|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-576 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 603.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 1 MGIFKKLGWYFKQESRRYLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYLFRYGWRTR 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG-DLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 81 IWGGAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRL 160
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL-FVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 161 TLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMI 240
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 241 DGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETST 320
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 321 IIEAPNAIQ-TPATGDINYAVQKFTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH 399
Cdd:COG1132 324 IPDPPGAVPlPPVRGEIEFENVSFSYPGDR-PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 400 DIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQK 479
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQR 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 480 QRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALL 559
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELL 562
|
570
....*....|....*..
gi 2018945286 560 AEDGWYAEMWLKQQLSQ 576
Cdd:COG1132 563 ARGGLYARLYRLQFGEE 579
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-581 |
0e+00 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 543.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFM 101
Cdd:PRK10789 1 VALLIIIAMLQLIPPKVVGIIVDGVTEQHMTTGQILMWIGTMVLIAVVVYLLRYVWRVLLFGASYQLAVELREDFYRQLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 102 KMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIFVDWRLTLMALIPMPLLAVASRQLGAH 181
Cdd:PRK10789 81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGDQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 182 LHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTII 261
Cdd:PRK10789 161 LHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 262 YGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIEAPNAIqtPAT-GDINYAV 340
Cdd:PRK10789 241 GGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPV--PEGrGELDVNI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 341 QKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDN 420
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 501 LSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQQLSQALGG 580
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDD 558
|
.
gi 2018945286 581 A 581
Cdd:PRK10789 559 A 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-573 |
1.38e-143 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 431.95 E-value: 1.38e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 6 KLGWYFK--QESRRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIDTHQLTPqkLIMWLGI-LLSAAILQYLFRYgWRTRI 81
Cdd:COG2274 143 GLRWFLRllRRYRRLLLQVLLAsLLINLLALATPLFTQVVIDRVLPNQDLS--TLWVLAIgLLLALLFEGLLRL-LRSYL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 82 WGGAA-KLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHAtNDLTAIQQ-VAGAGILTFADSIITggTTIIAMVIFVDWR 159
Cdd:COG2274 220 LLRLGqRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREfLTGSLLTALLDLLFV--LIFLIVLFFYSPP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 160 LTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNM 239
Cdd:COG2274 297 LALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 240 IDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETS 319
Cdd:COG2274 377 LSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPP 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 320 TIIEAPNAIQTPA-TGDInyAVQK--FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQI 396
Cdd:COG2274 457 EREEGRSKLSLPRlKGDI--ELENvsFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 397 DGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSG 476
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 477 GQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHE 556
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
570
....*....|....*..
gi 2018945286 557 ALLAEDGWYAEMWLKQQ 573
Cdd:COG2274 695 ELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
18-311 |
6.51e-130 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 381.76 E-value: 6.51e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 18 YLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLF 97
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQ 177
Cdd:cd18541 81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMM-FTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 178 LGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYI 257
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 258 VTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
16-568 |
4.59e-108 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 335.90 E-value: 4.59e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGV----IFLVLVAVVQIVPPKVIGTLVD---LIDTHQLTPQKLIMWLGILLSAAILQYlFRYGWRTRIwggAAKL 88
Cdd:TIGR02204 14 RPYRGRVlaalVALLITAAATLSLPYAVRLMIDhgfSKDSSGLLNRYFAFLLVVALVLALGTA-ARFYLVTWL---GERV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 89 ERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIfVDWRLTLMALIPM 168
Cdd:TIGR02204 90 VADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFI-TSPKLTSLVLLAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 169 PLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTI-----AINKRVNMIDGL 243
Cdd:TIGR02204 169 PLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYeaarqRIRTRALLTAIV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 244 FDPAISLIIGLTYIvtiiyGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTII- 322
Cdd:TIGR02204 249 IVLVFGAIVGVLWV-----GAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKa 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 323 -EAPNAIQTPATGDINYAVQKFTYPGD-KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHD 400
Cdd:TIGR02204 324 pAHPKTLPVPLRGEIEFEQVNFAYPARpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 401 IRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQ 480
Cdd:TIGR02204 404 LRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 481 RIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:TIGR02204 484 RIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563
|
....*...
gi 2018945286 561 EDGWYAEM 568
Cdd:TIGR02204 564 KGGLYARL 571
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-566 |
1.10e-104 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 327.06 E-value: 1.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 3 IFKKLGWYFKQESRRYLWGVIFLVLVAVVQIVPPKVIGTLVDliDTHQLTPQKLIMWL-----GILLSAAILQYLFRY-- 75
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLD--DGFGGRDRSVLWWVplvviGLAVLRGICSFVSTYll 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 76 GWRTRiwggaaKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTaiqQVAGAGIltfaDSIIT---GGTTIIAM 152
Cdd:TIGR02203 79 SWVSN------KVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSE---QVASAAT----DAFIVlvrETLTVIGL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 153 VIFV---DWRLTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTK 229
Cdd:TIGR02203 146 FIVLlyySWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 230 TIAINKRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYD 309
Cdd:TIGR02203 226 NRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 310 RVDQLLKETSTIIEAPNAIQTpATGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ 389
Cdd:TIGR02203 306 SLFTLLDSPPEKDTGTRAIER-ARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 390 YQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDR-SQAAVEDAAIASAVHDDILTFAQGYETVVG 468
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQaDRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 469 ERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQ 548
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570
....*....|....*...
gi 2018945286 549 IIERGTHEALLAEDGWYA 566
Cdd:TIGR02203 545 IVERGTHNELLARNGLYA 562
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-572 |
5.51e-98 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 297.99 E-value: 5.51e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPgDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNF 421
Cdd:cd03253 7 TFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:cd03253 86 LFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 502 SAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQ 572
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
92-569 |
1.61e-96 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 305.54 E-value: 1.61e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAmVIFVDWRLTLMALIPMPLL 171
Cdd:COG4987 90 LRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAF-LAFFSPALALVLALGLLLA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQA-AFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISL 250
Cdd:COG4987 169 GLLLPLLAARLGRRAGRRLAaARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 251 IIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIEAPNAIQT 330
Cdd:COG4987 249 AAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 331 PATGDInyAVQK--FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDA 408
Cdd:COG4987 329 PGGPSL--ELEDvsFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 409 LLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAM 488
Cdd:COG4987 407 LRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 489 MTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEM 568
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
.
gi 2018945286 569 W 569
Cdd:COG4987 567 Y 567
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
249-573 |
6.11e-96 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 305.21 E-value: 6.11e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 249 SLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIEAPNAI 328
Cdd:COG5265 270 ALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 329 QTPATGDinyAVQ----KFTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDY 404
Cdd:COG5265 350 PLVVGGG---EVRfenvSFGYDPER-PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDV 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 405 SLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAI 484
Cdd:COG5265 426 TQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAI 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 485 ARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGW 564
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGL 585
|
....*....
gi 2018945286 565 YAEMWLKQQ 573
Cdd:COG5265 586 YAQMWARQQ 594
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
343-569 |
6.93e-95 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 289.90 E-value: 6.93e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03251 88 FNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMW 569
Cdd:cd03251 168 ALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
91-576 |
2.97e-92 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 295.00 E-value: 2.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 91 TLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDltaIQQVAGA--GILTfadSIITGGTTII---AMVIFVDWRLTLMAL 165
Cdd:PRK11176 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYD---SEQVASSssGALI---TVVREGASIIglfIMMFYYSWQLSLILI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFD 245
Cdd:PRK11176 173 VIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISD 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 246 PAISLIIGLTyIVTIIYGGTL--VMHhSISIGQLISFISYIAALVWPMFAigrLFNV---LERGNASYDRVDQLL----- 315
Cdd:PRK11176 253 PIIQLIASLA-LAFVLYAASFpsVMD-TLTAGTITVVFSSMIALMRPLKS---LTNVnaqFQRGMAACQTLFAILdleqe 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 316 KETSTI-IEapnaiqtPATGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVI 394
Cdd:PRK11176 328 KDEGKRvIE-------RAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 395 QIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDR-SQAAVEDAAIASAVHDDILTFAQGYETVVGERGVS 473
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 474 LSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
490 500
....*....|....*....|...
gi 2018945286 554 THEALLAEDGWYAEMWlKQQLSQ 576
Cdd:PRK11176 561 THAELLAQNGVYAQLH-KMQFGQ 582
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-563 |
1.66e-88 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 284.34 E-value: 1.66e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 15 SRRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLR 93
Cdd:COG4988 15 ARRWLALAVLLgLLSGLLIIAQAWLLASLLAGLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 94 SRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQ--------QVAGAGILTFadsiitggtTIIAMVIFVDWRLTLMAL 165
Cdd:COG4988 95 RRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDgyfarylpQLFLAALVPL---------LILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTK----TIAInKRVNMID 241
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrTMKV-LRVAFLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 242 GLfdpAISLIIGLTYIVTIIYGGTLVMHHSISIGQLIsFISYIAALV-WPMFAIGRLFNVLERGNASYDRVDQLLKETST 320
Cdd:COG4988 245 SA---VLEFFASLSIALVAVYIGFRLLGGSLTLFAAL-FVLLLAPEFfLPLRDLGSFYHARANGIAAAEKIFALLDAPEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 321 IIEAPNAiQTPATGDINYAVQK--FTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDG 398
Cdd:COG4988 321 AAPAGTA-PLPAAGPPSIELEDvsFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 399 HDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQ 478
Cdd:COG4988 399 VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 479 KQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEAL 558
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558
|
....*
gi 2018945286 559 LAEDG 563
Cdd:COG4988 559 LAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-572 |
2.16e-88 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 273.26 E-value: 2.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDK-QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDN 420
Cdd:cd03249 7 SFRYPSRPdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:cd03249 87 VLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 501 LSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQ 572
Cdd:cd03249 167 TSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
60-572 |
2.86e-86 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 282.02 E-value: 2.86e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 60 LGILLSAAILQYLFRYGWRTRIWG-GAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHaTNDLTAIQQ-VAGAGILT 137
Cdd:TIGR01846 181 LALAMLAVAIFEPALGGLRTYLFAhLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVAR-VRELEQIRNfLTGSALTV 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 138 FADSIITggTTIIAMVIFVDWRLTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEE 217
Cdd:TIGR01846 260 VLDLLFV--VVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEP 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 218 ADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRL 297
Cdd:TIGR01846 338 QFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 298 FNVLERGNASYDRVDQLLKETSTIIEAPNAIQTPATGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKT 377
Cdd:TIGR01846 418 WQDFQQTGIALERLGDILNSPTEPRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKS 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 378 TLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDIL 457
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFIS 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 458 TFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMH 537
Cdd:TIGR01846 578 ELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRA 657
|
490 500 510
....*....|....*....|....*....|....*
gi 2018945286 538 ADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQ 572
Cdd:TIGR01846 658 CDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
3-568 |
7.82e-85 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 278.91 E-value: 7.82e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 3 IFKKLGwYFKQESRRYLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQlTPQKL---IMWLGIL-----LSAAILQYLFR 74
Cdd:TIGR00958 149 LFRLLG-LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDK-GPPALasaIFFMCLLsiassVSAGLRGGSFN 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 75 YGwrtriwggAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvI 154
Cdd:TIGR00958 227 YT--------MARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM-L 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 155 FVDWRLTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAIN 234
Cdd:TIGR00958 298 WLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 235 KRvNMIDGLFDPAISLIIGLTYIVTII-YGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQ 313
Cdd:TIGR00958 378 KR-KALAYAGYLWTTSVLGMLIQVLVLyYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 314 LLKETSTIieAPNAIQTPA--TGDINYAVQKFTYPG-DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQY 390
Cdd:TIGR00958 457 YLDRKPNI--PLTGTLAPLnlEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 391 QGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGER 470
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 471 GVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETiLMNLKTmRADQTTIITANRLSSVMHADEIIVMDDGQII 550
Cdd:TIGR00958 615 GSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQL-LQESRS-RASRTVLLIAHRLSTVERADQILVLKKGSVV 692
|
570
....*....|....*...
gi 2018945286 551 ERGTHEALLAEDGWYAEM 568
Cdd:TIGR00958 693 EMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
334-563 |
5.02e-77 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 243.29 E-value: 5.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 334 GDINYAVQKFTYpGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSI 413
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 414 GYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPE 493
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDG 563
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
10-568 |
1.17e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 251.42 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 10 YFKQESRRYLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLG-----ILLSAAILQYLFRYGWRTRIwgg 84
Cdd:PRK13657 13 YLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGDIFPLLAAWAGfglfnIIAGVLVARHADRLAHRRRL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 85 aaklerTLRSRLFWHFMKMDTTFFQKHRTGDLMaHATndLTAIQQVAGAGILTFAD--SIITGGTTIIAMVIFVDWRLTL 162
Cdd:PRK13657 90 ------AVLTEYFERIIQLPLAWHSQRGSGRAL-HTL--LRGTDALFGLWLEFMREhlATLVALVVLLPLALFMNWRLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 163 MaLIPMPLLAVASRQLGAHlHTAFGQSQ--AAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMI 240
Cdd:PRK13657 161 V-LVVLGIVYTLITTLVMR-KTKDGQAAveEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 241 DGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALvwpmfaIGRL------FNVLERGNASYDRVDQL 314
Cdd:PRK13657 239 WALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLL------IGRLdqvvafINQVFMAAPKLEEFFEV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 315 LKETSTIIEAPNAIQTP-ATGDINYAVQKFTYPGdKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGV 393
Cdd:PRK13657 313 EDAVPDVRDPPGAIDLGrVKGAVEFDDVSFSYDN-SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 394 IQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVS 473
Cdd:PRK13657 392 ILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQ 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 474 LSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
570
....*....|....*
gi 2018945286 554 THEALLAEDGWYAEM 568
Cdd:PRK13657 552 SFDELVARGGRFAAL 566
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
343-572 |
1.40e-72 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 232.38 E-value: 1.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQ 572
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
343-548 |
1.60e-68 |
|
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: 219.18 E-value: 1.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03228 8 FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIrfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03228 88 FSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILILDEATS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQ 548
Cdd:cd03228 126 ALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-568 |
5.57e-65 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 225.39 E-value: 5.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 13 QESRRYLWGVIFLVLVAVVQIVppkviGT--LVDLIDTHqlTPQKLIMWLGI----LLSAAILQYLFRYGWRTRIWGGAA 86
Cdd:TIGR01193 153 RQKKLIVNIVIAAIIVTLISIA-----GSyyLQKIIDTY--IPHKMMGTLGIisigLIIAYIIQQILSYIQIFLLNVLGQ 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 87 KLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATnDLTAIQQVAGAGILT-FADSIITGGTTIIamVIFVDWRLTLMAL 165
Cdd:TIGR01193 226 RLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSlFLDMWILVIVGLF--LVRQNMLLFLLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADvadFNEIVTKTIA-INKR-VNMIDGL 243
Cdd:TIGR01193 303 LSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAER---YSKIDSEFGDyLNKSfKYQKADQ 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 244 FDPAISLIIGLTYIVTIIY-GGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTII 322
Cdd:TIGR01193 380 GQQAIKAVTKLILNVVILWtGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFI 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 323 EAPNAIQTP-ATGDINYAVQKFTYpGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI 401
Cdd:TIGR01193 460 NKKKRTELNnLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 402 RDYSLDALLDSIGYVPQDNFLFSTDVRDNIRF-ADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQ 480
Cdd:TIGR01193 539 KDIDRHTLRQFINYLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQ 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 481 RIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRaDQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD 697
|
....*...
gi 2018945286 561 EDGWYAEM 568
Cdd:TIGR01193 698 RNGFYASL 705
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
18-311 |
8.00e-64 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 211.14 E-value: 8.00e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 18 YLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTpQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLF 97
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLR-ELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQ 177
Cdd:cd18542 80 DHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIM-FSINWKLTLISLAIIPFIALFSYV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 178 LGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYI 257
Cdd:cd18542 159 FFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 258 VTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18542 239 LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-561 |
2.04e-63 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 218.08 E-value: 2.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 13 QESRRYLWGV-IFLVLVAVVQIVPP--------KVIG-----TLVDLIdthqltpqkLIMwLGILLSAAILQYLfrygwR 78
Cdd:COG4618 16 RACRRAFLSVgLFSFFINLLMLTPPlymlqvydRVLTsrsvdTLLMLT---------LLA-LGLYAVMGLLDAV-----R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 79 TRIWG-GAAKLERTLRSRLFwhfmkmdTTFFQKHRTGDLMAHAT--NDLTAIQQ-VAGAGILTFADSIIT---------- 144
Cdd:COG4618 81 SRILVrVGARLDRRLGPRVF-------DAAFRAALRGGGGAAAQalRDLDTLRQfLTGPGLFALFDLPWApiflavlflf 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 145 ----GGTTIIAMVIfvdwrLTLMALI-------PMPLLAVASRQLGAHLHTAFGQSQ---------AAFSRLNDKTQESV 204
Cdd:COG4618 154 hpllGLLALVGALV-----LVALALLnerltrkPLKEANEAAIRANAFAEAALRNAEvieamgmlpALRRRWQRANARAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 205 SgikvlktfgqEEADVADFNEIVTktiAINKRVNMIdglfdpAISLIIGLtyivtiiyGGTLVMHHSISIGQLI--SFIS 282
Cdd:COG4618 229 A----------LQARASDRAGGFS---ALSKFLRLL------LQSAVLGL--------GAYLVIQGEITPGAMIaaSILM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 283 ---------YIAAlvWPMFAIGRlfnvlergnASYDRVDQLLKETStiiEAPNAIQTPA-TGDInyAVQKFTY--PGDKQ 350
Cdd:COG4618 282 gralapieqAIGG--WKQFVSAR---------QAYRRLNELLAAVP---AEPERMPLPRpKGRL--SVENLTVvpPGSKR 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDN 430
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAEN 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 I-RFADFDRsqAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTE 509
Cdd:COG4618 426 IaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGE 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 510 ETILMNLKTMRADQTT-IITANRLSSVMHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG4618 504 AALAAAIRALKARGATvVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-553 |
3.41e-60 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 198.97 E-value: 3.41e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03245 90 FYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
19-311 |
1.26e-59 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 200.08 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQkLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFW 98
Cdd:cd07346 2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL-LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 99 HFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQL 178
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVIL-FYLNWKLTLVALLLLPLYVLILRYF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 179 GAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIV 258
Cdd:cd07346 160 RRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 259 TIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd07346 240 VLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
16-544 |
2.22e-59 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 206.37 E-value: 2.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFLVLVAVVQIVPPK-VIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFryGWRTRIWG--GAAKLERTL 92
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAwLLARVVDGLISAGEPLAELLPALGALALVLLLRALL--GWLQERAAarAAAAVKSQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 93 RSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQ--------QVAGAGILTFAdsiitggttIIAMVIFVDWRLTLMA 164
Cdd:TIGR02857 80 RERLLEAVAALGPRWLQGRPSGELATLALEGVEALDgyfarylpQLVLAVIVPLA---------ILAAVFPQDWISGLIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 165 LIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIV----TKTIAInKRVNMI 240
Cdd:TIGR02857 151 LLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSeeyrERTMRV-LRIAFL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 241 DGLfdpAISLIIGLTYIVTIIYGGTLVMHhsisiGQLISFISYIAALVWPMF-----AIGRLFNVLERGNASYDRVDQLL 315
Cdd:TIGR02857 230 SSA---VLELFATLSVALVAVYIGFRLLA-----GDLDLATGLFVLLLAPEFylplrQLGAQYHARADGVAAAEALFAVL 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 316 KETstiiEAPNAIQTPATGDINYAVQ----KFTYPGdKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQ 391
Cdd:TIGR02857 302 DAA----PRPLAGKAPVTAAPASSLEfsgvSVAYPG-RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 392 GVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERG 471
Cdd:TIGR02857 377 GSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGG 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 472 VSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVM 544
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
343-548 |
6.15e-55 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 184.60 E-value: 6.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQ---PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGhdirdysldalldSIGYVPQD 419
Cdd:cd03250 8 FTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFA---DFDRSQAAVEdaaiASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:cd03250 75 PWIQNGTIRENILFGkpfDEERYEKVIK----ACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 497 LDDSLSAVDAKTEETILMN--LKTMRADQTTIITANRLSSVMHADEIIVMDDGQ 548
Cdd:cd03250 151 LDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
21-578 |
1.30e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 194.94 E-value: 1.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVD-LIDTHQLtPQKLIMWLG---ILLS--AAILQYlfrygWRTRIWGGAA-KLERTLR 93
Cdd:PRK10790 28 AVLMLWVAAAAEVSGPLLISYFIDnMVAKGNL-PLGLVAGLAaayVGLQllAAGLHY-----AQSLLFNRAAvGVVQQLR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 94 SRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIfVDWRLTLMALI--PMPLL 171
Cdd:PRK10790 102 TDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFS-LDWRMALVAIMifPAVLV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQlgaHLHTAF-GQSQAAFSRLNDKTQESVSGIKVLKTFGQEeadvADFNEIVTKTIAINKRVNM----IDG-LFD 245
Cdd:PRK10790 181 VMVIYQ---RYSTPIvRRVRAYLADINDGFNEVINGMSVIQQFRQQ----ARFGERMGEASRSHYMARMqtlrLDGfLLR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 246 PAISLIIGLTYI-VTIIYGGTLVmhHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLketstiiEA 324
Cdd:PRK10790 254 PLLSLFSALILCgLLMLFGFSAS--GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM-------DG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 325 P-----NAIQTPATGDINYAVQKFTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH 399
Cdd:PRK10790 325 PrqqygNDDRPLQSGRIDIDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 400 DIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADfDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQK 479
Cdd:PRK10790 404 PLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 480 QRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALL 559
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL 562
|
570
....*....|....*....
gi 2018945286 560 AEDGWYAEMWLKQQLSQAL 578
Cdd:PRK10790 563 AAQGRYWQMYQLQLAGEEL 581
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
306-569 |
2.32e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 193.89 E-value: 2.32e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 306 ASYDRVDQLLKETSTIIEAPNAIQTPATGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLR 385
Cdd:PRK11160 309 ASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTR 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 386 EYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSqaaveDAAIASAVH----DDILTFAQ 461
Cdd:PRK11160 389 AWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-----DEALIEVLQqvglEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 462 GYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEI 541
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260
....*....|....*....|....*...
gi 2018945286 542 IVMDDGQIIERGTHEALLAEDGWYAEMW 569
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
4.38e-54 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 185.41 E-value: 4.38e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVD---LIDTHQLTPQKLIMWLGILLSAAILQYLFRYGwRTRI--WGGAaKLERTLR 93
Cdd:cd18563 2 ILGFLLMLLGTALGLVPPYLTKILIDdvlIQLGPGGNTSLLLLLVLGLAGAYVLSALLGIL-RGRLlaRLGE-RITADLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 94 SRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIIT--GgttIIAMVIFVDWRLTLMALIPMPLL 171
Cdd:cd18563 80 RDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMiiG---IGVVLFSLNWKLALLVLIPVPLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLI 251
Cdd:cd18563 157 VWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 252 IGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18563 237 TSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
249-561 |
3.07e-52 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 187.17 E-value: 3.07e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 249 SLIIGLTYIVTI---IYGGTLVMHhSISIGQLISFISYIAAlVWPMFAIGRlfnvlergnASYDRVDQLLKETStiiEAP 325
Cdd:TIGR01842 240 SLVLGLGAYLAIdgeITPGMMIAG-SILVGRALAPIDGAIG-GWKQFSGAR---------QAYKRLNELLANYP---SRD 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 326 NAIQTPA-TGDInyAVQKFTY--PGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR 402
Cdd:TIGR01842 306 PAMPLPEpEGHL--SVENVTIvpPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 403 DYSLDALLDSIGYVPQDNFLFSTDVRDNI-RFADFDRSQAAVEdAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQR 481
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIaRFGENADPEKIIE-AAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQR 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 482 IAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQ-TTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:TIGR01842 463 IALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
.
