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Conserved domains on  [gi|225703056|ref|NP_780419|]
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ATP-binding cassette sub-family A member 12 [Mus musculus]

Protein Classification

NosY and ABC_subfamily_A domain-containing protein (domain architecture ID 10003372)

NosY and ABC_subfamily_A domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2254-2477 5.32e-98

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


:

Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 317.52  E-value: 5.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqliHKKI-IAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGsLGHVDSHSSL 2332
Cdd:cd03263     1 LQIRNLTKTY---KKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2333 VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILL 2412
Cdd:cd03263    77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 2413 LDEPSSGMDPKSKRHLWRIISEEVQNKcSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIK 2477
Cdd:cd03263   157 LDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1350-1565 8.08e-96

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


:

Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 311.36  E-value: 8.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGS--KTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHD 1427
Cdd:cd03263     5 NLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1428 VLFSYLTTKEHLLLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:cd03263    85 ALFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1508 GVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1565
Cdd:cd03263   163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
1108-1269 1.81e-03

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 224196  Cd Length: 278  Bit Score: 41.30  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1108 FFAWLIESIGFLLVTIAILIVILKF-GNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFP 1186
Cdd:COG1277   113 ALLVILIIILISFISLLTLLLLFGFpGNVSSISRLLLFLGSSLLYGLVLLSISLLISSLFSSSSLALLVSIILLLLFIIA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1187 FIVLVTVEDELSYVIKVFMSLLSPTAFSYASQYIAryeeQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAW 1266
Cdd:COG1277   193 FSLILLFISVLLIGIAPTLNTLSLLLPLYLLAELA----FTILLQSGFSDSILTLNESLLLAWFNILILIIYILIFLSIA 268

                  ...
gi 225703056 1267 YVR 1269
Cdd:COG1277   269 YLI 271
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
749-2569 0e+00

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


:

Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 1259.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   749 NHTKDFLTYKLTKEEIAskYGIPLNATPFCFSLYKDIINMPAGPVIWAFLKPMLLGKILYSPYNPTTKAIMEKSNVTLRQ 828
Cdd:TIGR01257  343 NNYKAFLGIDSTRKDPI--YSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   829 LAELREKSQEWMDKSPIFMNSFHLLNQtIPMLQNTLRNPFVQVFVKFSVGLDAV--ELL----------KQIDDLDVLRL 896
Cdd:TIGR01257  421 LERVRKLVKAWEEVGPQIWYFFDKSTQ-MTMIRDTLQNPTVKDFINRQLGEEGItaEAVlnflyngpreKQADDMTNFDW 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   897 KlvnniDIIDQLNTLSSLTVNISSCVLYDRIQASDTVEEMETVAEQLYKSNELFGSVIFKlpsngslhrGFDPEKVSLPP 976
Cdd:TIGR01257  500 R-----DIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFP---------DMYPWTSSLPP 565
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   977 IVRYTIRMSLKTAQTTRSIRTKIWAPGPHNSPSHN--QIYGrAFIYLQDSIERAIIELQTgRNSQEVAVQVQAVPYPCFM 1054
Cdd:TIGR01257  566 HVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDfrYIWG-GFAYLQDMVEQGITRSQM-QAEPPVGIYLQQMPYPCFV 643
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1055 KDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESIGFLLVTIAILIVILKFGN 1134
Cdd:TIGR01257  644 DDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGR 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1135 ILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLSPTAFS 1214
Cdd:TIGR01257  724 ILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFG 803
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1215 YASQYIARYEEQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAWYVRNVFPGTYGMAAPWYFPILPSYWKER 1294
Cdd:TIGR01257  804 FGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGG 883
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1295 FGCAeVKHEKSnglmftnimMQNTNPSASKTSpDCAFPSNI-----EPEPKDLQVGVALHGVTKIY--GSKTAVENLNLN 1367
Cdd:TIGR01257  884 EGCS-TREERA---------LEKTEPLTEEME-DPEHPEGIndsffERELPGLVPGVCVKNLVKIFepSGRPAVDRLNIT 952
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1368 FYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKV 1447
Cdd:TIGR01257  953 FYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKG 1032
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1448 PHWTKTQLheEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTA 1527
Cdd:TIGR01257 1033 RSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1528 RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKK----KSPNLDTNAIC------------- 1590
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKmkniQSQRGGCEGTCsctskgfstrcpa 1190
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1591 -------------DTVAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKvSGAYLSLLRALDKGMGKLNIGCYGISDTTV 1657
Cdd:TIGR01257 1191 rvdeitpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFK-QRAYASLFRELEETLADLGLSSFGISDTPL 1269
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1658 EEVFLNLTKDS-----------QKSSNMSLEHltqrKVGNPSANGTSTPDDLSVSSSNFTDRDDKVLTRSEKlEGFG--- 1723
Cdd:TIGR01257 1270 EEIFLKVTEDAdsgslfaggaqQKRENANLRH----PCSGPTEKAGQTPQASHTCSPGQPAAHPEGQPPPEP-EDPGvpl 1344
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1724 -----LLLKKIMAILIKRFHHTRRNWKGLIAQVILPIVFVATAMGLGTLRDSSNSYPEIMISPSIYGtsEQTAFYANFDP 1798
Cdd:TIGR01257 1345 ntgarLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYG--QQYTFFSMDEP 1422
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1799 ST---SGLVSALWNFPGIDNVCLNTSDLQCLKKDDLGKWNTSG--------------EAIDNFGVCSCSDN-----VQEC 1856
Cdd:TIGR01257 1423 NSehlEVLADVLLNKPGFGNRCLKEEWLPEYPCGNSTPWKTPSvspnithlfqkqkwTAAHPSPSCRCSTRekltmLPEC 1502
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1857 PK--FNYHPPHRRTYSSQVIYNLTGKHMENYLITTANHFV-----------QKRYGGWSFGMKLT-------------ND 1910
Cdd:TIGR01257 1503 PEgaGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIrsslkskfwvnEQRYGGISIGGKLPaipitgealvgflSD 1582
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1911 L--RFDVTAVPDNRTLA----------------KVWYDPEGYHSLPAYLNSLNNFLLRVNM-SEYDAARHGIIMYSHPYP 1971
Cdd:TIGR01257 1583 LgqMMNVSGGPVTREASkempdflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLpKDRDPEEYGITVISQPLN 1662
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1972 GVQDQ--EQATISSLIDILVALSILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFS 2049
Cdd:TIGR01257 1663 LTKEQlsEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLV 1742
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2050 IGVIAIFKLPAFYSGNNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSivslSVVYFLSKEKPN 2129
Cdd:TIGR01257 1743 VGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINS----SAITFVLELFEN 1818
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2130 DPTLELISETLKRIFLIFPQFCFGYGLIELSQQQAVLDFLKAYGVEYPSETFEMDKLGAMFVALVSQGTMFFLLRLLINE 2209
Cdd:TIGR01257 1819 NRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQH 1898
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2210 wlikklRLFFRKFTSSPIMETV-DEDEDVRAERFRVESGAAEFDLVQLHRLTKTYQLIHKKiiAVNNISLGIPAGECFGL 2288
Cdd:TIGR01257 1899 ------HFFLSRWIAEPAKEPIfDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGL 1970
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2289 LGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLvGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKD 2368
Cdd:TIGR01257 1971 LGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM-GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEK 2049
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2369 TVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHS 2448
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2449 MEECEALCTRLAIMVNGRFQCIGSLQHIKSRFGRGFTVKVHLKNNK----VSMETLTKFMQLHFPKTYLKDQHLSMLEYH 2524
Cdd:TIGR01257 2130 MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQ 2209
                         1930      1940      1950      1960
                   ....*....|....*....|....*....|....*....|....*
gi 225703056  2525 VPVTAggVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQ 2569
Cdd:TIGR01257 2210 VSSSS--LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
 
