQDPAT-------LSGGQRARVALLRAL 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:COG4136    150 LAQPKALLLDEPFSRLDVALRDQFRQW-VFSEVRAAGIPTVQVTHDLQDVPAGSRVIEM 207
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
718-937 8.83e-15

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 75.45  E-value: 8.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVAYASQK 797
Cdd:cd03299     15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLN-------GKD-------ITNLPPEKRD-ISYVPQN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIIF----ESPFNKQRYKMVIE-ACSLqpDIDILPHGDQTqigergiNLSGGQRQRISVARALYQHANV 871
Cdd:cd03299     80 YALFpHMTVYKNIAYglkkRKVDKKEIERKVLEiAEML--GIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKI 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  872 VFLDDPFSALDIHLSDHLMqagilELLRDDKR----TVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03299    151 LLLDEPFSALDVRTKEKLR-----EELKKIRKefgvTVLHVTHDFeEAWALADKVAIMLNGKLIQVGKPEE 216
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
1104-1336 1.33e-14

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 76.31  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1104 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYV-- 1181
Cdd:cd18552     60 TYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLdw 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1182 --TPVFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDttqlpLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSN--- 1255
Cdd:cd18552    140 klTLIALVVLPLAALPIRRIGKRLRKISRRSQeSMGD-----LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLrrl 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1256 NIASLFLTAANRWLevrMEYIGACVVLIAAVTSISNSLHRELSAG-LVGLgLTYALMVSNYLnwmvRNLADM--ELQ--L 1330
Cdd:cd18552    215 SMKIARARALSSPL---MELLGAIAIALVLWYGGYQVISGELTPGeFISF-ITALLLLYQPI----KRLSNVnaNLQrgL 286

                   ....*.
gi 1189438336 1331 GAVKRI 1336
Cdd:cd18552    287 AAAERI 292
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
718-938 1.42e-14

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224051 [Multi-domain]  Cd Length: 240  Bit Score: 74.85  E-value: 1.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFwsslpdseIGEDpsperETATDLDIRK-RGPVAYA 794
Cdd:COG1126     18 LKGISLSVEKGEVVVIIGPSGSGKSTLLrcLNGLEEPD--SGSIT--------VDGE-----DVGDKKDILKlRRKVGMV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWLL-NATVEENIIfESPFN---------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:COG1126     83 FQQFNLFpHLTVLENVT-LAPVKvkklskaeaREKALELLEKVGLADKADAYPA-----------QLSGGQQQRVAIARA 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:COG1126    151 LAMDPKVMLFDEPTSALDPELVGEVLD--VMKDLAEEGMTMIIVTHEMGFAREvADRVIFMDQGKIIEEGPPEEF 223
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
718-913 2.41e-14

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224042 [Multi-domain]  Cd Length: 253  Bit Score: 74.50  E-value: 2.41e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwssLPDSEIgedpspeRETATD-LDIRKRgpV 791
Cdd:COG1117     23 LKDINLDIPKNKVTALIGPSGCGKSTLLrclnrMNDLIPGARVEGEVL---LDGKNI-------YDPKVDvVELRRR--V 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIF---ESPFNKQRYKMVIEAcSLQ--------PDidilphgdqtQIGERGINLSGGQRQRIS 860
Cdd:COG1117     91 GMVFQKPNPFPMSIYDNVAYglrLHGIKDKELDEIVES-SLKkaalwdevKD----------RLHKSALGLSGGQQQRLC 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRD--DKRTVVLVTHKLQ 913
Cdd:COG1117    160 IARALAVKPEVLLMDEPTSALDP-----ISTLKIEELITElkKKYTIVIVTHNMQ 209
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
709-933 2.91e-14

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 73.36  E-value: 2.91e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  709 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERetatdldirkr 788
Cdd:TIGR01277    7 RYEYEHLPMEFDLNVA--DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSI---KVNDQSHTGLAPYQR----------- 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 gPVAYASQKPWLL-NATVEENIIFE-SPFNK----QRYKMVIEACSLQPD--IDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:TIGR01277   71 -PVSMLFQENNLFaHLTVRQNIGLGlHPGLKlnaeQQEKVVDAAQQVGIAdyLDRLPE-----------QLSGGQRQRVA 138
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:TIGR01277  139 LARCLVRPNPILLLDEPFSALDPLLREE-MLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKIKVVS 211
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
712-936 3.00e-14

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 226927 [Multi-domain]  Cd Length: 245  Bit Score: 74.37  E-value: 3.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdsEIGEDPSPERetatdldiRKRGPV 791
Cdd:COG4555     12 GSKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGV---DTVRDPSFVR--------RKIGVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLnaTVEENIIFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARA 864
Cdd:COG4555     81 FGERGLYARL--TARENLKYFARLNglsrkeiKARIAELSKRLQLLEYLD-----------RRVGEFSTGMKQKVAIARA 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 936
Cdd:COG4555    148 LVHDPSILVLDEPTSGLDIRTRRKFHD--FIKQLKNEGRAVIFSSHIMQEVEAlCDRVIVLHKGEVVLEGSIE 218
cbiO PRK13644
energy-coupling factor transporter ATPase;
1366-1589 3.51e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 74.64  E-value: 3.51e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSL------------AFFRMVDTFEghiiidgidIAK 1433
Cdd:PRK13644     2 IRLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALhlngllrpqkgkVLVSGIDTGD---------FSK 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPlhTLRSRLSIILQDP-VLFSG-TIRFNL--DPERKCSDSTlwealEIAqlKLVVKALPG-GLDAIITEGGENFSQGQR 1508
Cdd:PRK13644    72 LQ--GIRKLVGIVFQNPeTQFVGrTVEEDLafGPENLCLPPI-----EIR--KRVDRALAEiGLEKYRHRSPKTLSGGQG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKL 1587
Cdd:PRK13644   143 QCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222

                   ..
gi 1189438336 1588 LS 1589
Cdd:PRK13644   223 LS 224
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
713-910 3.68e-14

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 76.03  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPERetatdldirkrgPVA 792
Cdd:PRK11607    30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM---LDGVDLSHVPPYQR------------PIN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIFESPFNK-------QRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:PRK11607    95 MMFQSYALFpHMTVEQNIAFGLKQDKlpkaeiaSRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARS 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH 910
Cdd:PRK11607   164 LAKRPKLLLLDEPMGALDKKLRDR-MQLEVVDILERVGVTCVMVTH 208
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
711-929 4.31e-14

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 224026 [Multi-domain]  Cd Length: 263  Bit Score: 74.28  E-value: 4.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGP 790
Cdd:COG1101     15 TPLEKRALNGLSLEIAEGDFVTVIGSNGAGKSTLLNAIAGDLKPTSGQILID-------GVD-------VTKKSVAKRAN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 -VAYASQKPWLLNA---TVEENII----------FESPFNKQRYKmvieacSLQPDIDILPHGDQTQIGERGINLSGGQR 856
Cdd:COG1101     81 lLARVFQDPLAGTApelTIEENLAlaesrgkkrgLSSALNERRRS------SFRERLARLGLGLENRLSDRIGLLSGGQR 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTI 929
Cdd:COG1101    155 QALSLLMATLHPPKILLLDEHTAALDPKTAEFVMEL-TAKIVEEHKLTTLMVTHNMeDALDYGNRLIMLHSGKI 227
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
1085-1336 4.54e-14

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 74.51  E-value: 4.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1164
Cdd:cd07346     41 IALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYVTPV-FLVALLPLAIVCYFIQKYF---RVASRDLQQLDDTtqlpLLSHFAETVEGLTTIRAFRY 1240
Cdd:cd07346    121 LSDVLTLIGALVILFYLNWKlTLVALLLLPLYVLILRYFRrriRKASREVRESLAE----LSAFLQESLSGIRVVKAFAA 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1241 EARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSLHRELSAGlvglGLTYALMVSNYLNWMV 1320
Cdd:cd07346    197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG----ELVAFLAYLGMLFGPI 272
                          250       260
                   ....*....|....*....|
gi 1189438336 1321 RNLADMELQ----LGAVKRI 1336
Cdd:cd07346    273 QRLANLYNQlqqaLASLERI 292
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
713-913 4.78e-14

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 73.97  E-value: 4.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDseigEDPSPEREtatdldirkrgpVA 792
Cdd:PRK11248    12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERG------------VV 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQK--PWLlnaTVEENIIFespfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHA 869
Cdd:PRK11248    76 FQNEGllPWR---NVQDNVAF-----GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIwQLSGGQRQRVGIARALAANP 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  870 NVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:PRK11248   148 QLLLLDEPFGALDAFTREQ-MQTLLLKLWQETGKQVLLITHDIE 190
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
710-914 5.13e-14

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 72.20  E-value: 5.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFwsslpdseIGEDPSPEREtatdldIRK 787
Cdd:cd03213     17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLnaLAGRRTGLGVSGEVL--------INGRPLDKRS------FRK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 RgpVAYASQKPWLL-NATVEENIIFespfnkqrykmvieACSLQpdidilphgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:cd03213     83 I--IGYVPQDDILHpTLTVRETLMF--------------AAKLR-------------------GLSGGERKRVSIALELV 127
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY 914
Cdd:cd03213    128 SNPSLLFLDEPTSGLDSSSALQVMS--LLRRLADTGRTIICSIHQPSS 173
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
715-932 6.88e-14

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226647 [Multi-domain]  Cd Length: 228  Bit Score: 72.82  E-value: 6.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPeretatdlDIRKRGpVAYA 794
Cdd:COG4181     23 LSILKGVELVVKRGETVAIVGPSGSGKSTLLAVLAGLDDPSSGEVRLLGQPLHKLDEDARA--------ALRARH-VGFV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWLL-NATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:COG4181     94 FQSFHLIpNLTALENVALplelrgeSSADSRAGAKALLEAVGLGKRLTHYPA-----------QLSGGEQQRVALARAFA 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLmqAGIL-ELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:COG4181    163 GRPDVLFADEPTGNLDRATGDKI--ADLLfALNRERGTTLVLVTHDPQLAARCDRQLRLRSGRLVED 227
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
708-938 7.53e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 73.53  E-value: 7.53e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  708 FTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ---KVSGAVfwsslpdsEIGEDPSPERETATD 782
Cdd:PRK14258    13 LSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLkcLNRMNELEsevRVEGRV--------EFFNQNIYERRVNLN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  783 ldiRKRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKM----VIEACSLQPDI-DILPHgdqtQIGERGINLSGGQRQ 857
Cdd:PRK14258    85 ---RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLeiddIVESALKDADLwDEIKH----KIHKSALDLSGGQQQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  858 RISVARALYQHANVVFLDDPFSALDIHLS---DHLMQAGILEllrdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK14258   158 RLCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRLR----SELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQ 233

                   ....
gi 1189438336  935 LKDF 938
Cdd:PRK14258   234 LVEF 237
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
718-942 8.37e-14

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226929 [Multi-domain]  Cd Length: 259  Bit Score: 73.16  E-value: 8.37e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpspereTATDLdIRKRGPVAYASQK 797
Cdd:COG4559     17 LDGVSLDLRPGEVLAILGPNGAGKSTLLKALSGELSPDSGEVTLNGVPLNSW---------PPEEL-ARHRAVLPQNSSL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 --PWLLNATVEENII-FESPFNKQRYKMVIEACSLQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHANVV-- 872
Cdd:COG4559     87 afPFTVQEVVQMGRIpHRSGREPEEDERIAAQALAATDLSGLAGRDYRT-------LSGGEQQRVQLARVLAQLWPPVps 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  873 ----FLDDPFSALDIHlsdHlmQAGILELLRD---DKRTVVLVTHKL----QYlphADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:COG4559    160 grwlFLDEPTSALDIA---H--QHHTLRLARQlarEGGAVLAVLHDLnlaaQY---ADRIVLLHQGRVIASGSPQDVLTD 231

                   .
gi 1189438336  942 E 942
Cdd:COG4559    232 E 232
MalK COG3839
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1366-1599 9.77e-14

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 226359 [Multi-domain]  Cd Length: 338  Bit Score: 74.22  E-value: 9.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGhiiidgidiaklP---------- 1435
Cdd:COG3839      4 LELKNVRKSFGS--FEVLKDVNLDIEDGEFVVLLGPSGCGKSTL----LRMIAGLEE------------Ptsgeilidgr 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 ----LHTLRSRLSIILQDPVLF-SGTIRFNL--------DPERKCsDSTLWEALEIAQLKLVVKALPGGLdaiiteggen 1502
Cdd:COG3839     66 dvtdLPPEKRGIAMVFQNYALYpHMTVYENIafglklrgVPKAEI-DKRVKEVAKLLGLEHLLNRKPLQL---------- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1503 fSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAIL 1579
Cdd:COG3839    135 -SGGQRQRVALARALVRKPKVFLLDEPLSNLDAKLRVLMRSEIKKLHERLgtTTIYVTHDQVEAMTlADRIVVMNDGRIQ 213
                          250       260
                   ....*....|....*....|.
gi 1189438336 1580 EFDKPEKLLSRKDSVF-ASFV 1599
Cdd:COG3839    214 QVGTPLELYERPANLFvAGFI 234
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
721-941 1.15e-13

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 74.38  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWSSLPDSEIGEDPSPERetatdldiRKrgpVAYASQKP 798
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIrlIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEK--------RR---IGYVFQEA 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  799 WLL-NATVEENIIF-----ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQHANVV 872
Cdd:TIGR02142   85 RLFpHLSVRGNLRYgmkraRPSERRISFERVIELLGIGHLLGRLPG-----------RLSGGEKQRVAIGRALLSSPRLL 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  873 FLDDPFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:TIGR02142  154 LMDEPLAALDDPRKYEILP--YLERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWAS 222
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1366-1590 1.37e-13

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 75.31  E-value: 1.37e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHI----IIDGIDIAKLPLHTL 1439
Cdd:COG1123      6 LEVENLTVEFatDGGRVPAVRDVSFEVEPGEILGIVGESGSGKSTLALALMGLLPEGGRITsgevILDGRDLLGLSEREM 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1440 RS----RLSIILQDP------------VLFSGTIRFNLDPERKCSDSTLwEALEIAQL--KLVVKALPggldaiiteggE 1501
Cdd:COG1123     86 RKlrgkRIAMIFQDPmtslnpvmtigdQIREALRLHGKGSRAEARKRAV-ELLEQVGLpdPERRDRYP-----------H 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1502 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH--RVHTILsADLVIVLKRGA 1577
Cdd:COG1123    154 QLSGGMRQRVMIAMALALKPKLLIADEPTTALDVTTQAQILDLLKDLQRELgmAVLFITHdlGVVAEL-ADRVVVMYKGE 232
                          250
                   ....*....|...
gi 1189438336 1578 ILEFDKPEKLLSR 1590
Cdd:COG1123    233 IVETGPTEEILSN 245
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1366-1575 1.40e-13

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 71.73  E-value: 1.40e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSS--LKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1443
Cdd:cd03293      1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTL----LRIIAGLERPTSGEVLVDGE-PVTGPGPDR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFS-GTIRFN--LDPERKCSDSTlwEALEIAQ--LKLVvkalpgGLdaiitEGGENF-----SQGQRQLFCL 1513
Cdd:cd03293     76 GYVFQQDALLPwLTVLDNvaLGLELQGVPKA--EARERAEelLELV------GL-----SGFENAyphqlSGGMRQRVAL 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVH-TILSADLVIVLKR 1575
Cdd:cd03293    143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSA 207
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
721-924 1.76e-13

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 73.59  E-value: 1.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWssLPDSEIGEDPSPERETATDLDIRKRGPVAyaSQKPWL 800
Cdd:PRK15079    40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAW--LGKDLLGMKDDEWRAVRSDIQMIFQDPLA--SLNPRM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  801 lnaTVEEnIIFEsPFN-----------KQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALYQH 868
Cdd:PRK15079   116 ---TIGE-IIAE-PLRtyhpklsrqevKDRVKAMMLKVGLLPNlINRYPH-----------EFSGGQCQRIGIARALILE 179
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  869 ANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK15079   180 PKLIICDEPVSALDVSI-----QAQVVNLLQQLQRemglSLIFIAHDLAVVKHiSDRVLVM 235
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
713-934 1.83e-13

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 75.14  E-value: 1.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGemqkvsgavfWSSLPDSEIGEDPSPeRETATDLDIRKRgpVA 792
Cdd:PRK10790   352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMG----------YYPLTEGEIRLDGRP-LSSLSHSVLRQG--VA 418
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVV 872
Cdd:PRK10790   419 MVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  873 FLDDPFSALDIHLSDHLMQAgiLELLRdDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10790   499 ILDEATANIDSGTEQAIQQA--LAAVR-EHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGT 557
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
718-929 2.07e-13

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 71.02  E-value: 2.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwsslpdsEIGEDPSPERETATDLdIRKRgpVAYAS 795
Cdd:cd03262     16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLrcINLLEEPD--SGTI--------IIDGLKLTDDKKNINE-LRQK--VGMVF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLL-NATVEENIIfESP---FNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANV 871
Cdd:cd03262     83 QQFNLFpHLTVLENIT-LAPikvKGMSKAEAEERALELLEKVGLADKADA-----YPAQLSGGQQQRVAIARALAMNPKV 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  872 VFLDDPFSALDIHlsdhlMQAGILELLRD---DKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03262    157 MLFDEPTSALDPE-----LVGEVLDVMKDlaeEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
1089-1594 2.62e-13

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 226968 [Multi-domain]  Cd Length: 546  Bit Score: 74.45  E-value: 2.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1089 FTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLEcLSRST 1168
Cdd:COG4615     54 FLGLLLLFMVSSLISQLGLTTLGQHFIYKLRSEFIKKILDTPLERIERLGSARLLAGLTSDVRNISFAFSRLPE-LVQAI 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1169 LLCVSALAVISYVTPVFLvALLPLAIVCYFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEGLTTIRAFR---- 1239
Cdd:COG4615    133 ILTLGSAAYLAYLSPKMF-LLTVVWIVVTIWGGFVLMARvykhmAAARETEDK----LQNDYQTILEGRKELTLNRerae 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1240 --YEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMeyigacVVLIAAVTSISNSLHRELSAGLVGLGLTYaLMVSNYLN 1317
Cdd:COG4615    208 yvHNNLYIPDAQEYRHHIIRANTFHLLAVNWSNIML------LGLIGLVFWLALSLGWASTNVAATIVLVL-LFLRTPLL 280
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1318 WMVRNLADMELQLGAVKRIHGLlkTEAESYEGLLAPSLIPknwpDQGKIQIQNlsVRYdsSLKPVLKHVNAL---IAPGQ 1394
Cdd:COG4615    281 SAVGILPTLLTAQVAFNKIAKL--ELAPYKADFPRPQAFP----DWKTLELRN--VRF--AYQDNAFHVGPInltIKRGE 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1395 KIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTirfnLDPERKCSDSTLWE 1474
Cdd:COG4615    351 LVFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVSAEQLEDYRKLFSAVFSDYHLFDQL----LGPEGKASPQLIEK 426
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1475 ALEIAQLKLVVKALPGGLDAIiteggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--R 1552
Cdd:COG4615    427 WLQRLELAHKTSLNDGRFSNL------KLSTGQKKRLALLLALLEERDILVLDEWAADQDPAFRREFYQVLLPLLKEqgK 500
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|..
gi 1189438336 1553 TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:COG4615    501 TIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDETARDAV 542
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
707-937 2.64e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 71.95  E-value: 2.64e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQkvSGAVFwssLPDSEIgedpspERETATDLd 784
Cdd:PRK13632    14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIskILTGLLKPQ--SGEIK---IDGITI------SKENLKEI- 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 irkRGPVAYASQKP--WLLNATVEENIIFeSPFNKQ--RYKM--VIEACSLQPDI-DILPHGDQtqigergiNLSGGQRQ 857
Cdd:PRK13632    82 ---RKKIGIIFQNPdnQFIGATVEDDIAF-GLENKKvpPKKMkdIIDDLAKKVGMeDYLDKEPQ--------NLSGGQKQ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  858 RISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13632   150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI-MVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
709-912 3.09e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 71.84  E-value: 3.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  709 TWTpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGavfwsslpdsEIGEDPSPERETAtdldirKR 788
Cdd:PRK15056    15 TWR-NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG----------KISILGQPTRQAL------QK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 GPVAYASQKP---WLLNATVEENII---------FESPfnKQRYKMVIEACSLQPDIDILPHgdqTQIGErginLSGGQR 856
Cdd:PRK15056    78 NLVAYVPQSEevdWSFPVLVEDVVMmgryghmgwLRRA--KKRDRQIVTAALARVDMVEFRH---RQIGE----LSGGQK 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKL 912
Cdd:PRK15056   149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARII--SLLRELRDEGKTMLVSTHNL 202
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
713-937 4.28e-13

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 72.67  E-value: 4.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRgPVA 792
Cdd:PRK09452    25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD-------GQD-------ITHVPAENR-HVN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIF-----ESPfNKQRYKMVIEA---CSLQPDIDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK09452    90 TVFQSYALFpHMTVFENVAFglrmqKTP-AAEITPRVMEAlrmVQLEEFAQRKPH-----------QLSGGQQQRVAIAR 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09452   158 AVVNKPKVLLLDESLSALDYKLRKQ-MQNELKALQRKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
cbiO PRK13646
energy-coupling factor transporter ATPase;
711-945 4.34e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 71.73  E-value: 4.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgEDPSPERETATdldIRKRGP 790
Cdd:PRK13646    16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV---TVDDITI-THKTKDKYIRP---VRKRIG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNATVEENIIFeSPFNkqrYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQHA 869
Cdd:PRK13646    89 MVFQFPESQLFEDTVEREIIF-GPKN---FKMNLDEVKNYAHRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVSILAMNP 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSECQL 945
Cdd:PRK13646   165 DIIVLDEPTAGLDPQSKRQVMRL-LKSLQTDENKTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDKKKL 240
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
707-948 4.67e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 71.20  E-value: 4.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGEDPSPEretATDLDIR 786
Cdd:PRK13635    12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI--------TVGGMVLSE---ETVWDVR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRgpVAYASQKP--WLLNATVEENIIF--EspfNKQ--RYKMV------IEACSLQPDIDILPHgdqtqigergiNLSGG 854
Cdd:PRK13635    81 RQ--VGMVFQNPdnQFVGATVQDDVAFglE---NIGvpREEMVervdqaLRQVGMEDFLNREPH-----------RLSGG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDihlsdhlmQAG---ILELLRDDKR----TVVLVTHKLQYLPHADWIIAMKDG 927
Cdd:PRK13635   145 QKQRVAIAGVLALQPDIIILDEATSMLD--------PRGrreVLETVRQLKEqkgiTVLSITHDLDEAAQADRVIVMNKG 216
                          250       260
                   ....*....|....*....|.
gi 1189438336  928 TIQREGTLKdfqrsecQLFEH 948
Cdd:PRK13635   217 EILEEGTPE-------EIFKS 230
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
714-933 4.70e-13

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 72.95  E-value: 4.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEDPSPERETATdldIRKRgpVAY 793
Cdd:PRK09536    15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL--------VAGDDVEALSARA---ASRR--VAS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDiDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQHANV 871
Cdd:PRK09536    82 VPQDTSLsFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVE-RAMERTGVAQFADRPVtSLSGGERQRVLLARALAQATPV 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  872 VFLDDPFSALDIHlsdHLMQAgiLELLR---DDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK09536   161 LLLDEPTASLDIN---HQVRT--LELVRrlvDDGKTAVAAIHDLDLAArYCDELVLLADGRVRAAG 221
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
1086-1336 5.16e-13

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 71.44  E-value: 5.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18557     39 ALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLL 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSA---LAVISY-VTPVFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFA-ETVEGLTTIRAF-- 1238
Cdd:cd18557    119 RNILQVIGGliiLFILSWkLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQD-----ALAKAGQVAeESLSNIRTVRSFsa 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -RYE-ARFQQKLLEYTDSnNIASLFLTAANRWLEVRMEYIGACVVLIAAVTSISNSlhrELSAGLVGLGLTYALMVSNYL 1316
Cdd:cd18557    194 eEKEiRRYSEALDRSYRL-ARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSG---QLTVGELTSFILYTIMVASSV 269
                          250       260
                   ....*....|....*....|
gi 1189438336 1317 NWMVRNLADMELQLGAVKRI 1336
Cdd:cd18557    270 GGLSSLLADIMKALGASERV 289
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
718-940 6.09e-13

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 72.04  E-value: 6.09e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSpeRETATDldiRKRGPV--AYAs 795
Cdd:PRK10851    18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFH-------GTDVS--RLHARD---RKVGFVfqHYA- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 qkpWLLNATVEENIIF--------ESPFN---KQRYKMVIEACSLQPDIDILPhgdqTQigerginLSGGQRQRISVARA 864
Cdd:PRK10851    85 ---LFRHMTVFDNIAFgltvlprrERPNAaaiKAKVTQLLEMVQLAHLADRYP----AQ-------LSGGQKQRVALARA 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQR 940
Cdd:PRK10851   151 LAVEPQILLLDEPFGALDAQVRKEL-RRWLRQLHEELKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQVWR 226
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
840-933 6.41e-13

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 70.38  E-value: 6.41e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  840 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-A 918
Cdd:PRK10619   142 DERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR--IMQQLAEEGKTMVVVTHEMGFARHvS 219
                           90
                   ....*....|....*
gi 1189438336  919 DWIIAMKDGTIQREG 933
Cdd:PRK10619   220 SHVIFLHQGKIEEEG 234
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
711-910 7.05e-13

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 226646 [Multi-domain]  Cd Length: 604  Bit Score: 73.50  E-value: 7.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMqkvsgavfWSslpdseIGEdpsperetaTDLDIRKRGP 790
Cdd:COG4178    402 TPDGQTLLSELNFEVRPGERLLITGESGAGKTSLL-RALAGL--------WP------WGS---------GRISMPADSA 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNATVEENIIF---ESPFNKQRYKMVIEACSLQPDIDILP-HGDQTQIgerginLSGGQRQRISVARALY 866
Cdd:COG4178    458 LLFLPQRPYLPQGTLREALCYpnaAPDFSDAELVAVLHKVGLGDLAERLDeEDRWDRV------LSGGEQQRLAFARLLL 531
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQAgILELLRDdkRTVVLVTH 910
Cdd:COG4178    532 HKPKWVFLDEATSALDEETEDRLYQL-LKEELPD--ATVISVGH 572
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
718-951 7.75e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 70.33  E-value: 7.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAVFwssLPDSEIGEDPSPEretatdldIRKRGPVA 792
Cdd:PRK14247    19 LDGVNLEIPDNTITALMGPSGSGKSTLLrvfnrLIELYPEARVSGEVY---LDGQDIFKMDVIE--------LRRRVQMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPwLLNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK14247    88 FQIPNP-IPNLSIFENVALGLKLNRlvkskkelqERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIAR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHLmQAGILELLRDdkRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGTLKD-F 938
Cdd:PRK14247   160 ALAFQPEVLLADEPTANLDPENTAKI-ESLFLELKKD--MTIVLVTH---FPQQAarisDYVAFLYKGQIVEWGPTREvF 233
                          250
                   ....*....|...
gi 1189438336  939 QRSECQLFEHWKT 951
Cdd:PRK14247   234 TNPRHELTEKYVT 246
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
718-911 8.70e-13

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 69.61  E-value: 8.70e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQK---VSGAVFWSslpdseiGEDPSPERetatdldIRKRgpVAYA 794
Cdd:cd03234     23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFN-------GQPRKPDQ-------FQKC--VAYV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWLL-NATVEENIIFESPF-------NKQRYKMVieacslqpDIDILPHGDQTQIGERGI-NLSGGQRQRISVARAL 865
Cdd:cd03234     87 RQDDILLpGLTVRETLTYTAILrlprkssDAIRKKRV--------EDVLLRDLALTRIGGNLVkGISGGERRRVSIAVQL 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHK 911
Cdd:cd03234    159 LWDPKVLILDEPTSGLDSFTALNLVS--TLSQLARRNRIVILTIHQ 202
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
714-937 1.02e-12

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223487 [Multi-domain]  Cd Length: 237  Bit Score: 69.42  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED----PSPEREtatdldirKRG 789
Cdd:COG0410     15 KIQALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFD-------GEDitglPPHERA--------RLG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 pVAYASQKPWLL-NATVEENII---FESPFNKQRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISVARAL 865
Cdd:COG0410     80 -IAYVPEGRRIFpRLTVEENLLlgaYARRDKEAQERDLEEVYELFPRL-------KERRNQRAGTLSGGEQQMLAIARAL 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:COG0410    152 MSRPKLLLLDEPSEGLAPKIVEEIFEA-IKELRKEGGMTILLVEQNARFaLEIADRGYVLENGRIVLSGTAAE 223
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
718-910 1.15e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 68.75  E-value: 1.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVfwsSLPDSEIgEDPSPeretatdldirkRGPVAYAS 795
Cdd:PRK13539    18 FSGLSFTLAAGEALVLTGPNGSGKTTLLrlIAGL--LPPAAGTI---KLDGGDI-DDPDV------------AEACHYLG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 Q----KPWLlnaTVEENIIFESPFNKQRYKMV---IEACSLQPDIDiLPHGdqtqigergiNLSGGQRQRISVARALYQH 868
Cdd:PRK13539    80 HrnamKPAL---TVAENLEFWAAFLGGEELDIaaaLEAVGLAPLAH-LPFG----------YLSAGQKRRVALARLLVSN 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1189438336  869 ANVVFLDDPFSALDIH--------LSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:PRK13539   146 RPIWILDEPTAALDAAavalfaelIRAHLAQGGI----------VIAATH 185
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1363-1591 1.36e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 69.56  E-value: 1.36e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1363 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF-----EGHIIIDGIDIAKLPLH 1437
Cdd:PRK14247     1 MNKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 TLRSRLSIILQDP------VLFSGT---IRFN-LDPERKCSDSTLWEALEIAQLKLVVKalpGGLDAiiteGGENFSQGQ 1507
Cdd:PRK14247    79 ELRRRVQMVFQIPnpipnlSIFENValgLKLNrLVKSKKELQERVRWALEKAQLWDEVK---DRLDA----PAGKLSGGQ 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVhtilsADLVIVLKRGAILE- 1580
Cdd:PRK14247   152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRI-----SDYVAFLYKGQIVEw 226
                          250
                   ....*....|....*..
gi 1189438336 1581 ------FDKPEKLLSRK 1591
Cdd:PRK14247   227 gptrevFTNPRHELTEK 243
FtsE COG2884
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome ...
712-913 1.41e-12

ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225438 [Multi-domain]  Cd Length: 223  Bit Score: 68.78  E-value: 1.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFW-----SSLPDSEIGEdpsperetatdldIR 786
Cdd:COG2884     12 PGGREALRDVSFHIPKGEFVFLTGPSGAGKSTLLKLIYGEERPTRGKILVnghdlSRLKGREIPF-------------LR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRGPVAYASQKpWLLNATVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRI 859
Cdd:COG2884     79 RQIGVVFQDFR-LLPDRTVYENVALplrvigkPPREIRRRVSEVLDLVGLKHKARALP-----------SQLSGGEQQRV 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQ 913
Cdd:COG2884    147 AIARAIVNQPAVLLADEPTGNLDPDLSWEIMR--LFEEINRLGTTVLMATHDLE 198
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
713-910 1.47e-12

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 68.15  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEigEDPSPEREtatdldirkrgpVA 792
Cdd:TIGR01189   11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE--QRDEPHEN------------IL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNA-TVEENIIFESPFNKQRYKMVIEACslqpdidilphgdqTQIGERGIN------LSGGQRQRISVARAL 865
Cdd:TIGR01189   77 YLGHLPGLKPElSALENLHFWAAIHGGAQRTIEDAL--------------AAVGLTGFEdlpaaqLSAGQQRRLALARLW 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  866 YQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:TIGR01189  143 LSRRPLWILDEPTTALDKagvallagLLRAHLARGGI----------VLLTTH 185
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
717-913 1.47e-12

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 69.42  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  717 TLSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQ------KVSGAVFWSslpdseiGEDP-SPERETatdLDIRKRg 789
Cdd:PRK14239    20 ALNSVSLDFYPNEITALIGPSGSGKSTLL-RSINRMNdlnpevTITGSIVYN-------GHNIySPRTDT---VDLRKE- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 pVAYASQKPWLLNATVEENIIFESPFN----KQRYKMVIEACSLQPDI-----DILpHgdqtqigERGINLSGGQRQRIS 860
Cdd:PRK14239    88 -IGMVFQQPNPFPMSIYENVVYGLRLKgikdKQVLDEAVEKSLKGASIwdevkDRL-H-------DSALGLSGGQQQRVC 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  861 VARALYQHANVVFLDDPFSALDiHLSDHLMQAGILELlrDDKRTVVLVTHKLQ 913
Cdd:PRK14239   159 IARVLATSPKIILLDEPTSALD-PISAGKIEETLLGL--KDDYTMLLVTRSMQ 208
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
717-949 1.69e-12

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226635 [Multi-domain]  Cd Length: 242  Bit Score: 69.09  E-value: 1.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  717 TLSNITIRIPRGQLTMIVGQVGCGKSSLL-------LAALGEMQKVSGAVFWSSLPDSEIGedpsperetatdLDIRKRG 789
Cdd:COG4161     17 ALFDITLDCPEGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLNIAGNHFDFSKTPSDKAI------------RDLRRNV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQKPWLlNATVEENIIfESPfnkQRYKMVIEACSLQPDIDILPHGDQTQIGER-GINLSGGQRQRISVARALYQH 868
Cdd:COG4161     85 GMVFQQYNLWP-HLTVQENLI-EAP---CRVLGLSKDQALARAEKLLKRLRLKPYADRyPLHLSGGQQQRVAIARALMME 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  869 ANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRSECQLFE 947
Cdd:COG4161    160 PQVLLFDEPTAALDPEITAQIVS--IIKELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASCFTEPQTEAFK 237

                   ..
gi 1189438336  948 HW 949
Cdd:COG4161    238 NY 239
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1366-1590 1.80e-12

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 71.84  E-value: 1.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS------SLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFSLAFFRMV--DTFEGHIIIDGIDIAKL 1434
Cdd:COG1123    281 LSVRNLSKRYGSrkglfvRERGEVKAVDDVsfdLREGETLGLVGESGSGKSTLARILAGLLppSSGSIIFDGQDLDLTGG 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 PLHTLRSRLSIILQDPVLF---SGTIRFNLDperkcsdstlwEALEI------AQLKLVVKAL-------PGGLDAIITE 1498
Cdd:COG1123    361 ELRRLRRRIQMVFQDPYSSlnpRMTVGDILA-----------EPLRIhgggsgAERRARVAELlelvglpPEFLDRYPHE 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1499 ggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMatenILQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVI 1571
Cdd:COG1123    430 ----LSGGQRQRVAIARALALEPKLLILDEPVSALDV----SVQAQVLNLLKDlqeelgLTYLFISHDLAVVRYiADRVA 501
                          250
                   ....*....|....*....
gi 1189438336 1572 VLKRGAILEFDKPEKLLSR 1590
Cdd:COG1123    502 VMYDGRIVEEGPTEKVFEN 520
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1367-1579 1.84e-12

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 67.46  E-value: 1.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLRSRLSII 1446
Cdd:cd03214      1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKS------------------------------TLLKTLAGL 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1447 LQdpvLFSGTIRFNLDPERKcsdstlWEALEIAQLKLVV----KALpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03214     49 LK---PSSGEILLDGKDLAS------LSPKELARKIAYVpqalELL--GLAHLADRPFNELSGGERQRVLLARALAQEPP 117
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1523 IFIMDEATASIDMATE-NILQKVV-MTAFADRTVVTIAHRV-HTILSADLVIVLKRGAIL 1579
Cdd:cd03214    118 ILLLDEPTSHLDIAHQiELLELLRrLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1366-1587 2.52e-12

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 68.30  E-value: 2.52e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLA----------FFRMVDTFEGHIIIdgidiak 1433
Cdd:cd03261      1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLlrLIVgllrpdsgevLIDGEDISGLSEAE------- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 lpLHTLRSRLSIILQDPVLFSG-TIR----FNLDPERKCSDSTLweaLEIAQLKLVVKALPGGLDAIITEggenFSQGQR 1508
Cdd:cd03261     72 --LYRLRRRMGMLFQSGALFDSlTVFenvaFPLREHTRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE----LSGGMK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMT--AFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPE 1585
Cdd:cd03261    143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPE 222

                   ..
gi 1189438336 1586 KL 1587
Cdd:cd03261    223 EL 224
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
716-937 3.17e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 68.96  E-value: 3.17e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdseigeDPSPERETatdLDIRKRGPVAYAS 795
Cdd:PRK13633    24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGL-------DTSDEENL---WDIRNKAGMVFQN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALYQ 867
Cdd:PRK13633    94 PDNQIVATIVEEDVAF-GPENlgippeeiRERVDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAM 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13633   162 RPECIIFDEPTAMLDPSGRREVVNT-IKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
713-941 3.24e-12

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 71.13  E-value: 3.24e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdseigedpspeRETATdldirkrgpVA 792
Cdd:COG0488    333 GGRLLLKDLSFRIDRGDRIAIVGPNGAGKSTLLKLLAGELGPLSGTVKV---------------GETVK---------IG 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQK--PWLLNATVEENIifeSPFNKQRYKMVIEACsLQpdiDILPHGDQ--TQIGErginLSGGQRQRISVARALYQH 868
Cdd:COG0488    389 YFDQHrdELDPDKTVLEEL---SEGFPDGDEQEVRAY-LG---RFGFTGEDqeKPVGV----LSGGEKARLLLAKLLLQP 457
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  869 ANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:COG0488    458 PNLLLLDEPTNHLDIE-----SLEALEEALLDFEGTVLLVSHDRYFLDRvATRIWLVEDKVEEFEGGYEDYLEQ 526
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1366-1592 3.53e-12

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226164 [Multi-domain]  Cd Length: 258  Bit Score: 68.43  E-value: 3.53e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:COG3638      4 IEVKNLSKTYPGG-HQALKDVNLEINQGEMVAIIGPSGAGKSTLLRSLNGLVDPTSGEILFNGVQITKLKgkeLRKLRRD 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDP-----------VLFS-----GTIR--FNLDPERKCSDSTlwEALEiaQLKLVVKALpggldaiitEGGENFS 1504
Cdd:COG3638     83 IGMIFQQFnlvprlsvlenVLLGrlgytSTWRslFGLFSKEDKAQAL--DALE--RVGILDKAY---------QRASTLS 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1505 QGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIVLKRGA 1577
Cdd:COG3638    150 GGQQQRVAIARALVQQPKIILADEPVASLD----PESAKKVMDILKDinqedgITVIVNLHQVDLAKKyADRIIGLKAGR 225
                          250
                   ....*....|....*
gi 1189438336 1578 ILeFDKPEKLLSRKD 1592
Cdd:COG3638    226 IV-FDGPASELTDEA 239
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
718-973 3.72e-12

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 70.74  E-value: 3.72e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslPDSEIG----EDPSPERETATDLDIRKRGPVAY 793
Cdd:COG0488     19 LENVSLTLNPGERIGLVGRNGAGKSTLLKILAGELEPDSGEVTRP--KGLRVGylsqEPPLDPEKTVLDYVIEGFGELRE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNATVEENIIFESPFNKQRYKMvIEACSLQPDIDILPHG-----DQTQIGErginLSGGQRQRISVARALYQH 868
Cdd:COG0488     97 LLAELEEAYALLADPDDELLAELEALLEE-LDGWTLEARAEEALLGlgfpdEDRPVSS----LSGGWRRRVALARALLEE 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  869 ANVVFLDDPFSALDIhlsDHLMQagiLE-LLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFqrsecqlF 946
Cdd:COG0488    172 PDLLLLDEPTNHLDL---ESIEW---LEdYLKRYPGTVIVVSHDRYFLDNvATHILELDRGKLTPYKGNYSS-------Y 238
                          250       260
                   ....*....|....*....|....*..
gi 1189438336  947 EHWKTLMNRQDQELEKETVTERKATEP 973
Cdd:COG0488    239 LEQKAERLRQEAAAYEKQQKELAKEQE 265
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
695-934 4.13e-12

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 68.26  E-value: 4.13e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  695 DADNCCVQImggyftwtpDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPS 774
Cdd:PRK13548     4 EARNLSVRL---------GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV---RLNGRPLADWSP 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  775 PEREtatdldiRKRgpvAYASQK-----PWllnaTVEENI---IFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQige 846
Cdd:PRK13548    72 AELA-------RRR---AVLPQHsslsfPF----TVEEVVamgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQ--- 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  847 rginLSGGQRQRISVARALYQHAN------VVFLDDPFSALDIHlsdHlmQAGILELLRD----DKRTVVLVTHKL---- 912
Cdd:PRK13548   135 ----LSGGEQQRVQLARVLAQLWEpdgpprWLLLDEPTSALDLA---H--QHHVLRLARQlaheRGLAVIVVLHDLnlaa 205
                          250       260
                   ....*....|....*....|..
gi 1189438336  913 QYlphADWIIAMKDGTIQREGT 934
Cdd:PRK13548   206 RY---ADRIVLLHQGRLVADGT 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1366-1587 4.73e-12

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224046 [Multi-domain]  Cd Length: 254  Bit Score: 68.02  E-value: 4.73e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHT--LRS 1441
Cdd:COG1121      5 IEVENLTVSYGN--RPVLEDISLSVEKGEITALIGPNGAGKSTLlkAILGLLKPSSGEIKIFGKPVRKRRKRLRIgyVPQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDP-----VLFSGT------IRFNLDPERKCSDSTLwEALEIAQLKlvvkalpgglDAIITEggenFSQGQRQL 1510
Cdd:COG1121     83 KSSVDRSFPitvkdVVLLGRygkkgwFRRLNKKDKEKVDEAL-ERVGMEDLR----------DRQIGE----LSGGQKQR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTILS-ADLVIVLKR-----GAILEFDK 1583
Cdd:COG1121    148 VLLARALAQNPDLLLLDEPFTGVDVAGQKEIYDLLKELRQEgKTVLMVTHDLGLVMAyFDRVICLNRhliasGPPEEVLT 227

                   ....
gi 1189438336 1584 PEKL 1587
Cdd:COG1121    228 EENL 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1367-1578 4.89e-12

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 66.79  E-value: 4.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRM-----------VDTFEGHIIIDGIDIAKLP 1435
Cdd:cd03235      1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTL----LKAilgllkptsgsIRVFGKPLEKERKRIGYVP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLRSRLS-IILQDPVLFSGTIRFNLDPERKCSDstlWEALEIAqLKLVvkalpgGLDAI----ITEggenFSQGQRQL 1510
Cdd:cd03235     75 QRRSIDRDFpISVRDVVLMGLYGHKGLFRRLSKAD---KAKVDEA-LERV------GLSELadrqIGE----LSGGQQQR 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD-RTVVTIAHRVHTIL-SADLVIVLKRGAI 1578
Cdd:cd03235    141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLeYFDRVLLLNRTVV 210
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
716-929 5.00e-12

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 68.01  E-value: 5.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsPERETATDLDIrkrgpvayAS 795
Cdd:cd03288     35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKL-----PLHTLRSRLSI--------IL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANVVFLD 875
Cdd:cd03288    102 QDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMD 181
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  876 DPFSALDIhLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTI 929
Cdd:cd03288    182 EATASIDM-ATENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGIL 232
cbiO PRK13640
energy-coupling factor transporter ATPase;
1366-1590 5.29e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 68.29  E-value: 5.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTL---RSR 1442
Cdd:PRK13640     6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdiREK 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDP-VLFSGT-----IRFNLDpERKCSDSTLwealeiaqLKLVVKALP--GGLDAIITEGgENFSQGQRQLFCLA 1514
Cdd:PRK13640    86 VGIVFQNPdNQFVGAtvgddVAFGLE-NRAVPRPEM--------IKIVRDVLAdvGMLDYIDSEP-ANLSGGQKQRVAIA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:PRK13640   156 GILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
cbiO PRK13645
energy-coupling factor transporter ATPase;
707-934 5.85e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 68.11  E-value: 5.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIgedPSPERETATDLDIR 786
Cdd:PRK13645    16 YAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTI---VGDYAI---PANLKKIKEVKRLR 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRGPVAYASQKPWLLNATVEENIIFeSPFN-----KQRYKMVIEACSLQPdidiLPhgdQTQIGERGINLSGGQRQRISV 861
Cdd:PRK13645    90 KEIGLVFQFPEYQLFQETIEKDIAF-GPVNlgenkQEAYKKVPELLKLVQ----LP---EDYVKRSPFELSGGQKRRVAL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK13645   162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINL-FERLNKEYKKRIIMVTHNMdQVLRIADEVIVMHEGKVISIGS 234
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
712-933 7.22e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 67.84  E-value: 7.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLL--AALGEMQKVSGAVFwsslpdseiGEDPSPERETatdlDIRKRg 789
Cdd:PRK13647    15 KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLhlNGIYLPQRGRVKVM---------GREVNAENEK----WVRSK- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 pVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRI 859
Cdd:PRK13647    81 -VGLVFQDPddQVFSSTVWDDVAF-GPVNmgldkdevERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREG 933
Cdd:PRK13647   148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLME--ILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEG 220
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
1079-1248 7.26e-12

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 67.92  E-value: 7.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAM--VFTV--LCSLGIVLCLVTSvtvewtGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID 1154
Cdd:cd18573     39 SLKTFALALlgVFVVgaAANFGRVYLLRIA------GERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVG 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1155 QHIPSTLECLSRSTLLCVSALAVISYVTP-VFLVALL---PLAIVCYFIQKYFRVASRDLQQ-LDDTTQLPllshfAETV 1229
Cdd:cd18573    113 KSLTQNLSDGLRSLVSGVGGIGMMLYISPkLTLVMLLvvpPIAVGAVFYGRYVRKLSKQVQDaLADATKVA-----EERL 187
                          170       180
                   ....*....|....*....|...
gi 1189438336 1230 EGLTTIRAF---RYE-ARFQQKL 1248
Cdd:cd18573    188 SNIRTVRAFaaeRKEvERYAKKV 210
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1366-1582 7.35e-12

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 66.39  E-value: 7.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtlRS 1441
Cdd:cd03259      1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGLERpdsgEILIDGRDVTGVPPE--RR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:cd03259     73 NIGMVFQDYALFPhltvaENIAFGLKlrgvPKAEIRARVR-ELLELVGLEGLLNRYPHEL-----------SGGQQQRVA 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMAT-ENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFD 1582
Cdd:cd03259    141 LARALAREPSLLLLDEPLSALDAKLrEELREELKeLQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
720-946 7.61e-12

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 68.59  E-value: 7.61e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperetATDLDIRKRGpVAYASQKPW 799
Cdd:PRK11432    24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-------GED-------VTHRSIQQRD-ICMVFQSYA 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 LL-NATVEENIIF-------ESPFNKQRYKmviEACSLqpdIDILPHGDQ--TQIgerginlSGGQRQRISVARALYQHA 869
Cdd:PRK11432    89 LFpHMSLGENVGYglkmlgvPKEERKQRVK---EALEL---VDLAGFEDRyvDQI-------SGGQQQRVALARALILKP 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  870 NVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLF 946
Cdd:PRK11432   156 KVLLFDEPLSNLDANLRRS-MREKIRELQQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
711-934 7.70e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 68.34  E-value: 7.70e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERETATDL------- 783
Cdd:PRK13631    35 QENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI---QVGDIYIGDKKNNHELITNPYskkiknf 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  784 -DIRKRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPD-IDILPHGdqtqigerginL 851
Cdd:PRK13631   112 kELRRR--VSMVFQFPeyQLFKDTIEKDIMF-GPVAlgvkkseaKKLAKFYLNKMGLDDSyLERSPFG-----------L 177
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagileLLRDDK---RTVVLVTHKL-QYLPHADWIIAMKDG 927
Cdd:PRK13631   178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQ-----LILDAKannKTVFVITHTMeHVLEVADEVIVMDKG 252

                   ....*..
gi 1189438336  928 TIQREGT 934
Cdd:PRK13631   253 KILKTGT 259
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1366-1584 8.27e-12

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 66.82  E-value: 8.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:cd03256      1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDpvlfsgtirFNLDPE----------RKCSDSTLW------------EALEIaqLKLVvkalpgGLDAIITEGG 1500
Cdd:cd03256     80 IGMIFQQ---------FNLIERlsvlenvlsgRLGRRSTWRslfglfpkeekqRALAA--LERV------GLLDKAYQRA 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIlqkvVMTAFAD------RTVVTIAHRVHTILS-ADLVIVL 1573
Cdd:cd03256    143 DQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ----VMDLLKRinreegITVIVSLHQVDLAREyADRIVGL 218
                          250
                   ....*....|.
gi 1189438336 1574 KRGAILeFDKP 1584
Cdd:cd03256    219 KDGRIV-FDGP 228
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1366-1580 8.28e-12

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224058 [Multi-domain]  Cd Length: 339  Bit Score: 68.43  E-value: 8.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK---PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFE-------GHIIIDGIDIAKLP 1435
Cdd:COG1135      2 IELENVSKTFGQTGTgtvTALDDVSLEIPKGEIFGIIGYSGAGKSTL----LRLINLLErptsgsvFVDGQDLTALSEAE 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLRSRLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLwEALEIAQLKLVVKALPGGLdaiiteggenfSQG 1506
Cdd:COG1135     78 LRQLRQKIGMIFQHFNLLSsrtvfENVAFPLElagvPKAEIKQRVA-ELLELVGLSDKADRYPAQL-----------SGG 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1507 QRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILE 1580
Cdd:COG1135    146 QKQRVAIARALANNPKILLCDEATSALDPEtTQSILELLKdINRELGLTIVLITHEMEVVKRiCDRVAVLDQGRLVE 222
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
1034-1336 8.83e-12

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 67.57  E-value: 8.83e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1034 LSLLVFSQLLKhmvlVAIDYWLAKWTDSALTltpaarncSLSQEcTLDQTVYAMV-FTVLCSL--GIVLCLVTSVTVewt 1110
Cdd:cd18572      2 FVFLVVAALSE----LAIPHYTGAVIDAVVA--------DGSRE-AFYRAVLLLLlLSVLSGLfsGLRGGCFSYAGT--- 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 glKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP----VFL 1186
Cdd:cd18572     66 --RLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWrltlLAF 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQ-LDDTTQLpllshfAETVEGL-TTIRAF---RYEA-RFQQKLLEYTDSN---NI 1257
Cdd:cd18572    144 ITVPVIALITKVYGRYYRKLSKEIQDaLAEANQV------AEEALSNiRTVRSFateEREArRYERALDKALKLSvrqAL 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1258 ASLFLTAANRWLevrmEYIGACVVLIAAVTSIsnsLHRELSAG-LVGLGLtYALMVSNYLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18572    218 AYAGYVAVNTLL----QNGTQVLVLFYGGHLV---LSGRMSAGqLVTFML-YQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
718-935 9.71e-12

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 66.38  E-value: 9.71e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperETATDLDIRKRgPVAYASQK 797
Cdd:PRK11629    25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKL--------SSAAKAELRNQ-KLGFIYQF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIIFESPFNKQRYKMVIEACSlqpdiDILPH-GDQTQIGERGINLSGGQRQRISVARALYQHANVVFLD 875
Cdd:PRK11629    96 HHLLpDFTALENVAMPLLIGKKKPAEINSRAL-----EMLAAvGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  876 DPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 935
Cdd:PRK11629   171 EPTGNLDARNADSIFQL-LGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELSL 229
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1381-1577 9.89e-12

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 67.57  E-value: 9.89e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1381 PVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIidgidiaklplHTlrSRLSIILQDPVLFSGTIRFN 1460
Cdd:cd03291     51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK-----------HS--GRISFSSQFSWIMPGTIKEN 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1461 L------DPERKCSdstlweALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:cd03291    118 IifgvsyDEYRYKS------VVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336 1535 MATEN-ILQKVVMTAFADRTVVTIAHRVHTILSADLVIVLKRGA 1577
Cdd:cd03291    192 VFTEKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGS 235
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
718-951 1.11e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 66.79  E-value: 1.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-----LAALGEMQKVSGAV--FWSSLPDSEIgeDPsperetatdLDIRKRGP 790
Cdd:PRK14267    20 IKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVrlFGRNIYSPDV--DP---------IEVRREVG 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLlNATVEENIIFESPFNK---------QRYKMVIEACSLQPDIdilphgdQTQIGERGINLSGGQRQRISV 861
Cdd:PRK14267    89 MVFQYPNPFP-HLTIYDNVAIGVKLNGlvkskkeldERVEWALKKAALWDEV-------KDRLNDYPSNLSGGQRQRLVI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  862 ARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKR--TVVLVTHK-LQYLPHADWIIAMKDGTIQREG-TLKD 937
Cdd:PRK14267   161 ARALAMKPKILLMDEPTANI-----DPVGTAKIEELLFELKKeyTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGpTRKV 235
                          250
                   ....*....|....
gi 1189438336  938 FQRSECQLFEHWKT 951
Cdd:PRK14267   236 FENPEHELTEKYVT 249
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
1089-1336 1.16e-11

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 67.12  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1089 FTVLCSLGIVLCLVTSV---TVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18575     39 FLLLLAVALVLALASALrfyLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSALAVISYVTP---VFLVALLPLAIV-CYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAFRY 1240
Cdd:cd18575    119 RNLLLLIGGLVMLFITSPkltLLVLLVIPLVVLpIILFGRRVRRLSRASQdRLADLS-----AFAEETLSAIKTVQAFTR 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1241 EARFQQKLLEYTDSNniaslfLTAANRWLEVRMEYIGACVVLI-AAVTSI-----SNSLHRELSAGLVGLGLTYALMVSN 1314
Cdd:cd18575    194 EDAERQRFATAVEAA------FAAALRRIRARALLTALVIFLVfGAIVFVlwlgaHDVLAGRMSAGELSQFVFYAVLAAG 267
                          250       260
                   ....*....|....*....|..
gi 1189438336 1315 YLNWMVRNLADMELQLGAVKRI 1336
Cdd:cd18575    268 SVGALSEVWGDLQRAAGAAERL 289
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
718-956 1.16e-11

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 66.70  E-value: 1.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPSPERETATdldIRK-RGPVAYASQ 796
Cdd:PRK11264    19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI---RVGDITIDTARSLSQQKGL---IRQlRQHVGFVFQ 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KPWLL-NATVEENIIfESPF---NKQRYKMVIEACSLQPDIDIlpHGDQTQIGERginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK11264    93 NFNLFpHRTVLENII-EGPVivkGEPKEEATARARELLAKVGL--AGKETSYPRR---LSGGQQQRVAIARALAMRPEVI 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  873 FLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKdfqrsecQLFEHWKT 951
Cdd:PRK11264   167 LFDEPTSALDPELVGEVLNT--IRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAK-------ALFADPQQ 237

                   ....*
gi 1189438336  952 LMNRQ 956
Cdd:PRK11264   238 PRTRQ 242
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1366-1576 1.22e-11

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224041 [Multi-domain]  Cd Length: 248  Bit Score: 66.43  E-value: 1.22e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaFFRMVDTFEGHIIIDGIDIAKlPLHTLRSRLSI 1445
Cdd:COG1116      4 LEIEGVSKSFGG--VEVLEDINLSVEKGEFVAILGPSGCGKST----LLRLIAGLEKPTSGEVLLDGR-PVTGPGPDIGY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLF-----SGTIRFNLDPERKCSDSTLW---EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAF 1517
Cdd:COG1116     77 VFQEDALLpwltvLDNVALGLELRGKSKAEARErakELLELVGLAGFEDKYPHQL-----------SGGMRQRVAIARAL 145
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1518 VRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVH-TILSADLVIVLKRG 1576
Cdd:COG1116    146 ATRPKLLLLDEPFGALDALTREELQDELLRLWEEtrKTVLLVTHDVDeAVYLADRVVVLSNR 207
FetA COG4619
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism] ...
1366-1578 1.26e-11

ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226970 [Multi-domain]  Cd Length: 223  Bit Score: 66.04  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNlsVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPlhTLRSRL 1443
Cdd:COG4619      4 LELKQ--VGYLAGDAKILNNISLSVRAGEFIAITGPSGCGKSTLlkIVASLISPTSGTLLFEGEDVSTLKPE--AYRQQV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSGTIRFNLD-PERKCSDSTLWEALeIAQLKLVvkALPgglDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:COG4619     80 SYCAQTPALFGDTVEDNLIfPWQIRNRRPDRAAA-LDLLARF--ALP---DSILTKNITELSGGEKQRIALIRNLQFMPK 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336 1523 IFIMDEATASIDMAT----ENILQKVVmtAFADRTVVTIAH-RVHTILSADLVIVLKRGAI 1578
Cdd:COG4619    154 ILLLDEITSALDESNkrniEEMIHRYV--REQNVAVLWITHdKDQAIRHADKVITLQPGHA 212
ModF COG1119
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion ...
713-935 1.34e-11

ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 224044 [Multi-domain]  Cd Length: 257  Bit Score: 66.57  E-value: 1.34e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdsEIGEdpsPERETATDLDIRKR-GPV 791
Cdd:COG1119     42 NGKKILGDLSWQVNPGEHWAIVGPNGAGKTTLLSLLTGEHPPSSGDVT-------LLGR---RFGKGETIFELRKRiGLV 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENII---FESpfnKQRYKMVIEACSLQPDIDILPHGDQTQIGERGI-NLSGGQRQRISVARALYQ 867
Cdd:COG1119    112 SSELHERFRVRETVRDVVLsgfFAS---IGIYQEDLTAEDLAAAQWLLELLGAKHLADRPFgSLSQGEQRRVLIARALVK 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQ-YLPHADWIIAMKDGTIQREGTL 935
Cdd:COG1119    189 DPELLILDEPAQGLDLIAREQLLNRLEELAASPGAPALLFVTHHAEeIPPCFTHRLLLKEGEVVAQGKL 257
cbiO PRK13637
energy-coupling factor transporter ATPase;
707-937 1.39e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 66.99  E-value: 1.39e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDldIR 786
Cdd:PRK13637    12 YMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-------GVDITDKKVKLSD--IR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 KRgpVAYASQKP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDI--DILPhgdqtqigergINLSGG 854
Cdd:PRK13637    83 KK--VGLVFQYPeyQLFEETIEKDIAF-GPINlglseeeiENRVKRAMNIVGLDYEDykDKSP-----------FELSGG 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  855 QRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:PRK13637   149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL-NKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQG 227