gi 2018945286 561 E 561
Cdd:TIGR01842 543 K 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
67-532 |
5.92e-52 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 186.41 E-value: 5.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 67 AILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGG 146
Cdd:TIGR02868 63 GIGRAVFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 147 TTIiAMVIFVDWRLT-------LMALIPMPLLAV-ASRQLGAHLhtafgqsQAAFSRLNDKTQESVSGIKVLKTFGQEEA 218
Cdd:TIGR02868 143 AAV-AAIAVLSVPAAlilaaglLLAGFVAPLVSLrAARAAEQAL-------ARLRGELAAQLTDALDGAAELVASGALPA 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 219 DVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLF 298
Cdd:TIGR02868 215 ALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 299 NVLERGNASYDRVDQLL--KETSTIIEAPNAIQTPATG-DINYAVQKFTYPGDkQPTLMNVAFTLPQGKTLGIVGKVGSG 375
Cdd:TIGR02868 295 QQLTRVRAAAERIVEVLdaAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 376 KTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDD 455
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADW 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 456 ILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRL 532
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
343-549 |
9.27e-51 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 174.20 E-value: 9.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPG-DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNF 421
Cdd:cd03248 19 FAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:cd03248 99 LFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2018945286 502 SAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQI 549
Cdd:cd03248 179 SALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
19-311 |
9.07e-50 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 173.73 E-value: 9.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVD-LIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLF 97
Cdd:cd18544 2 ILALLLLLLATALELLGPLLIKRAIDdYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQ 177
Cdd:cd18544 82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAM-FLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 178 LGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYI 257
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 258 VTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-311 |
9.89e-50 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 173.88 E-value: 9.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYgWRTRIWGGAA-KLERTLRSRLF 97
Cdd:cd18778 2 ILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNF-LRIYLNHVAEqKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITG-GTTIIAMVIfvDWRLTLMALIPMPLLAVASR 176
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLvGVAIILFSI--NPKLALLTLIPIPFLALGAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 177 QLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTY 256
Cdd:cd18778 159 LYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 257 IVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18778 239 VLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
343-554 |
1.68e-48 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 168.06 E-value: 1.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03244 10 LRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNI----RFADFDRsQAAVEDAAIASAVhddiLTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:cd03244 90 FSGTIRSNLdpfgEYSDEEL-WQALERVGLKEFV----ESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
1.92e-48 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 170.36 E-value: 1.92e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVD-LIDTHQLTPqkLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLF 97
Cdd:cd18543 2 ILALLAALLATLAGLAIPLLTRRAIDgPIAHGDRSA--LWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFAdSIITGGTTIIAMViFVDWRLTLMALIPMPLLAVASRQ 177
Cdd:cd18543 80 AHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLG-NLLTLVVGLVVML-VLSPPLALVALASLPPLVLVARR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 178 LGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYI 257
Cdd:cd18543 158 FRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 258 VTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18543 238 AVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
18-311 |
7.06e-48 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 168.75 E-value: 7.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 18 YLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYLFRYG---WRTRIwggAAKLERTLRS 94
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEK-DLEALLLVPLAIIGLFLLRGLASYLqtyLMAYV---GQRVVRDLRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 95 RLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVagagILTFADSIITGGTTIIAMV---IFVDWRLTLMALIPMPLL 171
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNA----LTSALTVLVRDPLTVIGLLgvlFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLI 251
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 252 IGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
3.23e-47 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 167.20 E-value: 3.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVV-QIVPPKVIGTLVDLIDTHQLTP-----QKLIMWLGILLSAAILQYLFRYGWrTRIWGGAA-KLERT 91
Cdd:cd18547 1 LILVIILAIISTLlSVLGPYLLGKAIDLIIEGLGGGggvdfSGLLRILLLLLGLYLLSALFSYLQ-NRLMARVSqRTVYD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLL 171
Cdd:cd18547 80 LRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMM-LYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLI 251
Cdd:cd18547 159 LLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 252 IGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18547 239 NNLGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
19-311 |
6.96e-47 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 166.10 E-value: 6.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQkLIMWLGILLSAAILQYLFRYgWRTRIWGGAA-KLERTLRSRLF 97
Cdd:cd18545 3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSG-LLIIALLFLALNLVNWVASR-LRIYLMAKVGqRILYDLRQDLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIIT--GgttIIAMVIFVDWRLTLMALIPMPLLAVAS 175
Cdd:cd18545 81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTlvG---IVIIMFSLNVRLALVTLAVLPLLVLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 176 RQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLT 255
Cdd:cd18545 158 FLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 256 YIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18545 238 TALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
26-310 |
1.08e-46 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 165.70 E-value: 1.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 26 VLVAVVQIVPPKVIGTLVD-LIDTHQLtpQKLIMWLGILLSAAILQYLFRYgWRTRiWGG--AAKLERTLRSRLFWHFMK 102
Cdd:cd18549 12 VLIAALDLVFPLIVRYIIDdLLPSKNL--RLILIIGAILLALYILRTLLNY-FVTY-WGHvmGARIETDMRRDLFEHLQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 103 MDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQLGAHL 182
Cdd:cd18549 88 LSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIIL-LTINVPLTLIVFALLPLMIIFTIYFNKKM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 183 HTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTIIY 262
Cdd:cd18549 167 KKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVA 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2018945286 263 GGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDR 310
Cdd:cd18549 247 GGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
348-568 |
1.18e-45 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 170.03 E-value: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLrEYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDV 427
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALL-GFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAK 507
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 508 TEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEM 568
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
21-311 |
4.76e-43 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 155.80 E-value: 4.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLI----DTHQLTpqKLIMWLGILLSAAILQYLFRYgWRTRIWGGaaKLERTLRSRL 96
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIikggDLDVLN--ELALILLAIYLLQSVFTFVRY-YLFNIAGE--RIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 97 FWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIIT--GGttiIAMVIFVDWRLTLMALIPMPLLAVA 174
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQviGG---LIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 175 SRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGL 254
Cdd:cd18557 153 SKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 255 TYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18557 233 SLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-565 |
2.26e-42 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 163.66 E-value: 2.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFL-VLVA-----VVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYgWRTRIwggAAKLERTLRSR 95
Cdd:PTZ00265 829 IIALsILVAgglypVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMFISETLKNY-YNNVI---GEKVEKTMKRR 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 96 LFWHFMKMDTTFFQ--KHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIF---VDWRLTLMALIPMPL 170
Cdd:PTZ00265 905 LFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFcpiVAAVLTGTYFIFMRV 984
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 171 LAVASRqLGAHLHT---AFGQSQAAFSRLNDK---------TQESVSGIKVLKTFGQEEAdvadFNEIVTKTIAINKR-- 236
Cdd:PTZ00265 985 FAIRAR-LTANKDVekkEINQPGTVFAYNSDDeifkdpsflIQEAFYNMNTVIIYGLEDY----FCNLIEKAIDYSNKgq 1059
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 237 -----VN-MIDGLFDPAISLIIGLTYIvtiiYGGTLVMHHSIsigQLISFISYIAALVWPMFAIGRLFNVL---ERGNAS 307
Cdd:PTZ00265 1060 krktlVNsMLWGFSQSAQLFINSFAYW----FGSFLIRRGTI---LVDDFMKSLFTFLFTGSYAGKLMSLKgdsENAKLS 1132
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 308 YDRVDQLLKETSTI-IEAPNAIQTPATGDINYAVQ----KFTYPGDKQ-PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIK 381
Cdd:PTZ00265 1133 FEKYYPLIIRKSNIdVRDNGGIRIKNKNDIKGKIEimdvNFRYISRPNvPIYKDLTFSCDSKKTTAIVGETGSGKSTVMS 1212
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 382 LLLREYD---------------------QYQ---------------------------------GVIQIDGHDIRDYSLD 407
Cdd:PTZ00265 1213 LLMRFYDlkndhhivfknehtndmtneqDYQgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLK 1292
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 408 ALLDSIGYVPQDNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARA 487
Cdd:PTZ00265 1293 DLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARA 1372
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 488 MMTDPEILILDDSLSAVDAKTEETI---LMNLKTmRADQTTIITANRLSSVMHADEIIVMDD----GQIIE-RGTHEALL 559
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIektIVDIKD-KADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELL 1451
|
....*..
gi 2018945286 560 -AEDGWY 565
Cdd:PTZ00265 1452 sVQDGVY 1458
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
21-311 |
8.69e-41 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 149.55 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLV-AVVQIVPPKVIGTLVDlidthQLTPQK---LIMWL-----GILLSAAILQYLFRYgWRTRIwggAAKLERT 91
Cdd:cd18550 3 LVLLLILLsALLGLLPPLLLREIID-----DALPQGdlgLLVLLalgmvAVAVASALLGVVQTY-LSARI---GQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIfVDWRLTLMALIPMPLL 171
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLA-LDWRLALLSLVLLPLF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQE--SVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAIS 249
Cdd:cd18550 153 VLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALG 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 250 LIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPmfaIGRLFNV---LERGNASYDRV 311
Cdd:cd18550 233 LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGP---LTQLLNIqvdLMTSLALFERI 294
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
21-311 |
1.40e-40 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 148.79 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLI---DTHQLTPQKLIMWLGILLSAAILQYLFRYgWRTRIwggAAKLERTLRSRLF 97
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAAlggGDTASLNQIALLLLGLFLLQAVFSFFRIY-LFARV---GERVVADLRKDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 98 WHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIIT--GGTTIIAmviFVDWRLTLMALIPMPLLAVAS 175
Cdd:cd18576 77 RHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTliGGVVLLF---FISWKLTLLMLATVPVVVLVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 176 RQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLT 255
Cdd:cd18576 154 VLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGA 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 256 YIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18576 234 IVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
343-553 |
1.48e-40 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 145.15 E-value: 1.48e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALLDSIGYVPQDNFL 422
Cdd:cd03247 8 FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISVLNQRPYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIrfadfdrsqaavedaaiasavhddiltfaqgyetvvgerGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03247 87 FDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:cd03247 128 GLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
343-549 |
4.40e-40 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 143.90 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03246 8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIrfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03246 88 FSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTT-IITANRLSSVMHADEIIVMDDGQI 549
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAGATrIVIAHRPETLASADRILVLEDGRV 173
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
202-567 |
7.90e-40 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 156.26 E-value: 7.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 202 ESVSGIKVLKTFGQEEADVADFNEI------VTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSisig 275
Cdd:TIGR00957 501 EILNGIKVLKLYAWELAFLDKVEGIrqeelkVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVDENNILDAEKA---- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 276 qLISfISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTiieAPNAIQ----TPATGD-INYAVQKFTYPGDKQ 350
Cdd:TIGR00957 577 -FVS-LALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEEL---EPDSIErrtiKPGEGNsITVHNATFTWARDLP 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGhdirdysldalldSIGYVPQDNFLFSTDVRDN 430
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLREN 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFA---DFDRSQAAVEdaaiASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAK 507
Cdd:TIGR00957 719 ILFGkalNEKYYQQVLE----ACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 508 TEETILMNL---KTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAE 567
Cdd:TIGR00957 795 VGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
19-311 |
8.75e-40 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 146.87 E-value: 8.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDL-IDTHQLTPqkLIMWLGILLSAAILQYLFRYgWRTRIWGGAA-KLERTLRSRL 96
Cdd:cd18546 2 ALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGV--LLLAAAAYLAVVLAGWVAQR-AQTRLTGRTGeRLLYDLRLRV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 97 FWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIFvDWRLTLMALIPMPLLAVASR 176
Cdd:cd18546 79 FAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVL-DPRLALVALAALPPLALATR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 177 QLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTY 256
Cdd:cd18546 158 WFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLAT 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 257 IVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18546 238 AAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
19-311 |
1.84e-39 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 145.65 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYgWRTRIwggAAKLERTLRSRLFW 98
Cdd:cd18551 2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSY-LLGRT---GERVVLDLRRRLWR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 99 HFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMvIFVDWRLTLMALIPMPLLAVASRQL 178
Cdd:cd18551 78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLM-FLLDWVLTLVTLAVVPLAFLIILPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 179 GAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIV 258
Cdd:cd18551 157 GRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLV 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 259 TIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18551 237 VLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-311 |
2.82e-39 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 145.73 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 32 QIVPPKVIGTLVDLIDTHQLTPQKL-----IMWLGILLSAAILQYLFRYGWrtrIWGGaaklER---TLRSRLFWHFMKM 103
Cdd:cd18564 28 DVLGDKPLPGLLGLAPLLGPDPLALlllaaAALVGIALLRGLASYAGTYLT---ALVG----QRvvlDLRRDLFAHLQRL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 104 DTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITggttIIAMVI---FVDWRLTLMALIPMPLLAVASRQLGA 180
Cdd:cd18564 101 SLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT----LVGMLGvmfWLDWQLALIALAVAPLLLLAARRFSR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 181 HLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTI 260
Cdd:cd18564 177 RIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 261 IYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18564 257 WFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
343-561 |
6.37e-39 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 142.47 E-value: 6.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKL---LLREYdqyQGVIQIDGHDIRDYSLDALLDSIGYVPQ- 418
Cdd:COG1122 8 FSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLlngLLKPT---SGEVLVDGKDITKKNLRELRRKVGLVFQn 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 -DNFLFSTDVRDNIRFA----DFDRSQAA--VEDAAiaSAVhdDILTFAqgyetvvgERGV-SLSGGQKQRIAIARAMMT 490
Cdd:COG1122 84 pDDQLFAPTVEEDVAFGpenlGLPREEIRerVEEAL--ELV--GLEHLA--------DRPPhELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 491 DPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITA-NRLSSVM-HADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAeLADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
353-499 |
2.77e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 138.16 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFS-TDVRDNI 431
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADFDRSQAAVEDAAIASAVHDdilTFAQGY--ETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALE---KLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
331-554 |
5.15e-38 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 139.47 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 331 PATGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALL 410
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 411 DSIGYVPQDNFLFSTDVRDNI-RFADFDrsqaaveDAAIASAVHddiltfaqgyetvVGERGVSLSGGQKQRIAIARAMM 489
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEYS-------DEEIYGALR-------------VSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 490 TDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
21-291 |
5.36e-38 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 141.24 E-value: 5.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTP-QKLIMWLGILLSAAILQYLFRYGwRTRIWGGAA-KLERTLRSRLFW 98
Cdd:pfam00664 4 AILLAILSGAISPAFPLVLGRILDVLLPDGDPEtQALNVYSLALLLLGLAQFILSFL-QSYLLNHTGeRLSRRLRRKLFK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 99 HFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIFvDWRLTLMALIPMPLLAVASRQL 178
Cdd:pfam00664 83 KILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLAVLPLYILVSAVF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 179 GAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIV 258
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241
|
250 260 270
....*....|....*....|....*....|...
gi 2018945286 259 TIIYGGTLVMHHSISIGQLISFISYIAALVWPM 291
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-311 |
9.98e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 141.55 E-value: 9.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 18 YLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQ-----LTPQKLI--------MWLGILLSA-----AILQYLFRYGWRT 79
Cdd:cd18565 1 LVLGLLASILNRLFDLAPPLLIGVAIDAVFNGEasflpLVPASLGpadprgqlWLLGGLTVAaflleSLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 80 riwgGAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGIltfADSIITGGTTIIAMVIFV--D 157
Cdd:cd18565 81 ----FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGA---NSIIRVVVTVLGIGAILFylN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 158 WRLTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRV 237
Cdd:cd18565 154 WQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 238 NMIDGLFDPAISLIIGLTYIVTIIYGGTLVMH------HSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18565 234 IRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDgpplftGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMASAKRV 313
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
60-568 |
3.75e-37 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 148.17 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 60 LGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFA 139
Cdd:TIGR00957 1008 LSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 140 DSIITGGTTIIamVIFVDWRLTLMALIPMPLL--------AVASRQLgAHLHTAfgQSQAAFSRLNdktqESVSGIKVLK 211
Cdd:TIGR00957 1088 GSLFNVIGALI--VILLATPIAAVIIPPLGLLyffvqrfyVASSRQL-KRLESV--SRSPVYSHFN----ETLLGVSVIR 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 212 TFGQEEadvaDFNEIVTKTIAINKRVnmidglFDPAIS----LIIGLTYI--VTIIYGG--TLVMHHSISIGQLISFISY 283
Cdd:TIGR00957 1159 AFEEQE----RFIHQSDLKVDENQKA------YYPSIVanrwLAVRLECVgnCIVLFAAlfAVISRHSLSAGLVGLSVSY 1228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 284 ----IAALVWPMfaigRLFNVLERGNASYDRvdqlLKETS-TIIEAPNAIQT-------PATGDINYAVQKFTYPGDKQP 351
Cdd:TIGR00957 1229 slqvTFYLNWLV----RMSSEMETNIVAVER----LKEYSeTEKEAPWQIQEtappsgwPPRGRVEFRNYCLRYREDLDL 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 352 TLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNI 431
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 R-FADFdrSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEE 510
Cdd:TIGR00957 1381 DpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 511 TILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEM 568
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
121-575 |
1.19e-36 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 146.33 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 121 TNDLTAIQQVAGAGILTFADSIITGGTTIIAMVI---FVDWRLTLMALIPMPLL----AVASRQLGAHLHTAFGQSQAAF 193
Cdd:PTZ00265 157 TSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIwslFKNARLTLCITCVFPLIyicgVICNKKVKINKKTSLLYNNNTM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 194 SRLndktQESVSGIKVLKTFGQEEADVADFN--------EIVTKTIAINKRVNMIDGLFdpAISLIIGLTYIVTII---- 261
Cdd:PTZ00265 237 SII----EEALVGIRTVVSYCGEKTILKKFNlseklyskYILKANFMESLHIGMINGFI--LASYAFGFWYGTRIIisdl 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 262 ---------YGGTLVmhhSISIGQLISFisYIAALVWPmfAIGRLFNVLERGNASYDRVDQllketSTIIEAPNAIQT-P 331
Cdd:PTZ00265 311 snqqpnndfHGGSVI---SILLGVLISM--FMLTIILP--NITEYMKSLEATNSLYEIINR-----KPLVENNDDGKKlK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 332 ATGDINYAVQKFTYPGDKQPTLM-NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQI-DGHDIRDYSLDAL 409
Cdd:PTZ00265 379 DIKKIQFKNVRFHYDTRKDVEIYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWW 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 410 LDSIGYVPQDNFLFSTDVRDNIRFA-------------------------------------DFD--------------- 437
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagDLNdmsnttdsneliemr 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 438 RSQAAVEDAAIASA-----VHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETI 512
Cdd:PTZ00265 539 KNYQTIKDSEVVDVskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 513 LMNLKTMRADQT--TIITANRLSSVMHADEIIVMDDGQ------------------------------------------ 548
Cdd:PTZ00265 619 QKTINNLKGNENriTIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkin 698
|
570 580 590
....*....|....*....|....*....|...
gi 2018945286 549 -----IIERGTHEALLA-EDGWYAEMWLKQQLS 575
Cdd:PTZ00265 699 nagsyIIEQGTHDALMKnKNGIYYTMINNQKVS 731
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-548 |
1.31e-36 |
|
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: 135.67 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ--DN 420
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQnpDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFA----DFDRSQAAVEDAAIASAVHDDILTFAQGYEtvvgergvsLSGGQKQRIAIARAMMTDPEILI 496
Cdd:cd03225 87 QFFGPTVEEEVAFGlenlGLPEEEIEERVEEALELVGLEGLRDRSPFT---------LSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRADQTTIITA-NRLSSVM-HADEIIVMDDGQ 548
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLeLADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
355-561 |
3.89e-36 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 134.81 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALLDSIGYVPQDNFLFST-DVRDNIRF 433
Cdd:COG1131 18 GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP-AEVRRRIGYVPQEPALYPDlTVRENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 AD--FDRSQAAVEDAAiasavhDDILTFAqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEET 511
Cdd:COG1131 97 FArlYGLPRKEARERI------DELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 512 ILMNLKTMRADQTTIItanrLSSvmH--------ADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG1131 170 LWELLRELAAEGKTVL----LST--HyleeaerlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
343-553 |
8.30e-36 |
|
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: 133.79 E-value: 8.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD---SIGYVPQD 419
Cdd:cd03257 11 FPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrkEIQMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 -----NFLFStdVRDNI----RFADFDRSQAAVEDAAIA--SAVHDDiltfaqgyETVVGERGVSLSGGQKQRIAIARAM 488
Cdd:cd03257 91 pmsslNPRMT--IGEQIaeplRIHGKLSKKEARKEAVLLllVGVGLP--------EEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 489 MTDPEILILDDSLSAVDAKTEETILMNLKTMRAD-QTTI--ITANrLSSVMH-ADEIIVMDDGQIIERG 553
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLlfITHD-LGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
343-560 |
1.12e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 140.42 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ---YQGVIQIDGHDIRDYSLDALLDSIGYVPQD 419
Cdd:COG1123 12 VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRIGMVFQD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 --NFLFSTDVRDNIRFA----DFDRSQAAVEDAAIASAVhddiltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPE 493
Cdd:COG1123 92 pmTQLNPVTVGDQIAEAlenlGLSRAEARARVLELLEAV---------GLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
348-563 |
2.56e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.06 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALlDSIGYVPQDNFLFSTD- 426
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQIGVLPDERGLYDRLt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIR-FADFDRSQAAVEDAAIASAVHDdiLTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:COG4555 91 VRENIRyFAELYGLFDEELKKRIEELIEL--LGLEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 506 AKTEETILMNLKTMRADQTTIItanrLSS-VMH-----ADEIIVMDDGQIIERGTHEALLAEDG 563
Cdd:COG4555 165 VMARRLLREILRALKKEGKTVL----FSShIMQevealCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
58-558 |
4.80e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 141.65 E-value: 4.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 58 MWLGILLSAAILQYLFRYGWRTRiwggaakleRTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGA--GI 135
Cdd:PLN03232 351 VTFGVLCESQYFQNVGRVGFRLR---------STLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQlhGL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 136 LTFADSIItggttiIAMVIFVDW--------RLTLMALIPMPLLAVAS-RQLgahlhtafgqSQAAFSRLNDK---TQES 203
Cdd:PLN03232 422 WSAPFRII------VSMVLLYQQlgvaslfgSLILFLLIPLQTLIVRKmRKL----------TKEGLQWTDKRvgiINEI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 204 VSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGlFDPAIslIIGLTYIVTIIYGGTLVM-HHSISIGQLISFIS 282
Cdd:PLN03232 486 LASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSA-FNSFI--LNSIPVVVTLVSFGVFVLlGGDLTPARAFTSLS 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 283 YIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIeAPNAIQTPATGDINYAVQKFTYPGD-KQPTLMNVAFTLP 361
Cdd:PLN03232 563 LFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERIL-AQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIP 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 362 QGKTLGIVGKVGSGKTTLIKLLLREYDQyqgvIQIDGHDIRDysldalldSIGYVPQDNFLFSTDVRDNIRF-ADFDRSQ 440
Cdd:PLN03232 642 VGSLVAIVGGTGEGKTSLISAMLGELSH----AETSSVVIRG--------SVAYVPQVSWIFNATVRENILFgSDFESER 709
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 441 AAveDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMN-LKTM 519
Cdd:PLN03232 710 YW--RAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDE 787
|
490 500 510
....*....|....*....|....*....|....*....