Name Accession Description Interval E-value
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2254-2477 5.32e-98

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 317.52  E-value: 5.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqliHKKI-IAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGsLGHVDSHSSL 2332
Cdd:cd03263     1 LQIRNLTKTY---KKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2333 VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILL 2412
Cdd:cd03263    77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 2413 LDEPSSGMDPKSKRHLWRIISEEVQNKcSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIK 2477
Cdd:cd03263   157 LDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1350-1565 8.08e-96

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 311.36  E-value: 8.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGS--KTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHD 1427
Cdd:cd03263     5 NLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1428 VLFSYLTTKEHLLLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:cd03263    85 ALFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1508 GVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1565
Cdd:cd03263   163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2273-2418 1.46e-35

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: 278435  Cd Length: 150  Bit Score: 135.47  E-value: 1.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2273 VNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHL 2352
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPNLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2353 YFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDR----STSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2418
Cdd:pfam00005   81 RLGLRLKGLSKREKDARAEEALEKLGLGDLLDRpvgeNPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1361-1507 2.26e-34

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: 278435  Cd Length: 150  Bit Score: 132.00  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1361 VENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNT-VRKNMGVCMQHDVLFSYLTTKEHL 1439
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPNLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225703056  1440 LLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVG----TLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:pfam00005   81 RLGLRLK--GLSKREKDARAEEALEKLGLGDLLDRPVGenpgTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
2275-2447 5.13e-19

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: 88.57  E-value: 5.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2275 NISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVgYCPQEDALDDLVTVEEHLYF 2354
Cdd:TIGR01189   18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL-YLGHLPGLKPELSALENLHF 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2355 YARVHGipekDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISE 2434
Cdd:TIGR01189   97 WAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
                          170
                   ....*....|...
gi 225703056  2435 EVQNKCSVILTSH 2447
Cdd:TIGR01189  173 HLARGGIVLLTTH 185
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1347-1544 1.41e-15

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: 78.17  E-value: 1.41e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1347 ALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQH 1426
Cdd:TIGR01189    2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1427 DVLFSYLTTKEHLLLYGSIKVPHwtktqlHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1506
Cdd:TIGR01189   82 PGLKPELSALENLHFWAAIHGGA------QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 225703056  1507 TGVDPCSRRSIWDVISKNkTAR--TIILSTHH---LDEAEVLS 1544
Cdd:TIGR01189  156 TALDKAGVALLAGLLRAH-LARggIVLLTTHQdlgLVEARELR 197
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1355-1536 4.37e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127  Cd Length: 200  Bit Score: 67.28  E-value: 4.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1355 YGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLT 1434
Cdd:PRK13540   11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1435 TKEHLLLYgsikvPHWTKTQLH-EEVKRTLKdtgLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDpcs 1513
Cdd:PRK13540   91 LRENCLYD-----IHFSPGAVGiTELCRLFS---LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD--- 159
                         170       180
                  ....*....|....*....|....*..
gi 225703056 1514 RRSIWDVISKNKTAR----TIILSTHH 1536
Cdd:PRK13540  160 ELSLLTIITKIQEHRakggAVLLTSHQ 186
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
2273-2447 1.55e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127  Cd Length: 200  Bit Score: 65.36  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2273 VNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKS--GSLGHVDSHSSLVGYcpqEDALDDLVTVEE 2350
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikKDLCTYQKQLCFVGH---RSGINPYLTLRE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2351 HLYFyarvhGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWR 2430
Cdd:PRK13540   94 NCLY-----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
                         170
                  ....*....|....*..
gi 225703056 2431 IISEEVQNKCSVILTSH 2447
Cdd:PRK13540  169 KIQEHRAKGGAVLLTSH 185
NosY COG1277
ABC-type transport system involved in multi-copper enzyme maturation, permease component ...
1108-1269 1.81e-03

ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 224196  Cd Length: 278  Bit Score: 41.30  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1108 FFAWLIESIGFLLVTIAILIVILKF-GNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFP 1186
Cdd:COG1277   113 ALLVILIIILISFISLLTLLLLFGFpGNVSSISRLLLFLGSSLLYGLVLLSISLLISSLFSSSSLALLVSIILLLLFIIA 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1187 FIVLVTVEDELSYVIKVFMSLLSPTAFSYASQYIAryeeQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAW 1266
Cdd:COG1277   193 FSLILLFISVLLIGIAPTLNTLSLLLPLYLLAELA----FTILLQSGFSDSILTLNESLLLAWFNILILIIYILIFLSIA 268

                  ...
gi 225703056 1267 YVR 1269
Cdd:COG1277   269 YLI 271
ABC2_membrane_4 pfam12730
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
1056-1209 2.39e-03

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 289500  Cd Length: 225  Bit Score: 40.89  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1056 DNFLTSVSYSLPIVLMVAWVVFIAAFVKKlvyEKDLRLHEYMKMMGVNS----CSHFFAWLIESIGFLLVTIAILIVILK 1131
Cdd:pfam12730   39 DSLLLFSVLLLGLFLPLLIAILASLLISR---EFKNGTIKLLLTLPISRkkifLAKLLVLLLLSLLALLLLLLLSLLAGL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1132 F--GNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLS 1209
Cdd:pfam12730  116 LlgGGGSFGLGLLLLLLLSLLLSLLLILLQLFLSLLFRNSAGAIGIGILGVLLGLLLLLLGLSIWLPFSYSIRLLPPLLG 195
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
749-2569 0e+00

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 1259.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   749 NHTKDFLTYKLTKEEIAskYGIPLNATPFCFSLYKDIINMPAGPVIWAFLKPMLLGKILYSPYNPTTKAIMEKSNVTLRQ 828
Cdd:TIGR01257  343 NNYKAFLGIDSTRKDPI--YSYDKRTTSFCNALIQSLESNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEE 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   829 LAELREKSQEWMDKSPIFMNSFHLLNQtIPMLQNTLRNPFVQVFVKFSVGLDAV--ELL----------KQIDDLDVLRL 896
Cdd:TIGR01257  421 LERVRKLVKAWEEVGPQIWYFFDKSTQ-MTMIRDTLQNPTVKDFINRQLGEEGItaEAVlnflyngpreKQADDMTNFDW 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   897 KlvnniDIIDQLNTLSSLTVNISSCVLYDRIQASDTVEEMETVAEQLYKSNELFGSVIFKlpsngslhrGFDPEKVSLPP 976
Cdd:TIGR01257  500 R-----DIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRALSLLEENRFWAGVVFP---------DMYPWTSSLPP 565
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056   977 IVRYTIRMSLKTAQTTRSIRTKIWAPGPHNSPSHN--QIYGrAFIYLQDSIERAIIELQTgRNSQEVAVQVQAVPYPCFM 1054
Cdd:TIGR01257  566 HVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDfrYIWG-GFAYLQDMVEQGITRSQM-QAEPPVGIYLQQMPYPCFV 643
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1055 KDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESIGFLLVTIAILIVILKFGN 1134
Cdd:TIGR01257  644 DDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGR 723
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1135 ILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLSPTAFS 1214
Cdd:TIGR01257  724 ILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFG 803
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1215 YASQYIARYEEQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAWYVRNVFPGTYGMAAPWYFPILPSYWKER 1294
Cdd:TIGR01257  804 FGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGG 883
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1295 FGCAeVKHEKSnglmftnimMQNTNPSASKTSpDCAFPSNI-----EPEPKDLQVGVALHGVTKIY--GSKTAVENLNLN 1367
Cdd:TIGR01257  884 EGCS-TREERA---------LEKTEPLTEEME-DPEHPEGIndsffERELPGLVPGVCVKNLVKIFepSGRPAVDRLNIT 952
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1368 FYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKV 1447
Cdd:TIGR01257  953 FYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKG 1032
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1448 PHWTKTQLheEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTA 1527
Cdd:TIGR01257 1033 RSWEEAQL--EMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1528 RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKK----KSPNLDTNAIC------------- 1590
Cdd:TIGR01257 1111 RTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKmkniQSQRGGCEGTCsctskgfstrcpa 1190
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1591 -------------DTVAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKvSGAYLSLLRALDKGMGKLNIGCYGISDTTV 1657
Cdd:TIGR01257 1191 rvdeitpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFK-QRAYASLFRELEETLADLGLSSFGISDTPL 1269
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1658 EEVFLNLTKDS-----------QKSSNMSLEHltqrKVGNPSANGTSTPDDLSVSSSNFTDRDDKVLTRSEKlEGFG--- 1723
Cdd:TIGR01257 1270 EEIFLKVTEDAdsgslfaggaqQKRENANLRH----PCSGPTEKAGQTPQASHTCSPGQPAAHPEGQPPPEP-EDPGvpl 1344
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1724 -----LLLKKIMAILIKRFHHTRRNWKGLIAQVILPIVFVATAMGLGTLRDSSNSYPEIMISPSIYGtsEQTAFYANFDP 1798
Cdd:TIGR01257 1345 ntgarLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYG--QQYTFFSMDEP 1422
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1799 ST---SGLVSALWNFPGIDNVCLNTSDLQCLKKDDLGKWNTSG--------------EAIDNFGVCSCSDN-----VQEC 1856
Cdd:TIGR01257 1423 NSehlEVLADVLLNKPGFGNRCLKEEWLPEYPCGNSTPWKTPSvspnithlfqkqkwTAAHPSPSCRCSTRekltmLPEC 1502
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1857 PK--FNYHPPHRRTYSSQVIYNLTGKHMENYLITTANHFV-----------QKRYGGWSFGMKLT-------------ND 1910
Cdd:TIGR01257 1503 PEgaGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIrsslkskfwvnEQRYGGISIGGKLPaipitgealvgflSD 1582
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1911 L--RFDVTAVPDNRTLA----------------KVWYDPEGYHSLPAYLNSLNNFLLRVNM-SEYDAARHGIIMYSHPYP 1971
Cdd:TIGR01257 1583 LgqMMNVSGGPVTREASkempdflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLpKDRDPEEYGITVISQPLN 1662
                         1370      1380      1390      1400      1410      1420      1430      1440
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1972 GVQDQ--EQATISSLIDILVALSILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFS 2049
Cdd:TIGR01257 1663 LTKEQlsEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLV 1742
                         1450      1460      1470      1480      1490      1500      1510      1520
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2050 IGVIAIFKLPAFYSGNNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSivslSVVYFLSKEKPN 2129
Cdd:TIGR01257 1743 VGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINS----SAITFVLELFEN 1818
                         1530      1540      1550      1560      1570      1580      1590      1600
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2130 DPTLELISETLKRIFLIFPQFCFGYGLIELSQQQAVLDFLKAYGVEYPSETFEMDKLGAMFVALVSQGTMFFLLRLLINE 2209
Cdd:TIGR01257 1819 NRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQH 1898
                         1610      1620      1630      1640      1650      1660      1670      1680
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2210 wlikklRLFFRKFTSSPIMETV-DEDEDVRAERFRVESGAAEFDLVQLHRLTKTYQLIHKKiiAVNNISLGIPAGECFGL 2288
Cdd:TIGR01257 1899 ------HFFLSRWIAEPAKEPIfDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP--AVDRLCVGVRPGECFGL 1970
                         1690      1700      1710      1720      1730      1740      1750      1760
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2289 LGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLvGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKD 2368
Cdd:TIGR01257 1971 LGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNM-GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEK 2049
                         1770      1780      1790      1800      1810      1820      1830      1840
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2369 TVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHS 2448
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
                         1850      1860      1870      1880      1890      1900      1910      1920
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2449 MEECEALCTRLAIMVNGRFQCIGSLQHIKSRFGRGFTVKVHLKNNK----VSMETLTKFMQLHFPKTYLKDQHLSMLEYH 2524
Cdd:TIGR01257 2130 MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNMLQFQ 2209
                         1930      1940      1950      1960
                   ....*....|....*....|....*....|....*....|....*
gi 225703056  2525 VPVTAggVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQ 2569
Cdd:TIGR01257 2210 VSSSS--LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1346-1582 2.43e-70

