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Conserved domains on  [gi|90421313|ref|NP_000483|]
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cystic fibrosis transmembrane conductance regulator [Homo sapiens]

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List of domain hits

Name Accession Description Interval E-value
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
389-670 0e+00

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: 586.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  389 TTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:cd03291    1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:cd03291   81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03291  161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 90421313  629 TFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFS 670
Cdd:cd03291  241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1208-1480 0e+00

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: 559.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:cd03289   81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1368 LLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRV 1447
Cdd:cd03289  161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 90421313 1448 KLFPHRNSSKCKSK--PQIAALKEETEEEVQDTRL 1480
Cdd:cd03289  241 KLFPRRNSSKSKRKprPQIQALQEETEEEVQDTRL 275
CFTR_R pfam14396
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
639-850 1.54e-137

Cystic fibrosis TM conductance regulator (CFTR), regulator domain;


:

Pssm-ID: 258564  Cd Length: 213  Bit Score: 423.81  E-value: 1.54e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    639 DFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTP 718
Cdd:pfam14396    1 DFSSKLLGLDSFDQFSAERRNSILTETLRRFSVDGDAGASWNEPKKQSFKQTGEFGEKRKNSILNPLNSARKFSFVQKSQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    719 LQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAP 798
Cdd:pfam14396   81 LQMNGIEEESDEPPERRLSLVPESEQGEAILPRSNMYNTGPTFQGRRRQSVLALMTRSINQGQSIHAQRSASVRKMSVVP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 90421313    799 QANL-TELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYL 850
Cdd:pfam14396  161 QSNLaSELDIYSRRLSQDSGLDISEEINEEDLKECFADDIESIFETTTWNTYL 213
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
862-1147 3.72e-49

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: 250039  Cd Length: 274  Bit Score: 177.87  E-value: 3.72e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    862 VLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHsRNNSYaviitstsSYYVFYIYVGVADTLLAMGFFRGLplVHTL 941
Cdd:pfam00664    1 LLIGILLLILAGATALVFPLLLGRFLDSLIDGNGDE-RSSLI--------SLAILLIAVGVLQGLLLQGYFYLG--ERLG 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    942 ITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVP 1021
Cdd:pfam00664   70 QRIRKRLFRALLRQILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1022 VIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:pfam00664  150 ILPLLILLSAVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFG 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 90421313   1102 RIEMIFVI-FFIAVTFISILttGEGEGRVGIILTLAMNIMSTLQWAV 1147
Cdd:pfam00664  230 ITQFISYLsYALALWFGGYL--VISGGLSVGTVFAFLSLGLQLSGPL 274
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
83-350 7.07e-41

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: 250039  Cd Length: 274  Bit Score: 153.99  E-value: 7.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     83 FYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:pfam00664    3 IGILLLILAGATALVFPLLLGRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYLGERLGQRIRKRLFRALLR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCG-LGFLIVLALFQAGLG 241
Cdd:pfam00664   83 QILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVlLAILPLLILLSAVLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    242 RMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQT-ELKLTRKAAYVRYfnssafffSGFFVVFL 320
Cdd:pfam00664  163 KKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDaEKAGIKKAIAAGL--------SFGITQFI 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 90421313    321 SVLPYALI----------KGIILRKIFTTISFCIVLRMAV 350
Cdd:pfam00664  235 SYLSYALAlwfggylvisGGLSVGTVFAFLSLGLQLSGPL 274
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
1-1480 0e+00

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: 2869.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313      1 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELAS-KKNPKLINALRRCFFW 79
Cdd:TIGR01271    1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     80 RFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSL 159
Cdd:TIGR01271   81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    160 IYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAG 239
Cdd:TIGR01271  161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    240 LGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVF 319
Cdd:TIGR01271  241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    320 LSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTA 399
Cdd:TIGR01271  321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    400 FWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSE 479
Cdd:TIGR01271  401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    480 GKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLA 559
Cdd:TIGR01271  481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    560 RAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPD 639
Cdd:TIGR01271  561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    640 FSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPV-SWTETKKQSFKQTG-EFGEKRKNS-ILNPINSIRKFSIVQK 716
Cdd:TIGR01271  641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVfSGPETIKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    717 TPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTASTRKV 794
Cdd:TIGR01271  721 GPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTSFRKK 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    795 SLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLA 872
Cdd:TIGR01271  800 SSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLA 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    873 EVAASLVVLWLLGNTP---LQDKGNSTHSRN--NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKI 947
Cdd:TIGR01271  880 EVAASLLGLWLITDNPsapNYVDQQHANASSpdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKR 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    948 LHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFI 1027
Cdd:TIGR01271  960 LHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFI 1039
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1028 MLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF 1107
Cdd:TIGR01271 1040 MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIF 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1108 VIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEG-KPTKSTKPYkngQ 1186
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEpRPSGGGGKY---Q 1196
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1187 LSKVMIIENSHVKKddIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGE 1266
Cdd:TIGR01271 1197 LSTVLVIENPHAQK--CWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1267 IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVL 1346
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
                         1450      1460      1470      1480      1490
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313   1427 IQKLLNERSLFRQAISPSDRVKLFP--HRNSSKCKSKPQIAALKEETEEEVQDTRL 1480
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADRLKLFPlhRRNSSKRKPQPKITALREEAEEEVQNTRL 1490
 