gi 2018945286 520 RADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEAL 558
Cdd:PLN03232 788 LKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
281-560 |
9.91e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 140.64 E-value: 9.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 281 ISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIeAPNAIQTPATGDINYAVQKFTY-PGDKQPTLMNVAFT 359
Cdd:PLN03130 561 LSLFAVLRFPLFMLPNLITQAVNANVSLKRLEELLLAEERVL-LPNPPLEPGLPAISIKNGYFSWdSKAERPTLSNINLD 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 360 LPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIdghdIRDysldalldSIGYVPQDNFLFSTDVRDNIRF-ADFDR 438
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV----IRG--------TVAYVPQVSWIFNATVRDNILFgSPFDP 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 439 SQaaVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMN-LK 517
Cdd:PLN03130 708 ER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcIK 785
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2018945286 518 TMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:PLN03130 786 DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-560 |
3.53e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.19 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLM---NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD---SIGY 415
Cdd:COG1123 267 SKRYPVRGKGGVRavdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNF--LFSTD-VRDNIRFA---DFDRSQAAVEDAAiasavhDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMM 489
Cdd:COG1123 347 VFQDPYssLNPRMtVGDIIAEPlrlHGLLSRAERRERV------AELLERVGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 490 TDPEILILDDSLSAVDAKTEETILMNLKTMRADQ-TTI--ITANrLSSV-MHADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgLTYlfISHD-LAVVrYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
349-549 |
4.74e-34 |
|
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: 127.13 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDsIGYVPQDNFLFST-DV 427
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNIRfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAK 507
Cdd:cd03230 91 RENLK-----------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2018945286 508 TEETILMNLKTMRADQTTIItanrLSS-VMH-----ADEIIVMDDGQI 549
Cdd:cd03230 130 SRREFWELLRELKKEGKTIL----LSShILEeaerlCDRVAILNNGRI 173
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
19-311 |
6.17e-34 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 130.60 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 19 LWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQkLIMWLGILLSAAILQYLFRygwrtrIWGG------AAKLERTL 92
Cdd:cd18548 2 ILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSY-ILRTGLLMLLLALLGLIAG------ILAGyfaakaSQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 93 RSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIaMVIFVDWRLTLMALIPMPLLA 172
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAII-MAFRINPKLALILLVAIPILA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 173 VASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLII 252
Cdd:cd18548 154 LVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIM 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 253 GLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18548 234 NLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
343-560 |
2.16e-33 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 127.61 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:COG1124 11 YGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 fSTD----VRDNI----RFADFDRSQAAVEDAAIASAVHDDILTfaqgyetvvgERGVSLSGGQKQRIAIARAMMTDPEI 494
Cdd:COG1124 91 -SLHprhtVDRILaeplRIHGLPDREERIAELLEQVGLPPSFLD----------RYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
342-562 |
1.14e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 126.64 E-value: 1.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ--D 419
Cdd:PRK13632 14 SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQnpD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 N-FLFSTdVRDNIRFadfdrsqaAVEDAAIASAVHDDILTFaqgYETVVGERGV------SLSGGQKQRIAIARAMMTDP 492
Cdd:PRK13632 94 NqFIGAT-VEDDIAF--------GLENKKVPPKKMKDIIDD---LAKKVGMEDYldkepqNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 493 EILILDDSLSAVDAKTEETILMNLKTMR--ADQTTI-ITANrLSSVMHADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLRktRKKTLIsITHD-MDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
21-311 |
2.83e-32 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 126.09 E-value: 2.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLIDTHQ-------LTPQKLIMWLGILLSAAIL-----QYLFRYGwrtriwggAAKL 88
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESgdieifgLSLKTFALALLGVFVVGAAanfgrVYLLRIA--------GERI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 89 ERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMViFVDWRLTLMALIPM 168
Cdd:cd18573 73 VARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMML-YISPKLTLVMLLVV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 169 PLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAI 248
Cdd:cd18573 152 PPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGST 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 249 SLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18573 232 GFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
343-561 |
2.97e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 124.43 E-value: 2.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYpgDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDalldsIGYVPQD--- 419
Cdd:COG1121 14 VSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IGYVPQRaev 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIR---------FADFDRSQAAVEDAAIAsAVhdDILTFAQgyeTVVGErgvsLSGGQKQRIAIARAMMT 490
Cdd:COG1121 87 DWDFPITVRDVVLmgrygrrglFRRPSRADREAVDEALE-RV--GLEDLAD---RPIGE----LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 491 DPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITAN-RLSSVM-HADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVThDLGAVReYFDRVLLLNRGLVAHGPPEEVLTPE 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
340-549 |
3.25e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 3.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQD 419
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFADFDRSQAAVEDAAIA--SAVH--DDILtfaqgyetvvgERGVS-LSGGQKQRIAIARAMMTDPEI 494
Cdd:COG4619 83 PALWGGTVRDNLPFPFQLRERKFDRERALEllERLGlpPDIL-----------DKPVErLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRAD-QTTI--ITANRLSSVMHADEIIVMDDGQI 549
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVlwVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
343-562 |
3.75e-32 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 124.39 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGdkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:COG1120 9 VGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 -FSTDVRDNI---RFA--DFDRSQAAVEDAAIASAVHD-DILTFAqgyetvvgERGV-SLSGGQKQRIAIARAMMTDPEI 494
Cdd:COG1120 87 pFGLTVRELValgRYPhlGLFGRPSAEDREAVEEALERtGLEHLA--------DRPVdELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRADQ-TTIITanrlssVMH--------ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERgRTVVM------VLHdlnlaaryADRLVLLKDGRIVAQGPPEEVLTPE 229
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
348-545 |
4.04e-32 |
|
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: 123.03 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSldallDSIGYVPQD---NFLFS 424
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER-----KRIGYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNIR---------FADFDRSQAAVEDAAIA----SAVHDDILTfaqgyetvvgergvSLSGGQKQRIAIARAMMTD 491
Cdd:cd03235 85 ISVRDVVLmglyghkglFRRLSKADKAKVDEALErvglSELADRQIG--------------ELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 492 PEILILDDSLSAVDAKTEETILMNLKTMRADQTTII-TANRLSSVM-HADEIIVMD 545
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILvVTHDLGLVLeYFDRVLLLN 206
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
348-553 |
5.45e-32 |
|
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: 122.63 E-value: 5.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFST 425
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIagLERPDS--GEILIDGRDVTG--VPPERRNIGMVFQDYALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 -DVRDNIRFA--DFDRSQAAVEDAAIASAVHDDILTFAQGYetvVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03259 87 lTVAENIAFGlkLRGVPKAEIRARVRELLELVGLEGLLNRY---PHE----LSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 503 AVDAKTEETILMNLKTMRADQ--TTI-ITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:cd03259 160 ALDAKLREELREELKELQRELgiTTIyVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
353-548 |
1.47e-31 |
|
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: 120.37 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLD--ALLDSIGYVPQDNFLFST-DVRD 429
Cdd:cd03229 16 LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRIGMVFQDFALFPHlTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFAdfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTE 509
Cdd:cd03229 96 NIALG---------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2018945286 510 ETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQ 548
Cdd:cd03229 137 REVRALLKSLQAQLgiTVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-578 |
1.87e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 122.92 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYS-LDALLDSIGYVPQ 418
Cdd:TIGR04520 7 SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLngLLLPTS--GKVTVDGLDTLDEEnLWEIRKKVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 --DNFLFSTDVRDNIRFA------DFDRSQAAVEDAAiaSAVhdDILTFAQgYETVvgergvSLSGGQKQRIAIARAMMT 490
Cdd:TIGR04520 85 npDNQFVGATVEDDVAFGlenlgvPREEMRKRVDEAL--KLV--GMEDFRD-REPH------LLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 491 DPEILILDDSLSAVDAKTEETILMNLKTMRADQ--TTI-ITANrLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAE 567
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVIsITHD-MEEAVLADRVIVMNKGKIVAEGTPREIFSQVELLKE 232
|
250
....*....|....*
gi 2018945286 568 MWLK----QQLSQAL 578
Cdd:TIGR04520 233 IGLDvpfiTELAKAL 247
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
21-311 |
2.90e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 123.04 E-value: 2.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLIdTHQLTPQKLIMWLGILLSAAILQYLFRyGWRTRIWGGA-AKLERTLRSRLFWH 99
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAV-VADGSREAFYRAVLLLLLLSVLSGLFS-GLRGGCFSYAgTRLVRRLRRDLFRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 100 FMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMViFVDWRLTLMALIPMPLLAVASRQLG 179
Cdd:cd18572 79 LLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMF-SLSWRLTLLAFITVPVIALITKVYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 180 AHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVT 259
Cdd:cd18572 158 RYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 260 IIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18572 238 LFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
343-549 |
5.71e-31 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; 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. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. 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: 119.90 E-value: 5.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDAL----LDSIG 414
Cdd:cd03255 8 KTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILggLDRPTS--GEVRVDGTDISKLSEKELaafrRRHIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 415 YVPQDNFLFST-DVRDNIRFADFDRSQAAVEDAAIASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPE 493
Cdd:cd03255 86 FVFQSFNLLPDlTALENVELPLLLAGVPKKERRERAEELLERV-----GLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 494 ILILDDSLSAVDAKTEETIlMNL--KTMRADQTTII--TANRlSSVMHADEIIVMDDGQI 549
Cdd:cd03255 161 IILADEPTGNLDSETGKEV-MELlrELNKEAGTTIVvvTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-560 |
6.40e-31 |
|
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: 120.38 E-value: 6.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKL--LLREYDQyqGVIQIDGHDIRDYSLDALLD---SIGYV 416
Cdd:cd03258 10 VFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCinGLERPTS--GSVLVDGTDLTLLSGKELRKarrRIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 417 PQD-NFLFSTDVRDNIRFAdfdRSQAAVEDAAIASAVhDDILTFAqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEIL 495
Cdd:cd03258 88 FQHfNLLSSRTVFENVALP---LEIAGVPKAEIEERV-LELLELV-GLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 496 ILDDSLSAVDAKTEETILMNLKTMRadQTTIITANRLSSVMH-----ADEIIVMDDGQIIERGTHEALLA 560
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDIN--RELGLTIVLITHEMEvvkriCDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
340-548 |
7.87e-31 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 117.73 E-value: 7.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQd 419
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 nflfstdvrdnirfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 500 SLSAVDAKTEETILMNLKTMRADQTTIITA--NRLSSVMHADEIIVMDDGQ 548
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVthDPELAELAADRVIVLKDGK 157
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
348-562 |
8.83e-31 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 119.91 E-value: 8.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS---LDALLDSIGYVPQDNFLF- 423
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 STDVRDNIRF---ADFDRSQAAVEDAAIasavhdDILTFaqgyetvVGERGV------SLSGGQKQRIAIARAMMTDPEI 494
Cdd:cd03261 91 SLTVFENVAFplrEHTRLSEEEIREIVL------EKLEA-------VGLRGAedlypaELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 495 LILDDSLSAVD----AKTEETIlMNLKtMRADQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:cd03261 158 LLYDEPTAGLDpiasGVIDDLI-RSLK-KELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
273-563 |
1.76e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 127.40 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 273 SIGQLISFISYIAALvwpMFAIGRLFNVLERGNASYDRVDQ---LLKETSTIIEAPNAIQT-PATGDINYAVQKFTYPGD 348
Cdd:PLN03232 1171 TMGLLLSYTLNITTL---LSGVLRQASKAENSLNSVERVGNyidLPSEATAIIENNRPVSGwPSRGSIKFEDVHLRYRPG 1247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVR 428
Cdd:PLN03232 1248 LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVR 1327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIR-FADFDRSQ--AAVEDAAIASAVHDDILtfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PLN03232 1328 FNIDpFSEHNDADlwEALERAHIKDVIDRNPF----GLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 506 AKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDG 563
Cdd:PLN03232 1404 VRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
344-551 |
4.12e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.84 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDAL----LDSIGY 415
Cdd:COG1136 13 SYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLDRPTS--GEVLIDGQDISSLSERELarlrRRHIGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNFLFST-DVRDNI----RFADFDRSQAAVEDAAIASAVH-DDILTF--AQgyetvvgergvsLSGGQKQRIAIARA 487
Cdd:COG1136 91 VFQFFNLLPElTALENValplLLAGVSRKERRERARELLERVGlGDRLDHrpSQ------------LSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 488 MMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQ-TTIITA---NRLSSvmHADEIIVMDDGQIIE 551
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVthdPELAA--RADRVIRLRDGRIVS 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-560 |
1.06e-29 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 125.28 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDghdirdysldallDSIGYVPQDNFLFSTDVRDNIR 432
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 FadFDRSQAA-VEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT--- 508
Cdd:PTZ00243 743 F--FDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVger 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 509 --EETILMNLktmrADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:PTZ00243 821 vvEECFLGAL----AGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-563 |
1.11e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 125.24 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 274 IGQLISFISYIAALvwpMFAIGRLFNVLERGNASYDRVDQLLKETStiiEAPNAIQT-------PATGDINYAVQKFTYP 346
Cdd:PLN03130 1175 MGLLLSYALNITSL---LTAVLRLASLAENSLNAVERVGTYIDLPS---EAPLVIENnrpppgwPSSGSIKFEDVVLRYR 1248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTD 426
Cdd:PLN03130 1249 PELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGT 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIR-FAdfDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PLN03130 1329 VRFNLDpFN--EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 506 AKTEETIlmnLKTMRAD---QTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDG 563
Cdd:PLN03130 1407 VRTDALI---QKTIREEfksCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-578 |
1.19e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ--D 419
Cdd:PRK13635 12 SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFA----------DFDRSQAAVEDAAIASavhddiltFAQgyetvvgERGVSLSGGQKQRIAIARAMM 489
Cdd:PRK13635 92 NQFVGATVQDDVAFGlenigvpreeMVERVDQALRQVGMED--------FLN-------REPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 490 TDPEILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAE 567
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
250
....*....|....*
gi 2018945286 568 MWL----KQQLSQAL 578
Cdd:PRK13635 237 IGLdvpfSVKLKELL 251
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
345-566 |
1.75e-29 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 117.32 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 345 YPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFS 424
Cdd:cd03288 29 YENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNI---RFADFDRSQAAVEDAAIASAVHddilTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:cd03288 109 GSIRFNLdpeCKCTDDRLWEALEIAQLKNMVK----SLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 502 SAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLA-EDGWYA 566
Cdd:cd03288 185 ASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFA 250
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
343-560 |
1.78e-29 |
|
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: 116.63 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03295 8 KRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FS-TDVRDNI----RFADFDRSQAAVEDAAIASAVHDDILTFAQGYETvvgergvSLSGGQKQRIAIARAMMTDPEILIL 497
Cdd:cd03295 87 FPhMTVEENIalvpKLLKWPKEKIRERADELLALVGLDPAEFADRYPH-------ELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 498 DDSLSAVDAKTEETILMNLKTM-RADQTTII--TANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLqQELGKTIVfvTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
345-553 |
2.25e-29 |
|
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: 115.74 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 345 YPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQ-----GVIQIDGHDIRDYSLD--ALLDSIGYVP 417
Cdd:cd03260 9 YYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDvlELRRRVGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 418 QDNFLFSTDVRDNIRFAD-----------FDRSQAAVEDAAIASAVHDDIltfaqgyetvvgeRGVSLSGGQKQRIAIAR 486
Cdd:cd03260 88 QKPNPFPGSIYDNVAYGLrlhgiklkeelDERVEEALRKAALWDEVKDRL-------------HALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 487 AMMTDPEILILDDSLSAVD----AKTEETIlMNLKtmraDQTTII-------TANRLssvmhADEIIVMDDGQIIERG 553
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDpistAKIEELI-AELK----KEYTIVivthnmqQAARV-----ADRTAFLLNGRLVEFG 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
355-553 |
3.58e-29 |
|
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: 113.68 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQdnflfstdvrdnirfa 434
Cdd:cd03214 17 DLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ---------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 dfdrsqaavedaAIASAvhdDILTFAqgyetvvgERGV-SLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETIL 513
Cdd:cd03214 81 ------------ALELL---GLAHLA--------DRPFnELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2018945286 514 MNLKTM-RADQTTIItanrlsSVMH--------ADEIIVMDDGQIIERG 553
Cdd:cd03214 138 ELLRRLaRERGKTVV------MVLHdlnlaaryADRVILLKDGRIVAQG 180
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
355-562 |
4.38e-29 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 115.46 E-value: 4.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS---LDALLDSIGYVPQDNFLFST-DVRDN 430
Cdd:COG1127 23 GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDSlTVFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFA---DFDRSQAAVEDAAiasavhDDILTFaqgyetvVGERGV------SLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:COG1127 103 VAFPlreHTDLSEAEIRELV------LEKLEL-------VGLPGAadkmpsELSGGMRKRVALARALALDPEILLYDEPT 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 502 SAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:COG1127 170 AGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
343-547 |
6.65e-29 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 114.35 E-value: 6.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYpGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD----SIGYVPQ 418
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSrnrySVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 DNFLFSTDVRDNIRFAD-FDRSQ-AAVEDAAiasAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:cd03290 87 KPWLLNATVEENITFGSpFNKQRyKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 497 LDDSLSAVDAKTEETILMN--LKTMRADQ-TTIITANRLSSVMHADEIIVMDDG 547
Cdd:cd03290 164 LDDPFSALDIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
22-288 |
9.43e-29 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 116.04 E-value: 9.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYL---FRYGWRTriWGGaaklERT---LRSR 95
Cdd:cd18575 2 LIALLIAAAATLALGQGLRLLIDQGFAAG-NTALLNRAFLLLLAVALVLALasaLRFYLVS--WLG----ERVvadLRKA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 96 LFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIIT--GGttiIAMVIFVDWRLTLMALIPMPLLAV 173
Cdd:cd18575 75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLliGG---LVMLFITSPKLTLLVLLVIPLVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 174 ASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFdpaISLIIG 253
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALL---TALVIF 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 2018945286 254 LTY--IVTIIY-GGTLVMHHSISIGQLISFISYiAALV 288
Cdd:cd18575 229 LVFgaIVFVLWlGAHDVLAGRMSAGELSQFVFY-AVLA 265
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
351-561 |
1.27e-28 |
|
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: 113.68 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS-IGYVPQDNFLFST-DVR 428
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRIFPElTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADFDRSQAAVEDaaiasavhddilTFAQGYET--VVGER----GVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03224 94 ENLLLGAYARRRAKRKA------------RLERVYELfpRLKERrkqlAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTII----TANRLSSVmhADEIIVMDDGQIIERGTHEALLAE 561
Cdd:cd03224 162 GLAPKIVEEIFEAIRELRDEGVTILlveqNARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
21-283 |
1.90e-28 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 115.04 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTP---------QKLIMWLGILLSAAILQYLfrygwrtRIWGGAAKLERT 91
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGgeealralnQAVLILLGVVLIGSIATFL-------RSWLFTLAGERV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 ---LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIitggTTIIAMVIF---VDWRLTLMAL 165
Cdd:cd18780 74 varLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYL----VQIIGGLVFmftTSWKLTLVML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFD 245
Cdd:cd18780 150 SVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFN 229
|
250 260 270
....*....|....*....|....*....|....*...
gi 2018945286 246 PAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISY 283
Cdd:cd18780 230 GFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLY 267
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
344-554 |
3.26e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKL--LLREYDQyqGVIQIDGHDIRDYSLDALLD---SIGYV 416
Cdd:COG1135 10 TFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCinLLERPTS--GSVLVDGVDLTALSERELRAarrKIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 417 PQ-DNFLFSTDVRDNIRF----ADFDRsqaavedAAIASAVhDDILTFaqgyetvVG--ERGVS----LSGGQKQRIAIA 485
Cdd:COG1135 88 FQhFNLLSSRTVAENVALpleiAGVPK-------AEIRKRV-AELLEL-------VGlsDKADAypsqLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 486 RAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRAD-QTTI--ITanrlssvmH--------ADEIIVMDDGQIIERGT 554
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIvlIT--------HemdvvrriCDRVAVLENGRIVEQGP 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
344-552 |
2.87e-27 |
|
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: 109.87 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDalldsIGYVPQDNF 421
Cdd:cd03293 9 TYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----RGYVFQQDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFS-TDVRDNIRF----ADFDRSQAAVEDAAIASAVHddiLT-FAQGYETvvgergvSLSGGQKQRIAIARAMMTDPEIL 495
Cdd:cd03293 84 LLPwLTVLDNVALglelQGVPKAEARERAEELLELVG---LSgFENAYPH-------QLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 496 ILDDSLSAVDAKTEETI---LMNLKtmRADQTTI--ITANRLSSVMHADEIIVMD--DGQIIER 552
Cdd:cd03293 154 LLDEPFSALDALTREQLqeeLLDIW--RETGKTVllVTHDIDEAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
353-559 |
1.14e-26 |
|
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: 108.58 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDAllDSIGYVPQDNFLF-STDVRDNI 431
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADFDRSQAAVEdaaIASAVHDdiLTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEET 511
Cdd:cd03299 93 AYGLKKRKVDKKE---IERKVLE--IAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 512 ILMNLKTMRAD-QTTII--TANRLSSVMHADEIIVMDDGQIIERGTHEALL 559
Cdd:cd03299 168 LREELKKIRKEfGVTVLhvTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
344-551 |
2.04e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.45 E-value: 2.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD---SIGYVPQD- 419
Cdd:COG2884 10 RYPGG-REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQDf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFAdfdrSQAA-VEDAAIASAVHdDILtfaqgyETV-VGERG----VSLSGGQKQRIAIARAMMTDPE 493
Cdd:COG2884 89 RLLPDRTVYENVALP----LRVTgKSRKEIRRRVR-EVL------DLVgLSDKAkalpHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTMRADQTTIITAnrlssvMHADEI--------IVMDDGQIIE 551
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIA------THDLELvdrmpkrvLELEDGRLVR 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
348-554 |
2.27e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 110.57 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI-------RDysldalldsIGYVPQDN 420
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---------VGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFS-TDVRDNIRFADfdrSQAAVEDAAIASAVhDDILtfaqgyETV----VGERGVS-LSGGQKQRIAIARAMMTDPEI 494
Cdd:COG3842 87 ALFPhLTVAENVAFGL---RMRGVPKAEIRARV-AELL------ELVglegLADRYPHqLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRADQ--TTIItanrlssVMH--------ADEIIVMDDGQIIERGT 554
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQRELgiTFIY-------VTHdqeealalADRIAVMNDGRIEQVGT 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-554 |
3.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 108.35 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKL---LLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ 418
Cdd:PRK13640 12 SFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 --DNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK13640 92 npDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADV-----GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 497 LDDSLSAVDAKTEETIL-MNLKTMRADQTTIIT-ANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK13640 167 LDESTSMLDPAGKEQILkLIRKLKKKNNLTVISiTHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
344-554 |
4.29e-26 |
|
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: 106.44 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRdYSLDALLDSIGYVPQDNFLF 423
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 ST-DVRDNIRFadFDRSQAaVEDAAIASAVHDDILTFaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03263 88 DElTVREHLRF--YARLKG-LPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIIT------ANRLssvmhADEIIVMDDGQIIERGT 554
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTthsmdeAEAL-----CDRIAIMSDGKLRCIGS 215
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-311 |
6.11e-26 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 107.95 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSR 95
Cdd:cd18540 2 KLLILLIILMLLVALLDAVFPLLTKYAIDHFITPG-TLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 96 LFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIfVDWRLTLMALIPMPLLAVAS 175
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLI-LNWKLALIVLAVVPVLAVVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 176 RQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLT 255
Cdd:cd18540 160 IYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 256 YIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
354-553 |
6.81e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 105.45 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 354 MNVAFTLPQGkTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS----IGYVPQDNFLFS-TDVR 428
Cdd:cd03297 15 LKIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkIGLVFQQYALFPhLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADFDRSQAAVED--AAIASAVHDDILTFAQGYEtvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:cd03297 94 ENLAFGLKRKRNREDRIsvDELLDLLGLDHLLNRYPAQ---------LSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2018945286 507 KTEETILMNLKTMRAD--QTTIITANRLSSV-MHADEIIVMDDGQIIERG 553
Cdd:cd03297 165 ALRLQLLPELKQIKKNlnIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
351-558 |
1.59e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 106.48 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHdirdysldalldsIGYVPQDNFLFSTDVRDN 430
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFA---DFDRSQAAVEdaaiASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAK 507
Cdd:cd03291 118 IIFGvsyDEYRYKSVVK----ACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 508 TEETILMN-LKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEAL 558
Cdd:cd03291 194 TEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
343-551 |
2.98e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.17 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDalldsIGYVPQDNFL 422
Cdd:COG1116 17 FPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RGVVFQEPAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 F--STdVRDNIRFAdfdrsqaaVEDAAIASAVHDDIltfAQGYETVVGERGVS------LSGGQKQRIAIARAMMTDPEI 494
Cdd:COG1116 92 LpwLT-VLDNVALG--------LELRGVPKAERRER---ARELLELVGLAGFEdayphqLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 495 LILDDSLSAVDAKTEETilMN---LKTMRADQTTI--ITANRLSSVMHADEIIVMDD--GQIIE 551
Cdd:COG1116 160 LLMDEPFGALDALTRER--LQdelLRLWQETGKTVlfVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
343-554 |
9.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 104.06 E-value: 9.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYV---PQD 419
Cdd:PRK13648 15 FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVfqnPDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTdVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQG-YETVvgergvSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK13648 95 QFVGSI-VKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERAdYEPN------ALSGGQKQRVAIAGVLALNPSVIILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRADQ-TTIIT-ANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK13648 168 EATSMLDPDARQNLLDLVRKVKSEHnITIISiTHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
355-560 |
9.94e-25 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 105.95 E-value: 9.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKL---LLREYdqyQGVIQIDGHDirdysldaLLDS------------IGYVPQD 419
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLERPD---SGRIRLGGEV--------LQDSargiflpphrrrIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFST-DVRDNIRFAdFDRSQAAVEDAAIASAVhdDILtfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:COG4148 86 ARLFPHlSVRGNLLYG-RKRAPRAERRISFDEVV--ELL----GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRaDQTTI----IT-----ANRLssvmhADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG4148 159 EPLAALDLARKAEILPYLERLR-DELDIpilyVShsldeVARL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
353-554 |
3.16e-24 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIrDYSLDALLDSIGYVPQDNFLF-STDVRD 429
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIagLETPDS--GRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFADFDRSQAAVEDAAIAsavhDDILTFAQ--GYEtvvgERGVS-LSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:COG1118 95 NIAFGLRVRPPSKAEIRARV----EELLELVQleGLA----DRYPSqLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 507 KTEETILMNLKTMRADQ--TTII-TANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:COG1118 167 KVRKELRRWLRRLHDELggTTVFvTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-561 |
4.18e-24 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 107.69 E-value: 4.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 17 RYLWGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGI-----------LLSAAI--LQYLfryGWRTRIwg 83
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALglcllfivrtlLLHPAIfgLHHL---GMQMRI-- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 84 gaaklerTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQvaGAGILTFAdsIITGGTTIIAMVIFvdWRL--- 160
Cdd:TIGR01271 156 -------ALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDE--GLALAHFV--WIAPLQVILLMGLI--WELlev 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 161 -TLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNM 239
Cdd:TIGR01271 223 nGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 240 IDgLFDPAISLIIGLTYIVTIIYGGTLVmhHSISIGQLISFISYIAAL-------------VW--PMFAIGRL------- 297
Cdd:TIGR01271 303 LR-YFYSSAFFFSGFFVVFLSVVPYALI--KGIILRRIFTTISYCIVLrmtvtrqfpgaiqTWydSLGAITKIqdflcke 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 298 ------FN------VLERGNASYDR-VDQLLKEtstiIEAPNAIQTPATGDINYAVQKFTYPGdkQPTLMNVAFTLPQGK 364
Cdd:TIGR01271 380 eyktleYNltttevEMVNVTASWDEgIGELFEK----IKQNNKARKQPNGDDGLFFSNFSLYV--TPVLKNISFKLEKGQ 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 365 TLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHdirdysldalldsIGYVPQDNFLFSTDVRDNIRFA---DFDRSQA 441
Cdd:TIGR01271 454 LLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGlsyDEYRYTS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 442 AVEdaaiASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMN-LKTMR 520
Cdd:TIGR01271 521 VIK----ACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLM 596
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 2018945286 521 ADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:TIGR01271 597 SNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
354-560 |
6.96e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 103.27 E-value: 6.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 354 MNVAFTLPQGKTLGIVGKVGSGKTTLIKL---LLREYdqyQGVIQIDGHDIRDYSLDALLD----SIGYVPQDNFLFS-T 425
Cdd:TIGR02142 14 LDADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPD---EGEIVLNGRTLFDSRKGIFLPpekrRIGYVFQEARLFPhL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIRFAdfdRSQAAVEDAAIASAVHDDILtfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:TIGR02142 91 SVRGNLRYG---MKRARPSERRISFERVIELL----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 506 AKTEETILMNLKTMRA--DQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:TIGR02142 164 DPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-549 |
7.99e-24 |
|
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: 99.64 E-value: 7.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysLDALLDSIGYVPQDNFLF-STD 426
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD--LPPKDRDIAMVFQNYALYpHMT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIRFADFDRSQAAVEdaaIASAVHD--DILtfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:cd03301 89 VYDNIAFGLKLRKVPKDE---IDERVREvaELL----QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2018945286 505 DAKTEETILMNLKTM--RADQTTI-ITANRLSSVMHADEIIVMDDGQI 549
Cdd:cd03301 162 DAKLRVQMRAELKRLqqRLGTTTIyVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
355-560 |
9.45e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.15 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLReYDQYQGVIQIDGHDIRDYSLDALLD---SIGYVPQDNFlFSTDVRDNI 431
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSRRALRPlrrRMQVVFQDPF-GSLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 rfadfdrsqaavedAAIAS---AVHDDILTFAQGYETVV---GERGVS----------LSGGQKQRIAIARAMMTDPEIL 495
Cdd:COG4172 382 --------------GQIIAeglRVHGPGLSAAERRARVAealEEVGLDpaarhrypheFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 496 ILDDSLSAVDAKTEETILMNLKTMRADQttiitanRLS--------SVMHA--DEIIVMDDGQIIERGTHEALLA 560
Cdd:COG4172 448 VLDEPTSALDVSVQAQILDLLRDLQREH-------GLAylfishdlAVVRAlaHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
353-562 |
1.27e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 99.67 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS-IGYVPQDNFLFST-DVRDN 430
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFADFDRSQAAVEDAAIASAvhddiltfaqgYET--VVGER----GVSLSGGQKQRIAIARAMMTDPEILILDD-SL-- 501
Cdd:COG0410 99 LLLGAYARRDRAEVRADLERV-----------YELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEpSLgl 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 502 --SAVdakteETILMNLKTMRADQTTII----TANRLSSVmhADEIIVMDDGQIIERGTHEALLAED 562
Cdd:COG0410 168 apLIV-----EEIFEIIRRLNREGVTILlveqNARFALEI--ADRAYVLERGRIVLEGTAAELLADP 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-553 |
1.38e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 98.39 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 335 DINYAVQKFTYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQYQGVIQIDGHDIrdySLDALLDS 412
Cdd:cd03213 8 NLTVTVKSSPSKSGKQ-LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 413 IGYVPQDNFLFSTD-VRDNIRFAdfdrsqaavedAAIasavhddiltfaqgyetvvgeRGvsLSGGQKQRIAIARAMMTD 491
Cdd:cd03213 84 IGYVPQDDILHPTLtVRETLMFA-----------AKL---------------------RG--LSGGERKRVSIALELVSN 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 492 PEILILDDSLSAVDAKTEETILMNLKTMRADQTTII-TANRLSSVMHA--DEIIVMDDGQIIERG 553
Cdd:cd03213 130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIIcSIHQPSSEIFElfDKLLLLSQGRVIYFG 194
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
353-560 |
1.94e-23 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 99.30 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDI--RDYSLDALLDSIGYVPQdNF-LFS--T 425
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCInlLEEPDS--GTITVDGEDLtdSKKDINKLRRKVGMVFQ-QFnLFPhlT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 dVRDNIRFAD---FDRSQAAVEDAAIAsavhddILtfaqgyETV-VGERG----VSLSGGQKQRIAIARAMMTDPEILIL 497
Cdd:COG1126 94 -VLENVTLAPikvKKMSKAEAEERAME------LL------ERVgLADKAdaypAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 498 DDSLSAVDAkteETILMNLKTMR--ADQ--TTIItanrlssVMH--------ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG1126 161 DEPTSALDP---ELVGEVLDVMRdlAKEgmTMVV-------VTHemgfarevADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
344-550 |
2.17e-23 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 99.36 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD---SIGYVPQD- 419
Cdd:COG3638 11 RYPGGT-PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRIGMIFQQf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNI----------------RFADFDRSQAAvedAAIASaVhdDILTFAQgyetvvgERGVSLSGGQKQRIA 483
Cdd:COG3638 90 NLVPRLSVLTNVlagrlgrtstwrsllgLFPPEDRERAL---EALER-V--GLADKAY-------QRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 484 IARAMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTIITAnrLSSV----MHADEIIVMDDGQII 550
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVN--LHQVdlarRYADRIIGLRDGRVV 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
347-553 |
2.37e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 99.34 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGV-----IQIDGHDIRDYSLD--ALLDSIGYVPQD 419
Cdd:COG1117 22 GDKQ-ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDIYDPDVDvvELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFA-----DFDRSQ--AAVE----DAAIASAVHDDIltfaqgyetvvGERGVSLSGGQKQRIAIARAM 488
Cdd:COG1117 101 PNPFPKSIYDNVAYGlrlhgIKSKSEldEIVEeslrKAALWDEVKDRL-----------KKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 489 MTDPEILILDDSLSAVD----AKTEETILmNLKtmraDQTTII--TAN-----RLSsvmhaDEIIVMDDGQIIERG 553
Cdd:COG1117 170 AVEPEVLLMDEPTSALDpistAKIEELIL-ELK----KDYTIVivTHNmqqaaRVS-----DYTAFFYLGELVEFG 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
332-560 |
2.69e-23 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 103.54 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 332 ATGDINYAVQKFTYPGdkqptLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALL 410
Cdd:PRK10762 252 APGEVRLKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 411 DSIGYVPQD----NFLFSTDVRDNIRFA---DFDRSQAAVEDAAIASAVHDDILTF---AQGYETVVGErgvsLSGGQKQ 480
Cdd:PRK10762 327 NGIVYISEDrkrdGLVLGMSVKENMSLTalrYFSRAGGSLKHADEQQAVSDFIRLFnikTPSMEQAIGL----LSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 481 RIAIARAMMTDPEILILDDSLSAVD--AKTEETILMNlkTMRADQTTIITanrLSSVM-----HADEIIVMDDGQI---- 549
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDvgAKKEIYQLIN--QFKAEGLSIIL---VSSEMpevlgMSDRILVMHEGRIsgef 477
|
250
....*....|..