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


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 241.06  E-value: 2.43e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYG-SKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCM 1424
Cdd:COG1131     5 IEVRNLTKKYGgDKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVKEPAKVRRRIGYVP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1425 QHDVLFSYLTTKEHLLLYGSIKVPhwTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1504
Cdd:COG1131    85 QEPSLYPELTVRENLEFFARLYGL--SKEEAEERIEELLELFGLEDKANKKVRTLSGGMKQRLSIALALLHDPELLILDE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1505 PSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKSP 1582
Cdd:COG1131   163 PTSGLDPESRREIWELLRelAKEGGVTILLSTHILEEAEELCDRVIILNDGKIIAEGTPEELKEKFGGKGVIELEPERLE 242
PRK13537 PRK13537
nodulation ABC transporter NodI; Provisional
1346-1567 1.13e-39

nodulation ABC transporter NodI; Provisional


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 152.65  E-value: 1.13e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQ 1425
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHLLLYGsiKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:PRK13537   88 FDNLDPDFTVRENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEP 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225703056 1506 STGVDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEA 1567
Cdd:PRK13537  166 TTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
1913-2174 3.80e-19

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 289468 [Multi-domain]  Cd Length: 345  Bit Score: 90.53  E-value: 3.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1913 FDVTAVPDNRTLAKVWYDPEGYHSLPAYLNSLNNFLLRVNMSEyDAARHGIIMYSHPYPGVQDQEQATISSLIDILVALS 1992
Cdd:pfam12698   89 FSRDLLKGESPTVTVYINSSNLLASKLILNALQSLLQQLNLSA-GVLPLEALSTSAPIPVESTPLFNPQSGYAYYLVGLI 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1993 ILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGVIaifkLPAFYSGNNLGAVSL 2072
Cdd:pfam12698  168 LFIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVYLLQLLIILLLL----FGFGIPFGNLGLLLL 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2073 LLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSIVSLsvvyflskekpndpTLELISETLKRIFLIFPQFCF 2152
Cdd:pfam12698  244 LFLLYGLAYIALGYLLGSLFKNSEDAQSIISIVILLLSGFFGGLF--------------PLEDPPSFLKWIFSIIPFFSP 309
                          250       260
                   ....*....|....*....|..
gi 225703056  2153 GYGLIELSQQQAVLDFLKAYGV 2174
Cdd:pfam12698  310 IDGLLRLIYGDSLWEIALSLII 331
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
7-86 2.67e-12