Name Accession Description Interval E-value
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
389-670 0e+00

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: 586.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  389 TTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:cd03291    1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:cd03291   81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03291  161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 90421313  629 TFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFS 670
Cdd:cd03291  241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1208-1480 0e+00

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: 559.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:cd03289   81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1368 LLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRV 1447
Cdd:cd03289  161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 90421313 1448 KLFPHRNSSKCKSK--PQIAALKEETEEEVQDTRL 1480
Cdd:cd03289  241 KLFPRRNSSKSKRKprPQIQALQEETEEEVQDTRL 275
CFTR_R pfam14396
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
639-850 1.54e-137

Cystic fibrosis TM conductance regulator (CFTR), regulator domain;


Pssm-ID: 258564  Cd Length: 213  Bit Score: 423.81  E-value: 1.54e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    639 DFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTP 718
Cdd:pfam14396    1 DFSSKLLGLDSFDQFSAERRNSILTETLRRFSVDGDAGASWNEPKKQSFKQTGEFGEKRKNSILNPLNSARKFSFVQKSQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    719 LQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAP 798
Cdd:pfam14396   81 LQMNGIEEESDEPPERRLSLVPESEQGEAILPRSNMYNTGPTFQGRRRQSVLALMTRSINQGQSIHAQRSASVRKMSVVP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 90421313    799 QANL-TELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYL 850
Cdd:pfam14396  161 QSNLaSELDIYSRRLSQDSGLDISEEINEEDLKECFADDIESIFETTTWNTYL 213
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
862-1147 3.72e-49

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: 250039  Cd Length: 274  Bit Score: 177.87  E-value: 3.72e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    862 VLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHsRNNSYaviitstsSYYVFYIYVGVADTLLAMGFFRGLplVHTL 941
Cdd:pfam00664    1 LLIGILLLILAGATALVFPLLLGRFLDSLIDGNGDE-RSSLI--------SLAILLIAVGVLQGLLLQGYFYLG--ERLG 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    942 ITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVP 1021
Cdd:pfam00664   70 QRIRKRLFRALLRQILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1022 VIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:pfam00664  150 ILPLLILLSAVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFG 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 90421313   1102 RIEMIFVI-FFIAVTFISILttGEGEGRVGIILTLAMNIMSTLQWAV 1147
Cdd:pfam00664  230 ITQFISYLsYALALWFGGYL--VISGGLSVGTVFAFLSLGLQLSGPL 274
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
83-350 7.07e-41

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: 250039  Cd Length: 274  Bit Score: 153.99  E-value: 7.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     83 FYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:pfam00664    3 IGILLLILAGATALVFPLLLGRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYLGERLGQRIRKRLFRALLR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCG-LGFLIVLALFQAGLG 241
Cdd:pfam00664   83 QILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVlLAILPLLILLSAVLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    242 RMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQT-ELKLTRKAAYVRYfnssafffSGFFVVFL 320
Cdd:pfam00664  163 KKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDaEKAGIKKAIAAGL--------SFGITQFI 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 90421313    321 SVLPYALI----------KGIILRKIFTTISFCIVLRMAV 350
Cdd:pfam00664  235 SYLSYALAlwfggylvisGGLSVGTVFAFLSLGLQLSGPL 274
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1227-1374 2.05e-38

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 or belong in different polypeptide chains.


Pssm-ID: 249501  Cd Length: 150  Bit Score: 142.79  E-value: 2.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSG-TFRKNL 1304
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPGLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313   1305 -------DPYEQWSDQEIWKVADEVGLrsvieqfPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:pfam00005   81 rlglllkGLSKREKDARAEEALEKLGL-------GDLLDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
441-575 4.00e-32

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 or belong in different polypeptide chains.


Pssm-ID: 249501  Cd Length: 150  Bit Score: 124.30  E-value: 4.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-------------HSGRISFCSQFSWIMPG-TIKENI 506
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPGLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313    507 IFGVsyDEYRYRSVIKACQLEEDISKFAEKD--NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:pfam00005   81 RLGL--LLKGLSKREKDARAEEALEKLGLGDllDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPT 149
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
432-614 5.07e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127  Cd Length: 200  Bit Score: 69.21  E-value: 5.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMP 499
Cdd:PRK13540    8 DFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyqkQLCFVGHRSGINP 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   500 G-TIKENIIFGVSYDEyryrsviKACQLEEDISKFAEKDNIVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK13540   88 YlTLRENCLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 90421313   579 DVLTekeiFESCVCKLMANKTR---ILVTSKME-HLKKAD 614
Cdd:PRK13540  159 DELS----LLTIITKIQEHRAKggaVLLTSHQDlPLNKAD 194
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1210-1378 1.65e-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  Cd Length: 198  Bit Score: 67.38  E-value: 1.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1210 MTVKDLTakYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIqidgvSWDSITLQQWRK 1284
Cdd:TIGR01189    1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTL----LRILAgllrpDSGEV-----RWNGTPLAEQRD 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1285 afgvIPQKVFIFSG---------TFRKNLD---PYEQWSDQEIWKVADEVGLRSvIEQFPGKldfvlvdggcVLSHGHKQ 1352
Cdd:TIGR01189   70 ----EPHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPAA----------QLSAGQQR 134
                          170       180
                   ....*....|....*....|....*.
gi 90421313   1353 LMCLARSVLSKAKILLLDEPSAHLDP 1378
Cdd:TIGR01189  135 RLALARLWLSRRPLWILDEPTTALDK 160
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
437-580 9.30e-11