gi 2018945286 550 -IERGTHEALLA 560
Cdd:PRK10762 478 tREQATQEKLMA 489
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
343-550 |
2.92e-23 |
|
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: 97.71 E-value: 2.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYpGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIrdySLDALLDSIGYVPQD--N 420
Cdd:cd03226 7 FSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDvdY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFadfdRSQAAVEDAAIASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:cd03226 83 QLFTDSVREELLL----GLKELDAGNEQAETVLKDL-----DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 501 LSAVDAKTEETILMNLKTMRADQTTIITANR----LSSVmhADEIIVMDDGQII 550
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQGKAVIVITHdyefLAKV--CDRVLLLANGAIV 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
355-561 |
2.94e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 100.51 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLR---EYDQYQGVIQIDGHDIRDYSLDALLD----SIGYVPQD-----NFL 422
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKELRKirgrEIQMIFQDpmtslNPV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FStdVRDNIR---FADFDRSQAAVEDAAIA--SAVHddiLTFAqgyETVVGERGVSLSGGQKQRIAIARAMMTDPEILIL 497
Cdd:COG0444 103 MT--VGDQIAeplRIHGGLSKAEARERAIEllERVG---LPDP---ERRLDRYPHELSGGMRQRVMIARALALEPKLLIA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 498 DDSLSAVDAKTEETILMNLKTMRAD-QTTI--ITANrLSSVMH-ADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG0444 175 DEPTTALDVTIQAQILNLLKDLQRElGLAIlfITHD-LGVVAEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
23-283 |
4.53e-23 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 99.69 E-value: 4.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 23 IFLVLVAVVQIVPPKVIGTLVD--LIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIwggAAKLERTLRSRLFWHF 100
Cdd:cd18784 3 FFLLAAAVGEIFIPYYTGQVIDgiVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLA---MARLNIRIRNLLFRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 101 MKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIfVDWRLTLMALIPMPLLAVASRQLGA 180
Cdd:cd18784 80 VSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFK-LSWQLSLVTLIGLPLIAIVSKVYGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 181 HLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTI 260
Cdd:cd18784 159 YYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTL 238
|
250 260
....*....|....*....|...
gi 2018945286 261 IYGGTLVMHHSISIGQLISFISY 283
Cdd:cd18784 239 YYGGHLVITGQISGGNLISFILY 261
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
21-307 |
1.07e-22 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 98.70 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 21 GVIFLVLVAVVQIVPPKVIGTLVDL--------IDTHQLTPQ--KLIMWLGIL-LSAAILQYLFRYGWRTRiwggAAKLE 89
Cdd:cd18577 4 GLLAAIAAGAALPLMTIVFGDLFDAftdfgsgeSSPDEFLDDvnKYALYFVYLgIGSFVLSYIQTACWTIT----GERQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 90 RTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAG---AGILTFADSIITGgtTIIAMVifVDWRLTLMALI 166
Cdd:cd18577 80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGeklGLLIQSLSTFIAG--FIIAFI--YSWKLTLVLLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 167 PMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDP 246
Cdd:cd18577 156 TLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLG 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 247 AISLIIGLTYIVTIIYGGTLVMHHSISIGQLIS-FISYIAAlvwpMFAIGRL---FNVLERGNAS 307
Cdd:cd18577 236 LLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTvFFAVLIG----AFSLGQIapnLQAFAKARAA 296
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
344-542 |
2.52e-22 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 95.55 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDA---LLDSIGYVPQDN 420
Cdd:cd03292 9 TYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFST-DVRDNIRFAdFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:cd03292 88 RLLPDrNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAE----LSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2018945286 500 SLSAVDAKTEETILMNLKTMRADQTTIITANrlssvmHADEII 542
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVAT------HAKELV 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
344-562 |
2.57e-22 |
|
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: 96.10 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS---IGYVPQD- 419
Cdd:cd03256 9 TYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIGMIFQQf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFADFDR--------SQAAVEDAAIASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTD 491
Cdd:cd03256 88 NLIERLSVLENVLSGRLGRrstwrslfGLFPKEEKQRALAALERV-----GLLDKAYQRADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 492 PEILILDDSLSAVDAKTEETILMNLK--TMRADQTTIITANRLSSVM-HADEIIVMDDGQIIERGTHEALLAED 562
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAELTDEV 236
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
355-554 |
4.63e-22 |
|
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: 95.20 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS-IGYVPQDNFLFST-DVRDNIR 432
Cdd:cd03219 18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLFPElTVLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 FA--------DFDRSQAAVEDAAIASAvhDDILTFAqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:cd03219 98 VAaqartgsgLLLARARREEREARERA--EELLERV-GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 505 DAkTEETILMNL-KTMRADQTTI-ITANRLSSVM-HADEIIVMDDGQIIERGT 554
Cdd:cd03219 175 NP-EETEELAELiRELRERGITVlLVEHDMDVVMsLADRVTVLDQGRVIAEGT 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
355-561 |
6.38e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.11 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD---SIGYVPQDNFLfSTD----V 427
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPlrrRMQMVFQDPYA-SLNprmtV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNIRFAdFD----RSQAAVEDAAIasavhdDILT-------FAQGY--EtvvgergvsLSGGQKQRIAIARAMMTDPEI 494
Cdd:COG4608 115 GDIIAEP-LRihglASKAERRERVA------ELLElvglrpeHADRYphE---------FSGGQRQRIGIARALALNPKL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAE 561
Cdd:COG4608 179 IVCDEPVSALDVSIQAQVLNLLEDLQDELglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
348-554 |
6.52e-22 |
|
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: 94.61 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFS-TD 426
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTVFQNYALFPhLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIRFAdfdRSQAAVEDAAIASAVHDDI-LTFAQGYEtvvGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:cd03300 89 VFENIAFG---LRLKKLPKAEIKERVAEALdLVQLEGYA---NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 506 AKTEETILMNLKTMRAD-QTTII--TANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:cd03300 163 LKLRKDMQLELKRLQKElGITFVfvTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
353-558 |
6.68e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 94.51 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS-IGYVPQDNFLFST-DVRDN 430
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQGREIFPRlTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IR--FADFDRSQAAVEDaaiasavhdDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSlsavdakT 508
Cdd:TIGR03410 96 LLtgLAALPRRSRKIPD---------EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP-------T 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 509 E----------ETILMNLKTMRaDQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEAL 558
Cdd:TIGR03410 160 EgiqpsiikdiGRVIRRLRAEG-GMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
343-553 |
7.14e-22 |
|
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: 94.18 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQptLMNVAFTLPQGKTlGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALLDSIGYVPQDNfl 422
Cdd:cd03264 8 KRYGKKRA--LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQEF-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 fstDVRDNIRFADFDRSQAA---VEDAAIASAVhDDILTfAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:cd03264 82 ---GVYPNFTVREFLDYIAWlkgIPSKEVKARV-DEVLE-LVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 500 SLSAVDAktEETI-LMN-LKTMRADQTTIITANRLSSV-MHADEIIVMDDGQIIERG 553
Cdd:cd03264 157 PTAGLDP--EERIrFRNlLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
343-561 |
9.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPgDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALLDSIGYV---PQ 418
Cdd:PRK13644 9 YSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVfqnPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 DNFLFSTdVRDNIRFADFDRSQAAVE-----DAAIASAvhddiltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPE 493
Cdd:PRK13644 88 TQFVGRT-VEEDLAFGPENLCLPPIEirkrvDRALAEI----------GLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTM-RADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
345-577 |
1.07e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 95.31 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 345 YPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQyQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFS 424
Cdd:cd03289 12 YTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNI----RFADFDRSQAAvEDAAIASAvhddILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:cd03289 91 GTFRKNLdpygKWSDEEIWKVA-EEVGLKSV----IEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 501 LSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEdgwyaEMWLKQQLSQA 577
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE-----KSHFKQAISPS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
347-549 |
1.09e-21 |
|
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: 93.36 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDI--RDYSLDALLDSIGYVPQDNFL 422
Cdd:cd03262 11 GDFH-VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEEPDS--GTIIIDGLKLtdDKKNINELRQKVGMVFQQFNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FS-TDVRDNIRFAD---FDRSQAAVEDAAIASAVHDDILTFAQGYEtvvgergVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:cd03262 88 FPhLTVLENITLAPikvKGMSKAEAEERALELLEKVGLADKADAYP-------AQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 499 DSLSAVDAkteETILMNLKTMRA---DQTTIITanrlssVMH--------ADEIIVMDDGQI 549
Cdd:cd03262 161 EPTSALDP---ELVGEVLDVMKDlaeEGMTMVV------VTHemgfarevADRVIFMDDGRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
353-562 |
2.01e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.07 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL-FSTDVRDNI 431
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADFDRSQAAVEDAAIASAVHD--DILTFAQGYETvvgergvSLSGGQKQRIAIARAMM------TDPEILILDDSLSA 503
Cdd:PRK13548 98 AMGRAPHGLSRAEDDALVAAALAqvDLAHLAGRDYP-------QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 504 VDAKTEETILMNLKTM-RADQTTIITanrlssVMH--------ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK13548 171 LDLAHQHHVLRLARQLaHERGLAVIV------VLHdlnlaaryADRIVLLHQGRLVADGTPAEVLTPE 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
351-554 |
3.17e-21 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 92.79 E-value: 3.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFS-TDVRD 429
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFADFDRSQAAVEDAA-IASAVHDdILTFAQ--GYEtvvgERGVS-LSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAeIRAKVHE-LLKLVQldWLA----DRYPAqLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 506 AKTEETILMNLKTMRAD---QTTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:cd03296 169 AKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
335-562 |
4.94e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 4.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 335 DINYAVQKFTyPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDG----HDIRDYSLDALL 410
Cdd:PRK13646 7 NVSYTYQKGT-PYEHQ-AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 411 DSIGYVPQ--DNFLFSTDVRDNIRFA--DFDRSQAAVEDAAiasavHDDILTFaqGYE-TVVGERGVSLSGGQKQRIAIA 485
Cdd:PRK13646 85 KRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HRLLMDL--GFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 486 RAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVM-HADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDEnkTIILVSHDMNEVArYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-560 |
6.78e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.87 E-value: 6.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDK-QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDALLDSIGYVPQ 418
Cdd:PRK13650 11 TFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIdgLLEAES--GQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 --DNFLFSTDVRDNIRFAdfdrsqaaVEDAAIAsavHDDILTFAQGYETVVG-----ERGVS-LSGGQKQRIAIARAMMT 490
Cdd:PRK13650 89 npDNQFVGATVEDDVAFG--------LENKGIP---HEEMKERVNEALELVGmqdfkEREPArLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 491 DPEILILDDSLSAVDAKTEETILMNLKTMRAD-QTTIIT-ANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISiTHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
355-560 |
1.50e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.44 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH------------DIR------DYSLDALLdSIGYV 416
Cdd:COG4167 31 PVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdykyrckHIRmifqdpNTSLNPRL-NIGQI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 417 PQDNFLFSTDVRDNIRfadfdrsQAAVEDaaiasavhddilTFAQgyetvVGERG-------VSLSGGQKQRIAIARAMM 489
Cdd:COG4167 110 LEEPLRLNTDLTAEER-------EERIFA------------TLRL-----VGLLPehanfypHMLSSGQKQRVALARALI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 490 TDPEILILDDSLSAVDAkTEETILMNLktMRADQTT-----IITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG4167 166 LQPKIIIADEALAALDM-SVRSQIINL--MLELQEKlgisyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFA 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
355-561 |
2.46e-20 |
|
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: 91.17 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD----SIGYVPQDNFLF-STDVRD 429
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFADFDRSQAAVEDAAIASAVHDdiLTFAQGYETV-VGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA-- 506
Cdd:cd03294 122 NVAFGLEVQGVPRAEREERAAEALE--LVGLEGWEHKyPDE----LSGGMQQRVGLARALAVDPDILLMDEAFSALDPli 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 507 KTE-ETILMNLKTMRADQTTIIT-----ANRLssvmhADEIIVMDDGQIIERGTHEALLAE 561
Cdd:cd03294 196 RREmQDELLRLQAELQKTIVFIThdldeALRL-----GDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
344-554 |
2.89e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKL--LLREYDQyqGVIQIDGHDIRDYSLDALLD---SIGYV 416
Cdd:PRK11153 10 VFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCinLLERPTS--GRVLVDGQDLTALSEKELRKarrQIGMI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 417 PQD-NFLFSTDVRDNIRFAdfdRSQAAVEDAAIASAVhDDILtfaqgyETVvgerGVS---------LSGGQKQRIAIAR 486
Cdd:PRK11153 88 FQHfNLLSSRTVFDNVALP---LELAGTPKAEIKARV-TELL------ELV----GLSdkadrypaqLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 487 AMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTI--ITanrlssvmH--------ADEIIVMDDGQIIERGT 554
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIvlIT--------HemdvvkriCDRVAVIDAGRLVEQGT 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
320-551 |
4.38e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 90.25 E-value: 4.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 320 TIIEAPNAIQTPATGDINYAVQKftypgdkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH 399
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQR-------APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 400 DI------------RDYSLdALLDSIGYV-PQdnflfsTDVRDNIR-----FADFDRSQAAVEDAAIASAVHDDiltfaq 461
Cdd:TIGR02769 74 DLyqldrkqrrafrRDVQL-VFQDSPSAVnPR------MTVRQIIGeplrhLTSLDESEQKARIAELLDMVGLR------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 462 gyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTT--IITANRLSSVMH-A 538
Cdd:TIGR02769 141 --SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSfC 218
|
250
....*....|...
gi 2018945286 539 DEIIVMDDGQIIE 551
Cdd:TIGR02769 219 QRVAVMDKGQIVE 231
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
16-311 |
5.99e-20 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 90.58 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIDTHQLTpQKLIMWLGILLSAAILQYLFRYgWRTRIwggAAKLERTLRS 94
Cdd:cd18570 1 KKLLILILLLsLLITLLGIAGSFFFQILIDDIIPSGDI-NLLNIISIGLILLYLFQSLLSY-IRSYL---LLKLSQKLDI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 95 RL----FWHFMKMDTTFFQKHRTGDLMAHaTNDLTAIQQ-VAGAGILTFADSIITggttIIAMVI--FVDWRLTLMALIP 167
Cdd:cd18570 76 RLilgyFKHLLKLPLSFFETRKTGEIISR-FNDANKIREaISSTTISLFLDLLMV----IISGIIlfFYNWKLFLITLLI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 168 MPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPA 247
Cdd:cd18570 151 IPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 248 ISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18570 231 KGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-554 |
6.11e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.49 E-value: 6.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRD--YSLDALLDSIGYVPQ--DNFLFSTDVR 428
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADfdrSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:PRK13637 103 KDIAFGP---INLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2018945286 509 EETILMNLKTMRA--DQTTIITANRLSSVMH-ADEIIVMDDGQIIERGT 554
Cdd:PRK13637 180 RDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
353-554 |
6.51e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.46 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNIR 432
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD 1405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 -FadFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSA-VDAKTEE 510
Cdd:PTZ00243 1406 pF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILMDEATAnIDPALDR 1483
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2018945286 511 TILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PTZ00243 1484 QIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-321 |
1.49e-19 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 89.82 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 57 IMWLGI----LLSAAILQYLFRYGwrtriwggAAKLERTLRSRLFWHFMKMDTTFF--QKHRTGDLMAHATNDLTAIQQV 130
Cdd:cd18578 56 LMFLVLaivaGIAYFLQGYLFGIA--------GERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 131 AGAgilTFADSIITGGTTIIAMVI--FVDWRLTLMALIPMPLLAVASRqLGAHLHTAF-GQSQAAFSRLNDKTQESVSGI 207
Cdd:cd18578 128 VGD---RLGLILQAIVTLVAGLIIafVYGWKLALVGLATVPLLLLAGY-LRMRLLSGFeEKNKKAYEESSKIASEAVSNI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 208 KVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFdPAIS-LIIGLTYIVTIIYGGTLVMHHSISIGQLisFISYIaA 286
Cdd:cd18578 204 RTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG-FGLSqSLTFFAYALAFWYGGRLVANGEYTFEQF--FIVFM-A 279
|
250 260 270
....*....|....*....|....*....|....*...
gi 2018945286 287 LVWPMFAIGRLFNVL---ERGNASYDRVDQLLKETSTI 321
Cdd:cd18578 280 LIFGAQSAGQAFSFApdiAKAKAAAARIFRLLDRKPEI 317
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
321-561 |
1.71e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.05 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 321 IIEAPNAIQT-PATGDINyaVQKFT--YPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQyQGVIQID 397
Cdd:TIGR01271 1202 VIENPHAQKCwPSGGQMD--VQGLTakYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQID 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 398 GHDIRDYSLDALLDSIGYVPQDNFLFSTDVRDNI----RFADFDRSQAAvEDAAIASAVHDdiltFAQGYETVVGERGVS 473
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpyeQWSDEEIWKVA-EEVGLKSVIEQ----FPDKLDFVLVDGGYV 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 474 LSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:TIGR01271 1354 LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYD 1433
|
....*...
gi 2018945286 554 THEALLAE 561
Cdd:TIGR01271 1434 SIQKLLNE 1441
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
355-529 |
2.40e-19 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 86.38 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDySLDALLDSIGYVPQDNFLFST-DVRDNIRF 433
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 AdFDRSQAAVEDAAIASAVHDDILTfaqGYETV-VGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETI 512
Cdd:COG4133 99 W-AALYGLRADREAIDEALEAVGLA---GLADLpVRQ----LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALL 170
|
170
....*....|....*..
gi 2018945286 513 LMNLKTMRADQTTIITA 529
Cdd:COG4133 171 AELIAAHLARGGAVLLT 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
348-554 |
5.25e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.59 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDI-------RDysldalldsIGYVPQ 418
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLEDPTS--GEILIGGRDVtdlppkdRN---------IAMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 dNF-LF-STDVRDNIRF----ADFDRS--QAAVEDAAiaSAVH-DDILtfaqgyetvvgERGVS-LSGGQKQRIAIARAM 488
Cdd:COG3839 83 -SYaLYpHMTVYENIAFplklRKVPKAeiDRRVREAA--ELLGlEDLL-----------DRKPKqLSGGQRQRVALGRAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 489 MTDPEILILDDSLSAVDAKteetilmnLK-TMRA---------DQTTIItanrlssVMH--------ADEIIVMDDGQII 550
Cdd:COG3839 149 VREPKVFLLDEPLSNLDAK--------LRvEMRAeikrlhrrlGTTTIY-------VTHdqveamtlADRIAVMNDGRIQ 213
|
....
gi 2018945286 551 ERGT 554
Cdd:COG3839 214 QVGT 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
356-553 |
5.97e-19 |
|
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: 85.88 E-value: 5.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 356 VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLdSIGYVPQDNFLFS-TDVRDNIR-F 433
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTGLYDrLTARENLEyF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 ADF-----DRSQAAVEDAAiasavhdDILtfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:cd03266 103 AGLyglkgDELTARLEELA-------DRL----GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2018945286 509 EETILMNLKTMRADQTTIITAnrlSSVMH-----ADEIIVMDDGQIIERG 553
Cdd:cd03266 172 TRALREFIRQLRALGKCILFS---THIMQeverlCDRVVVLHRGRVVYEG 218
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
353-550 |
6.17e-19 |
|
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: 85.79 E-value: 6.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL---LREYDQYQGVIQIDGhdiRDYSLDALLDSIGYVPQDNFLFST-DVR 428
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADFDRSQAAVEDAaIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:cd03234 100 ETLTYTAILRLPRKSSDA-IRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2018945286 509 E-ETILMNLKTMRADQTTIITANRLSSVM--HADEIIVMDDGQII 550
Cdd:cd03234 179 AlNLVSTLSQLARRNRIVILTIHQPRSDLfrLFDRILLLSSGEIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
345-552 |
6.88e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 86.68 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 345 YPGdkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDAlldsiGYVPQDNFLFS 424
Cdd:PRK11248 11 YGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 -TDVRDNIRF----ADFDRSQAAVEDAAIASAVhddiltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:PRK11248 84 wRNVQDNVAFglqlAGVEKMQRLEIAHQMLKKV---------GLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 500 SLSAVDAKTEE---TILMNLKTMRADQTTIITANRLSSVMHADEIIVM--DDGQIIER 552
Cdd:PRK11248 155 PFGALDAFTREqmqTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVER 212
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
338-560 |
7.51e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.71 E-value: 7.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 338 YAVQKFTYPGDKQPTLMN-VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDA---LLDSI 413
Cdd:PRK11308 15 YPVKRGLFKPERLVKALDgVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 414 GYVPQDNFLfSTDVRDNIRF---------ADFDRSQAAVEDAAIASAV-----HddiltfAQGYETVvgergvsLSGGQK 479
Cdd:PRK11308 95 QIVFQNPYG-SLNPRKKVGQileepllinTSLSAAERREKALAMMAKVglrpeH------YDRYPHM-------FSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 480 QRIAIARAMMTDPEILILDDSLSAVDAKTEETIL---MNLKTMRADQTTIITANrLSSVMH-ADEIIVMDDGQIIERGTH 555
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLnlmMDLQQELGLSYVFISHD-LSVVEHiADEVMVMYLGRCVEKGTK 239
|
....*
gi 2018945286 556 EALLA 560
Cdd:PRK11308 240 EQIFN 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-553 |
9.54e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.28 E-value: 9.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGhdirdySLDALLD-SIGYVPQdnflFStdVRDNI 431
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGlGGGFNPE----LT--GRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RF--ADFDRSQAAVEdaaiasAVHDDILTFA---QGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:cd03220 106 YLngRLLGLSRKEID------EKIDEIIEFSelgDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2018945286 507 KTEETILMNLKTMRADQTTIITANR-LSSVM-HADEIIVMDDGQIIERG 553
Cdd:cd03220 176 AFQEKCQRRLRELLKQGKTVILVSHdPSSIKrLCDRALVLEKGKIRFDG 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
347-553 |
9.58e-19 |
|
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: 85.02 E-value: 9.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRdyslDALLDSIGYVPQDNFLF-ST 425
Cdd:cd03269 11 GRVT-ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLPEERGLYpKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIR-FADFdrsqAAVEDAAIASAVHDDILTFA-QGYETVVGERgvsLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:cd03269 86 KVIDQLVyLAQL----KGLKKEEARRRIDEWLERLElSEYANKRVEE---LSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 504 VDAKTEETILMNLKTMRADQTTII-TANRLSSVMH-ADEIIVMDDGQIIERG 553
Cdd:cd03269 159 LDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
348-554 |
1.03e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 88.08 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFS- 424
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIagFETPDS--GRIMLDGQDITH--VPAENRHVNTVFQSYALFPh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNIRFADfdRSQAaVEDAAIASAVHDdILTFAQgYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK09452 101 MTVFENVAFGL--RMQK-TPAAEITPRVME-ALRMVQ-LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 505 DAKTEETILMNLKTM-RADQTTII--TANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK09452 176 DYKLRKQMQNELKALqRKLGITFVfvTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
355-549 |
2.98e-18 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.87 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS-IGYVPQD---NFLFST-DVRD 429
Cdd:cd03215 18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDrkrEGLVLDlSVAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFADFdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTE 509
Cdd:cd03215 98 NIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2018945286 510 ETILMNLKTMRADQTTIITanrLSS----VMH-ADEIIVMDDGQI 549
Cdd:cd03215 141 AEIYRLIRELADAGKAVLL---ISSeldeLLGlCDRILVMYEGRI 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
343-578 |
3.10e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 3.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMN-VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ--D 419
Cdd:PRK13642 12 FKYEKESDVNQLNgVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFA----DFDRSQ--AAVEDAAIASAVHDdiltfaqgYETVVGERgvsLSGGQKQRIAIARAMMTDPE 493
Cdd:PRK13642 92 NQFVGATVEDDVAFGmenqGIPREEmiKRVDEALLAVNMLD--------FKTREPAR---LSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLK 571
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLD 240
|
....*..
gi 2018945286 572 QQLSQAL 578
Cdd:PRK13642 241 VPFSSNL 247
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
353-550 |
3.15e-18 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 82.09 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALLDSIGYVPQdnflfstdvrdni 431
Cdd:cd03216 16 LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 rfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEET 511
Cdd:cd03216 83 ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2018945286 512 ILMNLKTMRADQTTI--ITaNRLSSVMH-ADEIIVMDDGQII 550
Cdd:cd03216 121 LFKVIRRLRAQGVAVifIS-HRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
349-553 |
3.20e-18 |
|
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: 83.42 E-value: 3.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-----LDALLDSIGYVPQdnflf 423
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIealrrIGALIEAPGFYPN----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 sTDVRDNIRFADfdrSQAAVEDAAIasavhDDILtfaqgyeTVVGERGV------SLSGGQKQRIAIARAMMTDPEILIL 497
Cdd:cd03268 87 -LTARENLRLLA---RLLGIRKKRI-----DEVL-------DVVGLKDSakkkvkGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 498 DDSLSAVDA---KTEETILMNLktmRADQTTIITANRLSSVMH--ADEIIVMDDGQIIERG 553
Cdd:cd03268 151 DEPTNGLDPdgiKELRELILSL---RDQGITVLISSHLLSEIQkvADRIGIINKGKLIEEG 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
339-505 |
3.37e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 83.61 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 339 AVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ 418
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 DNFLFSTDVRDNIRFADFDRSQAAVEDAAIasavhDDILTFAQGyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK10247 89 TPTLFGDTVYDNLIFPWQIRNQQPDPAIFL-----DDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 2018945286 499 DSLSAVD 505
Cdd:PRK10247 163 EITSALD 169
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
92-560 |
4.07e-18 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 87.55 E-value: 4.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTtiIAMVIFVDWRLTLMALIPMPLL 171
Cdd:COG4615 83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVRLPELLQSVALVLGC--LAYLAWLSPPLFLLTLVLLGLG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKtFGQEEADvaDFNEIVTKTIAINKRVNMI--DGLFDPAIS 249
Cdd:COG4615 161 VAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELK-LNRRRRR--AFFDEDLQPTAERYRDLRIraDTIFALANN 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 250 LIIGLTYIV--TIIYGgtLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQL-LKETSTIIEAPN 326
Cdd:COG4615 238 WGNLLFFALigLILFL--LPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAAAD 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 327 AIQTPATGDINyAVQ----KFTYPGDKQP---TLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH 399
Cdd:COG4615 316 AAAPPAPADFQ-TLElrgvTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 400 DIRDYSLDALLDsigyvpqdnfLFSTdVrdnirFAD---FDR---SQAAVEDAAIASAVH----DDILTFAQGYETVvge 469
Cdd:COG4615 395 PVTADNREAYRQ----------LFSA-V-----FSDfhlFDRllgLDGEADPARARELLErlelDHKVSVEDGRFST--- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 470 rgVSLSGGQKQRIAIARAMMTDPEILILDdslsavdaktE--------------ETILMNLKtmrADQTTIItanrlsSV 535
Cdd:COG4615 456 --TDLSQGQRKRLALLVALLEDRPILVFD----------EwaadqdpefrrvfyTELLPELK---ARGKTVI------AI 514
|
490 500 510
....*....|....*....|....*....|..