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 71.58  E-value: 2.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056     7 QLRILVWKNWLGVKRQPLWTLVLILWPVIIFIILAITRTKFPPTAKPTCYLAPRNLPSAGFFPFLQTLLCDTDSKCKDTP 86
Cdd:TIGR01257    6 QIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNPCFQSP 85
 
Name Accession Description Interval E-value
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2254-2477 5.32e-98

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 317.52  E-value: 5.32e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqliHKKI-IAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGsLGHVDSHSSL 2332
Cdd:cd03263     1 LQIRNLTKTY---KKGTkPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2333 VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILL 2412
Cdd:cd03263    77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 2413 LDEPSSGMDPKSKRHLWRIISEEVQNKcSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIK 2477
Cdd:cd03263   157 LDEPTSGLDPASRRAIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1350-1565 8.08e-96

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 311.36  E-value: 8.08e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGS--KTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHD 1427
Cdd:cd03263     5 NLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1428 VLFSYLTTKEHLLLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:cd03263    85 ALFDELTVREHLRFYARLK--GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1508 GVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1565
Cdd:cd03263   163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1346-1555 1.40e-60

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: 208.41  E-value: 1.40e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQ 1425
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHLllygsikvphwtktqlheevkrtlkdtglyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:cd03230    81 EPSLYENLTVRENL--------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1506 STGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGL 1555
Cdd:cd03230   123 TSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1350-1565 3.29e-57

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 200.67  E-value: 3.29e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVL 1429
Cdd:cd03265     5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQDLSV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1430 FSYLTTKEHLLLYGSIKVPHWTKtqLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGV 1509
Cdd:cd03265    85 DDELTGWENLYIHARLYGVPGAE--RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1510 DPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLK 1565
Cdd:cd03265   163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2254-2467 6.01e-55

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: 192.23  E-value: 6.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqlihKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSgSLGHVDSHSSLV 2333
Cdd:cd03230     1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD-IKKEPEEVKRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFyarvhgipekdikdtvhkllrrlhlmaykdrstsmcSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03230    76 GYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLIL 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 225703056 2414 DEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGRF 2467
Cdd:cd03230   120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
2254-2477 1.98e-49

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 177.95  E-value: 1.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYQlihkKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNilirnksgslGHVDSHSSL- 2332
Cdd:cd03265     1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGR----------ATVAGHDVVr 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2333 --------VGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALAL 2404
Cdd:cd03265    67 eprevrrrIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 225703056 2405 IGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQ-NKCSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIK 2477
Cdd:cd03265   147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1346-1559 2.48e-48

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 174.69  E-value: 2.48e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGhITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQ 1425
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHL----LLYGsikVPHwtkTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1501
Cdd:cd03264    80 EFGVYPNFTVREFLdyiaWLKG---IPS---KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1502 LDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1559
Cdd:cd03264   154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2254-2468 3.27e-48

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 174.30  E-value: 3.27e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqlihKKIIAVNNISLGIPAGeCFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGsLGHVDSHSSLV 2333
Cdd:cd03264     1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV-LKQPQKLRRRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03264    75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 2414 DEPSSGMDPKSKRHLWRIISEEVQNKCsVILTSHSMEECEALCTRLAIMVNGRFQ 2468
Cdd:cd03264   155 DEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLV 208
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1350-1556 7.84e-48

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 173.17  E-value: 7.84e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTVRKNMGVCMQHDVL 1429
Cdd:cd03268     5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1430 FSYLTTKEHLLLYGSIK-VPhwtktqlHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1508
Cdd:cd03268    84 YPNLTARENLRLLARLLgIR-------KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 225703056 1509 VDPCSRRSIWDVI-SKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1556
Cdd:cd03268   157 LDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
2254-2466 5.64e-46

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 167.84  E-value: 5.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqlihKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSlghvDSHSSLV 2333
Cdd:cd03269     1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03269    73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225703056 2414 DEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03269   153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
2255-2466 9.56e-44

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: 161.10  E-value: 9.56e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2255 QLHRLTKTYQliHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVG 2334
Cdd:cd03225     1 ELKNLSFSYP--DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2335 YCPQeDALDDLV--TVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILL 2412
Cdd:cd03225    79 LVFQ-NPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 225703056 2413 LDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03225   158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1348-1553 2.95e-43

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: 159.94  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKT--AVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI-KTDLNTVRKNMGVCM 1424
Cdd:cd03225     2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1425 QH-DVLFSYLTTKE----HLLLYGsikvphWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1499
Cdd:cd03225    82 QNpDDQFFGPTVEEevafGLENLG------LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 1500 VILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2254-2466 5.63e-43

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 158.92  E-value: 5.63e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYqlihKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIrnKSGSLGHVDSHSSLV 2333
Cdd:cd03268     1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--DGKSYQKNIEALRRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIkdtvHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03268    75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225703056 2414 DEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03268   151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
2253-2466 5.97e-43

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 159.07  E-value: 5.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2253 LVQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSL 2332
Cdd:cd03266     1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2333 vGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILL 2412
Cdd:cd03266    81 -GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 225703056 2413 LDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03266   160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1348-1553 4.38e-42

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: 156.53  E-value: 4.38e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTVRKNMGVCMQHD 1427
Cdd:cd03259     3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQDY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1428 VLFSYLTTKEHlLLYGsIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:cd03259    82 ALFPHLTVAEN-IAFG-LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 225703056 1508 GVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03259   160 ALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEG 207
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1346-1553 8.12e-41

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 152.82  E-value: 8.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDlntVRKNMGVCMQ 1425
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHLLLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:cd03269    78 ERGLYPKMKVIDQLVYLAQLK--GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 225703056 1506 STGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03269   156 FSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKG 204
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1350-1561 1.78e-38