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  Cd Length: 198  Bit Score: 61.99  E-value: 9.30e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK------HSGRISFCSQFSWI--MPG-----TIK 503
Cdd:TIGR01189   12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngtplAEQRDEPHENILYLghLPGlkpelSAL 91
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313    504 ENIIFGVSYDEYRYRSVIKAcqLEE-DISKFAekDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:TIGR01189   92 ENLHFWAAIHGGAQRTIEDA--LAAvGLTGFE--DLPAA-----QLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1226-1384 9.92e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127  Cd Length: 200  Bit Score: 58.81  E-value: 9.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1226 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSwdsitLQQWRKAFgvipQKVFIFSGtFRKNL 1304
Cdd:PRK13540   16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQS-----IKKDLCTY----QKQLCFVG-HRSGI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1305 DPYEQWSDQ---EIWKVADEVGLRSVIEQFpgKLDFvLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT 1380
Cdd:PRK13540   86 NPYLTLRENclyDIHFSPGAVGITELCRLF--SLEH-LIDYPCgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162

                  ....
gi 90421313  1381 YQII 1384
Cdd:PRK13540  163 LLTI 166
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
1-1480 0e+00

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: 2869.18  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313      1 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELAS-KKNPKLINALRRCFFW 79
Cdd:TIGR01271    1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     80 RFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSL 159
Cdd:TIGR01271   81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    160 IYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAG 239
Cdd:TIGR01271  161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    240 LGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVF 319
Cdd:TIGR01271  241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    320 LSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTA 399
Cdd:TIGR01271  321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    400 FWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSE 479
Cdd:TIGR01271  401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    480 GKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLA 559
Cdd:TIGR01271  481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    560 RAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPD 639
Cdd:TIGR01271  561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    640 FSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPV-SWTETKKQSFKQTG-EFGEKRKNS-ILNPINSIRKFSIVQK 716
Cdd:TIGR01271  641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVfSGPETIKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    717 TPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTASTRKV 794
Cdd:TIGR01271  721 GPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTSFRKK 799
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    795 SLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLA 872
Cdd:TIGR01271  800 SSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLA 879
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    873 EVAASLVVLWLLGNTP---LQDKGNSTHSRN--NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKI 947
Cdd:TIGR01271  880 EVAASLLGLWLITDNPsapNYVDQQHANASSpdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKR 959
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    948 LHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFI 1027
Cdd:TIGR01271  960 LHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFI 1039
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1028 MLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF 1107
Cdd:TIGR01271 1040 MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIF 1119
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1108 VIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEG-KPTKSTKPYkngQ 1186
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEpRPSGGGGKY---Q 1196
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1187 LSKVMIIENSHVKKddIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGE 1266
Cdd:TIGR01271 1197 LSTVLVIENPHAQK--CWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1267 IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVL 1346
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
                         1450      1460      1470      1480      1490
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313   1427 IQKLLNERSLFRQAISPSDRVKLFP--HRNSSKCKSKPQIAALKEETEEEVQDTRL 1480
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADRLKLFPlhRRNSSKRKPQPKITALREEAEEEVQNTRL 1490
PLN03232 PLN03232
ABC transporter C family member; Provisional
5-1437 3.50e-161

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 528.78  E-value: 3.50e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     5 PLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRElASKKNPKLINALRRCFFWRFMFY 84
Cdd:PLN03232  228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRRPKPWLLRALNNSLGGRFWLG 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    85 GIFLYLGEVTKAVQPLLLGRIIASYDPDNKE----ERSIAIYLGIGLCLLFIVRTLLlhpaifGLHHIGMQMRIAMFSLI 160
Cdd:PLN03232  307 GIFKIGHDLSQFVGPVILSHLLQSMQEGDPAwvgyVYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRSTLVAAI 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL 240
Cdd:PLN03232  381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   241 GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL 320
Cdd:PLN03232  461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   321 SVLPYALIKG-IILRKIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKIQDFLQKQEyKTLEYNLT----TTEVVME 395
Cdd:PLN03232  541 SFGVFVLLGGdLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE-RILAQNPPlqpgAPAISIK 618
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   396 NVTAFWEEgfgelfekakqnnnnrKTSNgddslffsnfsllgtPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGEL 475
Cdd:PLN03232  619 NGYFSWDS----------------KTSK---------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   476 EPSE-GKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRA 554
Cdd:PLN03232  668 SHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQ 747
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   555 RISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 634
Cdd:PLN03232  748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   635 nlqpdfssklmgcdsfdqfsaerRNSILTETLhrfslegdapvswtetkkqsFKQTGEFGEKRKnsilnpinsirkfsiv 714
Cdd:PLN03232  828 -----------------------KSGSLFKKL--------------------MENAGKMDATQE---------------- 848
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   715 qktplqmngiEEDSDEPLerrlslvpdSEQGEAILPRISVISTGPTLQARRRQSVLnlmthsVNQGQnihrkttastrkv 794
Cdd:PLN03232  849 ----------VNTNDENI---------LKLGPTVTIDVSERNLGSTKQGKRGRSVL------VKQEE------------- 890
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   795 slapqanlteldiysrrlsQETGleiseeineedlkecffddmesipaVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEV 874
Cdd:PLN03232  891 -------------------RETG-------------------------IISWNVLMRYNKAVGGLWVVMILLVCYLTTEV 926
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   875 AASLVVLWLLGNTplqdkgnsTHSRNNSYaviitsTSSYYVFyIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLH 954
Cdd:PLN03232  927 LRVSSSTWLSIWT--------DQSTPKSY------SPGFYIV-VYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   955 SVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFL 1034
Cdd:PLN03232  992 SILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQ 1071
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1035 QTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF-VIFFIA 1113
Cdd:PLN03232 1072 STSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGgVMIWLT 1151
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1114 VTFiSILTTGEGEGRV------GIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPtkstkpykngql 1187
Cdd:PLN03232 1152 ATF-AVLRNGNAENQAgfastmGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATA------------ 1218
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1188 skvmIIENShvKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GE 1266
Cdd:PLN03232 1219 ----IIENN--RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGR 1292
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1267 IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVL 1346
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
                        1450
                  ....*....|..
gi 90421313  1427 IQKLL-NERSLF 1437
Cdd:PLN03232 1453 PQELLsRDTSAF 1464
PTZ00243 PTZ00243
ABC transporter; Provisional
69-1438 1.58e-125