gi 2018945286 536 MH-------ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG4615 515 SHddryfdlADRVLKMDYGKLVELTGPAALAA 546
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
355-558 |
4.20e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.98 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGhdirdySLDALLD-SIGYVPQdnflFStdVRDNIRF 433
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLElGAGFHPE----LT--GRENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 A----DFDRSQAAvedaaiasAVHDDILTFAQgyetvVGE------RgvSLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:COG1134 112 NgrllGLSRKEID--------EKFDEIVEFAE-----LGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVDEVLAV 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 504 VDA----KTEETIlmnlKTMRADQTTIITANR-LSSVM-HADEIIVMDDGQIIERG-THEAL 558
Cdd:COG1134 177 GDAafqkKCLARI----RELRESGRTVIFVSHsMGAVRrLCDRAIWLEKGRLVMDGdPEEVI 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
344-552 |
4.41e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.14 E-value: 4.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDAlldsiGYVPQD 419
Cdd:COG4525 12 RYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIagFLAPSS--GEITLDGVPVTGPGADR-----GVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFS-TDVRDNIRFADFDRSQAAVEDAAIAsavhDDILTFA--QGYEtvvgERGV-SLSGGQKQRIAIARAMMTDPEIL 495
Cdd:COG4525 85 DALLPwLNVLDNVAFGLRLRGVPKAERRARA----EELLALVglADFA----RRRIwQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 496 ILDDSLSAVDAKTEETI---LMNLKTMRADQTTIITANRLSSVMHADEIIVMDD--GQIIER 552
Cdd:COG4525 157 LMDEPFGALDALTREQMqelLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVER 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
349-559 |
5.30e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 5.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD-----QYQGVIQIDGHDIRDYSLDA--LLDSIGYVPQDNF 421
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFSTDVRDNIRFA-------DFDRSQAAVEDAAIASAVHDDIltfaqgyETVVGERGVSLSGGQKQRIAIARAMMTDPEI 494
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEV-------KDRLHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 495 LILDDSLSAVD----AKTEETiLMNLKtmraDQTTIIT-------ANRLSsvmhaDEIIVMDDGQIIERG-THEALL 559
Cdd:PRK14239 170 ILLDEPTSALDpisaGKIEET-LLGLK----DDYTMLLvtrsmqqASRIS-----DRTGFFLDGDLIEYNdTKQMFM 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
353-572 |
7.72e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIK----LLLREydqyQGVIQIDGHDIR----DYSLDALLDSIGYVPQ--DNFL 422
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQhfnaLLKPS----SGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNIRFADfdRSQAAVEDAAIASAVhdDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:PRK13641 99 FENTVLKDVEFGP--KNFGFSEDEAKEKAL--KWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 503 AVDAKTEETILMNLKT-MRADQTTIITANRLSSVM-HADEIIVMDDGQIIERGTHEALLAEDGWYAEMWLKQ 572
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAeYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDE 246
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
92-283 |
1.22e-17 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 83.66 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHaTNDLTAIQQVAGAGILTfadSIITGGTTIIAMVI--FVDWRLTLMALIPMp 169
Cdd:cd18567 77 WTSNLFRHLLRLPLSYFEKRHLGDIVSR-FGSLDEIQQTLTTGFVE---ALLDGLMAILTLVMmfLYSPKLALIVLAAV- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 170 LLAVASRQLG-AHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAI 248
Cdd:cd18567 152 ALYALLRLALyPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAAN 231
|
170 180 190
....*....|....*....|....*....|....*
gi 2018945286 249 SLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISY 283
Cdd:cd18567 232 GLLFGLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
353-579 |
1.97e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI----RDYSLDALLDSIGYVPQ--DNFLFSTD 426
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIRFA--DFDRSQAAVEDAAiasavhDDILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK13634 103 VEKDICFGpmNFGVSEEDAKQKA------REMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 505 DAKTEETILMNLKTM--RADQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAEDGWYAEMWL--------KQQ 573
Cdd:PRK13634 177 DPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADPDELEAIGLdlpetvkfKRA 256
|
....*.
gi 2018945286 574 LSQALG 579
Cdd:PRK13634 257 LEEKFG 262
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
87-283 |
2.26e-17 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 82.90 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 87 KLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGiLTFADSIITGGTTIIAMVIFVDWRLTLMALI 166
Cdd:cd18589 66 RIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSEN-LSLLMWYLARGLFLFIFMLWLSPKLALLTAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 167 PMPLLAVASRQLGaHLHTAFG-QSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKR------VNM 239
Cdd:cd18589 145 GLPLLLLVPKFVG-KFQQSLAvQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKeaaayaVSM 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2018945286 240 IDGLFDpAISLIIGLTYivtiiYGGTLVMHHSISIGQLISFISY 283
Cdd:cd18589 224 WTSSFS-GLALKVGILY-----YGGQLVTAGTVSSGDLVTFVLY 261
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
347-561 |
2.52e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 2.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLdSIGYVPQ-DNFLFST 425
Cdd:PRK13536 52 GDK-AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARA-RIGVVPQfDNLDLEF 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDN-IRFADFDRSQAAVEDAAIASavhddILTFAQgYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK13536 130 TVRENlLVFGRYFGMSTREIEAVIPS-----LLEFAR-LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 505 DAKTEETILMNLKTMRADQTTII-------TANRLssvmhADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILltthfmeEAERL-----CDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-554 |
3.01e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.59 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRdySLDALLDSIGYVPQDNFLFS-TDVRDNI 431
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRhMTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFA-----DFDRSQAAVEDAAIASAVHDDILT-FAQGYETvvgergvSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PRK10851 96 AFGltvlpRRERPNAAAIKAKVTQLLEMVQLAhLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 506 AKTEETI---LMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK10851 169 AQVRKELrrwLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-554 |
3.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIrDYSLDALLD---SIGYVPQ 418
Cdd:PRK13639 8 KYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEvrkTVGIVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 --DNFLFSTDVRDNIRFA------DFDRSQAAVEDAAIASAVhddiltfaQGYETVVGERgvsLSGGQKQRIAIARAMMT 490
Cdd:PRK13639 86 npDDQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGM--------EGFENKPPHH---LSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 491 DPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANR---LSSVmHADEIIVMDDGQIIERGT 554
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHdvdLVPV-YADKVYVMSDGKIIKEGT 220
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
338-551 |
3.98e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 338 YAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVI--------QIDGHDIRDYSLDAL 409
Cdd:PRK10419 13 YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaKLNRAQRKAFRRDIQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 410 L---DSIGYV-PQdnflfsTDVRDNIR-----FADFDRSQAAVEDAAIASAVHDDiltfaqgyETVVGERGVSLSGGQKQ 480
Cdd:PRK10419 93 MvfqDSISAVnPR------KTVREIIReplrhLLSLDKAERLARASEMLRAVDLD--------DSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 481 RIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTT---IITANrLSSVMH-ADEIIVMDDGQIIE 551
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaclFITHD-LRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
86-283 |
4.47e-17 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 82.00 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 86 AKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMViFVDWRLTLMAL 165
Cdd:cd18590 65 SRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFML-SLSWQLTLLTL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFD 245
Cdd:cd18590 144 IEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYL 223
|
170 180 190
....*....|....*....|....*....|....*...
gi 2018945286 246 PAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISY 283
Cdd:cd18590 224 LVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILY 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
355-498 |
4.53e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 4.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGhDIRdysldalldsIGYVPQDNFLFSTD-VRDNIRF 433
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQEPPLDDDLtVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 ADFDRSQAAVEDAAIASAVHD------------DILTFAQGYE---------------TVVGERGVS-LSGGQKQRIAIA 485
Cdd:COG0488 85 GDAELRALEAELEELEAKLAEpdedlerlaelqEEFEALGGWEaearaeeilsglgfpEEDLDRPVSeLSGGWRRRVALA 164
|
170
....*....|...
gi 2018945286 486 RAMMTDPEILILD 498
Cdd:COG0488 165 RALLSEPDLLLLD 177
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
355-560 |
5.09e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.91 E-value: 5.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGH--DIRDYSlDALLDSIGYVPQD---NFLFST-D 426
Cdd:COG1129 270 DVSFSVRAGEILGIAGLVGAGRTELARALfgADPADS--GEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgEGLVLDlS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIRFADFDR-------SQAAvEDAAIASAVHD-DILTfaQGYETVVGergvSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:COG1129 347 IRENITLASLDRlsrggllDRRR-ERALAEEYIKRlRIKT--PSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 499 DSLSAVD--AKTEetI--LMNlkTMRADQTTIITAnrlSS----VMH-ADEIIVMDDGQII-----ERGTHEALLA 560
Cdd:COG1129 420 EPTRGIDvgAKAE--IyrLIR--ELAAEGKAVIVI---SSelpeLLGlSDRILVMREGRIVgeldrEEATEEAIMA 488
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
353-560 |
6.24e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 6.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYdQYQGVIQIDGHDIRDYSLDALL---DSIGYVPQDNFlFSTDVRD 429
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLpvrHRIQVVFQDPN-SSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIrfadfdrsQAAVEDAAiasAVHDDILTFAQGYETVVG---ERGV----------SLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK15134 380 NV--------LQIIEEGL---RVHQPTLSAAQREQQVIAvmeEVGLdpetrhrypaEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLS---SVMHadEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHvvrALCH--QVIVLRQGEVVEQGDCERVFA 515
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
321-554 |
8.23e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 8.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 321 IIEAPNaiqtPATGDINYAVQKFTYPGD-KQP----TLMNVAFTLPQGKTLGIVGKVGSGKTTLIK----LLLREYdqyq 391
Cdd:PRK13631 9 KLKVPN----PLSDDIILRVKNLYCVFDeKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKY---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 392 GVIQID----GHDIRDYSLDALLDS------------IGYVPQ--DNFLFSTDVRDNIRFADFDRSQAAvEDAAIASAVH 453
Cdd:PRK13631 81 GTIQVGdiyiGDKKNNHELITNPYSkkiknfkelrrrVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 454 DDILTFAQGYEtvvgERG-VSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRAD-QTTIITANR 531
Cdd:PRK13631 160 LNKMGLDDSYL----ERSpFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHT 235
|
250 260
....*....|....*....|....
gi 2018945286 532 LSSVMH-ADEIIVMDDGQIIERGT 554
Cdd:PRK13631 236 MEHVLEvADEVIVMDKGKILKTGT 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
355-549 |
1.04e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.05 E-value: 1.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD-QYQGVIQIDGH--DIRDySLDALLDSIGYVPQDN----FLFSTDV 427
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRN-PQQAIAQGIAMVPEDRkrdgIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNIRFADFDR-SQAAVEDAAiasAVHDDILTFAQ--GYETVVGERGV-SLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:PRK13549 359 GKNITLAALDRfTGGSRIDDA---AELKTILESIQrlKVKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 504 VD--AKTEETILMNlktMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQI 549
Cdd:PRK13549 436 IDvgAKYEIYKLIN---QLVQQgvAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
349-561 |
1.17e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDnfLFSTD-- 426
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQH--HLTPEgi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 -VRDNIRFAdfdRS-------QAAVED-AAIASAVHD-DILTFAQgyetvvgERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK11231 92 tVRELVAYG---RSpwlslwgRLSAEDnARVNQAMEQtRINHLAD-------RRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 497 LDDSLSAVDAkTEETILMNL-KTMRADQTTIITanrlssVMH--------ADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK11231 162 LDEPTTYLDI-NHQVELMRLmRELNTQGKTVVT------VLHdlnqasryCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
354-578 |
1.19e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.46 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 354 MNVAFTLP-QGKTlGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDALLDS----IGYVPQDNFLFS-T 425
Cdd:PRK11144 15 LTVNLTLPaQGIT-AIFGRSGAGKTSLINAIsgLTRPQK--GRIVLNGRVLFDAEKGICLPPekrrIGYVFQDARLFPhY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIRF--ADFDRSQaavedaaiasavHDDILTFAqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:PRK11144 92 KVRGNLRYgmAKSMVAQ------------FDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 504 VDA--KTEetiLMN-LKTMRAD-QTTII-TANRLSSVMH-ADEIIVMDDGQIIERGTHEALlaedgWYAEM---WL-KQQ 573
Cdd:PRK11144 159 LDLprKRE---LLPyLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFGPLEEV-----WASSAmrpWLpKEE 230
|
....*
gi 2018945286 574 LSQAL 578
Cdd:PRK11144 231 QSSIL 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
350-562 |
1.29e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.41 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIgyVPQDNFLFS-TDVR 428
Cdd:COG3840 12 GDFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSM--LFQENNLFPhLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNI--------RFADFDRSQaaVEDAAiasavhddiltfAQ-GYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:COG3840 90 QNIglglrpglKLTAEQRAQ--VEQAL------------ERvGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 500 SLSAVD-AKTEEtILMNLKTMRAD-QTTIIT-------ANRLssvmhADEIIVMDDGQIIERGTHEALLAED 562
Cdd:COG3840 156 PFSALDpALRQE-MLDLVDELCRErGLTVLMvthdpedAARI-----ADRVLLVADGRIAADGPTAALLDGE 221
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-558 |
1.48e-16 |
|
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: 78.95 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALLDSIGYVPQDnflfstdvrdnirfA 434
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQD--------------L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 DFDRSQAAVEDAAIASAVH-----------DDILTFAQGYEtvVGERGVS-LSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03265 83 SVDDELTGWENLYIHARLYgvpgaerreriDELLDFVGLLE--AADRLVKtYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 503 AVDAKTEETILMNLKTMRADQ--TTIITANRLSSV-MHADEIIVMDDGQIIERGTHEAL 558
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
353-562 |
2.40e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.77 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALL-DSIGYVPQDNFLFS-TDVRDN 430
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMrEAVAIVPEGRRVFSrMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IR----FADFDRSQAAVEdaaiasAVHDdilTFAQGYETVVgERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:PRK11614 101 LAmggfFAERDQFQERIK------WVYE---LFPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 507 KTEETILMNLKTMRADQTTI--ITANRLSSVMHADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK11614 171 IIIQQIFDTIEQLREQGMTIflVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
355-562 |
2.81e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLdSIGYVPQ-DNFLFSTDVRDNIR- 432
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ-RVGVVPQfDNLDPDFTVRENLLv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 FADFDRSQAAVEDAAIASavhddILTFA---QGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTE 509
Cdd:PRK13537 104 FGRYFGLSAAAARALVPP-----LLEFAkleNKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 510 ETILMNLKTMRADQTTII-------TANRLssvmhADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK13537 175 HLMWERLRSLLARGKTILltthfmeEAERL-----CDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
353-557 |
2.92e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.60 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALLDSIGYVPQDNFLFST-DVRDN 430
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 I-------RFADFDRSQAAVEDAAIASAVHDDILTfaqgyETVVGErgvsLSGGQKQRIAIARAMMTDPEILILD---DS 500
Cdd:COG1129 100 IflgreprRGGLIDWRAMRRRARELLARLGLDIDP-----DTPVGD----LSVAQQQLVEIARALSRDARVLILDeptAS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 501 LSAVDAKteetILMNL-KTMRADQTTII-TANRLSSVM-HADEIIVMDDGQIIerGTHEA 557
Cdd:COG1129 171 LTEREVE----RLFRIiRRLKAQGVAIIyISHRLDEVFeIADRVTVLRDGRLV--GTGPV 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
355-549 |
4.32e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 4.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD-QYQGVIQIDGH--DIRDySLDALLDSIGYVPQDN----FLFSTDV 427
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRN-PAQAIRAGIAMVPEDRkrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNI------RFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGergvsLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:TIGR02633 357 GKNItlsvlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-----LSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 502 SAVD--AKTEETILMNLKTMRAdQTTIITANRLSSVMH-ADEIIVMDDGQI 549
Cdd:TIGR02633 432 RGVDvgAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
254-537 |
4.78e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.39 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 254 LTYIVTIIYGGTLVMHHSISIGQLI----SFISYIAALVWPMFAIGRLFNVlergNASYDRVDQL---LKETSTIIEAPN 326
Cdd:COG4178 278 LAVIFPILVAAPRYFAGEITLGGLMqaasAFGQVQGALSWFVDNYQSLAEW----RATVDRLAGFeeaLEAADALPEAAS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 327 AIQTPATGDInyAVQKFT-YPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDirdys 405
Cdd:COG4178 354 RIETSEDGAL--ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 406 lDALldsigYVPQDNFLFSTDVRDNIRFADfdrSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQRIAIA 485
Cdd:COG4178 427 -RVL-----FLPQRPYLPLGTLREALLYPA---TAEAFSDAELREALEAVGLGHLAERLDEEADWDQVLSLGEQQRLAFA 497
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 486 RAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADqTTIItanrlsSVMH 537
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVI------SVGH 542
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
22-281 |
7.16e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 78.36 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIdTHQLTPQKLIMWLGI------LLSAAILQYLFRYGWRTRIWGGAAKLERTLRSR 95
Cdd:cd18574 2 VLSALAAALVNIQIPLLLGDLVNVI-SRSLKETNGDFIEDLkkpalkLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 96 LFWHFMKMDTTFFQKHRTGDLMAHATNDL----TAIQQVAGAGILTFADSIitGGttIIAMvIFVDWRLTLMALIPMPLL 171
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVTQTV--GC--VVSL-YLISPKLTLLLLVIVPVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 172 AVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLI 251
Cdd:cd18574 156 VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLA 235
|
250 260 270
....*....|....*....|....*....|
gi 2018945286 252 IGLTYIVTIIYGGTLVMHHSISIGQLISFI 281
Cdd:cd18574 236 LNGIVLGVLYYGGSLVSRGELTAGDLMSFL 265
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-562 |
9.80e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 9.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFL-FSTDVR 428
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNI---------RFADFDRSQAAVEDAAIASAvhdDILTFAqgyetvvgERGV-SLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK09536 96 QVVemgrtphrsRFDTWTETDRAAVERAMERT---GVAQFA--------DRPVtSLSGGERQRVLLARALAQATPVLLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRADQTTIITA-NRLS-SVMHADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK09536 165 EPTASLDINHQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
353-556 |
1.08e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALldsIGYVPQD---NFLFSTDVRD 429
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFADFDR----SQAAVEDAAIASAV--HDDILTFAQgyeTVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:PRK15056 100 VVMMGRYGHmgwlRRAKKRDRQIVTAAlaRVDMVEFRH---RQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 504 VDAKTEETILMNLKTMRAD-QTTIITANRLSSVMHADEIIVMDDGQIIERGTHE 556
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
347-554 |
1.30e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIK----LLLREydqyQGVIQIDGHDIRDYS-LDALLDSIGYVPQ--D 419
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnaLLIPS----EGKVYVDGLDTSDEEnLWDIRNKAGMVFQnpD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFADfdrSQAAVEDAAIASAVhDDILTFAQGYETVVGERGVsLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:PRK13633 96 NQIVATIVEEDVAFGP---ENLGIPPEEIRERV-DESLKKVGMYEYRRHAPHL-LSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 500 SLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
349-558 |
1.47e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.59 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL-LREYDQyQGVIQIDGHDIrDYSLD-------ALLDSIGYVPQDN 420
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-SGQLNIAGHQF-DFSQKpsekairLLRQKVGMVFQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFS-TDVRDNIRFADFdRSQAAVEDAAIASAvhDDILT------FAQGYEtvvgergVSLSGGQKQRIAIARAMMTDPE 493
Cdd:COG4161 92 NLWPhLTVMENLIEAPC-KVLGLSKEQAREKA--MKLLArlrltdKADRFP-------LHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 494 ILILDDSLSAVDAK-TEE--TILMNLKTMRADQtTIIT-----ANRLSSvmhadEIIVMDDGQIIERGTHEAL 558
Cdd:COG4161 162 VLLFDEPTAALDPEiTAQvvEIIRELSQTGITQ-VIVThevefARKVAS-----QVVYMEKGRIIEQGDASHF 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
355-560 |
2.47e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR--DYSLDAllDSIGYVPQDNFLfSTDVRDNI- 431
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRS--QRIRMIFQDPST-SLNPRQRIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADF------DRSQAAVEDAAIASAVHDDILTFAQGYETVVgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PRK15112 108 QILDFplrlntDLEPEQREKQIIETLRQVGLLPDHASYYPHM------LAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 506 AKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
340-556 |
2.86e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.57 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysLDALLDSIGYVPQD 419
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFS-TDVRDNIRFAdfdRSQAAVEDAAIASAVHDdILTFAQGYEtVVGERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK11607 100 YALFPhMTVEQNIAFG---LKQDKLPKAEIASRVNE-MLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 499 DSLSAVDAKTEETilMNLKTM----RADQTTI-ITANRLSSVMHADEIIVMDDGQIIERGTHE 556
Cdd:PRK11607 175 EPMGALDKKLRDR--MQLEVVdileRVGVTCVmVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-554 |
2.97e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGH------DIrdYSLDA--LLDSIGYV-PQ 418
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDI--FQIDAikLRKEVGMVfQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 DNFLFSTDVRDNIRFADfdRSQAAVEDAAIASAVHDDILTFAQGYETV--VGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPL--KSHGIKEKREIKKIVEECLRKVGLWKEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMH-ADEIIVMDDGQIIERGT 554
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
353-562 |
3.05e-15 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 75.51 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ-YQGVIQIDGHDIRDYSLDALLDSIGYV-P--QDNFLFSTDVR 428
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKRIGLVsPalQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNI---RFADFDRSQAaVEDAAIASAvhDDILTFAqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:COG1119 99 DVVlsgFFDSIGLYRE-PTDEQRERA--RELLELL-GLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 506 AKTEETIlmnLKTMRadqtTIITANRLSSVM---HADEI-------IVMDDGQIIERGTHEALLAED 562
Cdd:COG1119 175 LGARELL---LALLD----KLAAEGAPTLVLvthHVEEIppgithvLLLKDGRVVAAGPKEEVLTSE 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
340-554 |
3.59e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.84 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD-----QYQGVIQIDGHDI--RDYSLDALLDS 412
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 413 IGYV-PQDNfLFSTDVRDNIRFA----------DFDrsqAAVEDAAIASAVHDDIltfaqgyETVVGERGVSLSGGQKQR 481
Cdd:PRK14258 90 VSMVhPKPN-LFPMSVYDNVAYGvkivgwrpklEID---DIVESALKDADLWDEI-------KHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 482 IAIARAMMTDPEILILDDSLSAVDAKTE---ETILMNLKtMRADQTTIITANRLSSV---------MHADEIIVmddGQI 549
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASmkvESLIQSLR-LRSELTMVIVSHNLHQVsrlsdftafFKGNENRI---GQL 234
|
....*
gi 2018945286 550 IERGT 554
Cdd:PRK14258 235 VEFGL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
340-561 |
4.32e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.17 E-value: 4.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKL--LLREYDQYQ---GVIQIDGHD--------IRdysl 406
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCinLLEQPEAGTirvGDITIDTARslsqqkglIR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 407 dALLDSIGYVPQDNFLFS-TDVRDNI-----RFADFDRSQAAVEDAAIASAVHddiltfAQGYETVVGERgvsLSGGQKQ 480
Cdd:PRK11264 82 -QLRQHVGFVFQNFNLFPhRTVLENIiegpvIVKGEPKEEATARARELLAKVG------LAGKETSYPRR---LSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 481 RIAIARAMMTDPEILILDDSLSAVDAkteETILMNLKTMRA----DQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTH 555
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPA 228
|
....*.
gi 2018945286 556 EALLAE 561
Cdd:PRK11264 229 KALFAD 234
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-554 |
5.22e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 75.92 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysldALLDSIGYVPQDNFLF-STDVRDNIRF 433
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYLPEERGLYpKMKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 adFDR----SQAAVEDAA--------IASAVHDDIltfaqgyETvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:COG4152 95 --LARlkglSKAEAKRRAdewlerlgLGDRANKKV-------EE--------LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 502 SAVDAKTEETILMNLKTMRADQTTII-TANRLSSVM-HADEIIVMDDGQIIERGT 554
Cdd:COG4152 158 SGLDPVNVELLKDVIRELAAKGTTVIfSSHQMELVEeLCDRIVIINKGRKVLSGS 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
354-553 |
5.24e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 74.07 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 354 MNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRdySLDALLDSIGYVPQDNFLFS-TDVRDNIR 432
Cdd:cd03298 15 MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAhLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 FADFDRSQ-AAVEDAAIASAVhddiltfAQ-GYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEE 510
Cdd:cd03298 93 LGLSPGLKlTAEDRQAIEVAL-------ARvGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2018945286 511 TILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERG 553
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
355-558 |
7.31e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 76.30 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDAllDSIGYVPQDNFLFS-TDVRDNIRF 433
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ--RDICMVFQSYALFPhMSLGENVGY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 434 AdfdRSQAAVEDAAIASAVHDDI-LTFAQGYEtvvgERGV-SLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEET 511
Cdd:PRK11432 102 G---LKMLGVPKEERKQRVKEALeLVDLAGFE----DRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 512 ilMNLKTMRADQTTIITAnrlSSVMH--------ADEIIVMDDGQIIERGTHEAL 558
Cdd:PRK11432 175 --MREKIRELQQQFNITS---LYVTHdqseafavSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
333-554 |
7.75e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 7.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 333 TGDINYAVQKFTYpGDKQP----TLMNVAFTLPQGKTLGIVGKVGSGKTTLIKL----LLREYDQyqgviQIDGhdirDY 404
Cdd:PRK13645 4 SKDIILDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtnglIISETGQ-----TIVG----DY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 405 SLDALLDSIGYVpqdnflfsTDVRDNI----RFADFDRSQAAVEDAAIASAVH------------DDILTFAQGYETVVG 468
Cdd:PRK13645 74 AIPANLKKIKEV--------KRLRKEIglvfQFPEYQLFQETIEKDIAFGPVNlgenkqeaykkvPELLKLVQLPEDYVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 469 ERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEE---TILMNLKTMRADQTTIITANRLSSVMHADEIIVMD 545
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
....*....