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 146.81  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCM--QHD 1427
Cdd:cd03219     5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtfQIP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1428 VLFSYLTTKEHLLLYGSIKVPHWT--------KTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRV 1499
Cdd:cd03219    85 RLFPELTVLENVMVAAQARTGSGLllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225703056 1500 VILDEPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03219   165 LLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1346-1550 1.98e-38

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


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 146.08  E-value: 1.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSK----TAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIktdlNTVRKNMG 1421
Cdd:cd03293     1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1422 VCMQHDVLFSYLTTKEHLLLygSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVI 1501
Cdd:cd03293    77 YVFQQDALLPWLTVLDNVAL--GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1502 LDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFL 1550
Cdd:cd03293   155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVL 205
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistant to organic solvents; ABC ...
1348-1561 3.55e-38

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: 145.72  E-value: 3.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI----KTDLNTVRKNMGVC 1423
Cdd:cd03261     3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMGML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1424 MQHDVLFSYLTTKEhlllygSIKVPHWTKTQLHEE-----VKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSR 1498
Cdd:cd03261    83 FQSGALFDSLTVFE------NVAFPLREHTRLSEEeireiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 1499 VVILDEPSTGVDPCSRRSIWDVIS--KNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03261   157 LLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1346-1556 1.70e-37

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 143.28  E-value: 1.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKT----AVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMG 1421
Cdd:cd03266     2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1422 VCMQHDVLFSYLTTKEHLLLYGSIkvpHWTK-TQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVV 1500
Cdd:cd03266    82 FVSDSTGLYDRLTARENLEYFAGL---YGLKgDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 225703056 1501 ILDEPSTGVDPCSRRSIWDVISKNKTA-RTIILSTHHLDEAEVLSDRIAFLEQGGLR 1556
Cdd:cd03266   159 LLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2254-2471 2.45e-37

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: 142.66  E-value: 2.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYQlihkKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSgsLGHVDSHSSLV 2333
Cdd:cd03259     1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD--VTGVPPERRNI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03259    75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 225703056 2414 DEPSSGMDPKSKRHLWRIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGRFQCIG 2471
Cdd:cd03259   155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1346-1561 2.33e-36

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: 140.90  E-value: 2.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIY-GSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIK-TDLNTVRKNMGVC 1423
Cdd:cd03295     1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKIGYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1424 MQHDVLFSYLTTKEHLLLygsikVP---HWTKTQLHEEVKRTLKDTGL----YSHRHKRvgTLSGGMKRKLSISIALIGG 1496
Cdd:cd03295    81 IQQIGLFPHMTVEENIAL-----VPkllKWPKEKIRERADELLALVGLdpaeFADRYPH--ELSGGQQQRVGVARALAAD 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225703056 1497 SRVVILDEPSTGVDPCSRRSIWDVISKNKTA--RTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03295   154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1346-1561 4.07e-36

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 139.68  E-value: 4.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTVRKNMGVCMQ 1425
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHlLLYGsIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:cd03300    80 NYALFPHLTVFEN-IAFG-LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1506 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03300   158 LGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1348-1553 7.18e-36

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: 136.61  E-value: 7.18e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI-KTDLNTVRKNMGVCMQh 1426
Cdd:cd00267     2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVPQ- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1427 dvlfsylttkehlllygsikvphwtktqlheevkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVILDEPS 1506
Cdd:cd00267    81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 225703056 1507 TGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd00267   109 SGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1348-1553 8.46e-36

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: 138.05  E-value: 8.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDlntvRKNMG-VCMQH 1426
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGyVPQRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1427 DVLFSY-LTTKEHLL--LYGSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILD 1503
Cdd:cd03235    78 SIDRDFpISVRDVVLmgLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1504 EPSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03235   158 EPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
2255-2466 1.44e-35

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: 135.84  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2255 QLHRLTKTYqlihKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVG 2334
Cdd:cd00267     1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2335 YCPQedalddlvtveehlyfyarvhgipekdikdtvhkllrrlhlmaykdrstsmCSYGTKRKLSTALALIGKPSILLLD 2414
Cdd:cd00267    77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 225703056 2415 EPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd00267   106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
2273-2418 1.46e-35

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: 278435  Cd Length: 150  Bit Score: 135.47  E-value: 1.46e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2273 VNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHL 2352
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPNLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  2353 YFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDR----STSMCSYGTKRKLSTALALIGKPSILLLDEPSS 2418
Cdd:pfam00005   81 RLGLRLKGLSKREKDARAEEALEKLGLGDLLDRpvgeNPGTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
2259-2466 7.61e-35

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 136.13  E-value: 7.61e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2259 LTKTYqlihKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSL-VGYCP 2337
Cdd:cd03218     6 LSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2338 QEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPS 2417
Cdd:cd03218    82 QEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 225703056 2418 SGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03218   162 AGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGK 210
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1361-1507 2.26e-34

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: 278435  Cd Length: 150  Bit Score: 132.00  E-value: 2.26e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056  1361 VENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNT-VRKNMGVCMQHDVLFSYLTTKEHL 1439
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPNLFPRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225703056  1440 LLYGSIKvpHWTKTQLHEEVKRTLKDTGLYSHRHKRVG----TLSGGMKRKLSISIALIGGSRVVILDEPST 1507
Cdd:pfam00005   81 RLGLRLK--GLSKREKDARAEEALEKLGLGDLLDRPVGenpgTLSGGQKQRVAIARALLTKPKLLLLDEPTA 150
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1346-1553 4.90e-34