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 429.58  E-value: 1.58e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    69 LINALRRCFFWRFMFygifLYLGEVTKAVQPLLLGRIIASYDPDNKeersiAIYLGIGLCLLFIVRTLLLHPAIFGLHHI 148
Cdd:PTZ00243  238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNA-----TWGRGLGLVLTLFLTQLIQSVCLHRFYYI 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   149 ----GMQMRIAMFSLIYKKTLKLSSRVLDK--ISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQAS 222
Cdd:PTZ00243  309 sircGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   223 AFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV 302
Cdd:PTZ00243  389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   303 RYFNSSAFFFSGFFVVFLSVLPYALIkGIILRK--IFTTISFCIVLRMAVtRQFPWAVQTWYDSLGAINKIQDFLQ---- 376
Cdd:PTZ00243  469 RVATSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdna 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   377 -------KQEYKTLEYNLTTT---EVVMEN--VTAFW------------------------------------------- 401
Cdd:PTZ00243  547 tcstvqdMEEYWREQREHSTAcqlAAVLENvdVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   402 -------------EEGFGELFEKAKQNNNNRKTSNGDDSLFFSnfsLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:PTZ00243  627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE---LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:PTZ00243  704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:PTZ00243  784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   629 TFSelqnlqpDFssklMGCDSFDQFSAErrnsiLTETLHRFSLEGDAPVSWTETKKqsfkqtgefgekrknsilnpinsi 708
Cdd:PTZ00243  864 SSA-------DF----MRTSLYATLAAE-----LKENKDSKEGDADAEVAEVDAAP------------------------ 903
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   709 rkfsivqktplqmnGIEEDSDEPLERRLSLvpdSEQGEAilprisviSTGPTLQARrrqsvlnLMThsvnqgqnihrktt 788
Cdd:PTZ00243  904 --------------GGAVDHEPPVAKQEGN---AEGGDG--------AALDAAAGR-------LMT-------------- 937
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   789 astrkvslapqanlteldiysrRLSQETGleiseeineedlkecffddmeSIPavttWNTYLRYITVHKSLIFVLIWCLV 868
Cdd:PTZ00243  938 ----------------------REEKASG---------------------SVP----WSTYVAYLRFCGGLHAAGFVLAT 970
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   869 IFLAEVAASLVVLWLlgntplqdkgnsthSRNNSYAVIITSTSSYYVfYIYVGVADTLlamgffrGLPL-----VHTLIT 943
Cdd:PTZ00243  971 FAVTELVTVSSGVWL--------------SMWSTRSFKLSAATYLYV-YLGIVLLGTF-------SVPLrfflsYEAMRR 1028
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   944 VSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVI 1023
Cdd:PTZ00243 1029 GSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCG 1108
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1024 VAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQpyfETLFHKALN----LHTANwFLYLSTLRWF 1099
Cdd:PTZ00243 1109 YLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA---HLVMQEALRrldvVYSCS-YLENVANRWL 1184
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1100 QMRIEMIFVIFFIAVTFISILTTGEGEGR--VGII---LTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFID------ 1168
Cdd:PTZ00243 1185 GVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVslsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevphed 1264
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1169 MPtEGKPTKSTKPYKNGQLSKV---MIIENSHVKKDDIWP-SGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLG 1244
Cdd:PTZ00243 1265 MP-ELDEEVDALERRTGMAADVtgtVVIEPASPTSAAPHPvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVG 1343
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1245 RTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVG 1323
Cdd:PTZ00243 1344 RTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVG 1423
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1324 LRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK-AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:PTZ00243 1424 LRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAH 1503
                        1450      1460      1470
                  ....*....|....*....|....*....|....*..
gi 90421313  1403 RIEAMLECQQFLVIEENKVRQYDSIQKL-LNERSLFR 1438
Cdd:PTZ00243 1504 RLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms]
856-1439 4.75e-76