                   ....
gi 1189438336  934 TLKD 937
Cdd:PRK13637   228 TPRE 231
cbiO PRK13643
energy-coupling factor transporter ATPase;
711-939 1.43e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 67.07  E-value: 1.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLpdseIGEDPSPERETATdldIRKRGP 790
Cdd:PRK13643    15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDI----VVSSTSKQKEIKP---VRKKVG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLnatvEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERG-INLSGGQRQRISVARALYQHA 869
Cdd:PRK13643    88 VVFQFPESQLF----EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAMEP 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQ 939
Cdd:PRK13643   164 EVLVLDEPTAGLDPKARIEMMQ--LFESIHQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDvFQ 233
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1366-1576 1.62e-11

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 64.52  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03229      1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLlrCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRI 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSG-TIRFNLdperkcsdstlwealeiaqlklvvkALPggldaiiteggenFSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03229     79 GMVFQDFALFPHlTVLENI-------------------------ALG-------------LSGGQQQRVALARALAMDPD 120
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03229    121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1366-1576 2.13e-11

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 63.96  E-value: 2.13e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaffrmvdtfeghiiidgidiaklplhTLRSRLSI 1445
Cdd:cd03230      1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTT-----------------------------LIKIILGL 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDpvlfSGTIR-FNLDPERkcsdstlwealEIAQLKLVVKALPGGlDAIITE--GGEN--FSQGQRQLFCLARAFVRK 1520
Cdd:cd03230     50 LKPD----SGEIKvLGKDIKK-----------EPEEVKRRIGYLPEE-PSLYENltVRENlkLSGGMKQRLALAQALLHD 113
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1521 TSIFIMDEATASIDMATENILQKVVMT-AFADRTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03230    114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNG 171
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
378-610 2.28e-11

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 66.42  E-value: 2.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  378 YVAIETGINLRGAIQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYIL 456
Cdd:cd07346     61 YLAARLGQRVVFDLRRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSsGLLQLLSDVLTLIGALVILFYLN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  457 GVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWE----NIFRTRVETTRRKEMTS 532
Cdd:cd07346    139 WKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEereiERFREANRDLRDANLRA 218
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  533 LRAFAIYTSISIFMNTaipIAAVLITFVGHVSFFKEaDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKL 610
Cdd:cd07346    219 ARLSALFSPLIGLLTA---LGTALVLLYGGYLVLQG-SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ModC COG4148
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
721-950 2.50e-11

ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226628 [Multi-domain]  Cd Length: 352  Bit Score: 66.98  E-value: 2.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVFWSSLPDSEIGEDPSPERetatdldiRKrgpVAYASQKP 798
Cdd:COG4148     17 ANFTLPARGITALFGPSGSGKTSLInmIAGLTRPDEGRIELNGRVLVDAEKGIFLPPEK--------RR---IGYVFQDA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  799 WLL-NATVEENIIFESPFNKQRY-KMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARALYQHANVVFLDD 876
Cdd:COG4148     86 RLFpHYTVRGNLRYGMWKSMRAQfDQLVALLGIEHLLDRYP-----------GTLSGGEKQRVAIGRALLTAPELLLMDE 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  877 PFSALDIHLSDHLMQagILELLRDDKRT-VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD-FQRSecqLFEHWK 950
Cdd:COG4148    155 PLASLDLPRKREILP--YLERLRDEINIpILYVSHSLDEVLRlADRVVVLENGKVKASGPLEEvWGSP---DFPPWL 226
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
713-910 3.68e-11

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 64.05  E-value: 3.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEigEDPSPEREtatdldirkrgpVA 792
Cdd:cd03231     11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF--QRDSIARG------------LL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNA-TVEENIIFESPFNKQrykmviEACslqpdIDILPHGDQTQIGERGIN-LSGGQRQRISVARALYQHAN 870
Cdd:cd03231     77 YLGHAPGIKTTlSVLENLRFWHADHSD------EQV-----EEALARVGLNGFEDRPVAqLSAGQQRRVALARLLLSGRP 145
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1189438336  871 VVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:cd03231    146 LWILDEPTTALDKagvarfaeAMAGHCARGGM----------VVLTTH 183
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1280-1580 3.82e-11

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 67.42  E-value: 3.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1280 VVLIAAVTSISNSLHRELSAGLvglgltyaLMVSNYLNwMVRNLAD--MELQLGAV---KRIHGLLKTEAESY-EGLLA- 1352
Cdd:PRK15134   189 VSVQAQILQLLRELQQELNMGL--------LFITHNLS-IVRKLADrvAVMQNGRCveqNRAATLFSAPTHPYtQKLLNs 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1353 -PSLIPKNWPDQGK--IQIQNLSV---------RYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDT- 1419
Cdd:PRK15134   260 ePSGDPVPLPEPASplLDVEQLQVafpirkgilKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSq 339
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1420 ----FEGHIIIDGIDIAKLPlhtLRSRLSIILQDPvlfsgtiRFNLDPeRKCSDSTLWEALEIAQLKL--------VVKA 1487
Cdd:PRK15134   340 geiwFDGQPLHNLNRRQLLP---VRHRIQVVFQDP-------NSSLNP-RLNVLQIIEEGLRVHQPTLsaaqreqqVIAV 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1488 LPG-GLDAII-----TEggenFSQGQRQLFCLARAFVRKTSIFIMDEATASID-------MATENILQKVVMTAFadrtv 1554
Cdd:PRK15134   409 MEEvGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqaqiLALLKSLQQKHQLAY----- 479
                          330       340
                   ....*....|....*....|....*..
gi 1189438336 1555 VTIAHRVHTILS-ADLVIVLKRGAILE 1580
Cdd:PRK15134   480 LFISHDLHVVRAlCHQVIVLRQGEVVE 506
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1366-1590 4.23e-11

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 64.52  E-value: 4.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFE-------GHIIIDGIDIAKLPL 1436
Cdd:cd03258      2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGLErptsgsvLVDGTDLTLLSGKEL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 HTLRSRLSIILQDPVLFS-----GTIRFNLD---PERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1508
Cdd:cd03258     78 RKARRRIGMIFQHFNLLSsrtvfENVALPLEiagVPKAEIEERVLELLELVGLEDKADAYPAQL-----------SGGQK 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMA-TENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKP 1584
Cdd:cd03258    147 QRVGIARALANNPKVLLCDEATSALDPEtTQSILAllRDINREL-GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225

                   ....*.
gi 1189438336 1585 EKLLSR 1590
Cdd:cd03258    226 EEVFAN 231
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1366-1560 6.04e-11

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 62.56  E-value: 6.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL-PLHT------ 1438
Cdd:cd03223      1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSL----FRAL--------------AGLwPWGSgrigmp 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTIRfnldperkcsdstlwealeiaqlklvvkalpgglDAIITEGGENFSQGQRQLFCLARAFV 1518
Cdd:cd03223     62 EGEDLLFLPQRPYLPLGTLR----------------------------------EQLIYPWDDVLSGGEQQRLAFARLLL 107
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1189438336 1519 RKTSIFIMDEATASIDMATENILQKVVMTAFAdrTVVTIAHR 1560
Cdd:cd03223    108 HKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
720-933 6.76e-11

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 65.82  E-value: 6.76e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMqkVSGAVFwsslpdseIGEdpsperETATDLDIRKRGpVAYASQK 797
Cdd:PRK11000    21 DINLDIHEGEFVVFVGPSGCGKSTLLrmIAGLEDI--TSGDLF--------IGE------KRMNDVPPAERG-VGMVFQS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 ----PWLlnaTVEENIIF-------ESPFNKQRYKMVIEACSLQPDIDILPHGdqtqigerginLSGGQRQRISVARALY 866
Cdd:PRK11000    84 yalyPHL---SVAENMSFglklagaKKEEINQRVNQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREG 933
Cdd:PRK11000   150 AEPSVFLLDEPLSNLDAALRVQ-MRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1362-1590 7.93e-11

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224042 [Multi-domain]  Cd Length: 253  Bit Score: 64.10  E-value: 7.93e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1362 DQGKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTF-------EGHIIIDGIDIAKL 1434
Cdd:COG1117      4 KIPAIEVRDLNLYYGD--KHALKDINLDIPKNKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvegEVLLDGKNIYDPKV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1435 PLHTLRSRLSIILQDPVLFSGTIRFNL--DPERKCS-----DSTLWEALEIAQLKLVVKALpggLDaiitEGGENFSQGQ 1507
Cdd:COG1117     82 DVVELRRRVGMVFQKPNPFPMSIYDNVayGLRLHGIkdkelDEIVESSLKKAALWDEVKDR---LH----KSALGLSGGQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVMTAFADRTVVTIAH------RVhtilsADLVIVLKRGAILE 1580
Cdd:COG1117    155 QQRLCIARALAVKPEVLLMDEPTSALDpISTLKI-EELITELKKKYTIVIVTHnmqqaaRV-----SDYTAFFYLGELVE 228
                          250
                   ....*....|
gi 1189438336 1581 FDKPEKLLSR 1590
Cdd:COG1117    229 FGPTDKIFTN 238
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
711-911 8.33e-11

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 66.70  E-value: 8.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSlLLAALGEMQKVSGAVfwsslpdseigedpsperetatdLDIRKRGP 790
Cdd:TIGR00954  461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSS-LFRILGELWPVYGGR-----------------------LTKPAKGK 516
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNATVEENIIF-ESPFNKQRYKMvieacSLQPDIDILPHGDQTQIGERGIN----------LSGGQRQRI 859
Cdd:TIGR00954  517 LFYVPQRPYMTLGTLRDQIIYpDSSEDMKRRGL-----SDKDLEQILDNVQLTHILEREGGwsavqdwmdvLSGGEKQRI 591
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHK 911
Cdd:TIGR00954  592 AMARLFYHKPQFAILDECTSAVSVD-----VEGYMYRLCREFGITLFSVSHR 638
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
711-942 8.37e-11

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226641 [Multi-domain]  Cd Length: 534  Bit Score: 66.53  E-value: 8.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  711 TPDG-IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSgavfwSSLPDSEI---GEDpspeRETATDLDIR 786
Cdd:COG4172     18 QEGGtVEAVKGISFDIEAGETLALVGESGSGKSVTALSILGLLPSPA-----AAHPSGSIlfdGED----LLAASERQLR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 K-RGP-VAYASQKPWL-LNAT------VEENIIFESPFNKQRYKMVIEACSLQ---PD----IDILPHgdqtqigergiN 850
Cdd:COG4172     89 GvRGNkIGMIFQEPMTsLNPLhtigkqLAEVLRLHRGLSRAAARARALELLELvgiPEpekrLDAYPH-----------E 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 925
Cdd:COG4172    158 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTV-----QAQILDLLKELQAelgmAILFITHDLGIVRKfADRVYVMQ 232
                          250
                   ....*....|....*...
gi 1189438336  926 DGTIQREGTLKD-FQRSE 942
Cdd:COG4172    233 HGEIVETGTTETlFAAPQ 250
ThiQ COG3840
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];
1390-1593 9.49e-11

ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];


Pssm-ID: 226360 [Multi-domain]  Cd Length: 231  Bit Score: 63.52  E-value: 9.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1390 IAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNLDPERk 1466
Cdd:COG3840     22 VPAGEIVAILGPSGAGKSTL----LNLIAGFETPASGEILINGVDHTASPPAErpVSMLFQENNLFAHlTVAQNIGLGL- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1467 cSDSTLWEALEiaQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVM 1546
Cdd:COG3840     97 -SPGLKLNAEQ--REKVEAAAAQVGLAGFLKRLPGELSGGQRQRVALARCLVREQPILLLDEPFSALDPALRAEMLALVS 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1547 TAFADR--TVVTIAHRVHTIL-SADLVIVLKRGAILEFDKPEKLLSRKDS 1593
Cdd:COG3840    174 QLCDERkmTLLMVTHHPEDAArIADRVVFLDNGRIAAQGSTQELLSGKAS 223
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
714-942 1.22e-10

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 63.22  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPSPEretatdldIRKRGpVAY 793
Cdd:cd03219     12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVL---FDGEDITGLPPHE--------IARLG-IGR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENII----------FESPFNKQRYKMVIEACSlqpdiDILphgDQTQIGERG----INLSGGQRQR 858
Cdd:cd03219     80 TFQIPRLFpELTVLENVMvaaqartgsgLLLARARREEREARERAE-----ELL---ERVGLADLAdrpaGELSYGQQRR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:cd03219    152 LEIARALATDPKLLLLDEPAAGLNPEETEELAE--LIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDE 229

                   ....*
gi 1189438336  938 FQRSE 942
Cdd:cd03219    230 VRNNP 234
YufO COG3845
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
718-912 1.35e-10

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226364 [Multi-domain]  Cd Length: 501  Bit Score: 65.64  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpDSEIGEDPSPEretatdlDIRKRGpVAYASQK 797
Cdd:COG3845     20 NDDVSLSVKKGEIHALLGENGAGKSTLMKILFGLYQPDSGEIRV----DGKEVRIKSPR-------DAIRLG-IGMVHQH 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIIF--ESPFN-KQRYKMV---IEACSLQPDIDILPHgdqtqigERGINLSGGQRQRISVARALYQHAN 870
Cdd:COG3845     88 FMLVpTLTVAENIILglEPSKGgLIDRRQArarIKELSERYGLPVDPD-------AKVADLSVGEQQRVEILKALYRGAR 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1189438336  871 VVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL 912
Cdd:COG3845    161 LLILDEPTAVLTPQEADELFE--ILRRLAAEGKTIIFITHKL 200
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
718-924 1.47e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 64.60  E-value: 1.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLllAALGEM--QKVSGAVFWSslpdseiGED-PSPERETATDLdiRKR------ 788
Cdd:PRK11308    31 LDGVSFTLERGKTLAVVGESGCGKSTL--ARLLTMieTPTGGELYYQ-------GQDlLKADPEAQKLL--RQKiqivfq 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 GPvaYASQKP-WLLNATVEENIIFESPFNKQRYKMVIEA----CSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVA 862
Cdd:PRK11308   100 NP--YGSLNPrKKVGQILEEPLLINTSLSAAERREKALAmmakVGLRPEhYDRYPH-----------MFSGGQRQRIAIA 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK11308   167 RALMLDPDVVVADEPVSALDVSV-----QAQVLNLMMDLQQelglSYVFISHDLSVVEHiADEVMVM 228
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
715-941 1.68e-10

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226952 [Multi-domain]  Cd Length: 325  Bit Score: 64.33  E-value: 1.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEDPSPERETAtdldIRKRGPVAYA 794
Cdd:COG4586     37 IEAVQDISFEIPKGEIVGFLGANGAGKSTTLKMLTGLLLPTSGKV-------RVNGKDPFRRREEY----LRSIGLVMGQ 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWLLNATVEE----NIIFESPFNKQRYKM--VIEACSLQPdidilphgdqtQIGERGINLSGGQRQRISVARALYQH 868
Cdd:COG4586    106 KLQLWWDLPALDSlevlKLIYEIPDDEFAERLdfLTEILDLEG-----------FLKWPVRKLSLGQRMRAELAAALLHP 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  869 ANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:COG4586    175 PKVLFLDEPTVGLDV-----NAQANIREFLKEYNEerqaTVLLTTHIFDDIATlCDRVLLIDQGQLVFDGTLAQLQEQ 247
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
851-934 1.77e-10

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226961 [Multi-domain]  Cd Length: 256  Bit Score: 63.21  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:COG4598    153 LSGGQQQRVAIARALAMEPEVMLFDEPTSALDPELVGEVL--KVMQDLAEEGRTMVVVTHEMGFARDvSSHVIFLHQGKI 230

                   ....*
gi 1189438336  930 QREGT 934
Cdd:COG4598    231 EEEGP 235
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1366-1602 1.80e-10

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224050 [Multi-domain]  Cd Length: 309  Bit Score: 63.85  E-value: 1.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:COG1125      2 IEFENVSKRYGN--KKAVDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILIDGEDISDLDPVELRRKIGY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSG-TIRFN--LDPERKCsdstlWEALEIAQ-----LKLVvkalpgGLDAIitEGGENF----SQGQRQLFCL 1513
Cdd:COG1125     80 VIQQIGLFPHlTVAENiaTVPKLLG-----WDKERIKKradelLDLV------GLDPS--EYADRYphelSGGQQQRVGV 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVV--MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:COG1125    147 ARALAADPPILLMDEPFGALDPITRKQLQEEIkeLQKELGKTIVFVTHDIDEALKlADRIAVMDAGEIVQYDTPDEILAN 226
                          250
                   ....*....|...
gi 1189438336 1591 -KDSVFASFVRAD 1602
Cdd:COG1125    227 pANDFVEDFFGES 239
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
713-910 1.84e-10

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 226617 [Multi-domain]  Cd Length: 209  Bit Score: 62.31  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPEretatdldirkrgpVA 792
Cdd:COG4133     13 GERTLFSDLSFTLNAGEALQITGPNGAGKTTLLRILAGLLRPDAGEVYWQGEPIQNVRESYHQA--------------LL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLLNA-TVEENIIFESPFNKQRYKMVIEACSlqpdidilphgdqTQIGERGI------NLSGGQRQRISVARAL 865
Cdd:COG4133     79 YLGHQPGIKTElTALENLHFWQRFHGSGNAATIWEAL-------------AQVGLAGLedlpvgQLSAGQQRRVALARLW 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336  866 YQHANVVFLDDPFSALDIH--------LSDHLMQAGIlellrddkrtVVLVTH 910
Cdd:COG4133    146 LSPAPLWILDEPFTALDKEgvalltalMAAHAAQGGI----------VLLTTH 188
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1366-1590 1.96e-10

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 226927 [Multi-domain]  Cd Length: 245  Bit Score: 62.82  E-value: 1.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFeghiiidgidiaklpLHTLRSRLSI 1445
Cdd:COG4555      2 LEVTDLTKSYGSKVQAV-RDVSFEAEEGEITGLLGENGAGKTTL----LRMIATL---------------LIPDSGKVTI 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ----ILQDP--------VLFSG-------TIRFNLDPERKCSDstLWEALEIAQLKLVVKALpgGLDAIITEGGENFSQG 1506
Cdd:COG4555     62 dgvdTVRDPsfvrrkigVLFGErglyarlTARENLKYFARLNG--LSRKEIKARIAELSKRL--QLLEYLDRRVGEFSTG 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1507 QRQLFCLARAFVRKTSIFIMDEATASIDMATENILQK-VVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKP 1584
Cdd:COG4555    138 MKQKVAIARALVHDPSILVLDEPTSGLDIRTRRKFHDfIKQLKNEGRAVIFSSHIMQEVEAlCDRVIVLHKGEVVLEGSI 217

                   ....*.
gi 1189438336 1585 EKLLSR 1590
Cdd:COG4555    218 EALDAR 223
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1366-1578 3.03e-10

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 60.52  E-value: 3.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrLSI 1445
Cdd:cd03216      1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKS------------------------------TL---MKI 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 I--LQDPVlfSGTIRFNldpERKCSDSTLWEALE-----IAQLklvvkalpggldaiiteggenfSQGQRQLFCLARAFV 1518
Cdd:cd03216     46 LsgLYKPD--SGEILVD---GKEVSFASPRDARRagiamVYQL----------------------SVGERQMVEIARALA 98
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1519 RKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03216     99 RNARLLILDEPTAALTPAeVERLFK--VIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
709-912 3.12e-10

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 61.91  E-value: 3.12e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  709 TWTPDGIPTLSNITIRipRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDpsperETATDLDIRkr 788
Cdd:PRK10771     8 TWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN-------GQD-----HTTTPPSRR-- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 gPVAYASQKPWLLN-ATVEENI-------IFESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRIS 860
Cdd:PRK10771    72 -PVSMLFQENNLFShLTVAQNIglglnpgLKLNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVA 139
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  861 VARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRD--DKR--TVVLVTHKL 912
Cdd:PRK10771   140 LARCLVREQPILLLDEPFSALDPAL-----RQEMLTLVSQvcQERqlTLLMVSHSL 190
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1366-1590 3.56e-10

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224051 [Multi-domain]  Cd Length: 240  Bit Score: 62.14  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGH-----IIIDGIDIAKLPLHTLR 1440
Cdd:COG1126      3 IEIKNLSKSFGD--KEVLKGISLSVEKGEVVVIIGPSGSGKSTL----LRCLNGLEEPdsgsiTVDGEDVGDKKDILKLR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIILQDPVLFSG-TIRFN--LDPE--RKCSDStlwEALEIAQ--LKLV-----VKALPGGLdaiiteggenfSQGQR 1508
Cdd:COG1126     77 RKVGMVFQQFNLFPHlTVLENvtLAPVkvKKLSKA---EAREKALelLEKVgladkADAYPAQL-----------SGGQQ 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADRT----VVT----IAHRVhtilsADLVIVLKRGAI 1578
Cdd:COG1126    143 QRVAIARALAMDPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEGmtmiIVThemgFAREV-----ADRVIFMDQGKI 214
                          250
                   ....*....|..
gi 1189438336 1579 LEFDKPEKLLSR 1590
Cdd:COG1126    215 IEEGPPEEFFDN 226
ModF COG1119
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion ...
1366-1565 3.84e-10

ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 224044 [Multi-domain]  Cd Length: 257  Bit Score: 62.33  E-value: 3.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKLPLHT-----LR 1440
Cdd:COG1119     32 IELKNVSVRRNG--KKILGDLSWQVNPGEHWAIVGPNGAGKTTL----LSLLTGEHPPSSGDVTLLGRRFGKGetifeLR 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIIlqdpvlfSGTIRFNLDPERKCSD---------STLWEA-LEIAQLKLVVKALP-GGLDAIITEGGENFSQGQRQ 1509
Cdd:COG1119    106 KRIGLV-------SSELHERFRVRETVRDvvlsgffasIGIYQEdLTAEDLAAAQWLLElLGAKHLADRPFGSLSQGEQR 178
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1510 LFCLARAFVRKTSIFIMDEATASIDM-ATE---NILQKVVMTAFAdRTVVTIAHRVHTIL 1565
Cdd:COG1119    179 RVLIARALVKDPELLILDEPAQGLDLiAREqllNRLEELAASPGA-PALLFVTHHAEEIP 237
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
719-919 3.91e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 60.97  E-value: 3.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  719 SNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgeMQKVSGAVFWSSLPdseigedpsperetatdldIRKRGPvAYASQ 796
Cdd:PRK13538    18 SGLSFTLNAGELVQIEGPNGAGKTSLLriLAGL--ARPDAGEVLWQGEP-------------------IRRQRD-EYHQD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KPWL--LNA-----TVEENIIFespfnkqrykmvieACSLQPDIDilphGDQT-----QIGERGI------NLSGGQRQR 858
Cdd:PRK13538    76 LLYLghQPGiktelTALENLRF--------------YQRLHGPGD----DEALwealaQVGLAGFedvpvrQLSAGQQRR 137
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDI--------HLSDHLMQAGIlellrddkrtVVLVTHklQYLPHAD 919
Cdd:PRK13538   138 VALARLWLTRAPLWILDEPFTAIDKqgvarleaLLAQHAEQGGM----------VILTTH--QDLPVAS 194
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1366-1559 4.32e-10

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 59.38  E-value: 4.32e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslaffrmvdtfeghiiidgidiaklplhtlrsrLSI 1445
Cdd:cd03221      1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTL---------------------------------LKL 45
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSGTIRFNldperkcsdstlwEALEIAQLklvvkalpggldaiiteggENFSQGQRQLFCLARAFVRKTSIFI 1525
Cdd:cd03221     46 IAGELEPDEGIVTWG-------------STVKIGYF-------------------EQLSGGEKMRLALAKLLLENPNLLL 93
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1189438336 1526 MDEATASIDMAT----ENILQKvvmtaFaDRTVVTIAH 1559
Cdd:cd03221     94 LDEPTNHLDLESiealEEALKE-----Y-PGTVILVSH 125
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
713-934 4.94e-10

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 64.05  E-value: 4.94e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQKVSGAVF----------WSSLPdSEIGEdPSPE---- 776
Cdd:TIGR03269   11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvLRGMDQYEPTSGRIIyhvalcekcgYVERP-SKVGE-PCPVcggt 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  777 -RETATDL---------DIRKRgpVAYASQKPWLL--NATVEENIIfeSPFNKQRYKmviEACSLQPDIDILphgDQTQI 844
Cdd:TIGR03269   89 lEPEEVDFwnlsdklrrRIRKR--IAIMLQRTFALygDDTVLDNVL--EALEEIGYE---GKEAVGRAVDLI---EMVQL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  845 GER----GINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhLMQAGILELLRDDKRTVVLVTHKLQYLPH-AD 919
Cdd:TIGR03269  159 SHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAK-LVHNALEEAVKASGISMVLTSHWPEVIEDlSD 237
                          250
                   ....*....|....*
gi 1189438336  920 WIIAMKDGTIQREGT 934
Cdd:TIGR03269  238 KAIWLENGEIKEEGT 252
ABC_FtsE_transporter cd03292
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic ...
1366-1578 5.62e-10

ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 60.88  E-value: 5.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:cd03292      1 IEFINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQDpvlfsgtirFNLDPERKCSDSTLWeALEIAQL--KLVVKALPGGLDAIITEGGEN-----FSQGQRQLFCLAR 1515
Cdd:cd03292     80 IGVVFQD---------FRLLPDRNVYENVAF-ALEVTGVppREIRKRVPAALELVGLSHKHRalpaeLSGGEQQRVAIAR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATE----NILQK-------VVMTAFADRTVVTIAHRvhtilsadlVIVLKRGAI 1578
Cdd:cd03292    150 AIVNSPTILIADEPTGNLDPDTTweimNLLKKinkagttVVVATHAKELVDTTRHR---------VIALERGKL 214
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
718-949 6.85e-10

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 61.18  E-value: 6.85e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL-------LAALGEMQkVSGAVFwsslpdsEIGEDPSPEretatdlDIRK-RG 789
Cdd:PRK11124    18 LFDITLDCPQGETLVLLGPSGAGKSSLLrvlnlleMPRSGTLN-IAGNHF-------DFSKTPSDK-------AIRElRR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQK----PWLlnaTVEENIIfESPFN---------KQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQR 856
Cdd:PRK11124    83 NVGMVFQQynlwPHL---TVQQNLI-EAPCRvlglskdqaLARAEKLLERLRLKPYADRFP-----------LHLSGGQQ 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTL 935
Cdd:PRK11124   148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS--IIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
                          250
                   ....*....|....
gi 1189438336  936 KDFQRSECQLFEHW 949
Cdd:PRK11124   226 SCFTQPQTEAFKNY 239
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
1085-1247 7.19e-10

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 62.02  E-value: 7.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECL 1164
Cdd:cd18544     43 LALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTL 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1165 SRSTLLCVSALAVISYV----TPVFLVALLPLAIVCYFIQKYFRVASRDL-QQLDDttqlpLLSHFAETVEGLTTIRAFR 1239
Cdd:cd18544    123 IGDLLLLIGILIAMFLLnwrlALISLLVLPLLLLATYLFRKKSRKAYREVrEKLSR-----LNAFLQESISGMSVIQLFN 197

                   ....*...
gi 1189438336 1240 YEARFQQK 1247
Cdd:cd18544    198 REKREFEE 205
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
718-948 1.49e-09

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 60.47  E-value: 1.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpSPERETATDLDIR---KRGPVAYA 794
Cdd:PRK10419    28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKL----NRAQRKAFRRDIQmvfQDSISAVN 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKpwllnaTVEEnIIFE--------SPFNKQ-RYKMVIEACSLQPDI-DILPHgdqtqigergiNLSGGQRQRISVARA 864
Cdd:PRK10419   104 PRK------TVRE-IIREplrhllslDKAERLaRASEMLRAVDLDDSVlDKRPP-----------QLSGGQLQRVCLARA 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLkdfq 939
Cdd:PRK10419   166 LAVEPKLLILDEAVSNLDLVL-----QAGVIRLLKKLQQqfgtACLFITHDLRLVERfCQRVMVMDNGQIVETQPV---- 236

                   ....*....
gi 1189438336  940 rSECQLFEH 948
Cdd:PRK10419   237 -GDKLTFSS 244
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1366-1580 1.57e-09

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224059 [Multi-domain]  Cd Length: 226  Bit Score: 59.83  E-value: 1.57e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLK--PVLKHVNALIAPGQKIGICGRTGSGKS------------SFSLAFFRMVDTFEGHIIidgidi 1431
Cdd:COG1136      2 IELKNVSKIYGLGGEkvEALKDVNLEIEAGEFVAIVGPSGSGKStllnllggldkpTSGEVLINGKDLTKLSEK------ 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1432 aklPLHTLR-SRLSIILQD-PVLFSGTIRFNLD-PERKCSDSTLWEALEIAQLKLVVkalpGGLDAIITEGGENFSQGQR 1508
Cdd:COG1136     76 ---ELAKLRrKKIGFVFQNfNLLPDLTVLENVElPLLIAGKSAGRRKRAAEELLEVL----GLEDRLLKKKPSELSGGQQ 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMATEnilqKVVMTAF------ADRTVVTIAHRVHTILSADLVIVLKRGAILE 1580
Cdd:COG1136    149 QRVAIARALINNPKIILADEPTGNLDSKTA----KEVLELLrelnkeRGKTIIMVTHDPELAKYADRVIELKDGKIEE 222
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1366-1559 1.80e-09