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


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 133.46  E-value: 4.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGA-----TAGTIFVYGKDI---KTDLNTVR 1417
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydlDVDVLELR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1418 KNMGVCMQHDVLFSyLTTKEHLL----LYGSikvphWTKTQLHEEVKRTLKDTGL--YSHRHKRVGTLSGGMKRKLSISI 1491
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIYDNVAyglrLHGI-----KLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLAR 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225703056 1492 ALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03260   155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNG 216
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1348-1553 5.84e-34

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 131.93  E-value: 5.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTV---RKNMGVCM 1424
Cdd:cd03229     3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGMVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1425 QHDVLFSYLTTKEHLLLygsikvphwtktqlheevkrtlkdtglyshrhkrvgTLSGGMKRKLSISIALIGGSRVVILDE 1504
Cdd:cd03229    83 QDFALFPHLTVLENIAL------------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1505 PSTGVDPCSRRSIWDVISKNKT--ARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03229   127 PTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARLADRVVVLRDG 177
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1348-1553 9.23e-34

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 132.56  E-value: 9.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNT---VRKNMGVCM 1424
Cdd:cd03224     3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI-TGLPPherARAGIGYVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1425 QHDVLFSYLTTKEHLLLYGSIKVPHWTKTQLhEEVKRTLKDtgLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDE 1504
Cdd:cd03224    82 EGRRIFPELTVEENLLLGAYARRRAKRKARL-ERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 225703056 1505 PSTGVDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03224   159 PSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERG 208
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
2254-2462 5.34e-33

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


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 130.28  E-value: 5.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSgslghVDSHSSLV 2333
Cdd:cd03293     1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03293    76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225703056 2414 DEPSSGMDPKSKRH----LWRIISEEVQnkcSVILTSHSMEECEALCTRLAIM 2462
Cdd:cd03293   156 DEPFSALDALTREQlqeeLLDIWRETGK---TVLLVTHDIDEAVFLADRVVVL 205
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1350-1561 1.28e-32

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


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 129.59  E-value: 1.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1350 GVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNT---VRKNMGVCMQH 1426
Cdd:cd03218     5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDI-TKLPMhkrARLGIGYLPQE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1427 DVLFSYLTTKEHLLLYGSIKVPhwTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPS 1506
Cdd:cd03218    84 ASIFRKLTVEENILAVLEIRGL--SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 225703056 1507 TGVDPCSRRSIWDVIsKNKTARTI-ILST-HHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03218   162 AGVDPIAVQDIQKII-KILKDRGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTP 217
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1346-1553 1.87e-32

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


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 129.24  E-value: 1.87e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSK----TAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKT----DLNTVR 1417
Cdd:cd03258     2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1418 KNMGVCMQHDVLFSYLTTKEHLLLygSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGS 1497
Cdd:cd03258    82 RRIGMIFQHFNLLSSRTVFENVAL--PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 225703056 1498 RVVILDEPSTGVDPCSRRSIWDVISK-NKTAR-TIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03258   160 KVLLCDEATSALDPETTQSILALLRDiNRELGlTIVLITHEMEVVKRICDRVAVMEKG 217
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1346-1553 7.30e-32

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 126.88  E-value: 7.30e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI---KTDLNTVRKNMGV 1422
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1423 CMQHDVLFSYLTTKEHLLLyGSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVIL 1502
Cdd:cd03262    81 VFQQFNLFPHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225703056 1503 DEPSTGVDPCSRRSIWDVIsKN--KTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03262   160 DEPTSALDPELVGEVLDVM-KDlaEEGMTMVVVTHEMGFAREVADRVIFMDDG 211
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1346-1553 2.76e-31

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: 123.65  E-value: 2.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKT--AVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKT-DLNTVRKNMGV 1422
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1423 CMQHDVLFSylttkehlllyGSIKvphwtktqlhEEVkrtlkdtglyshrhkrvgtLSGGMKRKLSISIALIGGSRVVIL 1502
Cdd:cd03228    81 VPQDPFLFS-----------GTIR----------ENI-------------------LSGGQRQRIAIARALLRDPPILIL 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1503 DEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEvLSDRIAFLEQG 1553
Cdd:cd03228   121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
2267-2466 3.44e-31

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 125.52  E-value: 3.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2267 HKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILI------RNKSGslgHVDSHSSLVGycpQED 2340
Cdd:cd03267    31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpwKRRKK---FLRRIGVVFG---QKT 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2341 ALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGM 2420
Cdd:cd03267   105 QLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 225703056 2421 DPKSKRHLWRIISEEVQN-KCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03267   185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
2270-2478 4.26e-31

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


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 125.24  E-value: 4.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2270 IIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSgslghvdshssLVGYCPQEDA-------- 2341
Cdd:cd03219    13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED-----------ITGLPPHEIArlgigrtf 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2342 -----LDDLvTVEE----------HLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIG 2406
Cdd:cd03219    82 qiprlFPEL-TVLEnvmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 225703056 2407 KPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIKS 2478
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1347-1559 7.53e-31

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: 122.93  E-value: 7.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1347 ALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKT-DLNTVRKNMGVcmq 1425
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAY--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 hdvlfsylttkehlllygsikVPhwtktQLheevkrtLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:cd03214    78 ---------------------VP-----QA-------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 225703056 1506 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCG 1559
Cdd:cd03214   125 TSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
2271-2471 9.94e-31

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: 123.41  E-value: 9.94e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2271 IAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHvdshsSLVGYCPQEDALD-DL-VTV 2348
Cdd:cd03235    13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRRSIDrDFpISV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2349 EE----HLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKS 2424
Cdd:cd03235    88 RDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 225703056 2425 KRHLWRIISEEVQNKCSVILTSHSMEECEALCTRlAIMVNGRFQCIG 2471
Cdd:cd03235   168 QEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1348-1553 1.04e-30