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


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 265.06  E-value: 4.75e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  856 HKSLIFVLIWCLVIFLAEVAASLVVLWLLgntplqDKGNSTHSRNNSYAVIItstssyyvFYIYVGVAdtllAMGFFRGL 935
Cdd:COG1132   13 YKLLLLAILLLLLSALLSLLLPLLIGRII------DALLADLGELLELLLLL--------LLLALLGG----VLRALQSY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  936 PLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYI 1015
Cdd:COG1132   75 LGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAKSGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1016 FVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLST 1095
Cdd:COG1132  155 ALILLLILPLLALVLSLLARKSRKLSRRVREALGELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1096 LRWFQMRIEMIFVIFFIAVTFISILTTGEGE---GRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTE 1172
Cdd:COG1132  235 EALLAPLMLLLSSLGTVLVLALGGFLVLSGSltvGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1173 gkptkstkpykngqlskvmiIENSHVKKddiWPSGGQMTVKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKST 1252
Cdd:COG1132  315 --------------------VEDPPDPL---KDTIGSIEFENVSFSY-PGKKPVLKDISFSIEPGEKVAIVGPSGSGKST 370
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1253 LLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQW-SDQEIWKVADEVGLRSVIEQ 1330
Cdd:COG1132  371 LIKLLLRLYdPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIALGRPDaTDEEIEEALKLANAHEFIAN 450
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1331 FPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLEC 1410
Cdd:COG1132  451 LPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEALIQDALKKLLKGRTTLIIAHRLSTIKNA 530
                        570       580
                 ....*....|....*....|....*....
gi 90421313 1411 QQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:COG1132  531 DRIIVLDNGRIVERGTHEELLAKGGLYAR 559
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1205-1439 3.23e-39

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 154.98  E-value: 3.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1205 PSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLN-----TEGEIQIDGVSWDSITL 1279
Cdd:PRK11160  334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTrawdpQQGEILLNGQPIADYSE 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1280 QQWRKAFGVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGkLDFVLVDGGCVLSHGHKQLMCL 1356
Cdd:PRK11160  410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGI 486
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSL 1436
Cdd:PRK11160  487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566

                  ...
gi 90421313  1437 FRQ 1439
Cdd:PRK11160  567 YYQ 569
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
450-613 8.20e-07

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: 49.29  E-value: 8.20e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     450 RGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKhsgrisfcsqfsWIMPGTIKENIIFgvsydeyryrsvikacqleed 529
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------YIDGEDILEEVLD--------------------- 47
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     530 iskfaEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR------ILV 603
Cdd:smart00382   48 -----QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknltvILT 122
                           170
                    ....*....|
gi 90421313     604 TSKMEHLKKA 613
Cdd:smart00382  123 TNDEKDLGPA 132
ycf16 CHL00131
sulfate ABC transporter protein; Validated
438-604 5.13e-04

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 42.32  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGelEPS----EGKIKHSGRiSFCSqfswIMPGTIKENIIF----- 508
Cdd:CHL00131   20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGE-SILD----LEPEERAHLGIFlafqy 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   509 -----GVSYDEY---RYRSVIKACQLEE-DISKF----AEKDNIV----------LGEGgitLSGGQRARISLARAVYKD 565
Cdd:CHL00131   93 pieipGVSNADFlrlAYNSKRKFQGLPElDPLEFleiiNEKLKLVgmdpsflsrnVNEG---FSGGEKKRNEILQMALLD 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 90421313   566 ADLYLLDSPFGYLDVLTEKEIFEScVCKLM-ANKTRILVT 604
Cdd:CHL00131  170 SELAILDETDSGLDIDALKIIAEG-INKLMtSENSIILIT 208
 
Name Accession Description Interval E-value
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
389-670 0e+00

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: 586.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  389 TTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:cd03291    1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:cd03291   81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03291  161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 90421313  629 TFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFS 670
Cdd:cd03291  241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1208-1480 0e+00

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: 559.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:cd03289   81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1368 LLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRV 1447
Cdd:cd03289  161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 90421313 1448 KLFPHRNSSKCKSK--PQIAALKEETEEEVQDTRL 1480
Cdd:cd03289  241 KLFPRRNSSKSKRKprPQIQALQEETEEEVQDTRL 275
CFTR_R pfam14396
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
639-850 1.54e-137

Cystic fibrosis TM conductance regulator (CFTR), regulator domain;


Pssm-ID: 258564  Cd Length: 213  Bit Score: 423.81  E-value: 1.54e-137
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    639 DFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTP 718
Cdd:pfam14396    1 DFSSKLLGLDSFDQFSAERRNSILTETLRRFSVDGDAGASWNEPKKQSFKQTGEFGEKRKNSILNPLNSARKFSFVQKSQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    719 LQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAP 798
Cdd:pfam14396   81 LQMNGIEEESDEPPERRLSLVPESEQGEAILPRSNMYNTGPTFQGRRRQSVLALMTRSINQGQSIHAQRSASVRKMSVVP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 90421313    799 QANL-TELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYL 850
Cdd:pfam14396  161 QSNLaSELDIYSRRLSQDSGLDISEEINEEDLKECFADDIESIFETTTWNTYL 213
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
392-623 2.09e-94