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 62.27  E-value: 1.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfslaFFRM--------------------------VDT 1419
Cdd:COG0488      4 ITLENLSLAY--GDRPLLENVSLTLNPGERIGLVGRNGAGKST----LLKIlagelepdsgevtrpkglrvgylsqePPL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1420 FEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPERKCSDStlWEAleIAQLKLVVKALP-GGLDAIITE 1498
Cdd:COG0488     78 DPEKTVLDYVIEGFGELRELLAELEEAYALLADPDDELLAELEALLEELDG--WTL--EARAEEALLGLGfPDEDRPVSS 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1499 ggenFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT----ENILQKvvmtafADRTVVTIAH 1559
Cdd:COG0488    154 ----LSGGWRRRVALARALLEEPDLLLLDEPTNHLDLESiewlEDYLKR------YPGTVIVVSH 208
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
718-935 1.83e-09

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 58.49  E-value: 1.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAalgemqkvsgaVFWSSLPDSEIGEDPSPERETATDLDirkrgpvayasqk 797
Cdd:cd03238     11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNE-----------GLYASGKARLISFLPKFSRNKLIFID------------- 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 pwllnatveeniifespfnkqrykmvieacSLQPDIDI----LPHGDQTQigergiNLSGGQRQRISVARALYQHA-NVV 872
Cdd:cd03238     67 ------------------------------QLQFLIDVglgyLTLGQKLS------TLSGGELQRVKLASELFSEPpGTL 110
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  873 F-LDDPFSALDIHLSDHLMqaGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTL 935
Cdd:cd03238    111 FiLDEPSTGLHQQDINQLL--EVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKV 172
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
1104-1251 1.98e-09

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 60.58  E-value: 1.98e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1104 SVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTP 1183
Cdd:cd18576     57 IYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISW 136
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1184 ---VFLVALLP-LAIVCYFIQKYFRVASRDLQ-QLDDTTqlpllSHFAETVEGLTTIRAF---RYEA-RFQQKLLEY 1251
Cdd:cd18576    137 kltLLMLATVPvVVLVAVLFGRRIRKLSKKVQdELAEAN-----TIVEETLQGIRVVKAFtreDYEIeRYRKALERV 208
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
718-933 2.23e-09

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 59.13  E-value: 2.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGqLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdldIRKRgpVAYASQK 797
Cdd:cd03264     16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID-------GQDVLKQPQK-----LRRR--IGYLPQE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 P-WLLNATVEENIIF-------ESPFNKQRYKMVIEAcslqpdIDILPHGDQtQIGErginLSGGQRQRISVARALYQHA 869
Cdd:cd03264     81 FgVYPNFTVREFLDYiawlkgiPSKEVKARVDEVLEL------VNLGDRAKK-KIGS----LSGGMRRRVGIAQALVGDP 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  870 NVVFLDDPFSALD----IHLSDHLMQAGilellrdDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:cd03264    150 SILIVDEPTAGLDpeerIRFRNLLSELG-------EDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1366-1564 2.28e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 60.05  E-value: 2.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM------------VDTFEGHIIIDgidiaK 1433
Cdd:PRK14258     8 IKVNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesevrvegrVEFFNQNIYER-----R 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHTLRSRLSIILQDPVLFSGTI---------------RFNLDP--ERKCSDSTLWEalEIAQlKLVVKALpggldaii 1496
Cdd:PRK14258    81 VNLNRLRRQVSMVHPKPNLFPMSVydnvaygvkivgwrpKLEIDDivESALKDADLWD--EIKH-KIHKSAL-------- 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1497 teggeNFSQGQRQLFCLARAFVRKTSIFIMDEATASID----MATENILQKVVMTafADRTVVTIAHRVHTI 1564
Cdd:PRK14258   150 -----DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSLRLR--SELTMVIVSHNLHQV 214
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1365-1590 2.48e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 60.03  E-value: 2.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK13635     5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDP-VLFSGT-----IRFNLDpERKCSDSTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFV 1518
Cdd:PRK13635    85 MVFQNPdNQFVGAtvqddVAFGLE-NIGVPREEMVERVDQA-LRQV------GMEDFLNREPHRLSGGQKQRVAIAGVLA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1519 RKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:PRK13635   157 LQPDIIILDEATSMLDpRGRREVLETVrQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1366-1579 2.52e-09

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 58.92  E-value: 2.52e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFeghiiidgidiaklplhtLRSRL 1443
Cdd:cd03266      2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTT----LRMLAGL------------------LEPDA 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIIL-------QDPVLFSGTIRFNLDPERKCSDSTLWEALEI---------AQLKLVVKALPGGLD--AIITEGGENFSQ 1505
Cdd:cd03266     60 GFATvdgfdvvKEPAEARRRLGFVSDSTGLYDRLTARENLEYfaglyglkgDELTARLEELADRLGmeELLDRRVGGFST 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1506 GQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAIL 1579
Cdd:cd03266    140 GMRQKVAIARALVHDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVV 215
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
718-934 2.95e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 59.68  E-value: 2.95e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQ----KVSGAVFWsslpdseIGEDpsperetATDLD-IRKRGP 790
Cdd:PRK14246    26 LKDITIKIPNNSIFGIMGPSGSGKSTLLkvLNRLIEIYdskiKVDGKVLY-------FGKD-------IFQIDaIKLRKE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKP-WLLNATVEENIIFesPF------NKQRYKMVIEACSLQPDIDILPHgdqTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK14246    92 VGMVFQQPnPFPHLSIYDNIAY--PLkshgikEKREIKKIVEECLRKVGLWKEVY---DRLNSPASQLSGGQQQRLTIAR 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  864 ALYQHANVVFLDDPFSALDIhLSDHLMQAGILELlrDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGT 934
Cdd:PRK14246   167 ALALKPKVLLMDEPTSMIDI-VNSQAIEKLITEL--KNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
1112-1248 2.96e-09

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 60.15  E-value: 2.96e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1112 LKVAKRLHRSLL----NRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPST-LECLSRSTLLCVSALAVISYVTPVFL 1186
Cdd:cd18570     67 LKLSQKLDIRLIlgyfKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTtISLFLDLLMVIISGIILFFYNWKLFL 145
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336 1187 VALLPL---AIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAFRYEARFQQKL 1248
Cdd:cd18570    146 ITLLIIplyILIILLFNKPFKKKNREVMESNAELN----SYLIESLKGIETIKSLNAEEQFLKKI 206
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
718-924 3.04e-09

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 58.81  E-value: 3.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSL---LLAALGEMQKVSGavfWSSLPDSEIGEDPSPERETATDLdirkrGPVAYA 794
Cdd:cd03270     11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdTIYAEGQRRYVES---LSAYARQFLGQMDKPDVDSIEGL-----SPAIAI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWLLN-----ATVEE-----NIIFESPFNKQRYKMVIEacslqpdidilphgdqtqIG------ERGIN-LSGGQRQ 857
Cdd:cd03270     83 DQKTTSRNprstvGTVTEiydylRLLFARVGIRERLGFLVD------------------VGlgyltlSRSAPtLSGGEAQ 144
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  858 RISVARALyqHANVV----FLDDPFSALdiHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:cd03270    145 RIRLATQI--GSGLTgvlyVLDEPSIGL--HPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDI 211
cbiO PRK13649
energy-coupling factor transporter ATPase;
707-942 3.22e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 59.76  E-value: 3.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  707 YFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgedpspeRETATDLDIR 786
Cdd:PRK13649    12 YQAGTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSV---RVDDTLI-------TSTSKNKDIK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 K-RGPVAYASQKPWllNATVEENIIFESPFNKQRYKM-VIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARA 864
Cdd:PRK13649    82 QiRKKVGLVFQFPE--SQLFEETVLKDVAFGPQNFGVsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13649   160 LAMEPKILVLDEPTAGLDPKGRKELMT--LFKKLHQSGMTIVLVTHLMDDVAnYADFVYVLEKGKLVLSGKPKDiFQDVD 237
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
718-937 3.73e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 59.43  E-value: 3.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedpsperETATDLDIRK-RGPVAYASQ 796
Cdd:PRK13652    20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--------------EPITKENIREvRKFVGLVFQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KP--WLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQRQRISVARALY 866
Cdd:PRK13652    86 NPddQIFSPTVEQDIAF-GPINlgldeetvAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIA 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMqAGILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13652   154 MEPQVLVLDEPTAGLDPQGVKELI-DFLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEE 224
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1366-1591 3.79e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 61.41  E-value: 3.79e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY---DSSLKPVLKHVNAL------IAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP- 1435
Cdd:PRK10261   314 LQVRNLVTRFplrSGLLNRVTREVHAVekvsfdLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 --LHTLRSRLSIILQDPVLfsgtirfNLDPERKCSDSTLwEALEIAQLkLVVKALPGGLDAIITEGG----------ENF 1503
Cdd:PRK10261   394 gkLQALRRDIQFIFQDPYA-------SLDPRQTVGDSIM-EPLRVHGL-LPGKAAAARVAWLLERVGllpehawrypHEF 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NI---LQKVVMTAFA----DRTVVT-IAHRVHTILSADLVI 1571
Cdd:PRK10261   465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRgqiiNLlldLQRDFGIAYLfishDMAVVErISHRVAVMYLGQIVE 544
                          250       260
                   ....*....|....*....|
gi 1189438336 1572 VLKRGAIleFDKPEKLLSRK 1591
Cdd:PRK10261   545 IGPRRAV--FENPQHPYTRK 562
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
718-934 3.80e-09

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 59.17  E-value: 3.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSL----LLAAL-----------GEMQKVSGAVFWSSLPD---SEIGEDPSPERET 779
Cdd:cd03271     11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtLYPALarrlhlkkeqpGNHDRIEGLEHIDKVIVidqSPIGRTPRSNPAT 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  780 ATDL--DIR---------KRgpvaYASQKpwL------------LNATVEENIIFESPFNKQRYKmvieacsLQPDIDIl 836
Cdd:cd03271     91 YTGVfdEIRelfcevckgKR----YNRET--LevrykgksiadvLDMTVEEALEFFENIPKIARK-------LQTLCDV- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  837 phG-DQTQIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTH 910
Cdd:cd03271    157 --GlGYIKLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGL--HFHDvkKLLE--VLQRLVDKGNTVVVIEH 230
                          250       260       270
                   ....*....|....*....|....*....|
gi 1189438336  911 KLQYLPHADWIIAM------KDGTIQREGT 934
Cdd:cd03271    231 NLDVIKCADWIIDLgpeggdGGGQVVASGT 260
cbiO PRK13642
energy-coupling factor transporter ATPase;
718-942 4.60e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 59.34  E-value: 4.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigeDPSPERETATDL-DIRKRGPVAYASQ 796
Cdd:PRK13642    23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKV------------KIDGELLTAENVwNLRRKIGMVFQNP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 KPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK13642    91 DNQFVGATVEDDVAFgmenQGIPREEMIKRVDEALLAVNMLDF-----KTREPAR---LSGGQKQRVAVAGIIALRPEII 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  873 FLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13642   163 ILDESTSMLDPTGRQEIMRV-IHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSElFATSE 232
cbiO PRK13650
energy-coupling factor transporter ATPase;
716-942 4.80e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 59.36  E-value: 4.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEretaTDLDIRKRGPVAYAS 795
Cdd:PRK13650    21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-------GDLLTEE----NVWDIRHKIGMVFQN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIIF----ESPFNKQRYKMVIEACSLQPDIDIlphgdQTQIGERginLSGGQRQRISVARALYQHANV 871
Cdd:PRK13650    90 PDNQFVGATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDF-----KEREPAR---LSGGQKQRVAIAGAVAMRPKI 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  872 VFLDDPFSALDihlsdhlmQAGILELLRDDKR-------TVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKD-FQRSE 942
Cdd:PRK13650   162 IILDEATSMLD--------PEGRLELIKTIKGirddyqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRElFSRGN 232
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
714-933 4.84e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 60.70  E-value: 4.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEDPSPERETATDLDirkrGPVAY 793
Cdd:PRK11288    16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL--------IDGQEMRFASTTAALA----AGVAI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENII---FESPFNKQRYKMVIEACSLQPD---IDILPhgdQTQIGErginLSGGQRQRISVARALY 866
Cdd:PRK11288    84 IYQELHLVpEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEhlgVDIDP---DTPLKY----LSIGQRQMVEIAKALA 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLqylphaDWIIAMKDG-TIQREG 933
Cdd:PRK11288   157 RNARVIAFDEPTSSLSAREIEQLFR--VIRELRAEGRVILYVSHRM------EEIFALCDAiTVFKDG 216
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
713-934 4.90e-09

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 58.15  E-value: 4.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQKVSGAVFwsslpdseiGEDPSpeRETAtdlDIRKRgp 790
Cdd:cd03265     11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTikMLTTLLKPTSGRATVA---------GHDVV--REPR---EVRRR-- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLLNA-TVEENI-IFESPFN------KQRYKMVIEAcslqpdIDILPHGDqtqigERGINLSGGQRQRISVA 862
Cdd:cd03265     75 IGIVFQDLSVDDElTGWENLyIHARLYGvpgaerRERIDELLDF------VGLLEAAD-----RLVKTYSGGMRRRLEIA 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHklqYLPHA----DWIIAMKDGTIQREGT 934
Cdd:cd03265    144 RSLVHRPEVLFLDEPTIGLDPQTRAHVWEY-IEKLKEEFGMTILLTTH---YMEEAeqlcDRVAIIDHGRIIAEGT 215
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1366-1578 5.49e-09

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 57.92  E-value: 5.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03262      1 IEIKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDpvlfsgtirFNLDPE--------------RKCSDStlwEALEIAQ--LKLVvkalpgGLDAIITEGGENFSQGQ 1507
Cdd:cd03262     79 GMVFQQ---------FNLFPHltvlenitlapikvKGMSKA---EAEERALelLEKV------GLADKADAYPAQLSGGQ 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASID--MATEnILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03262    141 QQRVAIARALAMNPKVMLFDEPTSALDpeLVGE-VLD--VMKDLAEEgmTMVVVTHEMGFAREvADRVIFMDDGRI 213
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
714-940 6.36e-09

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223488 [Multi-domain]  Cd Length: 250  Bit Score: 58.35  E-value: 6.36e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETAtdldIRKRGpVAY 793
Cdd:COG0411     16 GLTAVNDVSLEVRPGEIVGLIGPNGAGKTTLFNLITGFYKPSSGTVIFR-------GRDITGLPPHR----IARLG-IAR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENII--------FESPFNKQRYKM-----------VIEACSLQPDIDilphgdqtqigERGINLSG 853
Cdd:COG0411     84 TFQITRLFpGLTVLENVAvgaharlgLSGLLGRPRARKeerearerareLLEFVGLGELAD-----------RPAGNLSY 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  854 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL----QYlphADWIIAMKDGTI 929
Cdd:COG0411    153 GQQRRLEIARALATQPKLLLLDEPAAGLNPEETEELAEL-IRELRDRGGVTILLIEHDMklvmGL---ADRIVVLNYGEV 228
                          250
                   ....*....|.
gi 1189438336  930 QREGTLKDFQR 940
Cdd:COG0411    229 IAEGTPEEVRN 239
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1385-1578 6.81e-09

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 57.50  E-value: 6.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1385 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKLPLHTLRSR--LSIILQDPVLFSG-TIRFNL 1461
Cdd:cd03298     16 HFDLTFAQGEITAIVGPSGSGKSTL----LNLIAGFETPQSGRVLINGVDVTAAPPADrpVSMLFQENNLFAHlTVEQNV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1462 DPERkcsdSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENIL 1541
Cdd:cd03298     92 GLGL----SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1189438336 1542 QKVVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:cd03298    168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
713-882 1.05e-08

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 56.89  E-value: 1.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLA---ALGEMQKVSGAVFWSSLPDSEIGEdpsperetatdldiRKRG 789
Cdd:cd03233     18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAlanRTEGNVSVEGDIHYNGIPYKEFAE--------------KYPG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQK----PWLlnaTVEENIIFespfnkqrykmvieACSLQpdidilphGDQTQigeRGInlSGGQRQRISVARAL 865
Cdd:cd03233     84 EIIYVSEEdvhfPTL---TVRETLDF--------------ALRCK--------GNEFV---RGI--SGGERKRVSIAEAL 133
                          170
                   ....*....|....*..
gi 1189438336  866 YQHANVVFLDDPFSALD 882
Cdd:cd03233    134 VSRASVLCWDNSTRGLD 150
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1366-1591 1.08e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 57.93  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------- 1438
Cdd:PRK14267     5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSpdvdpie 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSG-TIRFNLDPERKCSD--STLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK14267    83 VRREVGMVFQYPNPFPHlTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQRLVIAR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHR-VHTILSADLVIVLKRGAILE-------FDKPEKL 1587
Cdd:PRK14267   163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEvgptrkvFENPEHE 242

                   ....
gi 1189438336 1588 LSRK 1591
Cdd:PRK14267   243 LTEK 246
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
713-928 1.35e-08

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 55.15  E-value: 1.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpdseigedpsperetatdldirkRGPVA 792
Cdd:cd03221     11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------------------TVKIG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQkpwllnatveeniifespfnkqrykmvieacslqpdidilphgdqtqigerginLSGGQRQRISVARALYQHANVV 872
Cdd:cd03221     67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  873 FLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGT 928
Cdd:cd03221     93 LLDEPTNHLDLESIEALEEA-----LKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1366-1578 1.38e-08

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 56.73  E-value: 1.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY--DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhTLrsrL 1443
Cdd:cd03255      1 IELKNLSKTYggGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS------------------------------TL---L 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SII--LQDPVlfSGTIRFNLDPERKCSDSTLWE--------------------ALEIAQLKLVVKALPG----------- 1490
Cdd:cd03255     48 NILggLDRPT--SGEVRVDGTDISKLSEKELAAfrrrhigfvfqsfnllpdltALENVELPLLLAGVPKkerreraeell 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1491 ---GLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKvvMTAFADRTVVTIAHRvHT 1563
Cdd:cd03255    126 ervGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGkevmELLRE--LNKEAGTTIVVVTHD-PE 202
                          250
                   ....*....|....*.
gi 1189438336 1564 ILS-ADLVIVLKRGAI 1578
Cdd:cd03255    203 LAEyADRIIELRDGKI 218
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1370-1576 1.75e-08

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 56.02  E-value: 1.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1370 NLSVRYDSSL----KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVdtfEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:cd03213      8 NLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLlnALAGRRTG---LGVSGEVLINGRPLDKRSFRKII 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFsgtirfnldperkcSDSTLWEALEI-AQLKlvvkalpgGLdaiiteggenfSQGQRQLFCLARAFVRKTS 1522
Cdd:cd03213     85 GYVPQDDILH--------------PTLTVRETLMFaAKLR--------GL-----------SGGERKRVSIALELVSNPS 131
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1523 IFIMDEATASIDMATENILQKVVMtAFAD--RTVVTIAHRVHTIL--SADLVIVLKRG 1576
Cdd:cd03213    132 LLFLDEPTSGLDSSSALQVMSLLR-RLADtgRTIICSIHQPSSEIfeLFDKLLLLSQG 188
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
718-934 1.78e-08

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 58.51  E-value: 1.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIgedpsperetaTDLDIR--KRGPVAYAS 795
Cdd:PRK10070    44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKI-----------SDAELRevRRKKIAMVF 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLL-NATVEENIIFESPFN----KQRYKMVIEACSlQPDIDILPHGDQTQigerginLSGGQRQRISVARALYQHAN 870
Cdd:PRK10070   113 QSFALMpHMTVLDNTAFGMELAginaEERREKALDALR-QVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPD 184
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  871 VVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK10070   185 ILLMDEAFSALDPLIRTE-MQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGT 248
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
715-932 1.86e-08

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 56.71  E-value: 1.86e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVFWSSLPDSEIGEDPSPEretatdldIRKRGpVA 792
Cdd:PRK10584    23 LSILTGVELVVKRGETIALIGESGSGKSTLLaiLAGLDDGS--SGEVSLVGQPLHQMDEEARAK--------LRAKH-VG 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWL---LNATveENIIFESPFNKQRykmviEACSLQPDIDILphgDQTQIGER----GINLSGGQRQRISVARAL 865
Cdd:PRK10584    92 FVFQSFMLiptLNAL--ENVELPALLRGES-----SRQSRNGAKALL---EQLGLGKRldhlPAQLSGGEQQRVALARAF 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  866 YQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:PRK10584   162 NGRPDVLFADEPTGNLDRQTGDKIADL-LFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
852-929 2.34e-08

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 56.86  E-value: 2.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKRT----VVLVTHKL---QYLPHAdwIIAM 924
Cdd:PRK11701   153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRElglaVVIVTHDLavaRLLAHR--LLVM 225

                   ....*
gi 1189438336  925 KDGTI 929
Cdd:PRK11701   226 KQGRV 230
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1366-1603 2.40e-08

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 56.54  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:cd03295      1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSG-TIRFN--LDPerkcsdsTL--WEALEIAQ-----LKLVvkalpgGLDaiITEGGENF----SQGQRQLF 1511
Cdd:cd03295     80 VIQQIGLFPHmTVEENiaLVP-------KLlkWPKEKIREradelLALV------GLD--PAEFADRYphelSGGQQQRV 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASIDMATENILQKvvmtAFAD------RTVVTIAHRV-HTILSADLVIVLKRGAILEFDKP 1584
Cdd:cd03295    145 GVARALAADPPLLLMDEPFGALDPITRDQLQE----EFKRlqqelgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTP 220
                          250       260
                   ....*....|....*....|
gi 1189438336 1585 EKLLSRKDSVF-ASFVRADK 1603
Cdd:cd03295    221 DEILRSPANDFvAEFVGADR 240
cbiO PRK13641
energy-coupling factor transporter ATPase;
718-937 2.42e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 57.15  E-value: 2.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQK 797
Cdd:PRK13641    23 LDNISFELEEGSFVALVGHTGSGKSTL-------MQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNATVEENIIFeSPFN--------KQRYKMVIEACSLQPDIdilphgdqtqIGERGINLSGGQRQRISVARALYQHA 869
Cdd:PRK13641    96 AQLFENTVLKDVEF-GPKNfgfsedeaKEKALKWLKKVGLSEDL----------ISKSPFELSGGQMRRVAIAGVMAYEP 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMQagileLLRDDKR---TVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKD 937
Cdd:PRK13641   165 EILCLDEPAAGLDPEGRKEMMQ-----LFKDYQKaghTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKE 231
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
716-933 3.16e-08

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 56.25  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALGEMQkvSGAVfwssLPDSEIGEDPSperetATDLDIRKRGPVAY 793
Cdd:PRK09493    15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrcINKLEEIT--SGDL----IVDGLKVNDPK-----VDERLIRQEAGMVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 asQKPWLL-NATVEENIIFeSPFnkqRYKMVIEACSLQPDIDILphgDQTQIGERG----INLSGGQRQRISVARALYQH 868
Cdd:PRK09493    84 --QQFYLFpHLTALENVMF-GPL---RVRGASKEEAEKQARELL---AKVGLAERAhhypSELSGGQQQRVAIARALAVK 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  869 ANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:PRK09493   155 PKLMLFDEPTSALDPELRHEVLK--VMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDG 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1366-1594 3.16e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 56.68  E-value: 3.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13648     8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPV-LFSGTI-----RFNLDPErkcsdstlweALEIAQLKLVVKALPGGLDAIITEGGE--NFSQGQRQLFCLARAF 1517
Cdd:PRK13648    88 VFQNPDnQFVGSIvkydvAFGLENH----------AVPYDEMHRRVSEALKQVDMLERADYEpnALSGGQKQRVAIAGVL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1518 VRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PRK13648   158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
716-882 3.24e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 56.55  E-value: 3.24e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperetatdLDIRKRGPVAYAS 795
Cdd:PRK13638    15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-----------------LDYSKRGLLALRQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKpwllnATVeeniiFESPfNKQRYKMVIE---ACSLQ----PDIDILPHGDQ--TQIGERGIN------LSGGQRQRIS 860
Cdd:PRK13638    78 QV-----ATV-----FQDP-EQQIFYTDIDsdiAFSLRnlgvPEAEITRRVDEalTLVDAQHFRhqpiqcLSHGQKKRVA 146
                          170       180
                   ....*....|....*....|..
gi 1189438336  861 VARALYQHANVVFLDDPFSALD 882
Cdd:PRK13638   147 IAGALVLQARYLLLDEPTAGLD 168
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
718-942 3.36e-08

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 56.33  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlAALGEMQKVSGAvfwsslpdsEIGEDPSPERETATDLDIRKrgpVAYASQK 797
Cdd:PRK10575    27 LHPLSLTFPAGKVTGLIGHNGSGKSTLL-KMLGRHQPPSEG---------EILLDAQPLESWSSKAFARK---VAYLPQQ 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 -PWLLNATVEENI-IFESP-------FNKQRYKMVIEACSLqpdIDILPhgdqtqIGERGIN-LSGGQRQRISVARALYQ 867
Cdd:PRK10575    94 lPAAEGMTVRELVaIGRYPwhgalgrFGAADREKVEEAISL---VGLKP------LAHRLVDsLSGGERQRAWIAMLVAQ 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  868 HANVVFLDDPFSALDI-HLSDHLmqAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREGTLKDFQRSE 942
Cdd:PRK10575   165 DSRCLLLDEPTSALDIaHQVDVL--ALVHRLSQERGLTVIAVLHDINMAArYCDYLVALRGGEMIAQGTPAELMRGE 239
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1366-1588 3.40e-08

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 223521 [Multi-domain]  Cd Length: 316  Bit Score: 57.20  E-value: 3.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPV--LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGID-----IAKLP--- 1435
Cdd:COG0444      2 LEVKNLSVSFPTDAGVVkaVDGVSFELKKGEILGIVGESGSGKSVLAKAIMGLLPKPNARIVGGEILfdgkdLLSLSeke 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 LHTLR-SRLSIILQDPvLFSgtirfnLDPERKCSDsTLWEALEI-------AQLKLVVKALpggLDAI-ITEGGE----- 1501
Cdd:COG0444     82 LRKIRgKEIAMIFQDP-MTS------LNPVMTIGD-QIAEVLRLhgkglskKEAKERAIEL---LELVgIPDPERrlksy 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1502 --NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMatenILQKVVMTAFAD------RTVVTIAHRVHTILS-ADLVIV 1572
Cdd:COG0444    151 phELSGGMRQRVMIAMALALNPKLLIADEPTTALDV----TVQAQILDLLKElqrekgTALILITHDLGVVAEiADRVAV 226
                          250
                   ....*....|....*.
gi 1189438336 1573 LKRGAILEFDKPEKLL 1588
Cdd:COG0444    227 MYAGRIVEEGPVEEIF 242
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
715-913 3.52e-08

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 56.19  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEDPSPEREtatdlDIRKRGPVAYA 794
Cdd:cd03267     34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-------RVAGLVPWKRRK-----KFLRRIGVVFG 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 --SQKPWLLNATVEENI---IFESPfnKQRYKMVIEACSlqpdiDILPHGDQTQIGERgiNLSGGQRQRISVARALYQHA 869
Cdd:cd03267    102 qkTQLWWDLPVIDSFYLlaaIYDLP--PARFKKRLDELS-----ELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEP 172
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  870 NVVFLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:cd03267    173 EILFLDEPTIGLDVV-AQENIRNFLKEYNRERGTTVLLTSHYMK 215
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
713-927 6.07e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 57.25  E-value: 6.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKVSGAVFWSSLPDSEIGEDPSPERETatdlDIR--KRGP 790
Cdd:PRK13549    16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLM--------KVLSGVYPHGTYEGEIIFEGEELQAS----NIRdtERAG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  791 VAYASQKPWLL-NATVEENIIFES---PFNKQRY-KMVIEACSL--QPDIDILPHgdqTQIGergiNLSGGQRQRISVAR 863
Cdd:PRK13549    84 IAIIHQELALVkELSVLENIFLGNeitPGGIMDYdAMYLRAQKLlaQLKLDINPA---TPVG----NLGLGQQQLVEIAK 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLSDHLmqagiLELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:PRK13549   157 ALNKQARLLILDEPTASLTESETAVL-----LDIIRDLKAhgiACIYISHKLNEVKAiSDTICVIRDG 219
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
714-942 6.28e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.98  E-value: 6.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLllaalgeMQKVSGAVfwssLPDS---EIGEDP----SPERetATDLDIr 786
Cdd:PRK15439    23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTL-------MKIIAGIV----PPDSgtlEIGGNPcarlTPAK--AHQLGI- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  787 krgpvaY-ASQKPWLL-NATVEENIIFESPFNKQRYKMVIE-----ACSLQPDIdilphgdqtQIGergiNLSGGQRQRI 859
Cdd:PRK15439    89 ------YlVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQllaalGCQLDLDS---------SAG----SLEVADRQIV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:PRK15439   150 EILRGLMRDSRILILDEPTASLTPAETERLFSR--IRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227

                   ....
gi 1189438336  939 QRSE 942
Cdd:PRK15439   228 STDD 231
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1366-1590 6.95e-08