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 124.22  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1348 LHGVTKIYGS-KTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI----KTDLNTVRKNMGV 1422
Cdd:cd03256     3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRRQIGM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1423 CMQHDVLFSYLTTKEHLLLyGSIKVPHWTKT---QLHEEVKR----TLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIG 1495
Cdd:cd03256    83 IFQQFNLIERLSVLENVLS-GRLGRRSTWRSlfgLFPKEEKQralaALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1496 GSRVVILDEPSTGVDPCSRRSIWDVISKNKTAR--TIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03256   162 QPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREYADRIVGLKDG 221
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1330-1561 1.92e-30

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


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 124.29  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1330 AFPSNIEPEPKDLQVGVALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDI 1409
Cdd:cd03294     9 IFGKNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1410 ----KTDLNTVR-KNMGVCMQHDVLFSYLTTKEHlLLYGsIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMK 1484
Cdd:cd03294    89 aamsRKELRELRrKKISMVFQSFALLPHRTVLEN-VAFG-LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQ 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 225703056 1485 RKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03294   167 QRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
2254-2484 4.04e-30

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 122.35  E-value: 4.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2254 VQLHRLTKTYQlihkKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSgsLGHVDSHSSLV 2333
Cdd:cd03300     1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2334 GYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLL 2413
Cdd:cd03300    75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 225703056 2414 DEPSSGMDPKSKRHLwRIISEEVQNKC--SVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHI----KSRFGRGF 2484
Cdd:cd03300   155 DEPLGALDLKLRKDM-QLELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRFVADF 230
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1346-1553 4.29e-30

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 121.83  E-value: 4.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGS----KTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTV----- 1416
Cdd:cd03255     1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1417 -RKNMGVCMQHDVLFSYLTTKEHLLLYGSI-KVPhwtKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALI 1494
Cdd:cd03255    80 rRRHIGFVFQSFNLLPDLTALENVELPLLLaGVP---KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 225703056 1495 GGSRVVILDEPSTGVDPCSRRSIWDVISK-NKTA-RTIILSTHHLDEAEvLSDRIAFLEQG 1553
Cdd:cd03255   157 NDPKIILADEPTGNLDSETGKEVMELLRElNKEAgTTIVVVTHDPELAE-YADRIIELRDG 216
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
2253-2466 3.70e-29

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: 119.15  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2253 LVQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNK---SGSLGHVDSH 2329
Cdd:cd03257     1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2330 SSLVGYCPQE--DALDDLVTVEEHLYFYARVHGIPEKD--IKDTVHKLLRRLHLMA-YKDRSTSMCSYGTKRKLSTALAL 2404
Cdd:cd03257    81 RKEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 225703056 2405 IGKPSILLLDEPSSGMDPKSKRHLWRIISE-EVQNKCSVILTSHSMEECEALCTRLAIMVNGR 2466
Cdd:cd03257   161 ALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1346-1556 4.25e-29

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 118.51  E-value: 4.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1346 VALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTVRKNMGVCMQ 1425
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMVFQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1426 HDVLFSYLTTKEHLLLygSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEP 1505
Cdd:cd03301    80 NYALYPHMTVYDNIAF--GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 225703056 1506 STGVDPCSRRSIWDVISK--NKTARTIILSTHHLDEAEVLSDRIAFLEQGGLR 1556
Cdd:cd03301   158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1353-1553 1.73e-28

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II 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. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most 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: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 116.59  E-value: 1.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1353 KIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKtdLNTVRKNMGVCMQH--DVLF 1430
Cdd:cd03226     8 SYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYVMQDvdYQLF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1431 SYlTTKEHLLLygSIKVPHWTKTQLhEEVkrtLKDTGLYS--HRHKRvgTLSGGMKRKLSISIALIGGSRVVILDEPSTG 1508
Cdd:cd03226    86 TD-SVREELLL--GLKELDAGNEQA-ETV---LKDLDLYAlkERHPL--SLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 225703056 1509 VDPCSRRSIWDVISK-NKTARTIILSTHHLDEAEVLSDRIAFLEQG 1553
Cdd:cd03226   157 LDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
2255-2465 1.17e-27

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II 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. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most 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: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 114.28  E-value: 1.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2255 QLHRLTKTYqliHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGhvdSHSSLVG 2334
Cdd:cd03226     1 RIENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 2335 YCPQEdaLDD---LVTVEEHLYFyarvhGIPEK-DIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSI 2410
Cdd:cd03226    75 YVMQD--VDYqlfTDSVREELLL-----GLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 225703056 2411 LLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNG 2465
Cdd:cd03226   148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1361-1561 6.51e-27

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 112.81  E-value: 6.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1361 VENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIkTDLNTVRKNMGVCMQHDVLFSYLTTKEHLL 1440
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1441 lYGsIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIW-- 1518
Cdd:cd03299    94 -YG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRee 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 225703056 1519 --DVISKNKTarTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSP 1561
Cdd:cd03299   172 lkKIRKEFGV--TVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1363-1559 1.79e-26

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 111.21  E-value: 1.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1363 NLNLNFYEGHITSLLGPNGAGKTTTISMLTGLF---GATAGTIFVYGKDIKTDLntVRKNMGVCMQHDVLFSYLTTKEHL 1439
Cdd:cd03234    25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQPRKPDQ--FQKCVAYVRQDDILLPGLTVRETL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225703056 1440 LLYGSIKVP-HWTKTQLHEEVKRT-LKDTGLYSH