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: 303.62  E-value: 2.09e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  392 VVMENVTAFWEEGFGElfekakqnnnnrktsngddslffsnfsllGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI 471
Cdd:cd03250    1 ISVEDASFTWDSGEQE-----------------------------TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  472 MGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGG 551
Cdd:cd03250   52 LGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGG 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313  552 QRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCK-LMANKTRILVTSKMEHLKKADKILILHEGS 623
Cdd:cd03250  132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1208-1426 5.67e-92

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: 297.48  E-value: 5.67e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDLRSRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03244   81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:cd03244  161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1204-1426 1.11e-57

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: 199.95  E-value: 1.11e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1204 WPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQW 1282
Cdd:cd03369    1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVadevgLRsvieqfpgkldfvLVDGGCVLSHGHKQLMCLARSVLS 1362
Cdd:cd03369   81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA-----LR-------------VSEGGLNLSQGQRQLLCLARALLK 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1363 KAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:cd03369  143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1210-1420 7.90e-53

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: 184.51  E-value: 7.90e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03228    1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03228   81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENK 1420
Cdd:cd03228  120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1207-1437 6.91e-50

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: 179.33  E-value: 6.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1207 GGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKA 1285
Cdd:cd03288   17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03288   97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLL-NERSLF 1437
Cdd:cd03288  177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
862-1147 3.72e-49

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: 250039  Cd Length: 274  Bit Score: 177.87  E-value: 3.72e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    862 VLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHsRNNSYaviitstsSYYVFYIYVGVADTLLAMGFFRGLplVHTL 941
Cdd:pfam00664    1 LLIGILLLILAGATALVFPLLLGRFLDSLIDGNGDE-RSSLI--------SLAILLIAVGVLQGLLLQGYFYLG--ERLG 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    942 ITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVP 1021
Cdd:pfam00664   70 QRIRKRLFRALLRQILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVLLA 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1022 VIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:pfam00664  150 ILPLLILLSAVLAKKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDAEKAGIKKAIAAGLSFG 229
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 90421313   1102 RIEMIFVI-FFIAVTFISILttGEGEGRVGIILTLAMNIMSTLQWAV 1147
Cdd:pfam00664  230 ITQFISYLsYALALWFGGYL--VISGGLSVGTVFAFLSLGLQLSGPL 274
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
437-623 3.11e-43

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: 159.03  E-value: 3.11e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-----------------KHSGRISFCSQFSWIMP 499
Cdd:cd03290   13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  500 GTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03290   93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 90421313  580 VLTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGS 623
Cdd:cd03290  173 IHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
437-622 4.19e-43

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: 156.77  E-value: 4.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:cd03228   14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  504 ENIifgvsydeyryrsvikacqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03228   94 ENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 90421313  584 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03228  133 ALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1221-1431 1.60e-42

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: 157.00  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1221 EGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGT 1299
Cdd:cd03254   13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1300 FRKNL---DPYEQwsDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:cd03254   93 IMENIrlgRPNAT--DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1377 DPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLL 1431
Cdd:cd03254  171 DTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
83-350 7.07e-41

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: 250039  Cd Length: 274  Bit Score: 153.99  E-value: 7.07e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313     83 FYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:pfam00664    3 IGILLLILAGATALVFPLLLGRFLDSLIDGNGDERSSLISLAILLIAVGVLQGLLLQGYFYLGERLGQRIRKRLFRALLR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCG-LGFLIVLALFQAGLG 241
Cdd:pfam00664   83 QILGLFMSFFDTNSVGELTSRLTNDVSKIRDGLGDKLGLFFQSLATVVGGFIVMFYYGWKLTLVlLAILPLLILLSAVLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    242 RMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQT-ELKLTRKAAYVRYfnssafffSGFFVVFL 320
Cdd:pfam00664  163 KKLRKLNRKEQKAYAKAGSVAEESLSGIRTVKAFGREEYELERYDKALEDaEKAGIKKAIAAGL--------SFGITQFI 234
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 90421313    321 SVLPYALI----------KGIILRKIFTTISFCIVLRMAV 350
Cdd:pfam00664  235 SYLSYALAlwfggylvisGGLSVGTVFAFLSLGLQLSGPL 274
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1211-1439 7.85e-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: 146.61  E-value: 7.85e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd03251    2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRRQIGLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03251   82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1208-1421 9.70e-39

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: 145.81  E-value: 9.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:cd03245    1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1363
Cdd:cd03245   81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1364 AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIeAMLE-CQQFLVIEENKV 1421
Cdd:cd03245  159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSGRI 216
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1227-1374 2.05e-38

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 or belong in different polypeptide chains.