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 57.12  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFsLAFFRMVDTFEGHIIIDGIDIAKLP---------- 1435
Cdd:TIGR03269    1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVL-MHVLRGMDQYEPTSGRIIYHVALCEkcgyverpsk 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1436 --------------------------LHTLRSRLSIILQDPvlfsgtirFNLDPERKCSDSTLwEALEIAQLKlVVKALP 1489
Cdd:TIGR03269   78 vgepcpvcggtlepeevdfwnlsdklRRRIRKRIAIMLQRT--------FALYGDDTVLDNVL-EALEEIGYE-GKEAVG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1490 GGLDAI--------ITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAH 1559
Cdd:TIGR03269  148 RAVDLIemvqlshrITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSH 227
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1189438336 1560 RVHTILS-ADLVIVLKRGAILEFDKPEKLLSR 1590
Cdd:TIGR03269  228 WPEVIEDlSDKAIWLENGEIKEEGTPDEVVAV 259
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
1366-1586 6.95e-08

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 224026 [Multi-domain]  Cd Length: 263  Bit Score: 55.41  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDiaKLPLHTLR 1440
Cdd:COG1101      2 ISLSNATKTFFKGTpleKRALNGLSLEIAEGDFVTVIGSNGAGKSTLlnAIAGDLKPTSGQILIDGVDVT--KKSVAKRA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIILQDPVlfsgtirfnldpERKCSDSTLWEALEIAQL-------------------KLVVKALPGGLDAIITEGGE 1501
Cdd:COG1101     80 NLLARVFQDPL------------AGTAPELTIEENLALAESrgkkrglssalnerrrssfRERLARLGLGLENRLSDRIG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1502 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRV-HTILSADLVIVLKRGAI 1578
Cdd:COG1101    148 LLSGGQRQALSLLMATLHPPKILLLDEHTAALDPKTAEFVMELTAKIVEEHklTTLMVTHNMeDALDYGNRLIMLHSGKI 227

                   ....*....
gi 1189438336 1579 -LEFDKPEK 1586
Cdd:COG1101    228 vLDVTGEEK 236
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
1113-1247 8.32e-08

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 55.49  E-value: 8.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1113 KVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-LVALL- 1190
Cdd:cd18547     75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLtLIVLVt 154
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1191 -PLAIVC-YFI----QKYFRVASRDLQQLDdttqlpllSHFAETVEGLTTIRAFRYEARFQQK 1247
Cdd:cd18547    155 vPLSLLVtKFIakrsQKYFRKQQKALGELN--------GYIEEMISGQKVVKAFNREEEAIEE 209
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
851-934 8.39e-08

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223256 [Multi-domain]  Cd Length: 935  Bit Score: 57.21  E-value: 8.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAM- 924
Cdd:COG0178    823 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGL--HFDDikKLLE--VLHRLVDKGNTVIVIEHNLDVIKTADWIIDLg 898
                           90
                   ....*....|....*
gi 1189438336  925 -----KDGTIQREGT 934
Cdd:COG0178    899 peggdGGGEIVASGT 913
PhnK COG4107
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and ...
840-933 8.92e-08

ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226592 [Multi-domain]  Cd Length: 258  Bit Score: 55.14  E-value: 8.92e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  840 DQTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYL 915
Cdd:COG4107    141 DLDRIDDLPRTFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSV-----QARLLDLLRGLVRelglAVVIVTHDLAVA 215
                           90
                   ....*....|....*....
gi 1189438336  916 P-HADWIIAMKDGTIQREG 933
Cdd:COG4107    216 RlLADRLMVMKQGQVVESG 234
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
701-939 9.34e-08

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 55.16  E-value: 9.34e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  701 VQIMGGYFTWTPDGIptLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGED-PSPERET 779
Cdd:PRK11831     8 VDMRGVSFTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFD-------GENiPAMSRSR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  780 AtdLDIRKRGPVAYASqKPWLLNATVEENIIF--------ESPFNKQRYKMVIEACSLQPDIDILPHgdqtqigergiNL 851
Cdd:PRK11831    79 L--YTVRKRMSMLFQS-GALFTDMNVFDNVAYplrehtqlPAPLLHSTVMMKLEAVGLRGAAKLMPS-----------EL 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALD-------IHLSDHLMQA-GIlellrddkrTVVLVTHKL-QYLPHAD--W 920
Cdd:PRK11831   145 SGGMARRAALARAIALEPDLIMFDEPFVGQDpitmgvlVKLISELNSAlGV---------TCVVVSHDVpEVLSIADhaY 215
                          250
                   ....*....|....*....
gi 1189438336  921 IIAmkDGTIQREGTLKDFQ 939
Cdd:PRK11831   216 IVA--DKKIVAHGSAQALQ 232
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1366-1581 1.10e-07

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 54.12  E-value: 1.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQkIGICGRTGSGKSSFslafFRMVDTF----EGHIIIDGIDIAKLPlHTLRS 1441
Cdd:cd03264      1 LQLENLTKRYGK--KRALDGVSLTLGPGM-YGLLGPNGAGKTTL----MRILATLtppsSGTIRIDGQDVLKQP-QKLRR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFSG-TIRFNLD--------PERKCsDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:cd03264     73 RIGYLPQEFGVYPNfTVREFLDyiawlkgiPSKEV-KARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVG 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1513 LARAFVRKTSIFIMDEATASID----MATENILQKVVmtafADRTVVTIAHRVHTILS-ADLVIVLKRGAILEF 1581
Cdd:cd03264    141 IAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELG----EDRIVILSTHIVEDVESlCNQVAVLNKGKLVFE 210
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
713-927 1.11e-07

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 56.37  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqKVSGAVFWSSLPDSEIGEDPSPERetATDLDIRKRGPVA 792
Cdd:TIGR02633   12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLM--------KILSGVYPHGTWDGEIYWSGSPLK--ASNIRDTERAGIV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPWLL-NATVEENIIFES----PFNKQRYKMVIEACS---LQPDIDILPhgDQTQIGERGinlsGGQRQRISVARA 864
Cdd:TIGR02633   82 IIHQELTLVpELSVAENIFLGNeitlPGGRMAYNAMYLRAKnllRELQLDADN--VTRPVGDYG----GGQQQLVEIAKA 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  865 LYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:TIGR02633  156 LNKQARLLILDEPSSSLTEKETE-----ILLDIIRDLKAhgvACVYISHKLNEVKAvCDTICVIRDG 217
cbiO PRK13650
energy-coupling factor transporter ATPase;
1366-1592 1.27e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 55.12  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDS-SLKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVD-TFEGHIIIDGIDIAKLPLHT---LR 1440
Cdd:PRK13650     5 IEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTT----VRLIDgLLEAESGQIIIDGDLLTEENvwdIR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIILQDP-VLFSGT-----IRFNLDP---ERKCSDSTLWEALEIAqlklvvkalpgGLDAIITEGGENFSQGQRQLF 1511
Cdd:PRK13650    81 HKIGMVFQNPdNQFVGAtveddVAFGLENkgiPHEEMKERVNEALELV-----------GMQDFKEREPARLSGGQKQRV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASID--------MATENILQKVVMTafadrtVVTIAHRVHTILSADLVIVLKRGAILEFDK 1583
Cdd:PRK13650   150 AIAGAVAMRPKIIILDEATSMLDpegrleliKTIKGIRDDYQMT------VISITHDLDEVALSDRVLVMKNGQVESTST 223

                   ....*....
gi 1189438336 1584 PEKLLSRKD 1592
Cdd:PRK13650   224 PRELFSRGN 232
hmuV PRK13547
heme ABC transporter ATP-binding protein;
718-942 1.41e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 54.83  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQ--------KVSGAVFWSSLPDSEIgedpsPERETAtdldiRKRG 789
Cdd:PRK13547    17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAI-----DAPRLA-----RLRA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  790 PVAYASQKPWLLnaTVEENIIFespfnkQRYKMVIEACSL-QPDIDILPH-----GDQTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK13547    87 VLPQAAQPAFAF--SAREIVLL------GRYPHARRAGALtHRDGEIAWQalalaGATALVGRDVTTLSGGELARVQFAR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  864 ALYQ----HANVV-----FLDDPFSALDIHlSDHLMQAGILELLRDDKRTVVLVTHKLQYLP-HADWIIAMKDGTIQREG 933
Cdd:PRK13547   159 VLAQlwppHDAAQpprylLLDEPTAALDLA-HQHRLLDTVRRLARDWNLGVLAIVHDPNLAArHADRIAMLADGAIVAHG 237

                   ....*....
gi 1189438336  934 TLKDFQRSE 942
Cdd:PRK13547   238 APADVLTPA 246
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
725-921 1.58e-07

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 54.29  E-value: 1.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  725 IPR-GQLTMIVGQVGCGKSSLLLAALGEMQ----KVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGPVAYASQKPW 799
Cdd:cd03236     22 VPReGQVLGLVGPNGIGKSTALKILAGKLKpnlgKFDDPPDWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPK 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 LLNATVEENIIFESPFNKQRYkmVIEACSLQPdidilphgdqtqIGERGI-NLSGGQRQRISVARALYQHANVVFLDDPF 878
Cdd:cd03236    102 AVKGKVGELLKKKDERGKLDE--LVDQLELRH------------VLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPS 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  879 SALDIHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLPH-ADWI 921
Cdd:cd03236    168 SYLDIK--QRLNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYI 209
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
850-979 1.65e-07

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 55.19  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  850 NLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAM 924
Cdd:PRK11153   140 QLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR-----SILELLKDINRelglTIVLITHEMDVVKRiCDRVAVI 214
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  925 KDGTIQREGTLKDfqrsecqLFEHWKTLMNRQ------DQELEkETVTERKATEPPQGLSR 979
Cdd:PRK11153   215 DAGRLVEQGTVSE-------VFSHPKHPLTREfiqstlHLDLP-EDYLARLQAEPTTGSGP 267
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1501-1578 1.66e-07

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 55.59  E-value: 1.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:COG1129    144 GDLSIAQRQMVEIARALSFDARVLILDEPTAALTVKeTERLFD--LIRRLKAQgvAIIYISHRLDEVFEiADRITVLRDG 221

                   ..
gi 1189438336 1577 AI 1578
Cdd:COG1129    222 RV 223
SapF COG4167
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
721-937 1.98e-07

ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];


Pssm-ID: 226637 [Multi-domain]  Cd Length: 267  Bit Score: 54.06  E-value: 1.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLP----DSE--------IGEDPSperetaTDLDIRKR 788
Cdd:COG4167     32 VSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEILINDHPlhfgDYSfrskrirmIFQDPN------TSLNPRLR 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  789 gpvayASQkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPD-IDILPHgdqtqigergiNLSGGQRQRISVARALYQ 867
Cdd:COG4167    106 -----IGQ---ILDFPLRLNTDLEPEQRRKQIFETLRMVGLLPDhANYYPH-----------MLAPGQKQRVALARALIL 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1189438336  868 HANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:COG4167    167 RPKIIIADEALASLDMSMRSQLINL-MLELQEKQGISYIYVTQHIGMIKHiSDQVLVMHEGEVVERGSTAD 236
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
713-942 2.21e-07

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 227019 [Multi-domain]  Cd Length: 249  Bit Score: 53.88  E-value: 2.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  713 DGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSlpDSEIGEDPSPEretatdldIRKRGpVA 792
Cdd:COG4674     16 GGFKALNDLSFSVDPGELRVLIGPNGAGKTTLMDVITGKTRPQEGEVLFDG--DTDLTKLPEHR--------IARAG-IG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 YASQKPW-LLNATVEENI---------IFESPF------NKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 856
Cdd:COG4674     85 RKFQKPTvFENLTVRENLelalnrdksVFASLFarlraeERRRIDELLATIGLGDERDRLAA-----------LLSHGQK 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDihlSDHLMQAGilELLRD--DKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:COG4674    154 QWLEIGMLLAQDPKLLLLDEPVAGMT---DAETEKTA--ELLKSlaGKHSILVVEHDMGFVREiADKVTVLHEGSVLAEG 228

                   ....*....
gi 1189438336  934 TLKDFQRSE 942
Cdd:COG4674    229 SLDEVQNDP 237
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1311-1560 2.25e-07

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 226646 [Multi-domain]  Cd Length: 604  Bit Score: 55.39  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1311 MVSNYLNWMVRNLADMELQLGAVKRIHGL------LKTEAESYEGLLAPSLIPKNwpDQGKIQIQNLSVRYDSSlKPVLK 1384
Cdd:COG4178    334 QVHSSLSWFIDNYDAIADWRATLLRLAEFrqaleaAQMDTEKPARTGRRIDFDDN--ADHGITLENLSLRTPDG-QTLLS 410
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1385 HVNALIAPGQKIGICGRTGSGKSSFslafFRMVdtfeghiiidgidiAKL----------PLHtlrSRLSIILQDPVLFS 1454
Cdd:COG4178    411 ELNFEVRPGERLLITGESGAGKTSL----LRAL--------------AGLwpwgsgrismPAD---SALLFLPQRPYLPQ 469
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1455 GTIRFNL---DPERKCSDSTLWEALEIAQLKlvvkALPGGLDAIITEGGEnFSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:COG4178    470 GTLREALcypNAAPDFSDAELVAVLHKVGLG----DLAERLDEEDRWDRV-LSGGEQQRLAFARLLLHKPKWVFLDEATS 544
                          250       260
                   ....*....|....*....|....*....
gi 1189438336 1532 SIDMATENILQKVVMTAFADRTVVTIAHR 1560
Cdd:COG4178    545 ALDEETEDRLYQLLKEELPDATVISVGHR 573
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
725-921 2.33e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 224166 [Multi-domain]  Cd Length: 591  Bit Score: 55.38  E-value: 2.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  725 IPR-GQLTMIVGQVGCGKSSLLLAALGEMQKVSGAvfwsslPDSEIGEDPSPERETATDL----------DIRKRGPVAY 793
Cdd:COG1245     96 TPRpGKVVGILGPNGIGKSTALKILAGELKPNLGR------YEDPPSWDEVIKRFRGTELqnyfkklyegELRAVHKPQY 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNATVEEniIFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigeRGIN-LSGGQRQRISVARALYQHANVV 872
Cdd:COG1245    170 VDLIPKVVKGKVGE--LLKKVDERGKFDEVVERLGLENVLD------------RDVSeLSGGELQRVAIAAALLRDADVY 235
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1189438336  873 FLDDPFSALDIHlsDHLMQAGILELLRDDKRTVVLVTHKLQYLphaDWI 921
Cdd:COG1245    236 FFDEPSSYLDIR--QRLNAARVIRELAEDGKYVIVVEHDLAVL---DYL 279
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
714-937 2.43e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 55.18  E-value: 2.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIgedPSPERETATDLDIrkrgPVAY 793
Cdd:PRK09700    17 PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI---TINNINY---NKLDHKLAAQLGI----GIIY 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 asQKPWLLNA-TVEENI--------------IFESPFNKQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQR 858
Cdd:PRK09700    87 --QELSVIDElTVLENLyigrhltkkvcgvnIIDWREMRVRAAMMLLRVGLKVDLD-----------EKVANLSISHKQM 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  859 ISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09700   154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL--IMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSD 231
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
721-933 2.59e-07

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 53.14  E-value: 2.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEI-GEDPSPERetatdLDIRKRGPVAYASQK-- 797
Cdd:cd03266     24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------TVdGFDVVKEP-----AEARRRLGFVSDSTGly 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLlnaTVEENIIFESPFN-------KQRYKMVIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHAN 870
Cdd:cd03266     91 DRL---TARENLEYFAGLYglkgdelTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIARALVHDPP 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  871 VVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREG 933
Cdd:cd03266    157 VLLLDEPTTGLDVMATRALRE--FIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
712-934 2.67e-07

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 54.46  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLL--LAALgemQKVSGAvfwsslpDSEIGEDPSPERETAtDLDIRK-- 787
Cdd:PRK11650    14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLrmVAGL---ERITSG-------EIWIGGRVVNELEPA-DRDIAMvf 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  788 -----------RGPVAYAsqkpwLLNATVEENIIfespfnKQRYKMVIEACSLQPDIDILPHgdqtqigergiNLSGGQR 856
Cdd:PRK11650    83 qnyalyphmsvRENMAYG-----LKIRGMPKAEI------EERVAEAARILELEPLLDRKPR-----------ELSGGQR 140
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  857 QRISVARALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKRTVVLVTH-KLQYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11650   141 QRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQ-MRLEIQRLHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
712-912 2.69e-07

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 55.79  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEdpspeRETATDLDIRKRGPV 791
Cdd:TIGR01257  940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL--------VGG-----KDIETNLDAVRQSLG 1006
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYASQKPWLLNATVEENIIFESPFNKQRYkmviEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHANV 871
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1189438336  872 VFLDDPFSALDIHlsdhlMQAGILELLRDDK--RTVVLVTHKL 912
Cdd:TIGR01257 1083 VVLDEPTSGVDPY-----SRRSIWDLLLKYRsgRTIIMSTHHM 1120
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
1079-1267 2.74e-07

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 53.96  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSLGIVLCL------VTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNT 1152
Cdd:cd18554     36 TLDEKVYKLFTIIGIMFFIFLILrppveyYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQ 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1153 IDQHIPSTLECLSRSTLLCVSALAVISYVTPVFLVA---LLPLAIVC-YFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1228
Cdd:cd18554    116 TKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVslvIFPFYILAvKYFFGRLRKLTKERSQALAEVQ----GFLHER 191
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1189438336 1229 VEGLTTIRAFRYEARFQQkllEYTDSNNiasLFLTAANR 1267
Cdd:cd18554    192 IQGMSVIKSFALEKHEQK---QFDKRNG---HFLTRALK 224
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1366-1601 2.76e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 53.97  E-value: 2.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13647     5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDP--VLFSGTI-------RFNLDPERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARA 1516
Cdd:PRK13647    84 VFQDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAGV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATenilQKVVMTAFAD-----RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEkLLSR 1590
Cdd:PRK13647   153 LAMDPDVIVLDEPMAYLDPRG----QETLMEILDRlhnqgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTD 227
                          250
                   ....*....|.
gi 1189438336 1591 KDSVFASFVRA 1601
Cdd:PRK13647   228 EDIVEQAGLRL 238
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
718-929 2.80e-07

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 52.43  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETatdlDIRKRGpVAYAS-- 795
Cdd:cd03215     16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD-------GKPVTRRSPR----DAIRAG-IAYVPed 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 --QKPWLLNATVEENIIFespfnkqrykmvieacslqpdidilphgdqtqigerGINLSGGQRQRISVARALYQHANVVF 873
Cdd:cd03215     84 rkREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLARWLARDPRVLI 127
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  874 LDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTI 929
Cdd:cd03215    128 LDEPTRGVDVGAKAEIYR--LIRELADAGKAVLLISSELDELLGlCDRILVMYEGRI 182
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
710-931 2.91e-07

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 53.70  E-value: 2.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  710 WTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAAL------GEMQkVSGaVFWSSLPDSEIgedpsperetatdl 783
Cdd:cd03289     12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQ-IDG-VSWNSVPLQKW-------------- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  784 dirkRGPVAYASQKPWLLNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVAR 863
Cdd:cd03289     76 ----RKAFGVIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  864 ALYQHANVVFLDDPFSALDiHLSDHLMQAGILELLRDdkRTVVLVTHKLQYLPHADWIIAMKDGTIQR 931
Cdd:cd03289    152 SVLSKAKILLLDEPSAHLD-PITYQVIRKTLKQAFAD--CTVILSEHRIEAMLECQRFLVIEENKVRQ 216
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
721-932 3.32e-07

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 226968 [Multi-domain]  Cd Length: 546  Bit Score: 54.81  E-value: 3.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  721 ITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeigeDPSPERetatdldirKRGPVAYASQKPWL 800
Cdd:COG4615    342 INLTIKRGELVFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVS----AEQLED---------YRKLFSAVFSDYHL 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  801 LNATV-------EENIIFESPFNKQRYKMVIEACSLQPdidilphgdqtqigergINLSGGQRQRISVARALYQHANVVF 873
Cdd:COG4615    409 FDQLLgpegkasPQLIEKWLQRLELAHKTSLNDGRFSN-----------------LKLSTGQKKRLALLLALLEERDILV 471
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  874 LDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQRE 932
Cdd:COG4615    472 LDEWAADQDPAFRREFYQV-LLPLLKEQGKTIFAISHDDHYFIHADRLLEMRNGQLSEL 529
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1383-1589 3.74e-07

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 54.27  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRS----RLSIILQDpvlfsgtir 1458
Cdd:PRK10070    44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQS--------- 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1459 FNLDPERKCSDSTLWeALEIAQLKLVVKAlPGGLDAIITEGGENF--------SQGQRQLFCLARAFVRKTSIFIMDEAT 1530
Cdd:PRK10070   115 FALMPHMTVLDNTAF-GMELAGINAEERR-EKALDALRQVGLENYahsypdelSGGMRQRVGLARALAINPDILLMDEAF 192
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1531 ASID--MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK10070   193 SALDplIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILN 254
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
1366-1592 3.78e-07

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223487 [Multi-domain]  Cd Length: 237  Bit Score: 52.86  E-value: 3.78e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTlRSRLSI 1445
Cdd:COG0410      4 LEVENLSAGYGKI--QALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFDGEDITGLPPHE-RARLGI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 IL--QDPVLFSG-TIRFNL------DPERKCSDSTLWEALEI-AQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLAR 1515
Cdd:COG0410     81 AYvpEGRRIFPRlTVEENLllgayaRRDKEAQERDLEEVYELfPRLKERRNQRAGTL-----------SGGEQQMLAIAR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1516 AFVRKTSIFIMDEATA----SIdmaTENILQKVVMtaFADRTVVTI---AHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1587
Cdd:COG0410    150 ALMSRPKLLLLDEPSEglapKI---VEEIFEAIKE--LRKEGGMTIllvEQNARFALEiADRGYVLENGRIVLSGTAAEL 224

                   ....*
gi 1189438336 1588 LSRKD 1592
Cdd:COG0410    225 LADPD 229
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1029-1594 3.89e-07

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 54.59  E-value: 3.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1029 AGILLLSLLvfSQLLKHMVLVAIDYWLAKWTDSALTLTPAarncslsqectldqtvyamvFTVLCSLGIVLCLVTSVTVE 1108
Cdd:PRK10522    16 ISVMALSLA--SAALGIGLIAFINQRLIETADTSLLVLPE--------------------FLGLLLLLMAVTLGSQLALT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1109 WTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID---QHIPStlecLSRSTLLCVSALAVISYVTP-V 1184
Cdd:PRK10522    74 TLGHHFVYRLRSEFIKRILDTHVERIEQLGSASLLASLTSDVRNITiafVRLPE----LVQGIILTLGSAAYLAWLSPkM 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1185 FLVALLPLAIVcyFIQKYFRVAS-----RDLQQLDDTtqlpLLSHFAETVEG-----LTTIRA-FRYEARFQQKLLEYTD 1253
Cdd:PRK10522   150 LLVTAIWMAVT--IWGGFVLVARvykhmATLRETEDK----LYNDYQTVLEGrkeltLNRERAeYVFENEYEPDAQEYRH 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1254 SNNIASLFLTAANRWLEVRMeyIGAcvvlIAAVTSISNSLhrelsaGLVGLGL--TYALMVSNYLNWMVRNLADMELQLG 1331
Cdd:PRK10522   224 HIIRADTFHLSAVNWSNIMM--LGA----IGLVFYMANSL------GWADTNVaaTYSLTLLFLRTPLLSAVGALPTLLS 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1332 AVKRIHGLLKTEAESYEGLLAPSLIPKNWPdqgKIQIQNLSVRYDS---SLKPVlkhvNALIAPGQKIGICGRTGSGKSS 1408
Cdd:PRK10522   292 AQVAFNKLNKLALAPYKAEFPRPQAFPDWQ---TLELRNVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKST 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1409 FSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTirfnLDPERKCSDSTLWEA-LEIAQLKlvvka 1487
Cdd:PRK10522   365 LAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQL----LGPEGKPANPALVEKwLERLKMA----- 435
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1488 lpgglDAIITEGGE----NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRV 1561
Cdd:PRK10522   436 -----HKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmgKTIFAISHDD 510
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1189438336 1562 HTILSADLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PRK10522   511 HYFIHADRLLEMRNGQLSELTGEERDAASRDAV 543
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1364-1536 4.01e-07

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 226620 [Multi-domain]  Cd Length: 213  Bit Score: 52.53  E-value: 4.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1364 GKIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKS---SFSLAFFRMVDTFEGHIIIDGIDIAKLPLHtlR 1440
Cdd:COG4136      1 GMLCLKNVSLRLPGSC--LLANVNFTIAKGEIVTLMGPSGCGKStllSWMIGALAGQFSCTGELWLNEQRLDMLPAA--Q 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SRLSIILQDPVLFS-----GTIRFNLDPERKCSdstlwealeiAQLKLVVKALP-GGLDAIITEGGENFSQGQRQLFCLA 1514
Cdd:COG4136     77 RQIGILFQDALLFPhlsvgQNLLFALPATLKGN----------ARRNAANAALErSGLDGAFHQDPATLSGGQRARVALL 146
                          170       180
                   ....*....|....*....|..
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMA 1536
Cdd:COG4136    147 RALLAQPKALLLDEPFSRLDVA 168
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
847-933 4.64e-07

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 52.14  E-value: 4.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  847 RGIN--LSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADWI 921
Cdd:cd03217     99 RYVNegFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDI---DALrLVAEVINKLREEGKSVLIITHYQRLLDYikPDRV 175
                           90
                   ....*....|..
gi 1189438336  922 IAMKDGTIQREG 933
Cdd:cd03217    176 HVLYDGRIVKSG 187
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
718-927 4.64e-07

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 52.28  E-value: 4.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPdseigedpsperetatdLDIRKRGPVAYASQK 797
Cdd:cd03269     16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP-----------------LDIAARNRIGYLPEE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWL-LNATVEENIIFESpfnkQRYKMVIEACSLQPD-----IDILPHGDQtQIGErginLSGGQRQRISVARALYQHANV 871
Cdd:cd03269     79 RGLyPKMKVIDQLVYLA----QLKGLKKEEARRRIDewlerLELSEYANK-RVEE----LSKGNQQKVQFIAAVIHDPEL 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  872 VFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDG 927
Cdd:cd03269    150 LILDEPFSGLDPVNVELLKDV-IRE-LARAGKTVILSTHQMELVEElCDRVLLLNKG 204
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport ...
1366-1599 6.66e-07

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport and metabolism];


Pssm-ID: 226361 [Multi-domain]  Cd Length: 352  Bit Score: 53.44  E-value: 6.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEG----HIIIDGIDIAKLPLHtlRS 1441
Cdd:COG3842      6 LEIRNVSKSFGD--FTAVDDISLDIKKGEFVTLLGPSGCGKTTL----LRMIAGFEQpssgEILLDGEDITDVPPE--KR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLFS-----GTIRFNLDPERKCSDSTLW----EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFC 1512
Cdd:COG3842     78 PIGMVFQSYALFPhmtveENVAFGLKVRKKLKKAEIKarveEALELVGLEGFADRKPHQL-----------SGGQQQRVA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG3842    147 LARALVPEPKVLLLDEPLSALDAKLREQMRKELKELQRELgiTFVYVTHDQEEALAmSDRIAVMNDGRIEQVGTPEEIYE 226
                          250
                   ....*....|.
gi 1189438336 1590 RKDSVF-ASFV 1599
Cdd:COG3842    227 RPATRFvADFI 237
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
800-932 7.52e-07

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 53.67  E-value: 7.52e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 LLNATVEENIIFES--------PFNKQRYKMVIEAcsLQPDIDILPHGDQTQIGergiNLSGGQRQRISVARALYQHANV 871
Cdd:COG1129    349 VLDMSIAENITLASlrrfsrrgLIDRRKERALAER--YIRRLRIKTPSPEQPIG----TLSGGNQQKVVLARWLATDPKV 422
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  872 VFLDDPFSALDIHlsdhlMQAGILELLR---DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQRE 932
Cdd:COG1129    423 LILDEPTRGIDVG-----AKAEIYRLIRelaAEGKAILMISSELPELLGlSDRILVMREGRIVGE 482
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1380-1591 7.59e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 52.36  E-value: 7.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIA------KLPLHTLRSRLSIILQDPVLF 1453
Cdd:PRK14246    23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMVFQQPNPF 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1454 SG-TIRFNLD-PERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:PRK14246   103 PHlSIYDNIAyPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1532 SIDMATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILE-------FDKPEKLLSRK 1591
Cdd:PRK14246   183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEwgssneiFTSPKNELTEK 250
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
852-915 9.30e-07

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 53.56  E-value: 9.30e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALdihlsDHLMQAGILELLRDDKRtvvlvTHKLQYL 915
Cdd:PRK15134   427 SGGQRQRIAIARALILKPSLIILDEPTSSL-----DKTVQAQILALLKSLQQ-----KHQLAYL 480
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1365-1587 9.37e-07