gi 2018945286 546 DGQIIERGT 554
Cdd:PRK13645 226 EGKVISIGS 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
343-574 |
8.08e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.27 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPgDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIrDYSLDALLD---SIGYVPQ- 418
Cdd:PRK13636 13 YNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKlreSVGMVFQd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 -DNFLFSTDVRDNIRFADF------DRSQAAVEDAAIASavhddiltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTD 491
Cdd:PRK13636 91 pDNQLFSASVYQDVSFGAVnlklpeDEVRKRVDNALKRT-----------GIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 492 PEILILDDSLSAVDAKTEETILMNLKTMRA--DQTTIITANRLSSV-MHADEIIVMDDGQIIERGTHEALLAEdgwyAEM 568
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAE----KEM 235
|
....*.
gi 2018945286 569 WLKQQL 574
Cdd:PRK13636 236 LRKVNL 241
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
353-557 |
1.11e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 73.62 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDALL----DSIGYVPQdNF--LFS 424
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLagLDRPTS--GTVRLAGQDLFALDEDARArlraRHVGFVFQ-SFqlLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNI-------RFAD-FDRSQAAVEdaaiasAVhddiltfaqGyetvVGERG----VSLSGGQKQRIAIARAMMTDP 492
Cdd:COG4181 105 LTALENVmlplelaGRRDaRARARALLE------RV---------G----LGHRLdhypAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 493 EILILDDSLSAVDAKTEETILMNLKTMRADQ-TT--IIT-----ANRlssvmhADEIIVMDDGQIIERGTHEA 557
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERgTTlvLVThdpalAAR------CDRVLRLRAGRLVEDTAATA 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
343-560 |
1.12e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 76.65 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKT----TLIKLLLREYDQYQGVIQIDGHDIRDYSLDALL----DSIG 414
Cdd:COG4172 16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 415 YVPQD-----NFLFStdVRDNIR---FADFDRSQAAVEDAAIAsavhddilTFAQgyetvVG----ERGVS-----LSGG 477
Cdd:COG4172 96 MIFQEpmtslNPLHT--IGKQIAevlRLHRGLSGAAARARALE--------LLER-----VGipdpERRLDayphqLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 478 QKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTT---IITANrLSSVMH-ADEIIVMDDGQIIERG 553
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMallLITHD-LGVVRRfADRVAVMRQGEIVEQG 239
|
....*..
gi 2018945286 554 THEALLA 560
Cdd:COG4172 240 PTAELFA 246
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
16-280 |
1.21e-14 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 74.55 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYLFRYgWRTRIWGGAA-KLERTLR 93
Cdd:cd18782 1 RRALIEVLALsFVVQLLGLANPLLFQVIIDKVLVQQ-DLATLYVIGVVMLVAALLEAVLTA-LRTYLFTDTAnRIDLELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 94 SRLFWHFMKMDTTFFQKHRTGDLMAHaTNDLTAIQQVA-GAGILTFAD---SIITggttiIAMVIFVDWRLTLMALIPMP 169
Cdd:cd18782 79 GTIIDHLLRLPLGFFDKRPVGELSTR-ISELDTIRGFLtGTALTTLLDvlfSVIY-----IAVLFSYSPLLTLVVLATVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 170 LL----AVASRQLGAHLHTAFGQSQAAFSRLNdktqESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFD 245
Cdd:cd18782 153 LQllltFLFGPILRRQIRRRAEASAKTQSYLV----ESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSG 228
|
250 260 270
....*....|....*....|....*....|....*
gi 2018945286 246 PAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISF 280
Cdd:cd18782 229 SLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
16-311 |
1.50e-14 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 74.47 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIdthqLTPQKLIMWLGILLSAAIL---QYLFRYgWRTRIwggAAKLE-- 89
Cdd:cd18555 1 KKLLISILLLsLLLQLLTLLIPILTQYVIDNV----IVPGNLNLLNVLGIGILILfllYGLFSF-LRGYI---IIKLQtk 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 90 --RTLRSRLFWHFMKMDTTFFQKHRTGDLMAHAtNDLTAIQQV-AGAGILTFADSIITGgTTIIAMVIFvDWRLTLMALI 166
Cdd:cd18555 73 ldKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQIlSNQVISLIIDLLLLV-IYLIYMLYY-SPLLTLIVLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 167 PMPLLAVAS-------RQLGAHLHTAFGQSQAAFSrlndktqESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNM 239
Cdd:cd18555 150 LGLLIVLLLlltrkkiKKLNQEEIVAQTKVQSYLT-------ETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 240 IDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18555 223 LSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
343-562 |
1.54e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ--DN 420
Cdd:PRK13652 11 YSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFADFDrsqAAVEDAAIASAVHDDILTFaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:PRK13652 90 QIFSPTVEQDIAFGPIN---LGLDEETVAHRVSSALHML--GLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 501 LSAVDAKTEETIL--MNLKTMRADQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK13652 165 TAGLDPQGVKELIdfLNDLPETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
343-557 |
1.76e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYpGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL-LREYDQyQGVIQIDGH------DIRDYSLDALLDSIGY 415
Cdd:PRK11124 10 CFY-GAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-SGTLNIAGNhfdfskTPSDKAIRELRRNVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNFLFS-TDVRDNIRFADFdRSQAAVEDAAIASAvhDDILT------FAQGYEtvvgergVSLSGGQKQRIAIARAM 488
Cdd:PRK11124 87 VFQQYNLWPhLTVQQNLIEAPC-RVLGLSKDQALARA--EKLLErlrlkpYADRFP-------LHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 489 MTDPEILILDDSLSAVDAKTEETIlmnLKTMRADQTTIITAnrlSSVMH--------ADEIIVMDDGQIIERGTHEA 557
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQI---VSIIRELAETGITQ---VIVTHevevarktASRVVYMENGHIVEQGDASC 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
355-559 |
1.77e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.45 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALL-----DSIGYVPQDNFLFS-TDVR 428
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIS-DAELrevrrKKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADFDRSQAAVE--DAAIASAVHDDILTFAQGYETvvgergvSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:PRK10070 125 DNTAFGMELAGINAEErrEKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 507 KTEETILMNLKTMRA--DQTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALL 559
Cdd:PRK10070 198 LIRTEMQDELVKLQAkhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
16-280 |
1.95e-14 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 74.07 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVI----FLVLVAVV-----QIVPPKVIgtlvdlidTHQlTPQKLIMWLGILLSAAILQYLFRyGWRTRIWGG-A 85
Cdd:cd18588 1 KKLLGEVLlaslFLQLFALVtplffQVIIDKVL--------VHR-SLSTLDVLAIGLLVVALFEAVLS-GLRTYLFSHtT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 86 AKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHAtNDLTAIQQ-VAGAGILTFADSIITGgTTIIAMVIFvDWRLTLMA 164
Cdd:cd18588 71 NRIDAELGARLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQfLTGSALTLVLDLVFSV-VFLAVMFYY-SPTLTLIV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 165 LIPMPLLAVASRQLGAHLHTafgqsqaafsRLNDKTQ----------ESVSGIKVLKTFGQEEADVADFNEIVTKTIAIN 234
Cdd:cd18588 148 LASLPLYALLSLLVTPILRR----------RLEEKFQrgaenqsflvETVTGIETVKSLAVEPQFQRRWEELLARYVKAS 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2018945286 235 KRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISF 280
Cdd:cd18588 218 FKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAF 263
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
92-311 |
2.30e-14 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 73.99 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 92 LRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDltaIQQVAGAGILTFADSIITGGTTIIAMVI--FVDWRLTLMALIPMP 169
Cdd:cd18554 81 IRKDLFDHLQKLSLRYYANNRSGEIISRVIND---VEQTKDFITTGLMNIWLDMITIIIAICImlVLNPKLTFVSLVIFP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 170 LLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAIS 249
Cdd:cd18554 158 FYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVN 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 250 LIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18554 238 TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
349-560 |
2.85e-14 |
|
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: 72.58 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 349 KQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLD--ALLdSIGYVPQDNFLF-ST 425
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHkrARL-GIGYLPQEASIFrKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIR----FADFDRSQAAVEDAAIASAVHddiltfaqgYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:cd03218 91 TVEENILavleIRGLSKKEREEKLEELLEEFH---------ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 502 SAVDAKTEETIlmnlktmradQTTI-ITANRLSSVM----HADEII-------VMDDGQIIERGTHEALLA 560
Cdd:cd03218 162 AGVDPIAVQDI----------QKIIkILKDRGIGVLitdhNVRETLsitdrayIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
336-562 |
3.18e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 73.23 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 336 INYAVQ----KFTYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD 411
Cdd:PRK13647 1 MDNIIEvedlHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 412 SIGYVPQD--NFLFSTDVRDNIRFA------DFDRSQAAVEDAAIASAVHDdiLTFAQGYEtvvgergvsLSGGQKQRIA 483
Cdd:PRK13647 80 KVGLVFQDpdDQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWD--FRDKPPYH---------LSYGQKKRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 484 IARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLS--SVMHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVdlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
.
gi 2018945286 562 D 562
Cdd:PRK13647 229 D 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
353-561 |
4.16e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD-----QYQGVIQIDGHDIRDYSLD--ALLDSIGYVPQDNFLFST 425
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIRFA--------DFDR-SQAAVEDAAIASAVHDDIltfaqgyetvvGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK14243 106 SIYDNIAYGaringykgDMDElVERSLRQAALWDEVKDKL-----------KQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
353-568 |
5.52e-14 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 71.73 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLdsigyVPQDNFLFS-TDVRDNI 431
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFA------DFDRS--QAAVEDaaiasavHDDILTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:TIGR01184 76 ALAvdrvlpDLSKSerRAIVEE-------HIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 504 VDAKTEETI---LMNLKTMRADQTTIITANRLSSVMHADEIIVMDD------GQIIE----RGTHEALLAEDGWYAEM 568
Cdd:TIGR01184 145 LDALTRGNLqeeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNgpaaniGQILEvpfpRPRDRLEVVEDPSYYDL 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
353-554 |
7.90e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 74.31 E-value: 7.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL---LREYDQYQGVIQIDGHDIRDYSLDALldsIGYVPQDNFLFST-DVR 428
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrSPKGVKGSGSVLLNGMPIDAKEMRAI---SAYVQQDDLFIPTlTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRF-ADF--DRSQAAVEDAAIASAVHDDI-LTFAQgyETVVGERGV--SLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:TIGR00955 118 EHLMFqAHLrmPRRVTKKEKRERVDEVLQALgLRKCA--NTRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTII-TANRLSSVMHA--DEIIVMDDGQIIERGT 554
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIIcTIHQPSSELFElfDKIILMAEGRVAYLGS 250
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-560 |
9.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ-----YQGVIQIDGHDIRDYSlDAL--LDSIGYVPQDNFL 422
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYR-DVLefRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNI-----------RFADFDRSQAAVEDAAIASAVHDDIltfaqgyetvvGERGVSLSGGQKQRIAIARAMMTD 491
Cdd:PRK14271 113 FPMSIMDNVlagvrahklvpRKEFRGVAQARLTEVGLWDAVKDRL-----------SDSPFRLSGGQQQLLCLARTLAVN 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 492 PEILILDDSLSAVDAKTEETILMNLKTMrADQTT--IITANRLSSVMHADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK14271 182 PEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTviIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
356-558 |
1.20e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 356 VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS---IGYVPQDNfLFSTDVRDNI- 431
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDP-LASLNPRMTIg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 -------RFADFDRSQAAVEDAAIASAVHDDILtfaqgyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK15079 119 eiiaeplRTYHPKLSRQEVKDRVKAMMLKVGLL------PNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 505 DAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEAL 558
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
60-280 |
2.10e-13 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 71.07 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 60 LGILLSAAI-LQYLFRYGwRTRI--WGGAaKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHaTNDLTAI-QQVAGAGI 135
Cdd:cd18566 44 LVIGVVIAIlLESLLRLL-RSYIlaWIGA-RFDHRLSNAAFEHLLSLPLSFFEREPSGAHLER-LNSLEQIrEFLTGQAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 136 LTFAD---SIItggttIIAMVIFVDWRLTLMALIPMPLLAVASRQLGAHLHTAFGQSqaafSRLNDKTQ----ESVSGIK 208
Cdd:cd18566 121 LALLDlpfVLI-----FLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKER----SRADERRQnfliETLTGIH 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 209 VLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISF 280
Cdd:cd18566 192 TIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
353-558 |
3.02e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.89 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIK----LLLREydqyQGVIQIDghdIRDYSLDALLDSIGYVPQDNFLFSTDVR 428
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnaLLLPD----TGTIEWI---FKDEKNKKKTKEKEKVLEKLVIQKTRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 -----DNIR--------FADFDRSQAAVEDAAIASAV-----HDDILTFAQGYETVVG------ERG-VSLSGGQKQRIA 483
Cdd:PRK13651 96 kikkiKEIRrrvgvvfqFAEYQLFEQTIEKDIIFGPVsmgvsKEEAKKRAAKYIELVGldesylQRSpFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 484 IARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANR-LSSVMH-ADEIIVMDDGQIIERG-THEAL 558
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHdLDNVLEwTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
351-548 |
3.85e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 69.00 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREY----------DQYQGV--IQIDGHDIrdysLDALLDSIGYVPQ 418
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYlpdsgsilvrHDGGWVdlAQASPREI----LALRRRTIGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 dnFL-----FST-DVrdnirFADFDRSQAAVEDAAIASAvhDDILTFAQgyetvVGERGVSL-----SGGQKQRIAIARA 487
Cdd:COG4778 101 --FLrviprVSAlDV-----VAEPLLERGVDREEARARA--RELLARLN-----LPERLWDLppatfSGGEQQRVNIARG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 488 MMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIItanrlsSVMH--------ADEIIVMDDGQ 548
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII------GIFHdeevreavADRVVDVTPFS 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-559 |
4.11e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.35 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDIRDYSLDALL--DSIGYVPQDNFLF-ST 425
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEITS--GDLIVDGLKVNDPKVDERLirQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 426 DVRDNIRFADFDRSQAAVEDA-AIASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK09493 93 TALENVMFGPLRVRGASKEEAeKQARELLAKV-----GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 505 DAKTEETILMNLKTMRADQTTIITanrlssVMH--------ADEIIVMDDGQIIERGTHEALL 559
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVI------VTHeigfaekvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
343-562 |
4.84e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 69.43 E-value: 4.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGdkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDnfL 422
Cdd:PRK10575 19 FRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ--L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTD---VRDNI------------RFADFDRSQaaVEDaAIASAvhdDILTFAQgyetvvgeRGV-SLSGGQKQRIAIAR 486
Cdd:PRK10575 95 PAAEgmtVRELVaigrypwhgalgRFGAADREK--VEE-AISLV---GLKPLAH--------RLVdSLSGGERQRAWIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 487 AMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTIITanrlssVMH--------ADEIIVMDDGQIIERGTHEA 557
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIA------VLHdinmaaryCDYLVALRGGEMIAQGTPAE 234
|
....*
gi 2018945286 558 LLAED 562
Cdd:PRK10575 235 LMRGE 239
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
355-551 |
5.07e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIdGHDIRdysldalldsIGYVPQDNFLFSTD--VRDNIR 432
Cdd:COG0488 333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFDQHQEELDPDktVLDELR 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 fadfdrsqAAVEDAAIASAVH---------DDILTFaqgyetvVGergvSLSGGQKQRIAIARAMMTDPEILILD----- 498
Cdd:COG0488 402 --------DGAPGGTEQEVRGylgrflfsgDDAFKP-------VG----VLSGGEKARLALAKLLLSPPNVLLLDeptnh 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 499 ---DSLSAVdaktEE-------TILmnlktmradqttIITANR--LSSVmhADEIIVMDDGQIIE 551
Cdd:COG0488 463 ldiETLEAL----EEalddfpgTVL------------LVSHDRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
355-558 |
6.20e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI---RDYSLDALLDSIGYVPQDNFLfSTDVRDNI 431
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPYA-SLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADFD--RSQAAVEDAAIASAVhddiltfAQGYETVvgerGV----------SLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:PRK10261 421 GDSIMEplRVHGLLPGKAAAARV-------AWLLERV----GLlpehawryphEFSGGQRQRICIARALALNPKVIIADE 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 500 SLSAVDAKTEETILMNLKTMRADQTtiITANRLSSVMHADEII-----VMDDGQIIERGTHEAL 558
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFG--IAYLFISHDMAVVERIshrvaVMYLGQIVEIGPRRAV 551
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
340-550 |
6.56e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 67.67 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPG-DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL---LREYDQYQGVIQIDGHDIRDYSLDALLDSIgY 415
Cdd:cd03233 9 ISFTTGKGrSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNFLFST-DVRDNIRFAdfdrsqaavedaaiasavhddilTFAQGYETVvgeRGVSlsGGQKQRIAIARAMMTDPEI 494
Cdd:cd03233 88 VSEEDVHFPTlTVRETLDFA-----------------------LRCKGNEFV---RGIS--GGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMrADQ---TTIITANRLSSVMHA--DEIIVMDDGQII 550
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTM-ADVlktTTFVSLYQASDEIYDlfDKVLVLYEGRQI 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
355-561 |
8.62e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLlreYDQYQ---GVIQIDGH--DIRDySLDALLDSIGYVPQ-----DNFlfs 424
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKIL---YGLYQpdsGEILIDGKpvRIRS-PRDAIALGIGMVHQhfmlvPNL--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TdVRDNI-------RFADFDRSQAAvedaaiasavhDDILTFAQGY------ETVVGErgvsLSGGQKQRIAIARAMMTD 491
Cdd:COG3845 96 T-VAENIvlgleptKGGRLDRKAAR-----------ARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 492 PEILILDDSlSAV--DAKTEEtiLMN-LKTMRADQTTI--ITaNRLSSVM-HADEIIVMDDGQIIE----RGTHEALLAE 561
Cdd:COG3845 160 ARILILDEP-TAVltPQEADE--LFEiLRRLAAEGKSIifIT-HKLREVMaIADRVTVLRRGKVVGtvdtAETSEEELAE 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
355-537 |
1.33e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.02 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDirdysldALLdsigYVPQDNFLFSTDVRDNIRFA 434
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-------DLL----FLPQRPYLPLGTLREQLIYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 dfdrsqaavedaaiasavHDDILtfaqgyetvvgergvslSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILM 514
Cdd:cd03223 88 ------------------WDDVL-----------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170 180
....*....|....*....|...
gi 2018945286 515 NLKTMRadqTTIItanrlsSVMH 537
Cdd:cd03223 133 LLKELG---ITVI------SVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
350-554 |
1.51e-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: 70.81 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIrDYSLDALLDSIGYVPQDNFLFS-TDVR 428
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFADFDRSQAAVEDAAIASAVHDDiltfaQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLED-----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2018945286 509 EETILMNLKTMRADQTTIITANRLSSV-MHADEIIVMDDGQIIERGT 554
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
348-562 |
1.81e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLL--REYDQYQGVIQIDGHDIRDYSLD--ALLdSIGY-------V 416
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDerARA-GIFLafqypveI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 417 PqdnflfstdvrdNIRFADFDRsqaavedaAIASAVHDDILTFAQGYETV------VG------ERGV--SLSGGQKQRI 482
Cdd:COG0396 90 P------------GVSVSNFLR--------TALNARRGEELSAREFLKLLkekmkeLGldedflDRYVneGFSGGEKKRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 483 AIARAMMTDPEILILD--------DSLSAVdAKTeetilmnLKTMRADQTT--IITAN-RLSSVMHADEIIVMDDGQIIE 551
Cdd:COG0396 150 EILQMLLLEPKLAILDetdsgldiDALRIV-AEG-------VNKLRSPDRGilIITHYqRILDYIKPDFVHVLVDGRIVK 221
|
250
....*....|.
gi 2018945286 552 RGTHEalLAED 562
Cdd:COG0396 222 SGGKE--LALE 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
355-562 |
1.91e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 67.23 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDA-LLDSIGYVPQ-----------DNFL 422
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQeasifrrlsvyDNLM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FSTDVRDNI-RFADFDRSQAAVEDAAIaSAVHDDIltfaqgyetvvgerGVSLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:PRK10895 101 AVLQIRDDLsAEQREDRANELMEEFHI-EHLRDSM--------------GQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 502 SAVDAKTEETILMNLKTMR-ADQTTIITANRLSSVMHADE-IIVMDDGQIIERGTHEALLAED 562
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQDE 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-498 |
2.62e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.39 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIdGHDIRdysldalldsIGYVPQd 419
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYFEQ- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 420 nflfstdvrdnirfadfdrsqaavedaaiasavhddiltfaqgyetvvgergvsLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:cd03221 71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
355-562 |
3.13e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALLDSIGYVPQ---DNFLFST-DVRD 429
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NI---RFADFDRSQAAV------EDAAIASAVHDDILTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDS 500
Cdd:PRK09700 361 NMaisRSLKDGGYKGAMglfhevDEQRTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 501 LSAVDAKTEETIlmnLKTMR--ADQ--TTIITANRLSSVMHA-DEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK09700 437 TRGIDVGAKAEI---YKVMRqlADDgkVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
17-311 |
3.33e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 67.59 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 17 RYLWGVIFL--VLVAVVQIVPPKVIGTLVDLIDTHQlTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRS 94
Cdd:cd18568 1 RKLLAEILLasLLLQLLGLALPLFTQIILDRVLVHK-NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 95 RLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIitggTTIIAMVIFV--DWRLTLMALIPMPLLA 172
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRFQENQKIRRFLTRSALTTILDLL----MVFIYLGLMFyyNLQLTLIVLAFIPLYV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 173 ----VASRQLGAHLHTAFGQSQAAFSRLndktQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAI 248
Cdd:cd18568 156 lltlLSSPKLKRNSREIFQANAEQQSFL----VEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLIS 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 249 SLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18568 232 SLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-510 |
3.85e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.67 E-value: 3.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDAlldSIGYVPQDNFLFST-DVRDNI 431
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE---ACHYLGHRNAMKPAlTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RF-ADFDRSQAAVEDAAIASAVHDDILTFAQGYetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEE 510
Cdd:PRK13539 95 EFwAAFLGGEELDIAAALEAVGLAPLAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-554 |
6.15e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 66.31 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSI----GYVPQ--DNFLFS 424
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIrkkvGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNIRFA--DFDRSQAAVEDAAIASavhddiLTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:PRK13649 101 ETVLKDVAFGpqNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTTIITANRLSSVM--HADEIIVMDDGQIIERGT 554
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVanYADFVYVLEKGKLVLSGK 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
353-549 |
6.60e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.61 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLD----SIGYVPQDNFLFStdvr 428
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQFHHLLP---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 dnirfaDFDrsqaAVEDAA----IASAVHDDILTFAQGYETVVG------ERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK11629 101 ------DFT----ALENVAmpllIGKKKPAEINSRALEMLAAVGlehranHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRADQTT---IIT-----ANRLSSVMHadeiivMDDGQI 549
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNRLQGTaflVVThdlqlAKRMSRQLE------MRDGRL 223
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
355-505 |
7.26e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.44 E-value: 7.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTT-------LIKlllreydQYQGVIQIDGHDIRDYSLD--ALLdSIGYVPQDNFLF-- 423
Cdd:COG1137 21 DVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVK-------PDSGRIFLDGEDITHLPMHkrARL-GIGYLPQEASIFrk 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 -StdVRDNIR----FADFDRSQAavEDAAiasavhDDILT-FaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILIL 497
Cdd:COG1137 93 lT--VEDNILavleLRKLSKKER--EERL------EELLEeF--GITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
....*...
gi 2018945286 498 DDSLSAVD 505
Cdd:COG1137 161 DEPFAGVD 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
350-521 |
7.64e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysldallDSIGYVPQDNFLFSTD--- 426
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-------DLCTYQKQLCFVGHRSgin 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 ----VRDNIRFaDFDRSQAAVEDAAIASAVH-DDILTFAQGYetvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSL 501
Cdd:PRK13540 87 pyltLRENCLY-DIHFSPGAVGITELCRLFSlEHLIDYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180
....*....|....*....|
gi 2018945286 502 SAVDAKTEETILMNLKTMRA 521
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRA 175
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
78-306 |
1.09e-11 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 66.15 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 78 RTRIWGGAA-KLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIFv 156
Cdd:cd18558 79 QGSFWGLAAgRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 157 DWRLTLMALIPMPLLAVASrQLGAHLHTAFG-QSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINK 235
Cdd:cd18558 158 GWKLTLVILAISPVLGLSA-VVWAKILSGFTdKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGI 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 236 RVNMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFisYIAALVWPMFAIGRLFNVLERGNA 306
Cdd:cd18558 237 KKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTV--FFSVLIGAFSAGQQVPSIEAFANA 305
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
261-548 |
1.15e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.47 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 261 IYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRVDQLLKETSTIIEAPNAIQTPATGDINYAV 340
Cdd:TIGR00954 370 YNNGRLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQD 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 341 Q--KF------TYPGDKqptLMN-VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDirdysldalld 411
Cdd:TIGR00954 450 NgiKFeniplvTPNGDV---LIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG----------- 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 412 SIGYVPQDNFLFSTDVRDNIRFAD--FDRSQAAVEDA---AIASAVH-DDILTFAQGYETVVGERGVsLSGGQKQRIAIA 485
Cdd:TIGR00954 516 KLFYVPQRPYMTLGTLRDQIIYPDssEDMKRRGLSDKdleQILDNVQlTHILEREGGWSAVQDWMDV-LSGGEKQRIAMA 594
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 486 RAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRadqTTIITANRLSSVMHADEIIVMDDGQ 548
Cdd:TIGR00954 595 RLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFG---ITLFSVSHRKSLWKYHEYLLYMDGR 654
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
354-549 |
1.75e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 354 MNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREydQYQGVIQIDGHDIRDYS-LDALLDSIGYVPQDnflfstdvrdn 430
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLygLRP--ARGGRIMLNGKEINALStAQRLARGLVYLPED----------- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 irfadfdRSQAAVE-DAAIA----SAVHDDILTFAQ-GYETVVGER-----GV----------SLSGGQKQRIAIARAMM 489
Cdd:PRK15439 347 -------RQSSGLYlDAPLAwnvcALTHNRRGFWIKpARENAVLERyrralNIkfnhaeqaarTLSGGNQQKVLIAKCLE 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 490 TDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITanrLSSVMH-----ADEIIVMDDGQI 549
Cdd:PRK15439 420 ASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLF---ISSDLEeieqmADRVLVMHQGEI 481
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
353-553 |
2.36e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.16 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQY-----QGVIQIDGHDIRDYSLDALLDSIGYVPQ-DNFLFSTD 426
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNI-------RFAD-----FDRSQAAVEDAAIASAVHDDIltfaqgyetvvGERGVSLSGGQKQRIAIARAMMTDPEI 494
Cdd:PRK14247 99 IFENValglklnRLVKskkelQERVRWALEKAQLWDEVKDRL-----------DAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 495 LILDDSLSAVD----AKTEETILmnlkTMRADQTTIIT------ANRLSsvmhaDEIIVMDDGQIIERG 553
Cdd:PRK14247 168 LLADEPTANLDpentAKIESLFL----ELKKDMTIVLVthfpqqAARIS-----DYVAFLYKGQIVEWG 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
325-549 |
2.38e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 325 PNAIQTPatGDINYAVQKFTypGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDY 404
Cdd:PRK10982 240 PDKENKP--GEVILEVRNLT--SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNH 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 405 S-LDALLDSIGYVPQDNFlfST------DVRDNIRFADFDR---SQAAVEDAAIASA---VHDDILTFAQGYETVVGerg 471
Cdd:PRK10982 316 NaNEAINHGFALVTEERR--STgiyaylDIGFNSLISNIRNyknKVGLLDNSRMKSDtqwVIDSMRVKTPGHRTQIG--- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 472 vSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD--AKTEETILMnLKTMRADQTTIITANRLSSVMH-ADEIIVMDDGQ 548
Cdd:PRK10982 391 -SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFEIYQLI-AELAKKDKGIIIISSEMPELLGiTDRILVMSNGL 468
|
.