Pssm-ID: 249501  Cd Length: 150  Bit Score: 142.79  E-value: 2.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313   1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSG-TFRKNL 1304
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPGLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313   1305 -------DPYEQWSDQEIWKVADEVGLrsvieqfPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:pfam00005   81 rlglllkGLSKREKDARAEEALEKLGL-------GDLLDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1213-1439 5.02e-38

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: 144.30  E-value: 5.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQ 1291
Cdd:cd03253    4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDvSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 KVFIFSGTFRKNLDpYEQW--SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03253   83 DTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03253  162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
437-633 4.25e-37

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: 141.59  E-value: 4.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:cd03254   15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIM 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  504 ENIIFGVSY--DEyryrSVIKAC---QLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03254   95 ENIRLGRPNatDE----EVIEAAkeaGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90421313  579 DVLTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03254  171 DTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
437-633 2.75e-35

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: 136.21  E-value: 2.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-------------ISFCSQFSWIMPGTIK 503
Cdd:cd03251   14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  504 ENIIFGVS-YDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03251   94 ENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90421313  583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03251  174 ERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1212-1420 7.34e-33

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: 128.74  E-value: 7.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIP 1290
Cdd:cd03225    2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 Q--KVFIFSGTFR-------KNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLArSVL 1361
Cdd:cd03225   82 QnpDDQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIA-GVL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1362 S-KAKILLLDEPSAHLDPVTYQIIRRTLKQaFADC--TVILCEHRIEAMLE-CQQFLVIEENK 1420
Cdd:cd03225  150 AmDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1211-1439 1.02e-32

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: 128.81  E-value: 1.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKY-TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03249    2 EFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03249   82 VSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03249  160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1210-1439 2.97e-32

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: 127.60  E-value: 2.97e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03252    1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03252   81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03252  159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
441-575 4.00e-32

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 or belong in different polypeptide chains.


Pssm-ID: 249501  Cd Length: 150  Bit Score: 124.30  E-value: 4.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313    441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-------------HSGRISFCSQFSWIMPG-TIKENI 506
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPGLFPRlTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313    507 IFGVsyDEYRYRSVIKACQLEEDISKFAEKD--NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:pfam00005   81 RLGL--LLKGLSKREKDARAEEALEKLGLGDllDRPVGENPGTLSGGQKQRVAIARALLTKPKLLLLDEPT 149
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1211-1420 1.25e-31

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: 123.12  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd00267    1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQkvfifsgtfrknldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd00267   79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIE-AMLECQQFLVIEENK 1420
Cdd:cd00267  105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPElAELAADRVIVLKDGK 157
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
437-633 3.09e-31

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: 124.65  E-value: 3.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-----------HSGR--ISFCSQFSWIMPGTIK 503
Cdd:cd03253   13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRraIGVVPQDTVLFNDTIG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  504 ENIIFG-VSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03253   93 YNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90421313  583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03253  173 EREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1212-1421 4.76e-31

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: 121.94  E-value: 4.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIP 1290
Cdd:cd03246    3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSGTFRKNldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:cd03246   83 QDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVLD 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1371 EPSAHLDPVTYQIIRRTLKQA-FADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:cd03246  122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1210-1421 9.42e-31

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: 121.27  E-value: 9.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwDSITLQQWRKAFGV 1288
Cdd:cd03247    1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGVP-VSDLEKALSSLISV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevGLRsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03247   80 LNQRPYLFDTTLRNNL------------------GRR--------------------FSGGERQRLALARILLQDAPIVL 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:cd03247  122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
439-622 5.81e-29

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: 117.59  E-value: 5.81e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03244   18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSN 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  506 I-IFGVSYDEYRYRsVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 584
Cdd:cd03244   98 LdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 90421313  585 EIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03244  177 LIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
432-619 6.46e-29

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: 117.25  E-value: 6.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--------RISFCSQ---FSWIMPG 500
Cdd:cd03235    6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsIDRDFPI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  501 TIKE--------NIIFGVSYDEYRYRSVIKAcqLEE-DISKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03235   86 SVRDvvlmglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQDPDLLLL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 90421313  572 DSPFGYLDVLTEKEIFEsCVCKL-MANKTRILVTSKMEH-LKKADKILIL 619
Cdd:cd03235  157 DEPFAGVDPKTQEDIYE-LLRELrREGMTILVVTHDLGLvLEYFDRVLLL 205
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
439-622 1.01e-28

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: 115.39  E-value: 1.01e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFcsqfswimpgtikeniifgvSYDEYRYR 518
Cdd:cd03246   16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--------------------QWDPNELG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  519 SVIKAcqLEEDISKFAE--KDNIvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMA 596
Cdd:cd03246   76 DHVGY--LPQDDELFSGsiAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA 145
                        170       180
                 ....*....|....*....|....*.
gi 90421313  597 NKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03246  146 GATRIVIAHRPETLASADRILVLEDG 171
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
438-622 2.68e-28

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: 115.38  E-value: 2.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKE 504
Cdd:cd03245   17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  505 NIIFGVSY-DEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03245   97 NITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 90421313  584 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03245  177 ERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1212-1421 4.82e-28

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: 113.26  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLqQWRKAFGVIP 1290
Cdd:cd03230    3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNLDpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03230   80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHRIEAMLE-CQQFLVIEENKV 1421
Cdd:cd03230  120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1211-1421 1.25e-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: 112.53  E-value: 1.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd03214    1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQkvfifsgtfrknldpyeqwsdqeiwkVADEVGLRSVIEQFpgkldfvlVDggcVLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03214   79 PQ--------------------------ALELLGLAHLADRP--------FN---ELSGGERQRVLLARALAQEPPILLL 121
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1370 DEPSAHLDPvTYQI----IRRTLKQAFaDCTVILCEHRIE-AMLECQQFLVIEENKV 1421
Cdd:cd03214  122 DEPTSHLDI-AHQIelleLLRRLARER-GKTVVMVLHDLNlAARYADRVILLKDGRI 176
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1212-1420 1.45e-27