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 52.09  E-value: 9.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSSLkpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIdgidiAKLPLH------- 1437
Cdd:PRK14243    10 VLRTENLNVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVE-----GKVTFHgknlyap 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 -----TLRSRLSIILQDPVLFSGTI-------------RFNLDP--ERKCSDSTLWEALEiAQLKlvvkalpggldaiit 1497
Cdd:PRK14243    83 dvdpvEVRRRIGMVFQKPNPFPKSIydniaygaringyKGDMDElvERSLRQAALWDEVK-DKLK--------------- 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1498 EGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH------RVHTI---LSAD 1568
Cdd:PRK14243   147 QSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHnmqqaaRVSDMtafFNVE 226
                          250       260
                   ....*....|....*....|
gi 1189438336 1569 LVIVLKR-GAILEFDKPEKL 1587
Cdd:PRK14243   227 LTEGGGRyGYLVEFDRTEKI 246
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1501-1599 1.07e-06

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 51.57  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 ENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMAT-ENILQ--KVVMTAFaDRTVVTIAHRVHTILS-ADLVIVLKRG 1576
Cdd:cd03299    128 ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREelKKIRKEF-GVTVLHVTHDFEEAWAlADKVAIMLNG 206
                           90       100
                   ....*....|....*....|....
gi 1189438336 1577 AILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:cd03299    207 KLIQVGKPEEVFKKPKNEFvAEFL 230
cbiO PRK13642
energy-coupling factor transporter ATPase;
1366-1594 1.09e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 52.02  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYD-SSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK13642     5 LEVENLVFKYEkESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDP------VLFSGTIRFNLDPE---RKCSDSTLWEALeiaqlkLVVKALPggldaIITEGGENFSQGQRQLFCLAR 1515
Cdd:PRK13642    85 MVFQNPdnqfvgATVEDDVAFGMENQgipREEMIKRVDEAL------LAVNMLD-----FKTREPARLSGGQKQRVAVAG 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1516 AFVRKTSIFIMDEATASIDMATENILQKVVMtAFADR---TVVTIAHRVHTILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13642   154 IIALRPEIIILDESTSMLDPTGRQEIMRVIH-EIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSE 232

                   ..
gi 1189438336 1593 SV 1594
Cdd:PRK13642   233 DM 234
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
715-934 1.17e-06

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 51.42  E-value: 1.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpDSEIGEDPSpERETATDLDIRKRGPVAYA 794
Cdd:PRK11614    18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD---GKDITDWQT-AKIMREAVAIVPEGRRVFS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQkpwllnaTVEENIIFESPF-NKQRYKMVIEACslqpdIDILPHGDQTQIgERGINLSGGQRQRISVARALYQHANVVF 873
Cdd:PRK11614    94 RM-------TVEENLAMGGFFaERDQFQERIKWV-----YELFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  874 LDDPfsalDIHLSDHLMQA--GILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGT 934
Cdd:PRK11614   161 LDEP----SLGLAPIIIQQifDTIEQLREQGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDT 220
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
716-940 1.27e-06

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 51.62  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMqkvsgavfwsslpdseigedPSPERETATDLDIRKRgPVAyAS 795
Cdd:PRK10418    17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIL--------------------PAGVRQTAGRVLLDGK-PVA-PC 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLLNATVEENIifESPFNKQRyKM---VIEAC---SLQPDIDILPH-------GDQTQIGER-GINLSGGQRQRISV 861
Cdd:PRK10418    75 ALRGRKIATIMQNP--RSAFNPLH-TMhthARETClalGKPADDATLTAaleavglENAARVLKLyPFEMSGGMLQRMMI 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  862 ARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKRT----VVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLK 936
Cdd:PRK10418   152 ALALLCEAPFIIADEPTTDLDV-----VAQARILDLLESIVQKralgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVE 226

                   ....*
gi 1189438336  937 D-FQR 940
Cdd:PRK10418   227 TlFNA 231
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
720-941 1.30e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 52.05  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGeMQKVSGAVFWSSLP--DSEIGEDPSPERETATDLDirkrgpVAYASQK 797
Cdd:PRK11022    25 RISYSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRVMAEKLEfnGQDLQRISEKERRNLVGAE------VAMIFQD 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWL-LNA--TVEENII-----FESPFNKQRYKMVIEACSLQ--PD----IDILPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK11022    98 PMTsLNPcyTVGFQIMeaikvHQGGNKKTRRQRAIDLLNQVgiPDpasrLDVYPH-----------QLSGGMSQRVMIAM 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  864 ALYQHANVVFLDDPFSALDIhlsdhLMQAGILELL----RDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDF 938
Cdd:PRK11022   167 AIACRPKLLIADEPTTALDV-----TIQAQIIELLlelqQKENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241

                   ...
gi 1189438336  939 QRS 941
Cdd:PRK11022   242 FRA 244
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
718-894 1.38e-06

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 51.00  E-value: 1.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPsperetatdLDIRKRGPVAYASQK 797
Cdd:cd03218     16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIL---LDGQDITKLP---------MHKRARLGIGYLPQE 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENI--IFESpFNKQRYKMVIEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHANVVFL 874
Cdd:cd03218     84 ASIFrKLTVEENIlaVLEI-RGLSKKEREEKLEELLEEFHITHLRKS-----KASSLSGGERRRVEIARALATNPKFLLL 157
                          170       180
                   ....*....|....*....|....*..
gi 1189438336  875 DDPFSALD-IHLSD------HLMQAGI 894
Cdd:cd03218    158 DEPFAGVDpIAVQDiqkiikILKDRGI 184
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
1083-1324 1.61e-06

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 51.70  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1162
Cdd:cd18545     40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLI 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISYVTPVF-LVAL--LP-LAIVCYFIQKYFRVASRDLQQlddtTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:cd18545    120 NLIPDLLTLVGIVIIMFSLNVRLaLVTLavLPlLVLVVFLLRRRARKAWQRVRK----KISNLNAYLHESISGIRVIQSF 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 RYE----ARFQQKLLEYTDSNNIASLFLTAANRWLEVrMEYIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYA----- 1309
Cdd:cd18545    196 AREdeneEIFDELNRENRKANMRAVRLNALFWPLVEL-ISALGTALVYWYGGKLV---LGGAITVGVLVAFIGYVgrfwq 271
                          250
                   ....*....|....*..
gi 1189438336 1310 --LMVSNYLNWMVRNLA 1324
Cdd:cd18545    272 piRNLSNFYNQLQSAMA 288
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1380-1589 1.86e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 51.25  E-value: 1.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT------LRSRLSIILQDPVLF 1453
Cdd:PRK14271    34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNyrdvleFRRRVGMLFQRPNPF 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1454 SGTIRFN-LDPERKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATAS 1532
Cdd:PRK14271   114 PMSIMDNvLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1533 IDMATENILQKVVMTaFADR-TVVTIAHRV-HTILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK14271   194 LDPTTTEKIEEFIRS-LADRlTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLFS 251
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
716-894 1.96e-06

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224060 [Multi-domain]  Cd Length: 243  Bit Score: 50.66  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  716 PTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwssLPDSEIGEDPsperetatdLDIRKRGPVAYAS 795
Cdd:COG1137     18 KVVNDVSLEVNSGEIVGLLGPNGAGKTTTFYMIVGLVRPDSGKIL---LDDEDITKLP---------MHKRARLGIGYLP 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QKPWLL-NATVEENI--IFESpFNKQRYKMV--IEACSLQPDIDILPHGDQtqigeRGINLSGGQRQRISVARALYQHAN 870
Cdd:COG1137     86 QEASIFrKLTVEDNImaVLEI-REKDLKKAErkEELDALLEEFHITHLRDS-----KAYSLSGGERRRVEIARALAANPK 159
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1189438336  871 VVFLDDPFSALD-IHLSD------HLMQAGI 894
Cdd:COG1137    160 FILLDEPFAGVDpIAVIDiqriikHLKDRGI 190
FtsE COG2884
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome ...
1366-1576 1.96e-06

ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225438 [Multi-domain]  Cd Length: 223  Bit Score: 50.68  E-value: 1.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRSR 1442
Cdd:COG2884      2 IRFENVSKAYPGG-REALRDVSFHIPKGEFVFLTGPSGAGKSTLLKLIYGEERPTRGKILVNGHDLSRLKgreIPFLRRQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSIILQD-PVLFSGTIRFN-------LDPERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLA 1514
Cdd:COG2884     81 IGVVFQDfRLLPDRTVYENvalplrvIGKPPREIRRRVSEVLDLVGLKHKARALPSQL-----------SGGEQQRVAIA 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1515 RAFVRKTSIFIMDEATASID--MATE--NILQK-------VVMTAFADRTVVTIAHRVHTILSADLVIVLKRG 1576
Cdd:COG2884    150 RAIVNQPAVLLADEPTGNLDpdLSWEimRLFEEinrlgttVLMATHDLELVNRMRHRVLALEDGRLVRDESRG 222
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
720-910 2.30e-06

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 51.34  E-value: 2.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEdPSPERETatdldiRKRGPVAYASQKPW 799
Cdd:PRK13537    25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI-------SLCGE-PVPSRAR------HARQRVGVVPQFDN 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  800 L-LNATVEENI-IFESPFN------KQRYKMVIEACSLQPDIDilphgdqTQIGErginLSGGQRQRISVARALYQHANV 871
Cdd:PRK13537    91 LdPDFTVRENLlVFGRYFGlsaaaaRALVPPLLEFAKLENKAD-------AKVGE----LSGGMKRRLTLARALVNDPDV 159
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1189438336  872 VFLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 910
Cdd:PRK13537   160 LVLDEPTTGLDPQ-ARHLMWERLRSLLARGK-TILLTTH 196
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1366-1589 2.40e-06

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 50.13  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTlRSRLSI 1445
Cdd:cd03224      1 LEVENLNAGYGKS--QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE-RARAGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 IL--QDPVLFSG-TIRFNLD-PERKCSDSTLWEALEIaqlklVVKALPgGLDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:cd03224     78 GYvpEGRRIFPElTVEENLLlGAYARRRAKRKARLER-----VYELFP-RLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1522 SIFIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:cd03224    152 KLLLLDEPSEGLApKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
ModC COG4148
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1391-1592 2.43e-06

ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226628 [Multi-domain]  Cd Length: 352  Bit Score: 51.57  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1391 APGQKI-GICGRTGSGKSSF---------------SLAFFRMVDTFEGHIiidgidiakLPLHtlRSRLSIILQDPVLF- 1453
Cdd:COG4148     21 LPARGItALFGPSGSGKTSLinmiagltrpdegriELNGRVLVDAEKGIF---------LPPE--KRRIGYVFQDARLFp 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1454 ----SGTIRFNLDPERKCSDSTLWEALEIAQLklvVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEA 1529
Cdd:COG4148     90 hytvRGNLRYGMWKSMRAQFDQLVALLGIEHL---LDRYPGTL-----------SGGEKQRVAIGRALLTAPELLLMDEP 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1530 TASIDMAT--------ENILQKVvmtafaDRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:COG4148    156 LASLDLPRkreilpylERLRDEI------NIPILYVSHSLDEVLRlADRVVVLENGKVKASGPLEEVWGSPD 221
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
728-937 2.43e-06

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 50.94  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  728 GQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF------------WSSLPDSEIGEDPSperetaTDLDIRKRgpvayAS 795
Cdd:PRK15112    39 GQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhfgdysYRSQRIRMIFQDPS------TSLNPRQR-----IS 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  796 QkpwLLNATVEENIIFESPFNKQRYKMVIEACSLQPD-IDILPHGdqtqigerginLSGGQRQRISVARALYQHANVVFL 874
Cdd:PRK15112   108 Q---ILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDhASYYPHM-----------LAPGQKQRLGLARALILRPKVIIA 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  875 DDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKD 937
Cdd:PRK15112   174 DEALASLDMSMRSQLINL-MLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTAD 236
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
715-941 2.71e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 52.17  E-value: 2.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGP-VAY 793
Cdd:PRK10261    29 IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRGAdMAM 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWL-LNA--TVEENIIfESPFNKQ---RYKMVIEACSLQPDIDIlPHGdQTQIGERGINLSGGQRQRISVARALYQ 867
Cdd:PRK10261   109 IFQEPMTsLNPvfTVGEQIA-ESIRLHQgasREEAMVEAKRMLDQVRI-PEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  868 HANVVFLDDPFSALDIhlsdhLMQAGILELLR----DDKRTVVLVTHKLQYLPH-ADWIIAMKDGTIQREGTLKDFQRS 941
Cdd:PRK10261   186 RPAVLIADEPTTALDV-----TIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFHA 259
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
718-941 3.05e-06

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226631 [Multi-domain]  Cd Length: 300  Bit Score: 50.82  E-value: 3.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSE-----IGEDPSpERETATDLdirkrgpva 792
Cdd:COG4152     18 VDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLSQeiknrIGYLPE-ERGLYPKM--------- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 yasqkpwllnaTVEENIIFESPF-NKQRYKMVIEACSLQPDIDILPH-GDQTQigergiNLSGGQRQRISVARALYQHAN 870
Cdd:COG4152     88 -----------TVEDQLKYLAELkGMPKAEIQKKLQAWLERLEIVGKkTKKIK------ELSKGNQQKIQFISAVIHEPE 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  871 VVFLDDPFSALDIhLSDHLMQAGILElLRDDKRTVVLVTHKLQylpHA----DWIIAMKDGTIQREGTLKDFQRS 941
Cdd:COG4152    151 LLILDEPFSGLDP-VNVELLKDAIFE-LKEEGATIIFSSHRME---HVeelcDRLLMLKKGQTVLYGTVEDIRRS 220
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
843-934 3.91e-06

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 51.55  E-value: 3.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  843 QIGERGINLSGGQRQRISVARALYQHAN---VVFLDDPFSALdiHLSD--HLMQagILELLRDDKRTVVLVTHKLQYLPH 917
Cdd:TIGR00630  822 RLGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGL--HFDDikKLLE--VLQRLVDKGNTVVVIEHNLDVIKT 897
                           90       100
                   ....*....|....*....|...
gi 1189438336  918 ADWII------AMKDGTIQREGT 934
Cdd:TIGR00630  898 ADYIIdlgpegGDGGGTVVASGT 920
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1366-1589 4.85e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 50.61  E-value: 4.85e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK09536     4 IDVSDLSVEFGDT--TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVL---FSG--TIRFNLDPERK---CSDSTLWEALEIAQLKLVVKALpggLDAIITEggenFSQGQRQLFCLARAF 1517
Cdd:PRK09536    82 VPQDTSLsfeFDVrqVVEMGRTPHRSrfdTWTETDRAAVERAMERTGVAQF---ADRPVTS----LSGGERQRVLLARAL 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1518 VRKTSIFIMDEATASIDMATE-NILQKVVMTAFADRTVVTIAHRVHtiLSA---DLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK09536   155 AQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLD--LAArycDELVLLADGRVRAAGPPADVLT 228
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
1079-1261 5.17e-06

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 50.10  E-value: 5.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSLGIVLCLVTS-VTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHI 1157
Cdd:cd18541     35 TASQLLRYALLILLLALLIGIFRFLWrYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMAL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1158 PSTLECLSRSTLLCVSALAVISYVTPVF-LVALLPL---AIVCYFIQKYFRVASRDLQQ----LDDTTQlpllshfaETV 1229
Cdd:cd18541    115 GPGILYLVDALFLGVLVLVMMFTISPKLtLIALLPLpllALLVYRLGKKIHKRFRKVQEafsdLSDRVQ--------ESF 186
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1189438336 1230 EGLTTIRAF----RYEARFQQKLLEYTDSNN----IASLF 1261
Cdd:cd18541    187 SGIRVIKAFvqeeAEIERFDKLNEEYVEKNLrlarVDALF 226
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
1082-1254 5.58e-06

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 50.12  E-value: 5.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1082 QTVYAMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1161
Cdd:cd18551     37 GLLALLVALFL--LQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1162 -ECLSRSTLLCVS--ALAVISYVTPVFLVALLPLAIVC-YFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1236
Cdd:cd18551    115 pQLVTGVLTVVGAvvLMFLLDWVLTLVTLAVVPLAFLIiLPLGRRIRKASKRAQD-----ALGELSAALErALSAIRTVK 189
                          170
                   ....*....|....*...
gi 1189438336 1237 AFRYEARFQQKLLEYTDS 1254
Cdd:cd18551    190 ASNAEERETKRGGEAAER 207
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
727-910 6.06e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 47.75  E-value: 6.06e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336   727 RGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseigedpsperetatdldirkrgpvayasqkpwLLNATVE 806
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------YIDGEDI 41
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336   807 ENIIFESPFNkqrykmvieacslqpdidilphgdqTQIGERGINLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLS 886
Cdd:smart00382   42 LEEVLDQLLL-------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
                           170       180
                    ....*....|....*....|....*...
gi 1189438336   887 DHLMQAGILELL----RDDKRTVVLVTH 910
Cdd:smart00382   97 ALLLLLEELRLLlllkSEKNLTVILTTN 124
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
1091-1264 6.31e-06

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 49.80  E-value: 6.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1091 VLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILA--------PMRFFETTPLGSILNRFSSDCNTIDQHIPSTLE 1162
Cdd:cd18546     39 LLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRvfahlqrlSLDFHERETSGRIMTRMTSDIDALSELLQTGLV 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFiqkyFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAF 1238
Cdd:cd18546    119 QLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATRW----FRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAF 194
                          170       180
                   ....*....|....*....|....*....
gi 1189438336 1239 RYEARFQQKLLEYTDSN---NIASLFLTA 1264
Cdd:cd18546    195 RRERRNAERFAELSDDYrdaRLRAQRLVA 223
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1366-1590 6.37e-06

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226967 [Multi-domain]  Cd Length: 268  Bit Score: 49.52  E-value: 6.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSS-------LKPVLKHVNALIAPGQKIGICGRTGSGKSsfslaffrmvdtfeghiiidgidiaklplhT 1438
Cdd:COG4608      5 LEVKNLKKYFPVGkgfgkkrYVKAVDGVSFSIKEGETLGLVGESGCGKS------------------------------T 54
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LrSRLSIILQDPVlfSGTIRFNLDPERKcsdstLWEALEIAQLKLVVKALpgGL--DAIITEGGEnFSQGQRQLFCLARA 1516
Cdd:COG4608     55 L-GRLILGLEEPT--SGEILFEGKDITK-----LSKEERRERVLELLEKV--GLpeEFLYRYPHE-LSGGQRQRIGIARA 123
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATE----NIL---QKVVMTafadrTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLL 1588
Cdd:COG4608    124 LALNPKLIVADEPVSALDVSVQaqilNLLkdlQEELGL-----TYLFISHDLSVVRYiSDRIAVMYLGKIVEIGPTEEVF 198

                   ..
gi 1189438336 1589 SR 1590
Cdd:COG4608    199 SN 200
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
714-910 7.29e-06

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 48.72  E-value: 7.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPERETATDLDIRKRGPVAy 793
Cdd:PRK10908    14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-------GHDITRLKNREVPFLRRQIGMIF- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 aSQKPWLLNATVEENIIFespfnkqryKMVIEACSLQpDIDILPHGDQTQIG------ERGINLSGGQRQRISVARALYQ 867
Cdd:PRK10908    86 -QDHHLLMDRTVYDNVAI---------PLIIAGASGD-DIRRRVSAALDKVGlldkakNFPIQLSGGEQQRVGIARAVVN 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1189438336  868 HANVVFLDDPFSALDIHLSDhlmqaGILELLRDDKR---TVVLVTH 910
Cdd:PRK10908   155 KPAVLLADEPTGNLDDALSE-----GILRLFEEFNRvgvTVLMATH 195
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
851-927 7.72e-06

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 50.47  E-value: 7.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR----TVVLVTHKLQYLPH-ADWIIAMK 925
Cdd:PRK15134   157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSV-----QAQILQLLRELQQelnmGLLFITHNLSIVRKlADRVAVMQ 231

                   ..
gi 1189438336  926 DG 927
Cdd:PRK15134   232 NG 233
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
720-903 8.20e-06

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 50.62  E-value: 8.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWS-----SLPDSE----------IGEDPSperetaTDLD 784
Cdd:PRK10261   342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridTLSPGKlqalrrdiqfIFQDPY------ASLD 415
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  785 IRKrgPVAYASQKPWLLNAtveeniIFESPFNKQRYKMVIEACSLQPDIDI-LPHgdqtqigergiNLSGGQRQRISVAR 863
Cdd:PRK10261   416 PRQ--TVGDSIMEPLRVHG------LLPGKAAAARVAWLLERVGLLPEHAWrYPH-----------EFSGGQRQRICIAR 476
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1189438336  864 ALYQHANVVFLDDPFSALDIHLsdhlmQAGILELLRDDKR 903
Cdd:PRK10261   477 ALALNPKVIIADEAVSALDVSI-----RGQIINLLLDLQR 511
BtuD COG4138
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism];
728-963 8.96e-06

ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism];


Pssm-ID: 226622 [Multi-domain]  Cd Length: 248  Bit Score: 49.08  E-value: 8.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  728 GQLTMIVGQVGCGKSSLLlAALGEMQKVSGAVFWSSLPdseigedpsPERETATDLdIRKRgpvAYASQK---PWLLNat 804
Cdd:COG4138     25 GEILHLVGPNGAGKSTLL-ARMAGMTSGSGSIQFAGQP---------LEAWSATEL-ARHR---AYLSQQqtpPFAMP-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  805 VEENIIFESPfNKQRYKMVIEACSLQPDIDILPhgdqtqigeRGIN-LSGGQRQRISVARALYQ-------HANVVFLDD 876
Cdd:COG4138     89 VWHYLTLHQP-DKTRTELLNDVAGALALDDKLG---------RSTNqLSGGEWQRVRLAAVVLQitpdanpAGQLLLLDE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  877 PFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQY-LPHADWIIAMKDGTIQREGTLKDFQRSE--CQLFEhwktlM 953
Cdd:COG4138    159 PMNSLDVAQQSALDR--LLSALCQQGLAIVMSSHDLNHtLRHAHRAWLLKRGKLLASGRREEVLTPPvlAQAYG-----M 231
                          250
                   ....*....|
gi 1189438336  954 NRQDQELEKE 963
Cdd:COG4138    232 NFRRLDIEGH 241
SapF COG4167
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
1366-1589 9.38e-06

ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];


Pssm-ID: 226637 [Multi-domain]  Cd Length: 267  Bit Score: 49.05  E-value: 9.38e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLS--VRYDSSL-----KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHT 1438
Cdd:COG4167      5 LEVRNLSktFRYRTGLfrrqtVEAVKPVSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEILINDHPLHFGDYSF 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDP-----------VLFSGTIRFNLDPERKCSDSTLWEALEIAQLklvvkaLPGGLDAIIteggENFSQGQ 1507
Cdd:COG4167     85 RSKRIRMIFQDPntslnprlrigQILDFPLRLNTDLEPEQRRKQIFETLRMVGL------LPDHANYYP----HMLAPGQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1508 RQLFCLARAFVRKTSIFIMDEATASIDMATENILQKvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAILEFDK 1583
Cdd:COG4167    155 KQRVALARALILRPKIIIADEALASLDMSMRSQLIN-LMLELQEKqgiSYIYVTQHIGMIKHiSDQVLVMHEGEVVERGS 233

                   ....*.
gi 1189438336 1584 PEKLLS 1589
Cdd:COG4167    234 TADVLA 239
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1366-1544 9.97e-06

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 49.32  E-value: 9.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYD------------SSLKPVlKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAK 1433
Cdd:PRK15079     9 LEVADLKVHFDikdgkqwfwqppKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 L---PLHTLRSRLSIILQDPvLFSgtirfnLDPERKCSD------STLWEALEIAQLKLVVKAL---PGGLDAIITEGGE 1501
Cdd:PRK15079    88 MkddEWRAVRSDIQMIFQDP-LAS------LNPRMTIGEiiaeplRTYHPKLSRQEVKDRVKAMmlkVGLLPNLINRYPH 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1189438336 1502 NFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATE----NILQKV 1544
Cdd:PRK15079   161 EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaqvvNLLQQL 207
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
718-914 1.17e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.95  E-value: 1.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpsperETATDLDirkrgpVAYASQK 797
Cdd:PRK11147   335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------------HCGTKLE------VAYFDQH 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNA--TVEENIifesPFNKQ------RYKMVIEacSLQpdiDILPHGDQTQIGERGinLSGGQRQRISVARALYQHA 869
Cdd:PRK11147   391 RAELDPekTVMDNL----AEGKQevmvngRPRHVLG--YLQ---DFLFHPKRAMTPVKA--LSGGERNRLLLARLFLKPS 459
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMqagilELLRDDKRTVVLVTHKLQY 914
Cdd:PRK11147   460 NLLILDEPTNDLDVETLELLE-----ELLDSYQGTVLLVSHDRQF 499
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
1086-1336 1.20e-05

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 49.05  E-value: 1.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1086 AMVFTVLcsLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLS 1165
Cdd:cd18563     48 GLAGAYV--LSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1166 RSTLLCVSALAVISYVTPVF-LVALLPLAIVCYFIQKYFRVASRDLQQL----DDTTqlpllSHFAETVEGLTTIRAF-- 1238
Cdd:cd18563    126 TNILMIIGIGVVLFSLNWKLaLLVLIPVPLVVWGSYFFWKKIRRLFHRQwrrwSRLN-----SVLNDTLPGIRVVKAFgq 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -RYE-ARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEyIGACVVLIAAVTSIsnsLHRELSAGLVGLGLTYALMVSNYL 1316
Cdd:cd18563    201 eKREiKRFDEANQELLDANIRAEKLWATFFPLLTFLTS-LGTLIVWYFGGRQV---LSGTMTLGTLVAFLSYLGMFYGPL 276
                          250       260
                   ....*....|....*....|
gi 1189438336 1317 NWMVRNLADMELQLGAVKRI 1336
Cdd:cd18563    277 QWLSRLNNWITRALTSAERI 296
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
1083-1293 1.31e-05

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 49.00  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSdCNTIDQHIPSTLE 1162
Cdd:cd18567     42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFV 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAVI-SYVTPVFLVALLPLAIVC---YFIQKYFRVASRDLQQLDDTTQlpllSHFAETVEGLTTIRAF 1238
Cdd:cd18567    121 EALLDGLMAILTLVMMfLYSPKLALIVLAAVALYAllrLALYPPLRRATEEQIVASAKEQ----SHFLETIRGIQTIKLF 196
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1189438336 1239 RYEARFQQKLLE-YTDSNN------IASLFLTAANRWLeVRMEYIGacVVLIAAVTSISNSL 1293
Cdd:cd18567    197 GREAEREARWLNlLVDAINadirlqRLQILFSAANGLL-FGLENIL--VIYLGALLVLDGEF 255
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
851-942 1.35e-05

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223256 [Multi-domain]  Cd Length: 935  Bit Score: 49.89  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALY-QHANVVF-LDDPFSALdiHLSDH--LMQAgiLELLRDDKRTVVLVTHKLQYLPHADWIIAM-- 924
Cdd:COG0178    482 LSGGEAQRIRLATQIGsGLTGVLYvLDEPSIGL--HQRDNerLIET--LKRLRDLGNTVIVVEHDEDTIRAADHIIDIgp 557
                           90       100
                   ....*....|....*....|..
gi 1189438336  925 ----KDGTIQREGTLKDFQRSE 942
Cdd:COG0178    558 gageHGGEIVAEGTPEELLANP 579
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
718-910 1.36e-05

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 49.66  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemqkvsGAVFWSSLPDSEIGEDPSPERETATDLDIRKRGpvAYASQK 797
Cdd:TIGR00955   41 LKNVSGVAKPGELLAVMGSSGAGKTTLM-----------NALAFRSPKGVKGSGSVLLNGMPIDAKEMRAIS--AYVQQD 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLLNA-TVEENIIFESPF----------NKQRYKMVIEACSLQPDIDILphgdqTQIGERGINLSGGQRQRISVARALY 866
Cdd:TIGR00955  108 DLFIPTlTVREHLMFQAHLrmprrvtkkeKRERVDEVLQALGLRKCANTR-----IGVPGRVKGLSGGERKRLAFASELL 182
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  867 QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTH 910
Cdd:TIGR00955  183 TDPPLLFCDEPTSGLDSFMAYSVVQ--VLKGLAQKGKTIICTIH 224
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
714-933 1.48e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 48.55  E-value: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSSLPDSeiGEDPSPERETatdLDIRKRgpVAY 793
Cdd:PRK14271    33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLG--GRSIFNYRDV---LEFRRR--VGM 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNATVEENIIFESPFNK----QRYKMVIEACSLQPDidiLPHGDQTQIGERGINLSGGQRQRISVARALYQHA 869
Cdd:PRK14271   106 LFQRPNPFPMSIMDNVLAGVRAHKlvprKEFRGVAQARLTEVG---LWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336  870 NVVFLDDPFSALDIHLSDHlmqagILELLRD--DKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREG 933
Cdd:PRK14271   183 EVLLLDEPTSALDPTTTEK-----IEEFIRSlaDRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
718-882 1.50e-05