gi 2018945286 549 I 549
Cdd:PRK10982 469 V 469
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
356-512 |
2.40e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.28 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 356 VAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDG---HDIRDYSLDALLdSIGYVPQDNFLFStdVRDNIR 432
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgplDFQRDSIARGLL-YLGHAPGIKTTLS--VLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 FADFDRSQAAVEDAaiasavhddiltFAQGYETVVGERGV-SLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEET 511
Cdd:cd03231 96 FWHADHSDEQVEEA------------LARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
.
gi 2018945286 512 I 512
Cdd:cd03231 164 F 164
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-560 |
2.79e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLlREYDQYQgviQIDGHDIrdYSLdALLDSIGYVPQD 419
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVL-RGMDQYE---PTSGRII--YHV-ALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFL----------FSTDVRDNIRFAD-------------FDRSQAAVEDaaiaSAVHDDILTFAQ--GYEtvvGERGV-- 472
Cdd:TIGR03269 76 SKVgepcpvcggtLEPEEVDFWNLSDklrrrirkriaimLQRTFALYGD----DTVLDNVLEALEeiGYE---GKEAVgr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 473 -------------------SLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETIL-MNLKTMRADQTTIITANRL 532
Cdd:TIGR03269 149 avdliemvqlshrithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|
gi 2018945286 533 SSVMH--ADEIIVMDDGQIIERGTHEALLA 560
Cdd:TIGR03269 229 PEVIEdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
353-549 |
3.07e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.93 E-value: 3.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLlreydqyQGVIQIDGHDIRDYS--LDALLDSIGYVPQDNFLFS-TDVRD 429
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLL-------AGLETPSAGELLAGTapLAEAREDTRLMFQDARLLPwKKVID 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NI----RFADFDRSQAAVEdaaiasavhddiltfAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PRK11247 101 NVglglKGQWRDAALQALA---------------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2018945286 506 AKTE---ETILMNLKTMRADQTTIITANRLSSVMHADEIIVMDDGQI 549
Cdd:PRK11247 166 ALTRiemQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
344-558 |
3.64e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKqpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS--------IGY 415
Cdd:PRK11288 13 TFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAgvaiiyqeLHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQdnflfsTDVRDNI-------RFADFDRSQAAVEDAAIASAVHDDIltfaqGYETVVGErgvsLSGGQKQRIAIARAM 488
Cdd:PRK11288 91 VPE------MTVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDI-----DPDTPLKY----LSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 489 MTDPEILILDD---SLSAvdakTEETILMNL-KTMRADQTTII-TANRLSSVMH-ADEIIVMDDGQIIErgTHEAL 558
Cdd:PRK11288 156 ARNARVIAFDEptsSLSA----REIEQLFRViRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
353-560 |
3.70e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRdysldALLDSIGY--VPQDNFLFSTDVRDN 430
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTIN-----LVRDKDGQlkVADKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFADFDR-SQAAVEDAAIASAVHDDILTFAQGYETVV-------------GERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK10619 96 MVFQHFNLwSHMTVLENVMEAPIQVLGLSKQEARERAVkylakvgideraqGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRAD-QTTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
347-556 |
4.45e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.54 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLL--REYDQYQGVIQIDGHDIRDYSLD--ALLdSIGYVPQDNFL 422
Cdd:cd03217 11 GGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEerARL-GIFLAFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 423 FStdvrdNIRFADFDRSqaavedaaiasavhddiltfaqgyetvVGErgvSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:cd03217 89 IP-----GVKNADFLRY---------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 503 AVDAKTEETILMNLKTMRADQTT--IIT-ANRLSSVMHADEIIVMDDGQIIERGTHE 556
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGKSvlIIThYQRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
353-561 |
5.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.60 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDghDI------RDYSLDALLDSIGYVPQ--DNFLFS 424
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEIKPVRKKVGVVFQfpESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNIRFADFDRSQAAVEDAAIASAVHDDILTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFE----LSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 505 DAKTEETILMNLKTM-RADQTTIITANRLSSVM-HADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK13643 176 DPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
363-558 |
6.39e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 6.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 363 GKTLGIVGKVGSGKTTLIKLLLR--EYDQYQGVIQIDGHDIRDysldALLDSIGYVPQDNFLFS-TDVRDNIRFADFDR- 438
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTK----QILKRTGFVTQDDILYPhLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 439 --SQAAVEDAAIASAVHDDiLTFAQGYETVVGE---RGVSlsGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETIL 513
Cdd:PLN03211 170 pkSLTKQEKILVAESVISE-LGLTKCENTIIGNsfiRGIS--GGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2018945286 514 MNLKTMRADQTTIITA-NRLSSVMHA--DEIIVMDDGQIIERGT-HEAL 558
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSmHQPSSRVYQmfDSVLVLSEGRCLFFGKgSDAM 295
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
344-550 |
7.04e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.13 E-value: 7.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPT--LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALL----DSIGYVP 417
Cdd:PRK10535 13 SYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrrEHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 418 QDNFLFS-----TDVRDNIRFADFDRSQAavEDAAIAsavhddiLTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDP 492
Cdd:PRK10535 93 QRYHLLShltaaQNVEVPAVYAGLERKQR--LLRAQE-------LLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 493 EILILDDSLSAVDAKTEETILMNLKTMRAD-QTTIITANRLSSVMHADEIIVMDDGQII 550
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-513 |
9.96e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 345 YPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI---RDYSLDALLDSIGYVPQDN- 420
Cdd:PRK10908 11 YLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFSTDVRDNIRFAdfdrsqaavedAAIASAVHDDILTFAQGYETVVG------ERGVSLSGGQKQRIAIARAMMTDPEI 494
Cdd:PRK10908 90 LLMDRTVYDNVAIP-----------LIIAGASGDDIRRRVSAALDKVGlldkakNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170
....*....|....*....
gi 2018945286 495 LILDDSLSAVDAKTEETIL 513
Cdd:PRK10908 159 LLADEPTGNLDDALSEGIL 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
343-556 |
1.14e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 343 FTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-----LDALLDS----- 412
Cdd:PRK10261 22 FMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvieLSEQSAAqmrhv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 413 ----IGYVPQDN-------FLFSTDVRDNIRFadfdrSQAAVEDAAIASAVHDDILTFAQGYETVVGERGVSLSGGQKQR 481
Cdd:PRK10261 102 rgadMAMIFQEPmtslnpvFTVGEQIAESIRL-----HQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2018945286 482 IAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQT--TIITANRLSSVMH-ADEIIVMDDGQIIERGTHE 556
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVE 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
351-553 |
1.19e-10 |
|
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: 61.96 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLlreydqyQGVIQIDGHDIRDYSLDALLDSIGYVPQDNFLFSTD---- 426
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKIL-------SGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKtqlw 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 ----VRDNIRF------ADFDRSQAAVEDAAiasavhdDILTFAQGYETVVgeRGVSLsgGQKQRIAIARAMMTDPEILI 496
Cdd:cd03267 108 wdlpVIDSFYLlaaiydLPPARFKKRLDELS-------ELLDLEELLDTPV--RQLSL--GQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRAD-QTTIITAnrlSSVMH-----ADEIIVMDDGQIIERG 553
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLT---SHYMKdiealARRVLVIDKGRLLYDG 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
339-507 |
1.34e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 339 AVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI---RDYSLDALLdSIGY 415
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENIL-YLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNFLFStdVRDNIRF--ADFDRSQAAVEDA--AIASAVHDDILtFAQgyetvvgergvsLSGGQKQRIAIARAMMTD 491
Cdd:TIGR01189 81 LPGLKPELS--ALENLHFwaAIHGGAQRTIEDAlaAVGLTGFEDLP-AAQ------------LSAGQQRRLALARLWLSR 145
|
170
....*....|....*.
gi 2018945286 492 PEILILDDSLSAVDAK 507
Cdd:TIGR01189 146 RPLWILDEPTTALDKA 161
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
331-550 |
1.98e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.12 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 331 PATGDINYAVQKFTYPGDK-QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDAL 409
Cdd:COG3845 251 AEPGEVVLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 410 LDS-IGYVPQD--------NFlfstDVRDNIRFADFDRSQ---------AAVEDAAiASAVHD-DILTfaQGYETVVGer 470
Cdd:COG3845 331 RRLgVAYIPEDrlgrglvpDM----SVAENLILGRYRRPPfsrggfldrKAIRAFA-EELIEEfDVRT--PGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 471 gvSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTI--ITANrLSSVM-HADEIIVMDDG 547
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVllISED-LDEILaLSDRIAVMYEG 478
|
...
gi 2018945286 548 QII 550
Cdd:COG3845 479 RIV 481
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
369-553 |
2.82e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 62.35 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 369 VGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFS-TDVRDNIRF----ADFDRSQAA- 442
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVFQSYALYPhLSVAENMSFglklAGAKKEEINq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 443 -VEDAAiasavhdDILTFAQGYEtvvgERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKteetilmnLKT-MR 520
Cdd:PRK11000 113 rVNQVA-------EVLQLAHLLD----RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA--------LRVqMR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2018945286 521 AD--------QTTII--TANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:PRK11000 174 IEisrlhkrlGRTMIyvTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
332-553 |
3.45e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.18 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 332 ATGDINYAVQKftypgdkQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIrDYS---LDA 408
Cdd:PRK13638 3 ATSDLWFRYQD-------EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSkrgLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 409 LLDSIGYVPQD--NFLFSTDVRDNIRFAdfdRSQAAVEDAAIASAVhDDILTF--AQGYETvvgERGVSLSGGQKQRIAI 484
Cdd:PRK13638 75 LRQQVATVFQDpeQQIFYTDIDSDIAFS---LRNLGVPEAEITRRV-DEALTLvdAQHFRH---QPIQCLSHGQKKRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 485 ARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVMH--ADEIIVMDDGQIIERG 553
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeiSDAVYVLRQGQILTHG 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
353-505 |
3.84e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.51 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQidghdiRDYSLdalldSIGYVPQDNFLFSTDVRDNIR 432
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKL-----RIGYVPQKLYLDTTLPLTVNR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 433 FAdfdRSQAAVEDAAIASAvhddiLTFAQGyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVD 505
Cdd:PRK09544 89 FL---RLRPGTKKEDILPA-----LKRVQA-GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
22-226 |
4.22e-10 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 60.89 E-value: 4.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFM 101
Cdd:cd18584 2 VLLGLLAALLIIAQAWLLARIIAGVFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 102 KMDTTFFQKHRTGDLMAHATNDLTAIQ--------QVAGAGILTFAdsiitggttIIAMVIFVDWRLTLMALIPMPLL-- 171
Cdd:cd18584 82 ALGPALLRRQSSGELATLLTEGVDALDgyfarylpQLVLAAIVPLL---------ILVAVFPLDWVSALILLVTAPLIpl 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 172 ----------AVASRQLgahlhtafgqsqAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEI 226
Cdd:cd18584 153 fmiligkaaqAASRRQW------------AALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARA 205
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
355-562 |
5.06e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 5.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQdNFLFSTDVRDNIRFA 434
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-NATTPGDITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 D--------FDRSQAAVEDaAIASAVHddiltfAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:PRK10253 104 RgryphqplFTRWRKEDEE-AVTKAMQ------ATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 507 KTEETILMNLKTMRADQttiitANRLSSVMH--------ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK10253 177 SHQIDLLELLSELNREK-----GYTLAAVLHdlnqacryASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
355-553 |
5.51e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSI---------GYVPQD------ 419
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewGFVHQHprdglr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 -------NF---LFSTDVRD--NIRfadfDRSQAAVEDAAIASAVHDDILTfaqgyetvvgergvSLSGGQKQRIAIARA 487
Cdd:PRK11701 104 mqvsaggNIgerLMAVGARHygDIR----ATAGDWLERVEIDAARIDDLPT--------------TFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 488 MMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSV-MHADEIIVMDDGQIIERG 553
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVArLLAHRLLVMKQGRVVESG 234
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
325-553 |
6.21e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.43 E-value: 6.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 325 PNAIQTPATGDINYAvQKFTYpGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQ----GVIQIDGHD 400
Cdd:TIGR00956 51 PNALLKILTRGFRKL-KKFRD-TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 401 IRDYSLDALLDSIGYVPQDNFLFSTDVRDNIRFA-----------DFDRSQAAVEDAAIASAvhddILTFAQGYETVVGE 469
Cdd:TIGR00956 129 PEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAarcktpqnrpdGVSREEYAKHIADVYMA----TYGLSHTRNTKVGN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 470 ---RGVSlsGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMR--ADQTTIITANRLSSVMHA--DEII 542
Cdd:TIGR00956 205 dfvRGVS--GGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAniLDTTPLVAIYQCSQDAYElfDKVI 282
|
250
....*....|.
gi 2018945286 543 VMDDGQIIERG 553
Cdd:TIGR00956 283 VLYEGYQIYFG 293
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
474-560 |
1.03e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 474 LSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTT---IITANrLSSVMH-ADEIIVMDDGQI 549
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMgllFITHN-LSIVRKlADRVAVMQNGRC 235
|
90
....*....|.
gi 2018945286 550 IERGTHEALLA 560
Cdd:PRK15134 236 VEQNRAATLFS 246
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
20-311 |
1.25e-09 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 59.42 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 20 WGVIFLVLVAVVQIVPPKVIGTLVDLI-DTHQLTPQKLIMWLGILLSAAILQYLF--RYGWRTRIWGgaAKLERTLRSRL 96
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLsSYPDEPLSEGYLLALALFLVSLLQSLLlhQYFFLSFRLG--MRVRSALSSLI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 97 FWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAgagilTFADSIITGGTTIIAMVIFVDWRLTLMALIP-------MP 169
Cdd:cd18579 79 YRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFF-----LFLHYLWSAPLQIIVALYLLYRLLGWAALAGlgvllllIP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 170 LLAVASRQLGAHlhtafgqsQAAFSRLNDK----TQESVSGIKVLKTFGQEEAdvadFNEIVTKT----IAINKRVNMID 241
Cdd:cd18579 154 LQAFLAKLISKL--------RKKLMKATDErvklTNEILSGIKVIKLYAWEKP----FLKRIEELrkkeLKALRKFGYLR 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 242 GLFdpaISLIIGLTYIVTIIYGGTLV-MHHSISIGQLISFISYIAALVWPMFAIGRLFNVLERGNASYDRV 311
Cdd:cd18579 222 ALN---SFLFFSTPVLVSLATFATYVlLGNPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-560 |
1.34e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 342 KFTYPGDKQPtlMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYvpQDNF 421
Cdd:PRK10771 6 DITWLYHHLP--MRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF--QENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFS-TDVRDNI--------RFADFDRSQAAvedaAIASAVhddiltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDP 492
Cdd:PRK10771 82 LFShLTVAQNIglglnpglKLNAAQREKLH----AIARQM---------GIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2018945286 493 EILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
355-558 |
1.46e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 59.01 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDS---IGYVPQDNFLFsTD--VRD 429
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQSGALF-TDmnVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 NIRFAdfDRSQAAVEDAAIASAVHDDIltfaqgyeTVVGERGVS------LSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:PRK11831 104 NVAYP--LREHTQLPAPLLHSTVMMKL--------EAVGLRGAAklmpseLSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 504 VDAkteetILMNLKTMRADQ-------TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEAL 558
Cdd:PRK11831 174 QDP-----ITMGVLVKLISElnsalgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
355-561 |
2.73e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 59.82 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQID-GHDIRDYSLDALLDS------IGYVPQDNFLFS-TD 426
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRgrakryIGILHQEYDLYPhRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 427 VRDNIRFAdfdRSQAAVEDAAIASAVHD-DILTFAQGY-ETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:TIGR03269 382 VLDNLTEA---IGLELPDELARMKAVITlKMVGFDEEKaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2018945286 505 DAKTE----ETILMNLKTMraDQTTIITANRLSSV-MHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:TIGR03269 459 DPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
335-547 |
2.81e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 335 DINYAVQkftYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDqyQGVIQIDGHDIRDYSLDALLD-SI 413
Cdd:TIGR00956 764 NLTYEVK---IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVT--TGVITGGDRLVNGRPLDSSFQrSI 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 414 GYVPQ-DNFLFSTDVRDNIRFADFDRSQAAVEDAAIASAVHD--DILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMT 490
Cdd:TIGR00956 839 GYVQQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEviKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVA 918
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 491 DPEILI-LDDSLSAVDAKTEETIlmnLKTMR--AD--QTTIITANRLSSVMHA--DEIIVMDDG 547
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSI---CKLMRklADhgQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
344-508 |
3.75e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLlreydqyQGVIQidghdirDYSLDALLD---SIGYVPQDN 420
Cdd:TIGR03719 13 VVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVDK-------DFNGEARPQpgiKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 421 FLFST-DVRDNI------------RF-----------ADFD---RSQAAVEDAAIASAVHD---------DILTFAQGyE 464
Cdd:TIGR03719 78 QLDPTkTVRENVeegvaeikdaldRFneisakyaepdADFDklaAEQAELQEIIDAADAWDldsqleiamDALRCPPW-D 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2018945286 465 TVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:TIGR03719 157 ADVTK----LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
347-527 |
4.14e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.10 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQPT-LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR--DYSLDALL--DSIGYVPQDNF 421
Cdd:PRK10584 19 GEHELSiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmDEEARAKLraKHVGFVFQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFST-DVRDNIRFADFDRSQAAVEDAAIASAVHDDIltfaqgyetVVGER----GVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK10584 99 LIPTlNALENVELPALLRGESSRQSRNGAKALLEQL---------GLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|..
gi 2018945286 497 LDDSLSAVDAKTEETILMNLKTMRADQ-TTII 527
Cdd:PRK10584 170 ADEPTGNLDRQTGDKIADLLFSLNREHgTTLI 201
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
16-290 |
4.73e-09 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 57.94 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGVIFL-VLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGI-----------LLSAAILQYLfrygwRTRiwg 83
Cdd:cd18779 1 PGLLGQILLAsLLLQLLGLALPLLTGVLVDRVIPRGDRDLLGVLGLGLaalvltqllagLLRSHLLLRL-----RTR--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 84 gaakLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHaTNDLTAIQQVAGAGILtfadSIITGGTTIIAMVIFVDWRLTLM 163
Cdd:cd18779 73 ----LDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMR-LSSNATIRELLTSQTL----SALLDGTLVLGYLALLFAQSPLL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 164 ALIpmpLLAVASRQLGA------HLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRV 237
Cdd:cd18779 144 GLV---VLGLAALQVALllatrrRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRR 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2018945286 238 NMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWP 290
Cdd:cd18779 221 GRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALAGAFLAP 273
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
22-301 |
5.25e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 57.62 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIDTHQL-TPQKLIMWLGI----LLSAAILQYLFRYGWRtRIWGGAaklERTLRSRL 96
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNALTLAKVkDLESAVTLILLyallRFSSKLLKELRSLLYR-RVQQNA---YRELSLKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 97 FWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGILTFADSIITGGTTIIAMVIFVDWRLTLMALIPMPLLAVASR 176
Cdd:cd18560 78 FAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 177 QLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTY 256
Cdd:cd18560 158 KVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2018945286 257 IVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLFNVL 301
Cdd:cd18560 238 TLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMI 282
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
362-552 |
8.09e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 362 QGKTLGIVGKVGSGKTTLIKLLLREYDQYQ-GVIQIDGHDIRDYSLDALLdsigyvpqdnflfstdvrdnirfadfdrsq 440
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 441 aavedaaiasavhddiltfaqgyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETIL------M 514
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrL 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 2018945286 515 NLKTMRADQTTIITANRLSSVMHADEIIVMDDGQIIER 552
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
335-547 |
1.58e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.94 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 335 DINYAVQKftyPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL-LREYDQY-QGVIQIDGHDIRDYsldaLLDS 412
Cdd:cd03232 8 NLNYTVPV---KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLDKN----FQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 413 IGYVPQ-DNFLFSTDVRDNIRFAdfdrsqaavedAAIasavhddiltfaqgyetvvgeRGVSLSggQKQRIAIARAMMTD 491
Cdd:cd03232 81 TGYVEQqDVHSPNLTVREALRFS-----------ALL---------------------RGLSVE--QRKRLTIGVELAAK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 492 PEILILDDSLSAVDAKTEETIlMNL--KTMRADQTTIITANRLSSVM--HADEIIVMDDG 547
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNI-VRFlkKLADSGQAILCTIHQPSASIfeKFDRLLLLKRG 185
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
344-508 |
2.20e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.96 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGyvpqdnflf 423
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIG--------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 stdvrdniRFADFDRSQAAVEDAAIASAVhddilTFAQGYETvvgergvsLSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:COG2401 108 --------RKGDFKDAVELLNAVGLSDAV-----LWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
....*
gi 2018945286 504 VDAKT 508
Cdd:COG2401 167 LDRQT 171
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-553 |
2.59e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 55.23 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 356 VAFTLPQGKTLGIVGKVGSGKTTLIK-----LLLREYDQYQGVIQIDGHDIRDYSLDAL--LDSIGYVPQ-DNFLFSTDV 427
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIevRREVGMVFQyPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNI----RFADFDRSQAA----VEDAAIASAVHDDILTFAQGYETvvgergvSLSGGQKQRIAIARAMMTDPEILILDD 499
Cdd:PRK14267 103 YDNVaigvKLNGLVKSKKElderVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2018945286 500 SLSAVD----AKTEEtILMNLKTmraDQTTII-TANRLSSVMHADEIIVMDDGQIIERG 553
Cdd:PRK14267 176 PTANIDpvgtAKIEE-LLFELKK---EYTIVLvTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
359-545 |
2.73e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.11 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 359 TLPQGKTLGIVGKVGSGKTTLIKLLlreydqyQGVIQIDGHDIrdyslDALLDSIGYVPQ----DnflFSTDVRDNIRfa 434
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQyikaD---YEGTVRDLLS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 dfdrsqAAVEDAAIASAVHDDI---LTFAQGYETVVGErgvsLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT--- 508
Cdd:cd03237 84 ------SITKDFYTHPYFKTEIakpLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlm 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2018945286 509 -----EETILMNLKTMRADQTTIITANRLssvmhADEIIVMD 545
Cdd:cd03237 154 askviRRFAENNEKTAFVVEHDIIMIDYL-----ADRLIVFE 190
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
340-558 |
3.21e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQYQG--------VIQIDGHDIRDysLDAL 409
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsgLITGDKSAGshiellgrTVQREGRLARD--IRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 410 LDSIGYVPQD-NFLFSTDVRDNIR-------------FADFDRSQaavEDAAIASAVHDDILTFAQgyetvvgERGVSLS 475
Cdd:PRK09984 85 RANTGYIFQQfNLVNRLSVLENVLigalgstpfwrtcFSWFTREQ---KQRALQALTRVGMVHFAH-------QRVSTLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 476 GGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQ--TTIITANRLS-SVMHADEIIVMDDGQIIER 552
Cdd:PRK09984 155 GGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYD 234
|
....*.
gi 2018945286 553 GTHEAL 558
Cdd:PRK09984 235 GSSQQF 240
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
355-507 |
3.69e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDI---RDYSLDALLdSIGYVPQDNFLFSTDvrDNI 431
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqRDEYHQDLL-YLGHQPGIKTELTAL--ENL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFAdfdrsqaavedAAIASAVHDDILTFA------QGYETV-VGergvSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK13538 96 RFY-----------QRLHGPGDDEALWEAlaqvglAGFEDVpVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
...
gi 2018945286 505 DAK 507
Cdd:PRK13538 161 DKQ 163
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
353-550 |
4.24e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQYQGVIQIDGHDIRDYSL-DALLDSIGYVPQDNFLFST-DVR 428
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgVYPHGTYEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNI---------RFADFD----RSQAAVEDAAIASAVHddiltfaqgyeTVVGErgvsLSGGQKQRIAIARAMMTDPEIL 495
Cdd:PRK13549 101 ENIflgneitpgGIMDYDamylRAQKLLAQLKLDINPA-----------TPVGN----LGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 496 ILDDSLSAVDAKTEETILMNLKTMRA-DQTTIITANRLSSVMH-ADEIIVMDDGQII 550
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRDLKAhGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
340-563 |
6.95e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.28 E-value: 6.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 340 VQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQidghdirdYSLDAlldSIGYVPQD 419
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK--------WSENA---NIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NflfstdvrdnirFADFDRSQAAVEDAAIASAVHDDiltfaqgyETVVgeRGV----------------SLSGGQKQRIA 483
Cdd:PRK15064 391 H------------AYDFENDLTLFDWMSQWRQEGDD--------EQAV--RGTlgrllfsqddikksvkVLSGGEKGRML 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 484 IARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMradQTTII--TANR--LSSVmhADEIIVMDDGQIIE-RGTHEAL 558
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY---EGTLIfvSHDRefVSSL--ATRIIEITPDGVVDfSGTYEEY 523
|
....*
gi 2018945286 559 LAEDG 563
Cdd:PRK15064 524 LRSQG 528
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
355-550 |
9.29e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 9.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTL-IKLLLREYDQY-QGVIQIDGHDIRDYSLDALLDS-IGYVPQD----NFLFSTDV 427
Cdd:NF040905 278 DVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGKEVDVSTVSDAIDAgLAYVTEDrkgyGLNLIDDI 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 428 RDNIRFADFDR-SQAAV----EDAAIASAVHDDILTFAQGYETVVGergvSLSGGQKQRIAIARAMMTDPEILILDDSLS 502
Cdd:NF040905 358 KRNITLANLGKvSRRGVidenEEIKVAEEYRKKMNIKTPSVFQKVG----NLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 503 AVD--AKTEetILmnlktmradqtTIItaNRL----------SSVMH-----ADEIIVMDDGQII 550
Cdd:NF040905 434 GIDvgAKYE--IY-----------TII--NELaaegkgviviSSELPellgmCDRIYVMNEGRIT 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
357-561 |
1.53e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 357 AFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSLDALLDSIGYVPQDNflfSTDV----RDnir 432
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRN---NTDMlspgED--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 433 faDFDRSQAAVedaaIASAVHDDIL--TFAQ--GYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKT 508
Cdd:PRK10938 97 --DTGRTTAEI----IQDEVKDPARceQLAQqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 509 EETILMNLKTM-RADQTTIITANRLSSV-MHADEIIVMDDGQIIERGTHEALLAE 561
Cdd:PRK10938 171 RQQLAELLASLhQSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
355-558 |
1.58e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 52.68 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYSlDALLDSIGYVP--QDNFLF-STDVRDNI 431
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 432 RFADFDRSQAAV-------------EDAAIASAVH--DDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILI 496
Cdd:PRK11300 102 LVAQHQQLKTGLfsgllktpafrraESEALDRAATwlERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 497 LDDSLSAVDAKteETILMN--LKTMRADQ--TTIITANRLSSVMH-ADEIIVMDDGQIIERGTHEAL 558
Cdd:PRK11300 177 LDEPAAGLNPK--ETKELDelIAELRNEHnvTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
350-560 |
1.65e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKT----TLIKLLLREYDQYQGVIQIDGHDIRDYSLDA-LLDSIGYVPQDNFLFS 424
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGrKIATIMQNPRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVRDNIRFADFDRSQAAVeDAAIASAVHDDILTFAqgyETVVGERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:PRK10418 96 HTMHTHARETCLALGKPAD-DATLTAALEAVGLENA---ARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 505 DAKTEETIL---MNLKTMRADQTTIITAN-----RLssvmhADEIIVMDDGQIIERGTHEALLA 560
Cdd:PRK10418 172 DVVAQARILdllESIVQKRALGMLLVTHDmgvvaRL-----ADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
26-280 |
2.35e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 52.52 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 26 VLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLsAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFMKMDT 105
Cdd:cd18783 12 LILHVLALAPPIFFQIVIDKVLVHQSYSTLYVLTIGVVI-ALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 106 TFFQKHRTGDLMAHaTNDLTAIQQ-VAGAGILTFADSiiTGGTTIIAMVIFVDWRLT--------LMALIPMPLLAVASR 176
Cdd:cd18783 91 DFFERTPAGVLTKH-MQQIERIRQfLTGQLFGTLLDA--TSLLVFLPVLFFYSPTLAlvvlafsaLIALIILAFLPPFRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 177 QLGAhLHTAFGQSQAAFsrlndktQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAISLIIGLTY 256
Cdd:cd18783 168 RLQA-LYRAEGERQAFL-------VETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMT 239
|
250 260
....*....|....*....|....
