|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-584 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 684.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 2 KKTFSSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTGLPTTEISRNIangesiNFSYIFKCLIWITVVGIGYCI 81
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG------DLSALLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 82 SQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMM 161
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 162 FYIQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYF 241
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 242 GFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRVFE 321
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 322 ILDEPEEKENKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGA 401
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 402 IRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDN 481
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 482 VSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKG 561
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 488239013 562 THESLLAQGGFYEKLYNSQFAEE 584
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-580 |
2.41e-156 |
|
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: 464.69 E-value: 2.41e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 2 KKTFSSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTGLptteISRNIANGESINFSYIFkcLIWITVVGIGYCI 81
Cdd:COG2274 138 GEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQV----VIDRVLPNQDLSTLWVL--AIGLLLALLFEGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 82 SQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMM 161
Cdd:COG2274 212 LRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 162 FYIQPMMALISMIMIP----TSIWISKRVINASQKYFQSMqnslGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHS 237
Cdd:COG2274 291 FFYSPPLALVVLLLIPlyvlLGLLFQPRLRRLSREESEAS----AKRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 238 LKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATK 317
Cdd:COG2274 367 YLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALE 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 318 RVFEILDEPEEKENKVDVSLPETILGDVTFDHVDFAYDP-KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYD 396
Cdd:COG2274 447 RLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 397 VDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPIN 476
Cdd:COG2274 527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVG 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 477 AEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQ 556
Cdd:COG2274 607 EGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGR 686
|
570 580
....*....|....*....|....
gi 488239013 557 IIEKGTHESLLAQGGFYEKLYNSQ 580
Cdd:COG2274 687 IVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-583 |
1.05e-139 |
|
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: 417.20 E-value: 1.05e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 7 SLKRLARYIRPYRGTFLLVIlftVLTVAFNVALPYVTGlptteISRNIANGesiNFSYIFKCLIW---ITVVGIGYC--I 81
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAG---VAMILVAATESTLAA-----LLKPLLDD---GFGGRDRSVLWwvpLVVIGLAVLrgI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 82 SQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMM 161
Cdd:TIGR02203 70 CSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 162 FYIQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYF 241
Cdd:TIGR02203 150 LYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 242 GFRAAFISGLMMPLVQLTAYatyIGMAVL---GSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKR 318
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIAS---LALAVVlfiALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAES 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 319 VFEILDEPEEKENKVDVslPETILGDVTFDHVDFAYDPK-KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDV 397
Cdd:TIGR02203 307 LFTLLDSPPEKDTGTRA--IERARGDVEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 398 DKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKL-DATDYEVVDAAKTANVDHFIRTMPDGYEMPIN 476
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 477 AEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQ 556
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|....*..
gi 488239013 557 IIEKGTHESLLAQGGFYEKLYNSQFAE 583
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
8-581 |
2.00e-123 |
|
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: 375.58 E-value: 2.00e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 8 LKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTGLpttEISRNIANGESINFSYIFKCLIWITVVgigYCISQLLSG 87
Cdd:TIGR02204 6 LAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRL---MIDHGFSKDSSGLLNRYFAFLLVVALV---LALGTAARF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 88 VLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDV----DAVSGALQQAFIGIVNAILGITlaaaMMFY 163
Cdd:TIGR02204 80 YLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTtllqSVIGSSLSMALRNALMCIGGLI----MMFI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 164 IQPMMALISMIMIPTSI----WISKRVinasQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLK 239
Cdd:TIGR02204 156 TSPKLTSLVLLAVPLVLlpilLFGRRV----RKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 240 YFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISqpmGNVTQLSSV---LQSASAAT 316
Cdd:TIGR02204 232 EAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVA---GSIGTLSEVwgeLQRAAGAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 317 KRVFEILD-EPEEKENKVDVSLPETILGDVTFDHVDFAY--DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMR 393
Cdd:TIGR02204 309 ERLIELLQaEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 394 FYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEM 473
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 474 PINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMD 553
Cdd:TIGR02204 469 YLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMD 548
|
570 580
....*....|....*....|....*...
gi 488239013 554 QGQIIEKGTHESLLAQGGFYEKLYNSQF 581
Cdd:TIGR02204 549 QGRIVAQGTHAELIAKGGLYARLARLQF 576
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-571 |
3.21e-119 |
|
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: 352.30 E-value: 3.21e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFG 422
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKI 502
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-571 |
2.01e-118 |
|
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: 362.15 E-value: 2.01e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 9 KRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVtglptteISRNIAN--GESINFSYIFKCLIWITVVGIGYCISQLLS 86
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWL-------LASLLAGliIGGAPLSALLPLLGLLLAVLLLRALLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 87 GVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILgITLA-AAMMFYIQ 165
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAAL-VPLLiLVAVFPLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 166 PMMALI---SMIMIPTSIW-ISKRVINASQKYFQSMQNslgeLNGYVQENMTGFSVLKVYGREKETLEGFKKVNHslkyf 241
Cdd:COG4988 158 WLSGLIllvTAPLIPLFMIlVGKGAAKASRRQWRALAR----LSGHFLDRLRGLTTLKLFGRAKAEAERIAEASE----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 242 GFRA--------AFISGLMMPLVqltayaTYIGMAVlgsfyvitGAIVVGqlqafIQYIW-QIS---------------Q 297
Cdd:COG4988 229 DFRKrtmkvlrvAFLSSAVLEFF------ASLSIAL--------VAVYIG-----FRLLGgSLTlfaalfvlllapeffL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 298 PMgnvTQLSS---VLQSASAATKRVFEILDEPEEKENKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTV 374
Cdd:COG4988 290 PL---RDLGSfyhARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 375 AVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDA 454
Cdd:COG4988 367 ALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 455 AKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSF 534
Cdd:COG4988 447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
|
570 580 590
....*....|....*....|....*....|....*..