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: 112.95  E-value: 1.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEG---GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGEIQ-IDGVSwdsitlqQWRKAFG 1287
Cdd:cd03250    3 VEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSGSV-------SVPGSIA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNL---DPYEQwsdQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 1364
Cdd:cd03250   70 YVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1365 KILLLDEPSAHLDP-VTYQIIRRTLKQAFADC-TVILCEHRIEAMLECQQFLVIEENK 1420
Cdd:cd03250  147 DIYLLDDPLSAVDAhVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
439-633 4.69e-27

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: 112.25  E-value: 4.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-------------KHSGRISFCSQFSWIMPGTIKEN 505
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIAEN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  506 IIFG-----VSYDEyryrSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03249   97 IRYGkpdatDEEVE----EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90421313  581 LTEKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03249  173 ESEKLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
432-622 1.02e-25

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: 106.18  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIkhsgrisfcsqfswimpgTIKENIIFGVS 511
Cdd:cd00267    6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------LIDGKDIAKLP 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  512 YDEYRYRSVIKACqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCV 591
Cdd:cd00267   68 LEELRRRIGYVPQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
                        170       180       190
                 ....*....|....*....|....*....|..
gi 90421313  592 CKLMANKTRILVTSKMEHLKKA-DKILILHEG 622
Cdd:cd00267  125 ELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistant to organic solvents; ABC ...
1212-1432 4.57e-25

ATP-binding cassette transport system involved in resistant 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: 106.43  E-value: 4.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWRKAFG 1287
Cdd:cd03261    3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSG-TFRKN----LDPYEQWSDQEIWKVA----DEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1358
Cdd:cd03261   81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVT-YQIIR--RTLKQAFaDCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLLN 1432
Cdd:cd03261  150 ALALDPELLLYDEPTAGLDPIAsGVIDDliRSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1210-1425 1.33e-24

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: 104.52  E-value: 1.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQqwRK 1284
Cdd:cd03259    1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVPPE--RR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQK--------VF--IFSGtFRKNLDPYEQWSDQEIWkVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLM 1354
Cdd:cd03259   73 NIGMVFQDyalfphltVAenIAFG-LKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHE-----------LSGGQQQRV 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEH-RIEAMLECQQFLVIEENKVRQYD 1425
Cdd:cd03259  140 ALARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1211-1416 2.67e-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: 103.74  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGG--NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQ---WRK 1284
Cdd:cd03257    3 EVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSRRLrkiRRK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVF-----------IFSGTFRKNLDPYEQWSDQE-IWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHK 1351
Cdd:cd03257   83 EIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLpEEVLNRYPHE-----------LSGGQR 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1352 QLMCLARSVLSKAKILLLDEPSAHLDPVT-YQIIR--RTLKQAFaDCTVILCEHRIEAMLE-CQQFLVI 1416
Cdd:cd03257  152 QRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVM 219
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
437-648 5.50e-24

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: 103.15  E-value: 5.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPG-TI 502
Cdd:cd03295   13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  503 KENI-----IFGVSYDEYRYRsvikACQLEE----DISKFAEKdniVLGEggitLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03295   93 EENIalvpkLLKWPKEKIRER----ADELLAlvglDPAEFADR---YPHE----LSGGQQQRVGVARALAADPPLLLMDE 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313  574 PFGYLDVLTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSE-LQNLQPDFSSKLMGCD 648
Cdd:cd03295  162 PFGALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
440-633 6.81e-24

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: 102.95  E-value: 6.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKENI 506
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  507 IFGvsyDE-YRYRSVIKACQL---EEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03252   97 ALA---DPgMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 90421313  583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03252  174 EHAIMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
438-628 2.17e-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: 100.08  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03247   15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRNN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  506 IifgvsydeyryrsvikacqleediskfaekdnivlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 585
Cdd:cd03247   95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 90421313  586 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03247  137 LLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
437-622 3.86e-23

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: 100.29  E-value: 3.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-----------KHSGRISFCSQFSWIMPG-TIKE 504
Cdd:cd03259   12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDYALFPHlTVAE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  505 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03259   92 NIAFGlklrgVPKAEIRARvrELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSA 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 90421313  578 LDV-LTE------KEIFESCvcklmaNKTRILVTSKM-EHLKKADKILILHEG 622
Cdd:cd03259  161 LDAkLREelreelKELQREL------GITTIYVTHDQeEALALADRIAVMNEG 207
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
438-622 6.27e-23

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: 99.46  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-------------KHSGRISFC-----SQFswIMP 499
Cdd:cd03225   14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVfqnpdDQF--FGP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313  500 gTIKENIIFGVsydEYRYRSvikacqlEEDIskfAEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYL 570
Cdd:cd03225   92 -TVEEEVAFGL---ENLGLP-------EEEI---EERVEEALELVGLeglrdrspfTLSGGQKQRVAIAGVLAMDPDILL 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 90421313  571 LDSPFGYLDVLTEKEIFEScVCKLMA-NKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03225  158 LDEPTAGLDPAGRRELLEL-</