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 50.11  E-value: 1.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpDSEIGEDP-SPEretatDLDIRKRGPVAYASQ 796
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGV------EGVITYDGiTPE-----EIKKHYRGDVVYNAE 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  797 K----PWLlnaTVEENIIF----ESPFNkqRYKMVIEACSLQPDIDI------LPHGDQTQIGE---RGInlSGGQRQRI 859
Cdd:TIGR00956  146 TdvhfPHL---TVGETLDFaarcKTPQN--RPDGVSREEYAKHIADVymatygLSHTRNTKVGNdfvRGV--SGGERKRV 218
                          170       180
                   ....*....|....*....|...
gi 1189438336  860 SVARALYQHANVVFLDDPFSALD 882
Cdd:TIGR00956  219 SIAEASLGGAKIQCWDNATRGLD 241
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1366-1559 1.92e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 47.85  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD-------TFEGHIIIDGIDIAKLPLHT 1438
Cdd:PRK14239     6 LQVSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevtiTGSIVYNGHNIYSPRTDTVD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 LRSRLSIILQDPVLFSGTI--------RFNLDPERKCSDSTLWEALEIAQLKLVVKAlpggldaIITEGGENFSQGQRQL 1510
Cdd:PRK14239    84 LRKEIGMVFQQPNPFPMSIyenvvyglRLKGIKDKQVLDEAVEKSLKGASIWDEVKD-------RLHDSALGLSGGQQQR 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAH 1559
Cdd:PRK14239   157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR 205
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
714-913 1.99e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 47.97  E-value: 1.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsSLPDSEIGEDPsperetatdLDIRKRGPVAY 793
Cdd:PRK10895    15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI---IIDDEDISLLP---------LHARARRGIGY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNA-TVEENI-----IFESPFNKQRYKMVIEacsLQPDIDILPHGDQTqigerGINLSGGQRQRISVARALYQ 867
Cdd:PRK10895    83 LPQEASIFRRlSVYDNLmavlqIRDDLSAEQREDRANE---LMEEFHIEHLRDSM-----GQSLSGGERRRVEIARALAA 154
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1189438336  868 HANVVFLDDPFSALD-IHLSDhlmQAGILELLRDDKRTVVLVTHKLQ 913
Cdd:PRK10895   155 NPKFILLDEPFAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
1367-1585 2.20e-05

ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 223488 [Multi-domain]  Cd Length: 250  Bit Score: 47.57  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1367 QIQNLSVRYDSsLKpVLKHVNALIAPGQKIGICGRTGSGKSsfslAFFRMVDTFEGHIIIDGIDIAK----LPLHtLRSR 1442
Cdd:COG0411      6 EVRGLSKRFGG-LT-AVNDVSLEVRPGEIVGLIGPNGAGKT----TLFNLITGFYKPSSGTVIFRGRditgLPPH-RIAR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1443 LSII--LQDPVLFSG-----------------TIRFNLDPERKCSDSTLWEALEIaqLKLVvkalpgGLDAIITEGGENF 1503
Cdd:COG0411     79 LGIArtFQITRLFPGltvlenvavgaharlglSGLLGRPRARKEEREARERAREL--LEFV------GLGELADRPAGNL 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1504 SQGQRQLFCLARAFVRKTSIFIMDEATASIDmATE-----NILQKVvmTAFADRTVVTIAHRVHTILS-ADLVIVLKRGA 1577
Cdd:COG0411    151 SYGQQRRLEIARALATQPKLLLLDEPAAGLN-PEEteelaELIREL--RDRGGVTILLIEHDMKLVMGlADRIVVLNYGE 227

                   ....*...
gi 1189438336 1578 ILEFDKPE 1585
Cdd:COG0411    228 VIAEGTPE 235
cbiO PRK13641
energy-coupling factor transporter ATPase;
1383-1592 2.59e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 47.90  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1383 LKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMV----DTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDP--VLFSGT 1456
Cdd:PRK13641    23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLkpssGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPeaQLFENT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1457 IRFNLDPERKCSDSTLWEALEIAqLKLVVKAlpGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID-M 1535
Cdd:PRK13641   103 VLKDVEFGPKNFGFSEDEAKEKA-LKWLKKV--GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDpE 179
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1536 ATENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:PRK13641   180 GRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKE 237
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1370-1594 2.66e-05

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 47.69  E-value: 2.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1370 NLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIIL 1447
Cdd:PRK13638     6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVF 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1448 QDP---VLFS---GTIRFNLD----PE----RKCSDS-TLWEALEIAQLKLvvkalpggldaiiteggENFSQGQRQLFC 1512
Cdd:PRK13638    84 QDPeqqIFYTdidSDIAFSLRnlgvPEaeitRRVDEAlTLVDAQHFRHQPI-----------------QCLSHGQKKRVA 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASIDMATEN----ILQKVVMTAfadRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKL 1587
Cdd:PRK13638   147 IAGALVLQARYLLLDEPTAGLDPAGRTqmiaIIRRIVAQG---NHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEV 223

                   ....*..
gi 1189438336 1588 LSRKDSV 1594
Cdd:PRK13638   224 FACTEAM 230
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
849-912 2.72e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.41  E-value: 2.72e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336  849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKL 912
Cdd:cd03222     70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARA-IRRLSEEGKKTALVVEHDL 132
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
1084-1247 2.79e-05

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 48.01  E-value: 2.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1084 VYAMVFTVLC--SLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTL 1161
Cdd:cd18780     41 LNQAVLILLGvvLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1162 ECLSRSTLLCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQQlddttQLPLLSHFAE-TVEGLTTIR 1236
Cdd:cd18780    121 SMLLRYLVQIIGGLVFMFTTSWkltlVMLSVVPPLSIGAVIYGKYVRKLSKKFQD-----ALAAASTVAEeSISNIRTVR 195
                          170
                   ....*....|.
gi 1189438336 1237 AFRYEARFQQK 1247
Cdd:cd18780    196 SFAKETKEVSR 206
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
1474-1599 3.29e-05

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 47.87  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 EALEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKVV 1545
Cdd:TIGR01187   83 EALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDkklrdqMQLElkTIQEQLG 151
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1546 MtafadrTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:TIGR01187  152 I------TFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLFvARFI 201
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1366-1578 3.33e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 48.51  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYdsSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFS--LAFFRMVDTFEGHIIIDGIDIAKlPLHTLRSRL 1443
Cdd:PRK15439    12 LCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMkiIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLFSG-TIRFNL--------DPERKCSDstLWEALEiAQLKLVVKAlpGGLDAiiteggenfsqGQRQLFCLA 1514
Cdd:PRK15439    89 YLVPQEPLLFPNlSVKENIlfglpkrqASMQKMKQ--LLAALG-CQLDLDSSA--GSLEV-----------ADRQIVEIL 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336 1515 RAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK15439   153 RGLMRDSRILILDEPTASLTPAeTERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTI 218
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
718-979 3.80e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 48.24  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVF----WS-SLPDSEIGEDPSPERETATDLDIRKRgpva 792
Cdd:PRK10636    17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnWQlAWVNQETPALPQPALEYVIDGDREYR---- 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  793 yasQKPWLLNATVEENiifespfNKQRYKMV------IEACSLQPDIDILPHG---DQTQIGERGINLSGGQRQRISVAR 863
Cdd:PRK10636    93 ---QLEAQLHDANERN-------DGHAIATIhgkldaIDAWTIRSRAASLLHGlgfSNEQLERPVSDFSGGWRMRLNLAQ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  864 ALYQHANVVFLDDPFSALDihlsdhlMQAGI-LE-LLRDDKRTVVLVTHKLQYL-PHADWIIAMKDGTI-QREGTLKDFQ 939
Cdd:PRK10636   163 ALICRSDLLLLDEPTNHLD-------LDAVIwLEkWLKSYQGTLILISHDRDFLdPIVDKIIHIEQQSLfEYTGNYSSFE 235
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1189438336  940 RSECQLFEHWKTLMNRQDQELEK-ETVTER---KATEPPQGLSR 979
Cdd:PRK10636   236 VQRATRLAQQQAMYESQQERVAHlQSYIDRfraKATKAKQAQSR 279
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
720-935 4.31e-05

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 47.56  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSL--LLAALGEMQK----VSGAVfwssLPDSEIGEDPSPERetatdldiRKRGpvaY 793
Cdd:PRK11144    16 TVNLTLPAQGITAIFGRSGAGKTSLinAISGLTRPQKgrivLNGRV----LFDAEKGICLPPEK--------RRIG---Y 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLL-NATVEENIIFE-SPFNKQRYKMVIEACSLQPDIDILPhgdqtqigergINLSGGQRQRISVARALYQHANV 871
Cdd:PRK11144    81 VFQDARLFpHYKVRGNLRYGmAKSMVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPEL 149
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  872 VFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVL-VTHKLQYLPH-ADWIIAMKDGTIQREGTL 935
Cdd:PRK11144   150 LLMDEPLASLDLPRKRELLP--YLERLAREINIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPL 213
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
852-912 4.77e-05

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 47.41  E-value: 4.77e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALDIhlsdhLMQAGILELLRDDKR----TVVLVTHKL 912
Cdd:PRK09473   163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDV-----TVQAQIMTLLNELKRefntAIIMITHDL 222
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1366-1595 5.91e-05

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 224043 [Multi-domain]  Cd Length: 345  Bit Score: 46.96  E-value: 5.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHII-------IDGIDIAKLPLHt 1438
Cdd:COG1118      3 IRINNVKKRFGA--FGALDDISLDIKSGELVALLGPSGAGKSTL----LRIIAGLETPDAgrirlngRVLFDVSNLAVR- 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 lRSRLSIILQDPVLF-----SGTIRFNLD-----PERKCSDSTLWEALEIAQLKLVVKALPGGLdaiiteggenfSQGQR 1508
Cdd:COG1118     76 -DRKVGFVFQHYALFphmtvADNIAFGLKvrkerPSEAEIRARVEELLRLVQLEGLADRYPAQL-----------SGGQR 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1509 QLFCLARAFVRKTSIFIMDEATASIDMATENILQKvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKP 1584
Cdd:COG1118    144 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRR-WLRKLHDRlgvTTVFVTHDQEEALElADRVVVLNQGRIEQVGPP 222
                          250
                   ....*....|.
gi 1189438336 1585 EKLLSRKDSVF 1595
Cdd:COG1118    223 DEVYDHPASRF 233
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
1097-1311 6.02e-05

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 46.92  E-value: 6.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1097 IVLCLVTSVTVEWTGLK------VAKRLH---RSLLNR-IILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSR 1166
Cdd:cd18784     40 IIMGLLAIASSVAAGIRgglftlAMARLNiriRNLLFRsIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1167 STLLCVSALAVI---SYVTPVFLVALLPL-AIVCYFIQKYFRVASRDLQqlddtTQLPLLSHFA-ETVEGLTTIRAF--- 1238
Cdd:cd18784    120 SLVKAIGVIVFMfklSWQLSLVTLIGLPLiAIVSKVYGDYYKKLSKAVQ-----DSLAKANEVAeETISSIRTVRSFane 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1239 -----RYEARFQQ-------KLLEYTDSNNIASLFLTAanrwLEVRMEYIGACVVLIAAVTS---ISNSLHR-ELSAGLV 1302
Cdd:cd18784    195 dgeanRYSEKLKDtyklkikEALAYGGYVWSNELTELA----LTVSTLYYGGHLVITGQISGgnlISFILYQlELGSCLE 270
                          250
                   ....*....|
gi 1189438336 1303 GLGLTYA-LM 1311
Cdd:cd18784    271 SVGSVYTgLM 280
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
391-608 6.03e-05

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 46.65  E-value: 6.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  391 IQTKIYNKIMHLSTSNLSmgEMTAGQICNLVAIDTNQLMWFFF-LCPNLWAMPVQIIVGVILLYYI---LGVSALIGAAV 466
Cdd:cd18552     74 LRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTsALTVLVRDPLTVIGLLGVLFYLdwkLTLIALVVLPL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  467 IILlaPVQYFvATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENI----FRTRVETTRRKEMTSLRAFAIYTSI 542
Cdd:cd18552    152 AAL--PIRRI-GKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYeikrFRKANERLRRLSMKIARARALSSPL 228
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  543 SIFMnTAIPIAAVLItFVGHVSFfkEADFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQ 608
Cdd:cd18552    229 MELL-GAIAIALVLW-YGGYQVI--SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
846-933 7.70e-05

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 223473 [Multi-domain]  Cd Length: 251  Bit Score: 46.03  E-value: 7.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  846 ERGIN--LSGGQRQRISVARALYQHANVVFLDDPFSALDIhlsDHL-MQAGILELLRDDKRTVVLVTHKLQYLPH--ADW 920
Cdd:COG0396    138 ERYVNegFSGGEKKRNEILQLLLLEPKLAILDEPDSGLDI---DALkIVAEGINALREEGRGVLIITHYQRLLDYikPDK 214
                           90
                   ....*....|...
gi 1189438336  921 IIAMKDGTIQREG 933
Cdd:COG0396    215 VHVLYDGRIVKSG 227
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
714-927 8.56e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 47.03  E-value: 8.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEdpsperetatdldirkrgPVAY 793
Cdd:PRK10982    10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQ-------GK------------------EIDF 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWLLNA--------------TVEENIIF-----ESPFNKQRyKMVIEACSL--QPDIDILPHgdqtqigERGINLS 852
Cdd:PRK10982    65 KSSKEALENGismvhqelnlvlqrSVMDNMWLgryptKGMFVDQD-KMYRDTKAIfdELDIDIDPR-------AKVATLS 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  853 GGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKL-QYLPHADWIIAMKDG 927
Cdd:PRK10982   137 VSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFT--IIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1376-1600 9.06e-05

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 46.10  E-value: 9.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1376 DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLP---LHTLRS-RLSIILQDpv 1451
Cdd:cd03294     33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRkKISMVFQS-- 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1452 lfsgtirFNLDPERKCSDSTLWeALEIA-------------QLKLVvkALPGGLDAIITEggenFSQGQRQLFCLARAFV 1518
Cdd:cd03294    111 -------FALLPHRTVLENVAF-GLEVQgvpraereeraaeALELV--GLEGWEHKYPDE----LSGGMQQRVGLARALA 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1519 RKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLL-SRKDSV 1594
Cdd:cd03294    177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILtNPANDY 256

                   ....*.
gi 1189438336 1595 FASFVR 1600
Cdd:cd03294    257 VREFFR 262
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1366-1599 1.20e-04

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 45.31  E-value: 1.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK----LPLHtlRS 1441
Cdd:cd03300      1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAGFETPTSGEILLDGKditnLPPH--KR 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1442 RLSIILQDPVLF-----SGTIRFNLDpERKCSDSTLWEALEiAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARA 1516
Cdd:cd03300     73 PVNTVFQNYALFphltvFENIAFGLR-LKKLPKAEIKERVA-EALDLV------QLEGYANRKPSQLSGGQQQRVAIARA 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1517 FVRKTSIFIMDEATASIDMATENILQkVVMTAFADRTVVTIAHRVH----TILSADLVIVLKRGAILEFDKPEKLLSRKD 1592
Cdd:cd03300    145 LVNEPKVLLLDEPLGALDLKLRKDMQ-LELKRLQKELGITFVFVTHdqeeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223

                   ....*...
gi 1189438336 1593 SVF-ASFV 1599
Cdd:cd03300    224 NRFvADFI 231
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
846-942 1.25e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 46.93  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  846 ERGIN-LSGGQRQRISVARAL-YQHANVVF-LDDPfsALDIHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWII 922
Cdd:TIGR00630  483 SRAAGtLSGGEAQRIRLATQIgSGLTGVLYvLDEP--SIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVI 560
                           90       100
                   ....*....|....*....|....*.
gi 1189438336  923 AM------KDGTIQREGTLKDFQRSE 942
Cdd:TIGR00630  561 DIgpgageHGGEVVASGTPEEILANP 586
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
714-910 1.33e-04

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 45.98  E-value: 1.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  714 GIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdSEIGEdPSPERETATdldiRKRgpVAY 793
Cdd:PRK13536    53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-------TVLGV-PVPARARLA----RAR--IGV 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ASQKPWL-LNATVEENIIFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARALYQHANVV 872
Cdd:PRK13536   119 VPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSD----LSGGMKRRLTLARALINDPQLL 194
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1189438336  873 FLDDPFSALDIHlSDHLMQAGILELLRDDKrTVVLVTH 910
Cdd:PRK13536   195 ILDEPTTGLDPH-ARHLIWERLRSLLARGK-TILLTTH 230
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1366-1589 1.43e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 45.46  E-value: 1.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY----DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRM---------VDTFEGHIIIDgidia 1432
Cdd:PRK13633     5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALlipsegkvyVDGLDTSDEEN----- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1433 klpLHTLRSRLSIILQDP------------VLFsGTIRFNLDPE--RKCSDstlwEALEIAQLKLVVKALPGGLdaiite 1498
Cdd:PRK13633    80 ---LWDIRNKAGMVFQNPdnqivativeedVAF-GPENLGIPPEeiRERVD----ESLKKVGMYEYRRHAPHLL------ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1499 ggenfSQGQRQLFCLARAFVRKTSIFIMDEATASIDmateNILQKVVMTAFADR------TVVTIAHRVHTILSADLVIV 1572
Cdd:PRK13633   146 -----SGGQKQRVAIAGILAMRPECIIFDEPTAMLD----PSGRREVVNTIKELnkkygiTIILITHYMEEAVEADRIIV 216
                          250
                   ....*....|....*..
gi 1189438336 1573 LKRGAILEFDKPEKLLS 1589
Cdd:PRK13633   217 MDSGKVVMEGTPKEIFK 233
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
720-937 1.59e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 46.32  E-value: 1.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  720 NITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWSslpdseiGEDPSPEREtatdLDIRKRGpVAYASQKP- 798
Cdd:PRK09700   281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLN-------GKDISPRSP----LDAVKKG-MAYITESRr 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  799 ---WLLNATVEENIIFESPFNKQRYKMVI----------EACSLQPDIDILPHGDQTQIGErginLSGGQRQRISVARAL 865
Cdd:PRK09700   349 dngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWL 424
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1189438336  866 YQHANVVFLDDPFSALDIHlsdhlMQAGILELLR---DDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK09700   425 CCCPEVIIFDEPTRGIDVG-----AKAEIYKVMRqlaDDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRD 495
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1365-1589 1.66e-04

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 45.00  E-value: 1.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1365 KIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLS 1444
Cdd:PRK11231     2 TLRTENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1445 IILQDPVLFSG-TIRfNLDPERKCSDSTLWEALEIAQLKLVVKALPG-GLDAIITEGGENFSQGQRQLFCLARAFVRKTS 1522
Cdd:PRK11231    80 LLPQHHLTPEGiTVR-ELVAYGRSPWLSLWGRLSAEDNARVNQAMEQtRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1523 IFIMDEATASIDMATENILQKVV-MTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK11231   159 VVLLDEPTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVMT 227
PLN03211 PLN03211
ABC transporter G-25; Provisional
718-911 1.73e-04

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.03  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKvsgavfwSSLPDSEIGEDPSPERETatdldIRKRGpvaYASQK 797
Cdd:PLN03211    84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQG-------NNFTGTILANNRKPTKQI-----LKRTG---FVTQD 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLL-NATVEENIIFES----PFNKQRYKMVIEACSLQPDIDiLPHGDQTQIGE---RGInlSGGQRQRISVARALYQHA 869
Cdd:PLN03211   149 DILYpHLTVRETLVFCSllrlPKSLTKQEKILVAESVISELG-LTKCENTIIGNsfiRGI--SGGERKRVSIAHEMLINP 225
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1189438336  870 NVVFLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTHK 911
Cdd:PLN03211   226 SLLILDEPTSGLDATAAYRLVLT--LGSLAQKGKTIVTSMHQ 265
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1366-1589 1.77e-04

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 45.95  E-value: 1.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKPVLKHVNAL---IAPGQKIGICGRTGSGKSSFS--LA----------FFRM----VDTFEghiii 1426
Cdd:TIGR03269  280 IKVRNVSKRYISVDRGVVKAVDNVsleVKEGEIFGIVGTSGAGKTTLSkiIAgvleptsgevNVRVgdewVDMTK----- 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1427 dgidiaklPLHTLRSR----LSIILQDPVLFsgtirfnldPERKCSDStLWEAL------EIAQLKLVVKALPGGLD--- 1493
Cdd:TIGR03269  355 --------PGPDGRGRakryIGILHQEYDLY---------PHRTVLDN-LTEAIglelpdELARMKAVITLKMVGFDeek 416
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1494 --AIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVHTILS-AD 1568
Cdd:TIGR03269  417 aeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmeQTFIIVSHDMDFVLDvCD 496
                          250       260
                   ....*....|....*....|.
gi 1189438336 1569 LVIVLKRGAILEFDKPEKLLS 1589
Cdd:TIGR03269  497 RAALMRDGKIVKIGDPEEIVE 517
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
715-933 2.33e-04

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 45.56  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFWsslpdsEIGEDPsperetatdLDIRKRGPVAYA 794
Cdd:TIGR03269  297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV------RVGDEW---------VDMTKPGPDGRG 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  795 SQKPWL----------LNATVEEN----IIFESPFNKQRYKMVI----------EACSLqpdIDILPHgdqtqigergiN 850
Cdd:TIGR03269  362 RAKRYIgilhqeydlyPHRTVLDNlteaIGLELPDELARMKAVItlkmvgfdeeKAEEI---LDKYPD-----------E 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHANVVFLDDPFSALD----IHLSDHLMQAGIlELlrddKRTVVLVTHKLQY-LPHADWIIAMK 925
Cdd:TIGR03269  428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKARE-EM----EQTFIIVSHDMDFvLDVCDRAALMR 502

                   ....*...
gi 1189438336  926 DGTIQREG 933
Cdd:TIGR03269  503 DGKIVKIG 510
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
733-921 2.35e-04

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 45.70  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  733 IVGQVGCGKSSLLlaalgemqKVSGAVfwsslpDSEI-GED-PSPeretatdlDIRkrgpVAYASQKPWL-LNATVEENI 809
Cdd:TIGR03719   36 VLGLNGAGKSTLL--------RIMAGV------DKDFnGEArPQP--------GIK----VGYLPQEPQLdPTKTVRENV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  810 I-------------------FESP---FNKQRYKM-----VIEAC---SLQPDIDI------LPHGDQtQIGergiNLSG 853
Cdd:TIGR03719   90 EegvaeikdaldrfneisakYAEPdadFDKLAAEQaelqeIIDAAdawDLDSQLEIamdalrCPPWDA-DVT----KLSG 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336  854 GQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgilelLRDDKRTVVLVTHKLQYLPH-ADWI 921
Cdd:TIGR03719  165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERH-----LQEYPGTVVAVTHDRYFLDNvAGWI 228
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1356-1599 2.66e-04

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 45.21  E-value: 2.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1356 IPKNWPDQGK-----IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGID 1430
Cdd:PRK11607     5 IPRPQAKTRKaltplLEIRNLTKSFDG--QHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAGFEQPTAGQIML 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1431 IAKLPLHT--LRSRLSIILQDPVLF-----SGTIRFNLDPERKCSD---STLWEALEIAQLKLVVKALPGGLdaiitegg 1500
Cdd:PRK11607    79 DGVDLSHVppYQRPINMMFQSYALFphmtvEQNIAFGLKQDKLPKAeiaSRVNEMLGLVHMQEFAKRKPHQL-------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1501 enfSQGQRQLFCLARAFVRKTSIFIMDEATASID------MATE--NILQKV----VMTAFADRTVVTIAHRvhtilsad 1568
Cdd:PRK11607   151 ---SGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrMQLEvvDILERVgvtcVMVTHDQEEAMTMAGR-------- 219
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1189438336 1569 lVIVLKRGAILEFDKPEKLLSRKDSVF-ASFV 1599
Cdd:PRK11607   220 -IAIMNRGKFVQIGEPEEIYEHPTTRYsAEFI 250
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
1108-1255 2.68e-04

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 44.73  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1108 EWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALAVISYVTPVF-L 1186
Cdd:cd18542     64 EKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLtL 143
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1187 VALLPLAIVCYFIQKYFRVASRDLQQLDDttQLPLLSHFA-ETVEGLTTIRAF---RYE-ARFQQKLLEYTDSN 1255
Cdd:cd18542    144 ISLAIIPFIALFSYVFFKKVRPAFEEIRE--QEGELNTVLqENLTGVRVVKAFareDYEiEKFDKENEEYRDLN 215
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
718-884 2.71e-04

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 45.31  E-value: 2.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdsEIGE--------------DPSPE--RETAT 781
Cdd:TIGR03719  338 IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI--------EIGEtvklayvdqsrdalDPNKTvwEEISG 409
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  782 DLDIRKRGPV-----AYASQkpwllnatveeniifespFNkqrYKmvieacslqpdidilpHGDQTQ-IGErginLSGGQ 855
Cdd:TIGR03719  410 GLDIIKLGKReipsrAYVGR------------------FN---FK----------------GSDQQKkVGQ----LSGGE 448
                          170       180
                   ....*....|....*....|....*....
gi 1189438336  856 RQRISVARALYQHANVVFLDDPFSALDIH 884
Cdd:TIGR03719  449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
1083-1202 3.00e-04

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 44.77  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTID----QHIP 1158
Cdd:cd18577     47 NKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQdgigEKLG 126
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1189438336 1159 STLECLSrstlLCVSALaVISYV---------TPVFLVALLPLAIVCYFIQKY 1202
Cdd:cd18577    127 LLIQSLS----TFIAGF-IIAFIyswkltlvlLATLPLIAIVGGIMGKLLSKY 174
cbiO PRK13637
energy-coupling factor transporter ATPase;
1366-1578 3.18e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 44.65  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSL---KPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFR---------MVDTFEGHIIidgidiaK 1433
Cdd:PRK13637     3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGllkptsgkiIIDGVDITDK-------K 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHTLRSRLSIILQDP--VLFSGT----IRF---NLDPERKCSDSTLWEALEIAQLKlvvkalpggLDAIITEGGENFS 1504
Cdd:PRK13637    76 VKLSDIRKKVGLVFQYPeyQLFEETiekdIAFgpiNLGLSEEEIENRVKRAMNIVGLD---------YEDYKDKSPFELS 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1505 QGQRQLFCLARAFVRKTSIFIMDEATASID-MATENILQKV-VMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK13637   147 GGQKRRVAIAGVVAMEPKILILDEPTAGLDpKGRDEILNKIkELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKC 223
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
851-925 3.75e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 42.73  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALyQHANV-----VFLDDPFSALDIHLSDHLMQAgILELLrDDKRTVVLVTHKLQYLPHADWIIAMK 925
Cdd:cd03227     78 LSGGEKELSALALIL-ALASLkprplYILDEIDRGLDPRDGQALAEA-ILEHL-VKGAQVIVITHLPELAELADKLIHIK 154
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1366-1589 3.81e-04

ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226929 [Multi-domain]  Cd Length: 259  Bit Score: 43.88  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:COG4559      2 IRAENLSYSLAG--RRLLDGVSLDLRPGEVLAILGPNGAGKSTLLKALSGELSPDSGEVTLNGVPLNSWPPEELARHRAV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVL-FSGT----IRFNLDPERKCSDSTLWEALEIAQLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRK 1520
Cdd:COG4559     80 LPQNSSLaFPFTvqevVQMGRIPHRSGREPEEDERIAAQALAAT------DLSGLAGRDYRTLSGGEQQRVQLARVLAQL 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1521 T------SIFIMDEATASIDMA-TENILQkvVMTAFADR--TVVTIAHRVH-TILSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:COG4559    154 WppvpsgRWLFLDEPTSALDIAhQHHTLR--LARQLAREggAVLAVLHDLNlAAQYADRIVLLHQGRVIASGSPQDVLT 230
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1392-1585 4.11e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.36  E-value: 4.11e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  1392 PGQKIGICGRTGSGKSSFSLAFFRMVDtfeghiiidgidiaklplhtlrsrlsiilqdpVLFSGTIRFNLDPERKCSDST 1471
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELG--------------------------------PPGGGVIYIDGEDILEEVLDQ 48
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  1472 LWEAleiaqlklvvkalpggldaIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAF-- 1549
Cdd:smart00382   49 LLLI-------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLll 109
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1189438336  1550 -----ADRTVVTIAHRVHTILSADLVIVLKRgaILEFDKPE 1585
Cdd:smart00382  110 llkseKNLTVILTTNDEKDLGPALLRRRFDR--RIVLLLIL 148
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
715-937 4.26e-04

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224057 [Multi-domain]  Cd Length: 249  Bit Score: 43.76  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  715 IPTLSNITIRIPRGQLTMIVGQVGCGKSSLLlaalgemQKVSGAVFwsslPDSeiGEdpsperetatdldIRKRGPVAY- 793
Cdd:COG1134     40 FWALKDISFEIYKGERVGIIGHNGAGKSTLL-------KLIAGIYK----PTS--GK-------------VKVTGKVAPl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  794 ----ASQKPwllNATVEENIIFESPF-------NKQRYKMVIEACSLQPDIDilphgdqTQIGergiNLSGGQRQRISVA 862
Cdd:COG1134     94 ielgAGFDP---ELTGRENIYLRGLIlgltrkeIDEKVDEIIEFAELGDFID-------QPVK----TYSSGMYARLAFS 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  863 RALYQHANVVFLDDPFSALDIHLSDHlMQAGILELLRDDKrTVVLVTHKLQYLphADW---IIAMKDGTIQREGTLKD 937
Cdd:COG1134    160 VATHVEPDILLLDEVLAVGDAAFQEK-CLERLNELVEKNK-TIVLVSHDLGAI--KQYcdrAIWLEHGQIRMEGSPEE 233
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1366-1592 4.27e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 44.02  E-value: 4.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:PRK13652     4 IETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDP--VLFS---------GTIRFNLDPErkcsdsTLWEALEIAqLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLA 1514
Cdd:PRK13652    83 VFQNPddQIFSptveqdiafGPINLGLDEE------TVAHRVSSA-LHML------GLEELRDRVPHHLSGGEKKRVAIA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1515 RAFVRKTSIFIMDEATASID-MATENILQkvVMTAFADR---TVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK13652   150 GVIAMEPQVLVLDEPTAGLDpQGVKELID--FLNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFL 227