gi 2018945286 257 IVTIIYGGTLVMHHSISIGQLISF 280
Cdd:cd18783 240 VGVIWVGAYLVFAGSLTVGALIAF 263
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
353-547 |
4.11e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR--DYSLDALLdSIGYVPQD-NFLFSTDVRD 429
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQL-GIGIIYQElSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 430 N-------------IRFADFD--RSQAAvedaaiasavhddILTFAQGYETVVGERGVSLSGGQKQRIAIARAMMTDPEI 494
Cdd:PRK09700 100 NlyigrhltkkvcgVNIIDWRemRVRAA-------------MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 495 LILDDSLSAVDAKTEETILMNLKTMRADQTTII-TANRLSSVMH-ADEIIVMDDG 547
Cdd:PRK09700 167 IIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDG 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
358-565 |
6.06e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 51.65 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 358 FTLPQGKTLGIVGKVGSGKT-TLIKL--LLREYDQYQGVIQIDGHDIRDYSLDAL----LDSIGYVPQDNFlfsTDVRDN 430
Cdd:PRK09473 37 FSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKELnklrAEQISMIFQDPM---TSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 431 IRFAD-----------FDRSQAAVEDAAIASAV-----HDDILTFAQGYetvvgergvslSGGQKQRIAIARAMMTDPEI 494
Cdd:PRK09473 114 MRVGEqlmevlmlhkgMSKAEAFEESVRMLDAVkmpeaRKRMKMYPHEF-----------SGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 495 LILDDSLSAVDAKTEETI--LMN-LKtmRADQTTIITANRLSSVMHA--DEIIVMDDGQIIERGTheallAEDGWY 565
Cdd:PRK09473 183 LIADEPTTALDVTVQAQImtLLNeLK--REFNTAIIMITHDLGVVAGicDKVLVMYAGRTMEYGN-----ARDVFY 251
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
353-554 |
6.81e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYD--------QYQGVIQIDGHDIRDYSLDALLDSIGYVPQDN---F 421
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAqpaF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFStdVRDNI---RFADFDRSQA-AVEDAAIASAVhddiLTFAqGYETVVGERGVSLSGGQKQRIAIARAM--------- 488
Cdd:PRK13547 97 AFS--AREIVllgRYPHARRAGAlTHRDGEIAWQA----LALA-GATALVGRDVTTLSGGELARVQFARVLaqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 489 MTDPEILILDDSLSAVDAKTEETILMNLKTMRADQT----TIITANRLSSvMHADEIIVMDDGQIIERGT 554
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgvlAIVHDPNLAA-RHADRIAMLADGAIVAHGA 238
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
351-572 |
1.20e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLRE--YDQYQGVIQIDGHDIRDysLDALLDS-------------IGY 415
Cdd:CHL00131 21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD--LEPEERAhlgiflafqypieIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 416 VPQDNFLfstdvrdniRFAdFDRSQAAVEDAAIasavhdDILTFAQ---------GYETVVGERGVS--LSGGQKQRIAI 484
Cdd:CHL00131 99 VSNADFL---------RLA-YNSKRKFQGLPEL------DPLEFLEiineklklvGMDPSFLSRNVNegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 485 ARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITAN---RLSSVMHADEIIVMDDGQIIERGTHE-ALLA 560
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILIThyqRLLDYIKPDYVHVMQNGKIIKTGDAElAKEL 242
|
250
....*....|..
gi 2018945286 561 EDGWYAemWLKQ 572
Cdd:CHL00131 243 EKKGYD--WLKQ 252
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
355-556 |
1.42e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTtliklllreydqyqgviqidghdIRDYSLDALLDSIGYVPQDNFLFstDVRDNIRFA 434
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKS-----------------------VSSLAIMGLIDYPGRVMAEKLEF--NGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 DFDRSQAAVEDAAIasaVHDDILT-----FAQGYETVVG-------------ERGV--------------------SLSG 476
Cdd:PRK11022 80 EKERRNLVGAEVAM---IFQDPMTslnpcYTVGFQIMEAikvhqggnkktrrQRAIdllnqvgipdpasrldvyphQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 477 GQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETI---LMNLKTmRADQTTIITANRLSSVMH-ADEIIVMDDGQIIER 552
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIielLLELQQ-KENMALVLITHDLALVAEaAHKIIVMYAGQVVET 235
|
....
gi 2018945286 553 GTHE 556
Cdd:PRK11022 236 GKAH 239
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
22-291 |
1.95e-06 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 49.78 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTL----VD--LIDTHQ--LTPQKLIMWLGILLSAAI--LQ--YLFRygWRTriwggaaKLE 89
Cdd:cd18569 4 LLFVVLAGLLLVIPGLVIPVFsrifIDdiLVGGLPdwLRPLLLGMALTALLQGLLtwLQqyYLLR--LET-------KLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 90 RTLRSRLFWHFMKMDTTFFQKHRTGDLMAH-ATNDLTA---IQQVAGAGIltfadSIITGGTTIIAMVIFvDWRLTL--- 162
Cdd:cd18569 75 LSSSSRFFWHVLRLPVEFFSQRYAGDIASRvQSNDRVAnllSGQLATTVL-----NLVMAVFYALLMLQY-DVPLTLigi 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 163 -MALIPMPLLAVASRQLGahlhTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEadvaDFNEIV----TKTIAINKRV 237
Cdd:cd18569 149 aIALLNLLVLRLVSRKRV----DLNRRLLQDSGKLTGTTMSGLQMIETLKASGAES----DFFSRWagyqAKVLNAQQEL 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2018945286 238 NMIDGLFDPAISLIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPM 291
Cdd:cd18569 221 GRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPV 274
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
344-550 |
2.15e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKqpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR-DYSLDALLDSIGYVPQD-NF 421
Cdd:PRK10982 7 SFPGVK--ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 422 LFSTDVRDNIRFADFDRSQAAVEDAAI---ASAVHDDIltfaqGYETVVGERGVSLSGGQKQRIAIARAMMTDPEILILD 498
Cdd:PRK10982 85 VLQRSVMDNMWLGRYPTKGMFVDQDKMyrdTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 499 DSLSAVDAKTEETILMNLKTMRADQTTIITanrLSSVMH-----ADEIIVMDDGQII 550
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIVY---ISHKMEeifqlCDEITILRDGQWI 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
351-549 |
2.32e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 50.43 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 351 PTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDYS-LDALLDSIGYVPQDNFLF-STDVR 428
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFpNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRF--ADFDRSQAAVEDAAIASAVHDDILTFAQgyetvvgergvSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDA 506
Cdd:PRK15439 105 ENILFglPKRQASMQKMKQLLAALGCQLDLDSSAG-----------SLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2018945286 507 KTEETILMNLKTMRADQTTII-TANRLSSVMH-ADEIIVMDDGQI 549
Cdd:PRK15439 174 AETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTI 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
339-554 |
2.37e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 339 AVQKfTYPGdKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQyqGVIQIDGHDI-------RDysldal 409
Cdd:PRK11650 8 AVRK-SYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVagLERITS--GEIWIGGRVVnelepadRD------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 410 ldsIGYVPQDNFLFS-TDVRDNI----RFADFDRSQ--AAVEDAAiasavhdDILtfaqGYETVVGERGVSLSGGQKQRI 482
Cdd:PRK11650 78 ---IAMVFQNYALYPhMSVRENMayglKIRGMPKAEieERVAEAA-------RIL----ELEPLLDRKPRELSGGQRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 483 AIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTII--TANRLSSVMHADEIIVMDDGQIIERGT 554
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLhRRLKTTSLyvTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
468-563 |
2.56e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 468 GERGVSLSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRL--SSVMHADEIIVMD 545
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|....*...
gi 2018945286 546 DGQIIERGTHEALLAEDG 563
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
353-562 |
2.74e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 46.74 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 353 LMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ--YQGVIQIDGHDIRDYSL-DALLDSIGYVPQDNFLF-STDVR 428
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVpELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 429 DNIRFA-DFDRSQAAVEDAAI---ASAVHDDILTFAQGYETVVGERGvslsGGQKQRIAIARAMMTDPEILILDDSLSAV 504
Cdd:TIGR02633 97 ENIFLGnEITLPGGRMAYNAMylrAKNLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 505 DAKTEETILMNLKTMRADQTTII-TANRLSSVMH-ADEIIVMDDGQIIERGTHEALLAED 562
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVyISHKLNEVKAvCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
56-218 |
2.98e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 46.12 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 56 LIMWLGILLSAAILQYLFRYGWRTRIWGGAAKLERTLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGAGI 135
Cdd:cd18561 35 IMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 136 LTFADSIITGGTTIIAMViFVDWRLTLMALIPMPLLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQ 215
Cdd:cd18561 115 PQLLVALLGPLLILIYLF-FLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGA 193
|
...
gi 2018945286 216 EEA 218
Cdd:cd18561 194 SKR 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
344-551 |
4.18e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKqpTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLL--LREYDQYQGVIQIDG-----HDIRDySLD--------- 407
Cdd:NF040905 10 TFPGVK--ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgVYPHGSYEGEILFDGevcrfKDIRD-SEAlgiviihqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 408 -ALldsigyVPqdnfLFStdVRDNI-------RFADFDRSQAAVEDAAIASAV--HDDIltfaqgyETVVGERGVslsgG 477
Cdd:NF040905 87 lAL------IP----YLS--IAENIflgneraKRGVIDWNETNRRARELLAKVglDESP-------DTLVTDIGV----G 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 478 QKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRAdQ--TTIITANRLSSVMH-ADEIIVMDDGQIIE 551
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
91-273 |
5.46e-05 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 45.16 E-value: 5.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 91 TLRSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQV-------AGAGILTFAdsiitggtTIIAMVIFVDWRLTLM 163
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLylrvlspPVVALLVIL--------ATILFLAFFSPALALI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 164 ALIPMPLLAVASRQLGAHLHTAFGQSQAAF-SRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDG 242
Cdd:cd18585 141 LLAGLLLAGVVIPLLFYRLGKKIGQQLVQLrAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSG 220
|
170 180 190
....*....|....*....|....*....|.
gi 2018945286 243 LFDPAISLIIGLTYIVTIIYGGTLVMHHSIS 273
Cdd:cd18585 221 LSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
347-505 |
1.15e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKqPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ-YQGVIQIDGHdiRDYSLDALLD---SIGYVPQD--- 419
Cdd:PRK10938 271 NDR-PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQgYSNDLTLFGR--RRGSGETIWDikkHIGYVSSSlhl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 420 NFLFSTDVRDNIRFADFDrsqaaveDAAIASAVHDDILTFAQGYETVVGERGV-------SLSGGQkQRIA-IARAMMTD 491
Cdd:PRK10938 348 DYRVSTSVRNVILSGFFD-------SIGIYQAVSDRQQKLAQQWLDILGIDKRtadapfhSLSWGQ-QRLAlIVRALVKH 419
|
170
....*....|....
gi 2018945286 492 PEILILDDSLSAVD 505
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
355-505 |
1.50e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 44.73 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLlreydqyQGVIQ------------IDGHDI----RdysldalldsIGYVPQ 418
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKML-------TGLLPasegeawlfgqpVDAGDIatrrR----------VGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 419 DnflFS-----TdVRDNI----RFadFDrsqaaVEDAAIASAVHDDILTFaqGYETVVGERGVSLSGGQKQRIAIARAMM 489
Cdd:NF033858 347 A---FSlygelT-VRQNLelhaRL--FH-----LPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVI 413
|
170
....*....|....*.
gi 2018945286 490 TDPEILILDDSLSAVD 505
Cdd:NF033858 414 HKPELLILDEPTSGVD 429
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
355-560 |
1.64e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 43.92 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 355 NVAFTLPQGKTLGIVGKVGSGKTTLIKLLLreydqyqGVIQIDGHDIRdysldalldSIGYVPQdnflfstdvRDNIRFA 434
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLT-------GILVPTSGEVR---------VLGYVPF---------KRRKEFA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 435 D-----F-DRSQ-----AAVEDAAIASAVHD-DILTFAQGYETVVGERGVS---------LSGGQKQRIAIARAMMTDPE 493
Cdd:COG4586 95 RrigvvFgQRSQlwwdlPAIDSFRLLKAIYRiPDAEYKKRLDELVELLDLGelldtpvrqLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2018945286 494 ILILDDSLSAVDAKTEETILMNLKTMRAD-QTTIItanrLSSvmH--------ADEIIVMDDGQIIERGTHEALLA 560
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTIL----LTS--HdmddiealCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
346-554 |
3.80e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 346 PGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLL-REYDQY-QGVIQIDGHDIRDYSLDALldsIGYVPQdNFLF 423
Cdd:PLN03140 889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgRKTGGYiEGDIRISGFPKKQETFARI---SGYCEQ-NDIH 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 S--TDVRDNIRFADFDRSQAAVEDAAIASAVhDDILTFAQG---YETVVGERGVS-LSGGQKQRIAIARAMMTDPEILIL 497
Cdd:PLN03140 965 SpqVTVRESLIYSAFLRLPKEVSKEEKMMFV-DEVMELVELdnlKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2018945286 498 DDSLSAVDAKTEETIlmnlktMRADQTTIITANRLSSVMHA---------DEIIVMD-DGQIIERGT 554
Cdd:PLN03140 1044 DEPTSGLDARAAAIV------MRTVRNTVDTGRTVVCTIHQpsidifeafDELLLMKrGGQVIYSGP 1104
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
348-573 |
6.30e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 6.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 348 DKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLL--REYDQYQGVIQIDGHDIRDYSLD-----ALLDSIGY---VP 417
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEdrageGIFMAFQYpveIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 418 --QDNFLFSTDVR-----------DNIRFADFdrsqaaVEDAAIASAVHDDILTfaqgyETVvgerGVSLSGGQKQRIAI 484
Cdd:PRK09580 92 gvSNQFFLQTALNavrsyrgqeplDRFDFQDL------MEEKIALLKMPEDLLT-----RSV----NVGFSGGEKKRNDI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 485 ARAMMTDPEILILDDSLSAVDAKTEETILMNLKTMRADQTTIITA---NRLSSVMHADEIIVMDDGQIIERGTHEAL--L 559
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTLVkqL 236
|
250
....*....|....
gi 2018945286 560 AEDGWyaeMWLKQQ 573
Cdd:PRK09580 237 EEQGY---GWLTEQ 247
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
350-563 |
7.73e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.46 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 350 QPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIK----LLlreydQYQGVIQIDGHDIRDYSLDALLDSIGYVPQ-DNFLFS 424
Cdd:PRK03695 9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQqQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 425 TDVrdnirFADFDRSQAA-VEDAAIASAVH--------DDILtfaqgyetvvgERGVS-LSGGQKQRIAIARAMM-TDPE 493
Cdd:PRK03695 84 MPV-----FQYLTLHQPDkTRTEAVASALNevaealglDDKL-----------GRSVNqLSGGEWQRVRLAAVVLqVWPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 494 I------LILDDSLSAVDAkTEETILMNL-KTMRADQTTIITA----NRlsSVMHADEIIVMDDGQIIERGTHEALLAED 562
Cdd:PRK03695 148 InpagqlLLLDEPMNSLDV-AQQAALDRLlSELCQQGIAVVMSshdlNH--TLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
.
gi 2018945286 563 G 563
Cdd:PRK03695 225 N 225
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
22-298 |
7.78e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 41.72 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 22 VIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWL----GILLSAAIL-----QYLFrygwrTRIwggAAKLERTL 92
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLllayGLARILSSLfnelrDALF-----ARV---SQRAVRRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 93 RSRLFWHFMKMDTTFFQKHRTGDL---MAHATNdltAIQQVAGAGILTFADSIITGGTTIIAMVIFVDWRLTLMALIPMP 169
Cdd:cd18582 74 ALRVFRHLHSLSLRFHLSRKTGALsraIERGTR---GIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 170 LLAVASRQLGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFDPAIS 249
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2018945286 250 LIIGLTYIVTIIYGGTLVMHHSISIGQLISFISYIAALVWPMFAIGRLF 298
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
16-278 |
8.69e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 41.43 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 16 RRYLWGV-IFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLsAAILQYLFRYGwRTRIWG-GAAKLERTLR 93
Cdd:cd18586 1 RRVFVEVgLFSFFINLLALAPPIFMLQVYDRVLPSGSLSTLLGLTLGMVV-LLAFDGLLRQV-RSRILQrVGLRLDVELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 94 SRLFWHFMKMDTTFfqkhRTGDLMAHATNDLTAIQQ-VAGAGILTFADSIITggtTIIAMVIFV--DWrLTLMALIPMPL 170
Cdd:cd18586 79 RRVFRAVLELPLES----RPSGYWQQLLRDLDTLRNfLTGPSLFAFFDLPWA---PLFLAVIFLihPP-LGWVALVGAPV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 171 ---LAVAS-RQLGAHLHTAFGQSQAAfsrlNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIDGLFdp 246
Cdd:cd18586 151 lvgLAWLNhRATRKPLGEANEAQAAR----DALAAETLRNAETIKALGMLGNLRRRWEARHAETLELQIRASDLAGAI-- 224
|
250 260 270
....*....|....*....|....*....|....*
gi 2018945286 247 aISLIIGLTYIVTII---YGGTLVMHHSISIGQLI 278
Cdd:cd18586 225 -SAIGKTLRMALQSLilgVGAYLVIDGELTIGALI 258
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
26-297 |
9.02e-04 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 41.46 E-value: 9.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 26 VLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLS---AAILQYLF--RYGWRTRIWGGAAKLERTLRSRLFWHf 100
Cdd:cd18562 9 VALAGVQFAEPVLFGRVVDALSSGGDAFPLLALWAALGLFsilAGVLVALLadRLAHRRRLAVMASYFEHVITLPLSFH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 101 mkmdttffQKHRTGDLMaHATndLTAIQQVAGAgILTFADSIITGGTTIIAMV---IFVDWRLTLMALIPMPLLAVASRQ 177
Cdd:cd18562 88 --------SQRGSGRLL-RIM--LRGTDALFGL-WLGFFREHLAALVSLIVLLpvaLWMNWRLALLLVVLAAVYAALNRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 178 LGAHLHTAFGQSQAAFSRLNDKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRV----NMIDGLFDPAISliig 253
Cdd:cd18562 156 VMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPVlnwwALASVLTRAAST---- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2018945286 254 LTYIVTIIYGGTLVMHHSISIGQLISFISYIAALvwpmfaIGRL 297
Cdd:cd18562 232 LTMVAIFALGAWLVQRGELTVGEIVSFVGFATLL------IGRL 269
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
347-505 |
9.21e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.18 E-value: 9.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 347 GDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIR---DYSLDALLDSIGYVPQDNFLF 423
Cdd:PRK13545 34 GEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALiaiSSGLNGQLTGIENIELKGLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 424 STdVRDNIRfadfDRSQAAVEDAAIASAVHDDILTFaqgyetvvgergvslSGGQKQRIAIARAMMTDPEILILDDSLSA 503
Cdd:PRK13545 114 GL-TKEKIK----EIIPEIIEFADIGKFIYQPVKTY---------------SSGMKSRLGFAISVHINPDILVIDEALSV 173
|
..
gi 2018945286 504 VD 505
Cdd:PRK13545 174 GD 175
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
474-560 |
9.82e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 474 LSGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTIITANRLSSVMH--ADEIIVMDDGQII 550
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSqwADKINVLYCGQTV 238
|
90
....*....|
gi 2018945286 551 ERGTHEALLA 560
Cdd:PRK15093 239 ETAPSKELVT 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
303-396 |
1.35e-03 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 41.46 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 303 RGNASYDRVDQLLKETSTIIEAPNAIQTPA---TGDINYAVQKFTYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTL 379
Cdd:TIGR03719 285 KSKARLARYEELLSQEFQKRNETAEIYIPPgprLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90
....*....|....*..
gi 2018945286 380 IKLLLREYDQYQGVIQI 396
Cdd:TIGR03719 365 FRMITGQEQPDSGTIEI 381
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
344-548 |
1.43e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 344 TYPGDKQPTLMNVAFTLPQGKTLGIVGKVGSGKTTLIKLLLREYDQ-----------YQGVIQIDghdirdySLDALLD- 411
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKarlisflpkfsRNKLIFID-------QLQFLIDv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 412 SIGYVPqdnflfstdvrdnirfadfdrsqaavedaaiasavhddiltfaqgyetvVGERGVSLSGGQKQRIAIARAMMTD 491
Cdd:cd03238 75 GLGYLT-------------------------------------------------LGQKLSTLSGGELQRVKLASELFSE 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 492 PE--ILILDDSLSAVDAKTEETILMNLKTMRADQTTIITANRLSSVM-HADEIIVMDDGQ 548
Cdd:cd03238 106 PPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLsSADWIIDFGPGS 165
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
20-301 |
1.44e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 40.90 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 20 WGVIFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQKLIMWLGILLSAAI--LQYLF-----RYGWRTRIWGGAAKleRTL 92
Cdd:cd18597 1 LAGLLKLLADVLQVLSPLLLKYLINFVEDAYLGGPPPSIGYGIGYAIGLflLQLLSslllnHFFYRSMLTGAQVR--AAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 93 RSRLFWHFMKMDTTFFQKHRTGDLMAHATNDLTAIQQVAGagiltFADSIITGGTTIIAMVIFVDWRLTLMAL------- 165
Cdd:cd18597 79 TKAIYRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALG-----FFHFLWTAPIQIIIAIALLIVNLGPSALvgigvli 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 166 IPMPLLAVASRQLgahlhTAFGQSQAAF--SRLNdKTQESVSGIKVLKTFGQEEADVADFNEIVTKTIAINKRVNMIdgl 243
Cdd:cd18597 154 LSIPLQGFLMKKL-----FKLRKKANKItdKRVK-LTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQIL--- 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 244 fdpaISLIIGLTYIVTIiyggtlvmhhsisIGQLISFISYI-------AALVWPMFAigrLFNVL 301
Cdd:cd18597 225 ----RSILTAVAFSLPV-------------LASMLSFITYYatghtldPANIFSSLA---LFNVL 269
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
368-404 |
1.97e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 39.65 E-value: 1.97e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2018945286 368 IVGKVGSGKTTLIKLLLREYDQYQGVIQIDGHDIRDY 404
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFREL 52
|
|
| DUF815 |
pfam05673 |
Protein of unknown function (DUF815); This family consists of several bacterial proteins of ... |
373-426 |
3.48e-03 |
|
Protein of unknown function (DUF815); This family consists of several bacterial proteins of unknown function.
Pssm-ID: 428578 [Multi-domain] Cd Length: 250 Bit Score: 39.44 E-value: 3.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2018945286 373 GSGKTTLIKLLLREY-DQYQGVIQIDGHDIRDysLDALLDSIGYVPQDNFLFSTD 426
Cdd:pfam05673 63 GTGKSSLVKALLNEYaDQGLRLIEVDKEDLGD--LPDLVDLLRDRPYRFILFCDD 115
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
23-266 |
3.84e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 39.54 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 23 IFLVLVAVVQIVPPKVIGTLVDLIDTHQLTPQK--LIMWLGILLSAAIL-----QYLF---RYGWRTRIWGGAAKLERTL 92
Cdd:cd18594 4 ILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTeaYLYALGLSLCAFLRvllhhPYFFglhRYGMQLRIALSSLIYKKTL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 93 rsrlfwhfmKMDTTFFQKHRTGDLMAHATNDLTAIQQVagagiLTFADSIITGGTTIIAMVIFVdWRL----TLMALIPM 168
Cdd:cd18594 84 ---------KLSSSALSKITTGHIVNLLSNDVQKFDEV-----LVYLHFLWIAPLQVIVLTGLL-WREigpsSLAGLGVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 169 PLLAVasrqLGAHLHTAFGQSQAAFSRLNDK----TQESVSGIKVLKTFGQEEAdvadFNEIV----------TKTIAIN 234
Cdd:cd18594 149 LLLLP----LQAYLGKLFAKYRRKTAGLTDErvkiMNEIISGMRVIKMYTWEES----FAKLIenirkkelklIRKAAYI 220
|
250 260 270
....*....|....*....|....*....|..
gi 2018945286 235 KRVNMidGLFDPAISLIIGLTYIVTIIYGGTL 266
Cdd:cd18594 221 RAFNM--AFFFFSPTLVSFATFVPYVLTGNTL 250
|
|
| MobB |
pfam03205 |
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop. |
366-386 |
8.79e-03 |
|
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
Pssm-ID: 427196 [Multi-domain] Cd Length: 133 Bit Score: 36.76 E-value: 8.79e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
464-560 |
9.36e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2018945286 464 ETVVGE---RGVSlsGGQKQRIAIARAMMTDPEILILDDSLSAVDAKTEETILMNLKTM-RADQTTIItanrLSSVMHA- 538
Cdd:PLN03140 326 DTIVGDemiRGIS--GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVL----MSLLQPAp 399
|
90 100
....*....|....*....|....*...
gi 2018945286 539 ------DEIIVMDDGQIIERGTHEALLA 560
Cdd:PLN03140 400 etfdlfDDIILLSEGQIVYQGPRDHILE 427
|
|
| |