                   ...
gi 1189438336 1590 RKD 1592
Cdd:PRK13652   228 QPD 230
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1366-1582 5.02e-04

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 43.01  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAKL-----PLHtlR 1440
Cdd:cd03301      1 VELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAGLEEPTSGRIYIGGRDvtdlpPKD--R 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1441 SrLSIILQDPVLFS-----GTIRFNLD----PERKCSDSTLWEAlEIAQLKLVVKALPGGLdaiiteggenfSQGQRQLF 1511
Cdd:cd03301     73 D-IAMVFQNYALYPhmtvyDNIAFGLKlrkvPKDEIDERVREVA-ELLQIEHLLDRKPKQL-----------SGGQRQRV 139
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1189438336 1512 CLARAFVRKTSIFIMDEATASID------MATE-NILQKVVmtafaDRTVVTIAH-RVHTILSADLVIVLKRGAILEFD 1582
Cdd:cd03301    140 ALGRAIVREPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1362-1592 5.02e-04

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224060 [Multi-domain]  Cd Length: 243  Bit Score: 43.35  E-value: 5.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1362 DQGKIQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTF----EGHIIIDGIDIAKLPLH 1437
Cdd:COG1137      1 DMSTLVAENLAKSYKK--RKVVNDVSLEVNSGEIVGLLGPNGAGKTTT----FYMIVGLvrpdSGKILLDDEDITKLPMH 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1438 tLRSRLSI--ILQDPVLFSG-TIRFNLD------------PERKCSDSTLWEALEIAQLKlvvKALPGGLdaiiteggen 1502
Cdd:COG1137     75 -KRARLGIgyLPQEASIFRKlTVEDNIMavleirekdlkkAERKEELDALLEEFHITHLR---DSKAYSL---------- 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1503 fSQGQRQLFCLARAFVRKTSIFIMDEATASID-MATENIlQKVVmTAFADRTV-VTIA-HRVHTILS-ADLVIVLKRGAI 1578
Cdd:COG1137    141 -SGGERRRVEIARALAANPKFILLDEPFAGVDpIAVIDI-QRII-KHLKDRGIgVLITdHNVRETLDiCDRAYIISDGKV 217
                          250
                   ....*....|....
gi 1189438336 1579 LEFDKPEKLLSRKD 1592
Cdd:COG1137    218 LAEGSPEEIVNNED 231
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1390-1572 5.12e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 43.42  E-value: 5.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1390 IAPGQKIGICGRTGSGKSSF-SL-AFFRMVDTfeghiiidgidiAKLPL----HTL----RSRLSIILQDPVLFSG-TIR 1458
Cdd:PRK10771    22 VERGERVAILGPSGAGKSTLlNLiAGFLTPAS------------GSLTLngqdHTTtppsRRPVSMLFQENNLFSHlTVA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1459 FN----LDPERKCSDSTLWEALEIAQ---LKLVVKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATA 1531
Cdd:PRK10771    90 QNiglgLNPGLKLNAAQREKLHAIARqmgIEDLLARLPGQL-----------SGGQRQRVALARCLVREQPILLLDEPFS 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1189438336 1532 SIDMATENILQKVVMTAFADR--TVVTIAHRV---HTILSADLVIV 1572
Cdd:PRK10771   159 ALDPALRQEMLTLVSQVCQERqlTLLMVSHSLedaARIAPRSLVVA 204
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1366-1579 5.38e-04

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 43.19  E-value: 5.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSsLKpVLKHVNALIAPGQKIGICGRTGSGKSS-FSL-----------AFFRMVDTfeghiiidgidiAK 1433
Cdd:cd03219      1 LEVRGLTKRFGG-LV-ALDDVSFSVRPGEIHGLIGPNGAGKTTlFNLisgflrptsgsVLFDGEDI------------TG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1434 LPLHtLRSRLSII--LQDPVLFSG-TIRFNL-------------DPERKCSDSTLWE-ALEIaqLKLVvkalpgGLDAII 1496
Cdd:cd03219     67 LPPH-EIARLGIGrtFQIPRLFPElTVLENVmvaaqartgsgllLARARREEREARErAEEL--LERV------GLADLA 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1497 TEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLK 1574
Cdd:cd03219    138 DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLD 217

                   ....*
gi 1189438336 1575 RGAIL 1579
Cdd:cd03219    218 QGRVI 222
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
445-561 5.69e-04

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 43.65  E-value: 5.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  445 IIVGVILLYY--ILGVSALIGAAVIILLApvqYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLK--------LYAW 514
Cdd:cd18555    130 VIYLIYMLYYspLLTLIVLLLGLLIVLLL---LLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKslgsekniYKKW 206
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1189438336  515 ENIFRTRVETTRRKEMTSlrafAIYTSISIFMNTAIPIaavLITFVG 561
Cdd:cd18555    207 ENLFKKQLKAFKKKERLS----NILNSISSSIQFIAPL---LILWIG 246
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
718-912 5.82e-04

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 43.56  E-value: 5.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  718 LSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQkvsgavfwsslPDSEIGEDPSPERetatdldirkrgpVAYASQK 797
Cdd:PRK09544    20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA-----------PDEGVIKRNGKLR-------------IGYVPQK 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  798 PWLlNATVeeniifesPFNKQRYKMvieacsLQPDI---DILPHGDQTQIGERgIN-----LSGGQRQRISVARALYQHA 869
Cdd:PRK09544    76 LYL-DTTL--------PLTVNRFLR------LRPGTkkeDILPALKRVQAGHL-IDapmqkLSGGETQRVLLARALLNRP 139
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1189438336  870 NVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRT----VVLVTHKL 912
Cdd:PRK09544   140 QLLVLDEPTQGVDVN-----GQVALYDLIDQLRREldcaVLMVSHDL 181
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1363-1593 9.49e-04

ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226961 [Multi-domain]  Cd Length: 256  Bit Score: 42.80  E-value: 9.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1363 QGKIQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSfslaFFRMVDTFEG-----------------HII 1425
Cdd:COG4598      4 ENALEVEDLHKRYGEH--EVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFLEKpsagsirvngeeirlkrDKD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1426 IDGIDIAKLPLHTLRSRLSIILQDpvlfsgtirFNLDPERKCSDSTL-----------WEALEIAQlKLVVKAlpgGLDA 1494
Cdd:COG4598     78 GQLKPADKRQLQRLRTRLGMVFQH---------FNLWSHMTVLENVIeapvhvlgvskAEAIERAE-KYLAKV---GIAE 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1495 IITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDmatENILQKV--VMTAFAD--RTVVTIAHRVHTILS-ADL 1569
Cdd:COG4598    145 KADAYPAHLSGGQQQRVAIARALAMEPEVMLFDEPTSALD---PELVGEVlkVMQDLAEegRTMVVVTHEMGFARDvSSH 221
                          250       260
                   ....*....|....*....|....
gi 1189438336 1570 VIVLKRGAILEFDKPEKLLSRKDS 1593
Cdd:COG4598    222 VIFLHQGKIEEEGPPEQVFGNPQS 245
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1366-1592 1.11e-03

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 42.91  E-value: 1.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSLKpVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRL 1443
Cdd:PRK13636     6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpsSGRILFDGKPIDYSRKGLMKLRESV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDP--VLFSGTIRFNLdperkcsdstlweALEIAQLKLVVKALPGGLDAIITEGG---------ENFSQGQRQLFC 1512
Cdd:PRK13636    85 GMVFQDPdnQLFSASVYQDV-------------SFGAVNLKLPEDEVRKRVDNALKRTGiehlkdkptHCLSFGQKKRVA 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1513 LARAFVRKTSIFIMDEATASID-MATENILQKVVMTAFA-DRTVVTIAHRVHTI-LSADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:PRK13636   152 IAGVLVMEPKVLVLDEPTAGLDpMGVSEIMKLLVEMQKElGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFA 231

                   ...
gi 1189438336 1590 RKD 1592
Cdd:PRK13636   232 EKE 234
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
1117-1248 1.21e-03

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 42.85  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1117 RLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIdQHIPSTLECLSRSTLLCVSALAVISYVTP----VFLVALLPL 1192
Cdd:cd18543     73 DLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLV-QRFLAFGPFLLGNLLTLVVGLVVMLVLSPplalVALASLPPL 151
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1193 AIVCYFIQKYFRVASRDLQQL--DDTTqlpllsHFAETVEGLTTIRAFRYEARFQQKL 1248
Cdd:cd18543    152 VLVARRFRRRYFPASRRAQDQagDLAT------VVEESVTGIRVVKAFGRERRELDRF 203
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
846-912 1.25e-03

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 43.26  E-value: 1.25e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  846 ERGI-NLSGGQRQRISVARALYQHANVVFLDDPFSALDIH--LSdhlMQAGILELLRDdkRTVVLVTHKL 912
Cdd:PRK13409   207 DRDIsELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrLN---VARLIRELAEG--KYVLVVEHDL 271
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1366-1409 1.34e-03

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 42.45  E-value: 1.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1409
Cdd:PRK13548     3 LEARNLSVRLGG--RTLLDDVSLTLRPGEVVAILGPNGAGKSTL 44
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
1083-1254 1.35e-03

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 42.58  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1083 TVYAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIPSTLE 1162
Cdd:cd18782     42 YVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTAL 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1163 CLSRSTLLCVSALAV-ISYVTPVFLVAL--LPLAIVCYF---------IQKYFRVASRdlqqlddtTQlpllSHFAETVE 1230
Cdd:cd18782    121 TTLLDVLFSVIYIAVlFSYSPLLTLVVLatVPLQLLLTFlfgpilrrqIRRRAEASAK--------TQ----SYLVESLT 188
                          170       180
                   ....*....|....*....|....*
gi 1189438336 1231 GLTTIRAFRYEARFQQKLLE-YTDS 1254
Cdd:cd18782    189 GIQTVKAQNAELKARWRWQNrYARS 213
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
730-910 1.53e-03

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 41.87  E-value: 1.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  730 LTMIVGQVGCGKSSLLLAalgemqkVSGAVFwsslpdseiGEDPSPERETATDLDIrkrgpvayasqkpwllnATVEE-- 807
Cdd:cd03279     30 LFLICGPTGAGKSTILDA-------ITYALY---------GKTPRYGRQENLRSVF-----------------APGEDta 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  808 NIIFESPFNKQRYKmVIEACSLQPD----IDILPHGDQTQIGERGI-NLSGGQRQRISVARAL------YQHANVV---- 872
Cdd:cd03279     77 EVSFTFQLGGKKYR-VERSRGLDYDqftrIVLLPQGEFDRFLARPVsTLSGGETFLASLSLALalsevlQNRGGARleal 155
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1189438336  873 FLDDPFSALDIHLSDHLMQAgiLELLRDDKRTVVLVTH 910
Cdd:cd03279    156 FIDEGFGTLDPEALEAVATA--LELIRTENRMVGVISH 191
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1366-1599 1.56e-03

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 41.94  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSSlkPVLKHVNALIAPGQKIGICGRTGSGKSSFslafFRMVDTFEGHIIIDGIDIAK-LPLHTLRSR-L 1443
Cdd:cd03296      3 IEVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAGLERPDSGTILFGGEdATDVPVQERnV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1444 SIILQDPVLF-----SGTIRFNLDPERKcsdSTLWEALEIAQ-----LKLVvkalpgGLDAIITEGGENFSQGQRQLFCL 1513
Cdd:cd03296     77 GFVFQHYALFrhmtvFDNVAFGLRVKPR---SERPPEAEIRAkvhelLKLV------QLDWLADRYPAQLSGGQRQRVAL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1514 ARAFVRKTSIFIMDEATASIDMATENILQKVVmTAFADRTVVT---IAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLS 1589
Cdd:cd03296    148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWL-RRLHDELHVTtvfVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYD 226
                          250
                   ....*....|.
gi 1189438336 1590 RKDSVF-ASFV 1599
Cdd:cd03296    227 HPASPFvYSFL 237
YufO COG3845
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
712-945 1.71e-03

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 226364 [Multi-domain]  Cd Length: 501  Bit Score: 42.92  E-value: 1.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  712 PDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVFwsslpdseIGEDPSPERETATDldIRKRGpV 791
Cdd:COG3845    268 RRGVTAVKDVSFEVRAGEIVGIAGVAGNGQSELVEAISGLRKPASGRIL--------LNGKDVLGRLSPRE--RRRLG-L 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  792 AYA----SQKPWLLNATVEENIIFESPFNKQRYK------MVIEACS--LQPDIDILPHGDQTQIGergiNLSGGQRQRI 859
Cdd:COG3845    337 AYVpedrHGHGLVLDLSLAENLVLGRHDKKPFSRggfldrRAIRKFAreLIEEFDVRAPSPDAPAR----SLSGGNQQKL 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  860 SVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILElLRDDKRTVVLVTHKL-QYLPHADWIIAMKDGTIQREGTLKDF 938
Cdd:COG3845    413 ILARELARRPDLLIAAQPTRGLDVGAIEFIHER-LLE-LRDAGKAVLLISEDLdEILELSDRIAVIYEGRIVGIVPPEEA 490

                   ....*..
gi 1189438336  939 QRSECQL 945
Cdd:COG3845    491 TREEIGL 497
PLN03211 PLN03211
ABC transporter G-25; Provisional
1380-1594 1.79e-03

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 42.94  E-value: 1.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1380 KPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlplHTLRsRLSIILQDPVLFSG-T 1456
Cdd:PLN03211    81 RTILNGVTGMASPGEILAVLGPSGSGKSTLlnALAGRIQGNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYPHlT 156
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1457 IRFNLdpeRKCSDSTLWEALEiAQLKLVVKalpgglDAIITEGG----EN----------FSQGQRQLFCLARAFVRKTS 1522
Cdd:PLN03211   157 VRETL---VFCSLLRLPKSLT-KQEKILVA------ESVISELGltkcENtiignsfirgISGGERKRVSIAHEMLINPS 226
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1523 IFIMDEATASID-MATENILQKVVMTAFADRTVVTIAH----RVHTILsaDLVIVLKRGAILEFDKPEKLLSRKDSV 1594
Cdd:PLN03211   227 LLILDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHqpssRVYQMF--DSVLVLSEGRCLFFGKGSDAMAYFESV 301
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1366-1590 1.95e-03

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 226963 [Multi-domain]  Cd Length: 252  Bit Score: 41.91  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSI 1445
Cdd:COG4604      2 ITIENVSKSYGT--KVVLDDVSLDIPKGGITSIIGPNGAGKSTLLSMMSRLLKKDSGEITIDGLELTSTPSKELAKKLSI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1446 ILQDPVLFSG-TI--------------RFNLDPERKCSDSTlwEALEIAQLKlvvkalpgglDAIITEggenFSQGQRQL 1510
Cdd:COG4604     80 LKQENHINSRlTVrdlvgfgrfpysqgRLTKEDRRIINEAI--EYLHLEDLS----------DRYLDE----LSGGQRQR 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1511 FCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVH-TILSADLVIVLKRGAILEFDKPEKL 1587
Cdd:COG4604    144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQIMKILRRLADElgKTIVVVLHDINfASCYSDHIVALKNGKVVKQGSPDEI 223

                   ...
gi 1189438336 1588 LSR 1590
Cdd:COG4604    224 IQP 226
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
1085-1247 2.06e-03

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 42.05  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1085 YAMVFTVLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFF---ETTPlGSILNRFSSDCNTI----DQHI 1157
Cdd:cd18578     54 WALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddpENST-GALTSRLSTDASDVrglvGDRL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1158 PSTLECLsrSTLLCVSALAVISY--VTPVfLVALLPLAIVCYFIQKYF--RVASRDLQQLDDTTQLpllshFAETVEGLT 1233
Cdd:cd18578    133 GLILQAI--VTLVAGLIIAFVYGwkLALV-GLATVPLLLLAGYLRMRLlsGFEEKNKKAYEESSKI-----ASEAVSNIR 204
                          170
                   ....*....|....
gi 1189438336 1234 TIRAFRYEARFQQK 1247
Cdd:cd18578    205 TVASLTLEDYFLEK 218
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
838-957 2.13e-03

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 42.46  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  838 HGDQ-TQIGERginLSGGQRQRISVARALYQHANVVFLDDPFSALDIHlsdhlMQAGILELLRDDKRTVVLVTHKLQYL- 915
Cdd:PRK10636   420 QGDKvTEETRR---FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD-----MRQALTEALIDFEGALVVVSHDRHLLr 491
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1189438336  916 PHADWIIAMKDGTIQR-EGTLKDFQRsecqlfehWKTLMNRQD 957
Cdd:PRK10636   492 STTDDLYLVHDGKVEPfDGDLEDYQQ--------WLSDVQKQE 526
uvrA PRK00349
excinuclease ABC subunit UvrA;
851-934 2.22e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 42.75  E-value: 2.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  851 LSGGQRQRISVARALYQHAN---VVFLDDPFSAL---DIHlsdHLMQagILELLRDDKRTVVLVTHKLQYLPHADWIIAM 924
Cdd:PRK00349   831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIR---KLLE--VLHRLVDKGNTVVVIEHNLDVIKTADWIIDL 905
                           90
                   ....*....|....*.
gi 1189438336  925 ------KDGTIQREGT 934
Cdd:PRK00349   906 gpeggdGGGEIVATGT 921
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1366-1409 2.28e-03

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 42.62  E-value: 2.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1189438336 1366 IQIQNLSVRYDSSlKPVLKHVNALIAPGQKIGICGRTGSGKSSF 1409
Cdd:COG0488    322 LEFENVSKGYDGG-RLLLKDLSFRIDRGDRIAIVGPNGAGKSTL 364
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1398-1600 2.30e-03

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226643 [Multi-domain]  Cd Length: 386  Bit Score: 42.37  E-value: 2.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1398 ICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLR----SRLSIILQdpvlfsgtiRFNLDPERKCSDSTLW 1473
Cdd:COG4175     59 IMGLSGSGKSTLVRLLNRLIEPTRGEILVDGKDIAKLSAAELRelrrKKISMVFQ---------SFALLPHRTVLENVAF 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1474 ----------EALEIA--QLKLVvkalpgGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASID------M 1535
Cdd:COG4175    130 glevqgvpkaEREERAleALELV------GLEGYADKYPNELSGGMQQRVGLARALANDPDILLMDEAFSALDplirteM 203
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336 1536 ATENI-LQKVVmtafaDRTVVTIAHRVHTILS-ADLVIVLKRGAILEFDKPEKLLSR-KDSVFASFVR 1600
Cdd:COG4175    204 QDELLeLQAKL-----KKTIVFITHDLDEALRiGDRIAIMKDGEIVQVGTPEEILLNpANDYVRDFVR 266
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
844-935 2.34e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  844 IGERGINLSGGQRQRISVARALY---QHANVVFLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADW 920
Cdd:PRK00635  1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLV--QLRTLVSLGHSVIYIDHDPALLKQADY 1770
                           90
                   ....*....|....*
gi 1189438336  921 IIAMKDGTIQREGTL 935
Cdd:PRK00635  1771 LIEMGPGSGKTGGKI 1785
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1366-1580 2.39e-03

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 41.66  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSF--SLAFFRMVDTFEGHIIIDGIDIAKlPL------- 1436
Cdd:PRK11264     4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrCINLLEQPEAGTIRVGDITIDTAR-SLsqqkgli 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1437 HTLRSRLSIILQDpvlfsgtirFNLDPERKcsdstlweALE-IAQLKLVVKALPGG---------LDAIITEGGEN---- 1502
Cdd:PRK11264    81 RQLRQHVGFVFQN---------FNLFPHRT--------VLEnIIEGPVIVKGEPKEeatararelLAKVGLAGKETsypr 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1503 -FSQGQRQLFCLARAFVRKTSIFIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVHTILS-ADLVIVLKRGAI 1578
Cdd:PRK11264   144 rLSGGQQQRVAIARALAMRPEVILFDEPTSALDpeLVGE-VLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQGRI 222

                   ..
gi 1189438336 1579 LE 1580
Cdd:PRK11264   223 VE 224
PLN03073 PLN03073
ABC transporter F family; Provisional
852-915 2.66e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.54  E-value: 2.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1189438336  852 SGGQRQRISVARALYQHANVVFLDDPFSALDIH----LSDHLMQAgilellrddKRTVVLVTHKLQYL 915
Cdd:PLN03073   346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwLETYLLKW---------PKTFIVVSHAREFL 404
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
849-930 2.69e-03

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 42.27  E-value: 2.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  849 INLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGT 928
Cdd:PRK10522   448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV-LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526

                   ..
gi 1189438336  929 IQ 930
Cdd:PRK10522   527 LS 528
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1373-1573 2.79e-03

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 41.24  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1373 VRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDTFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVL 1452
Cdd:PRK10247    13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1453 FSGTIRFNL-----------DPERKCSDstlwealeiaqlkLVVKALPgglDAIITEGGENFSQGQRQLFCLARAFVRKT 1521
Cdd:PRK10247    93 FGDTVYDNLifpwqirnqqpDPAIFLDD-------------LERFALP---DTILTKNIAELSGGEKQRISLIRNLQFMP 156
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1189438336 1522 SIFIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVHTILSADLVIVL 1573
Cdd:PRK10247   157 KVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
725-912 2.93e-03

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 224166 [Multi-domain]  Cd Length: 591  Bit Score: 42.28  E-value: 2.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  725 IPRGQLTMIVGQVGCGKSSLLLAALGEMQKVSGAVfwsslpdseigedpsperetaTDLDIrkrgpvayaSQKPWLL--- 801
Cdd:COG1245    364 IYDGEVIGILGPNGIGKTTFVKLLAGVIKPDEGSE---------------------EDLKV---------SYKPQYIspd 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  802 -NATVEENI--IFESPFNKQRYKM-VIEACSLQPDIDilphgdqtqigERGINLSGGQRQRISVARALYQHANVVFLDDP 877
Cdd:COG1245    414 yDGTVEDLLrsAIRSAFGSSYFKTeIVKPLNLEDLLE-----------RPVDELSGGELQRVAIAAALSREADLYLLDEP 482
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1189438336  878 FSALDIhlSDHLMQA-GILELLRDDKRTVVLVTHKL 912
Cdd:COG1245    483 SAYLDV--EQRIIVAkVIRRFIENNEKTALVVDHDI 516
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
1111-1255 3.06e-03

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 41.38  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1111 GLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCntidQHIPSTLE-CLS---RSTLL---CVSALAVISYVTP 1183
Cdd:cd18574     70 GERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV----QEFKSSFKqCVSqglRSVTQtvgCVVSLYLISPKLT 145
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1189438336 1184 VFLVALLPLAIVC-YFIQKYFRVASRDLQQLDDTTqlplLSHFAETVEGLTTIRAFRYEAR----FQQKLLEYTDSN 1255
Cdd:cd18574    146 LLLLVIVPVVVLVgTLYGSFLRKLSRRAQAQVAKA----TGVADEALGNIRTVRAFAMEDRelelYEEEVEKAAKLN 218
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
1079-1247 3.36e-03

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 41.41  E-value: 3.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1079 TLDQTVYAMVFTVLCSlgIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFsSDCNTIDQHIP 1158
Cdd:cd18566     40 TLQVLVIGVVIAILLE--SLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLT 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1159 stleclSRSTLLCVSALAVISYVTPVF----------LVALLPLAIVCYFIQKYFRVASRDLQQLDDTTQlpllSHFAET 1228
Cdd:cd18566    117 ------GQALLALLDLPFVLIFLGLIWylggklvlvpLVLLGLFVLVAILLGPILRRALKERSRADERRQ----NFLIET 186
                          170
                   ....*....|....*....
gi 1189438336 1229 VEGLTTIRAFRYEARFQQK 1247
Cdd:cd18566    187 LTGIHTIKAMAMEPQMLRR 205
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
846-922 3.68e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.12  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  846 ERGIN-LSGGQRQRISVARALYQHANVV--FLDDPFSALDIHLSDHLMQagILELLRDDKRTVVLVTHKLQYLPHADWII 922
Cdd:PRK00635   471 ERALAtLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLIN--VIKKLRDQGNTVLLVEHDEQMISLADRII 548
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1388-1543 4.26e-03

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 40.36  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1388 ALIAPGQKIGICGRTGSGKSSF--SLAFFRMVD--TFEGHIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSG-TIRFNL- 1461
Cdd:cd03297     18 DFDLNEEVTGIFGASGAGKSTLlrCIAGLEKPDggTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHlNVRENLa 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1462 -------DPERKCSDSTLWEALEIAQLKlvvKALPGGLdaiiteggenfSQGQRQLFCLARAFVRKTSIFIMDEATASID 1534
Cdd:cd03297     98 fglkrkrNREDRISVDELLDLLGLDHLL---NRYPAQL-----------SGGEKQRVALARALAAQPELLLLDEPFSALD 163

                   ....*....
gi 1189438336 1535 MATENILQK 1543
Cdd:cd03297    164 RALRLQLLP 172
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
378-561 4.28e-03

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 40.84  E-value: 4.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  378 YVAIETGINLRgaiqTKIYNKIMHLSTSNlsMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAM-PVQIIVGVILLYYIL 456
Cdd:cd18548     65 KASQGFGRDLR----KDLFEKIQSFSFAE--IDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRaPIMLIGAIIMAFRIN 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  457 GVSALIGAAVIILLAPVQYFVATK---LSQAQRSTLEYSNERLKqtnEMLRGIKLLKLYAWENIFRTRVETTRRKEM-TS 532
Cdd:cd18548    139 PKLALILLVAIPILALVVFLIMKKaipLFKKVQKKLDRLNRVVR---ENLTGIRVIRAFNREDYEEERFDKANDDLTdTS 215
                          170       180
                   ....*....|....*....|....*....
gi 1189438336  533 LRAFAIYTSISIFMNTAIPIAAVLITFVG 561
Cdd:cd18548    216 LKAGRLMALLNPLMMLIMNLAIVAILWFG 244
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1366-1535 6.59e-03

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 40.44  E-value: 6.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1366 IQIQNLSVRY-------DSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSfsLAffRMVDTFEGHIIIDGIDIAKlPLHT 1438
Cdd:PRK10419     4 LNVSGLSHHYahgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKST--LA--RLLVGLESPSQGNVSWRGE-PLAK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1439 L--------RSRLSIILQDP---VLFSGTIRFNLD-PERKCSDstLWEALEIAQLKLVVKALpgGLDA-IITEGGENFSQ 1505
Cdd:PRK10419    79 LnraqrkafRRDIQMVFQDSisaVNPRKTVREIIRePLRHLLS--LDKAERLARASEMLRAV--DLDDsVLDKRPPQLSG 154
                          170       180       190
                   ....*....|....*....|....*....|
gi 1189438336 1506 GQRQLFCLARAFVRKTSIFIMDEATASIDM 1535
Cdd:PRK10419   155 GQLQRVCLARALAVEPKLLILDEAVSNLDL 184
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
1091-1266 6.71e-03

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 40.46  E-value: 6.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1091 VLCSLGIVLC-LVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTL 1169
Cdd:cd18548     46 LLLALLGLIAgILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPI 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336 1170 LCVSALAVISYVTP----VFLVALLPLAIVCYFIQKYFRVASRDLQ-QLDDTTQLpllshFAETVEGLTTIRAF---RYE 1241
Cdd:cd18548    126 MLIGAIIMAFRINPklalILLVAIPILALVVFLIMKKAIPLFKKVQkKLDRLNRV-----VRENLTGIRVIRAFnreDYE 200
                          170       180
                   ....*....|....*....|....*.
gi 1189438336 1242 -ARFQQKLLEYTDsNNIASLFLTAAN 1266
Cdd:cd18548    201 eERFDKANDDLTD-TSLKAGRLMALL 225
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
839-927 8.23e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.48  E-value: 8.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  839 GDQTQIGergiNLSGGQRQRISVARALYQHANVVFLDDPFSALDIHLSDHLMQAgILELLRDDKRTVVLVTHKLQYLPHA 918
Cdd:PRK10982   384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQL-IAELAKKDKGIIIISSEMPELLGIT 458

                   ....*....
gi 1189438336  919 DWIIAMKDG 927
Cdd:PRK10982   459 DRILVMSNG 467
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
846-937 8.48e-03

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 39.92  E-value: 8.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1189438336  846 ERGIN-LSGGQRQRISVARALYQ-------HANVVFLDDPFSALDI-------HLSDHLMQAGIlellrddkrTVVLVTH 910
Cdd:PRK03695   121 GRSVNqLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVaqqaaldRLLSELCQQGI---------AVVMSSH 191
                           90       100
                   ....*....|....*....|....*...
gi 1189438336  911 KLQY-LPHADWIIAMKDGTIQREGTLKD 937
Cdd:PRK03695   192 DLNHtLRHADRVWLLKQGKLLASGRRDE 219
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1366-1412 9.35e-03

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 39.05  E-value: 9.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1189438336 1366 IQIQNLSVRYDSslKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLA 1412
Cdd:cd03217      1 LEIKDLHVSVGG--KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKT 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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