gi 488239013 535 VIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:COG4988 527 LITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-319 |
6.87e-114 |
|
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: 341.31 E-value: 6.87e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTTEISRNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-577 |
2.25e-113 |
|
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: 337.28 E-value: 2.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLI-QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGM 423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLY 577
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
69-583 |
4.47e-111 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 343.92 E-value: 4.47e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 69 LIWITVVGIG-------------YCISQLLSGVLMTnvvqsamhdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDA 135
Cdd:PRK11176 64 LKWMPLVVIGlmilrgitsfissYCISWVSGKVVMT---------MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQ 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 136 VSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW----ISKRVINASQKyfqsMQNSLGELNGYVQEN 211
Cdd:PRK11176 135 VASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIairvVSKRFRNISKN----MQNTMGQVTTSAEQM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 212 MTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQY 291
Cdd:PRK11176 211 LKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 292 IWQISQPMGNVTQLSSVLQSASAATKRVFEILD-EPEEKENKVDVslpETILGDVTFDHVDFAYDPK-KPLIQDLNFEVK 369
Cdd:PRK11176 291 MIALMRPLKSLTNVNAQFQRGMAACQTLFAILDlEQEKDEGKRVI---ERAKGDIEFRNVTFTYPGKeVPALRNINFKIP 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 370 AGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDA-TD 448
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySR 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 449 YEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVM 528
Cdd:PRK11176 448 EQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 529 EGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQFAE 583
Cdd:PRK11176 528 KNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-578 |
1.58e-109 |
|
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: 339.43 E-value: 1.58e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 6 SSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTG-LptteISRNIANGESINFSYIfkcliwITVV---GIG--- 78
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGwL----IAAAALAPPILNLFVP------IVGVrafAIGrtv 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 79 --YcISQLLSgvlmtnvvqsamHD--------LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIV 148
Cdd:COG4987 71 frY-LERLVS------------HDatlrlladLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 149 NAILGITLAAAMMFYIQPMMALI-------SMIMIPtsiWISKRvinASQKYFQSMQNSLGELNGYVQENMTGFSVLKVY 221
Cdd:COG4987 138 VALLVILAAVAFLAFFSPALALVlalglllAGLLLP---LLAAR---LGRRAGRRLAAARAALRARLTDLLQGAAELAAY 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 222 GREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAI--------VVGQLQAFiqyiw 293
Cdd:COG4987 212 GALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALsgpllallVLAALALF----- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 294 qisQPMGNVTQLSSVLQSASAATKRVFEILD-EPEEKENKVDVSLPETilGDVTFDHVDFAYDP-KKPLIQDLNFEVKAG 371
Cdd:COG4987 287 ---EALAPLPAAAQHLGRVRAAARRLNELLDaPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGaGRPVLDGLSLTLPPG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 372 QTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEV 451
Cdd:COG4987 362 ERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEEL 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 452 VDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGR 531
Cdd:COG4987 442 WAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR 521
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 488239013 532 TSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYN 578
Cdd:COG4987 522 TVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-585 |
8.80e-109 |
|
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: 338.72 E-value: 8.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 265 IGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNvtqLSSV---LQSASAATKRVFEILDEPEEKENKVD-VSLPET 340
Cdd:COG5265 278 TAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNF---LGFVyreIRQALADMERMFDLLDQPPEVADAPDaPPLVVG 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 341 iLGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL 420
Cdd:COG5265 355 -GGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDP 500
Cdd:COG5265 434 IGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNP 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQ 580
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
....*
gi 488239013 581 FAEEA 585
Cdd:COG5265 594 QEEEE 598
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
107-581 |
1.62e-105 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 329.61 E-value: 1.62e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 107 EKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIWISKRV 186
Cdd:PRK13657 97 ERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSLVLVVLGIVYTLITTLV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 187 INASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGR---EKETLEGFkkVNHSLKyfgfraafisgLMMPLVQ------ 257
Cdd:PRK13657 177 MRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRieaETQALRDI--ADNLLA-----------AQMPVLSwwalas 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 258 -LTAYATYIGMA---VLGSFYVITGAIVVGQLQAFIQY----IWQISQPMGNVTQLSSvlqsASAATKRVFEILDEPEEK 329
Cdd:PRK13657 244 vLNRAASTITMLailVLGAALVQKGQLRVGEVVAFVGFatllIGRLDQVVAFINQVFM----AAPKLEEFFEVEDAVPDV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 330 ENKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDT 409
Cdd:PRK13657 320 RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 410 KSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQL 489
Cdd:PRK13657 400 RTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 490 LTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR 559
|
490
....*....|..
gi 488239013 570 GGFYEKLYNSQF 581
Cdd:PRK13657 560 GGRFAALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
345-580 |
1.86e-102 |
|
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: 309.47 E-value: 1.86e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYD--PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFG 422
Cdd:cd03249 1 IEFKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKI 502
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQ 580
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
345-580 |
3.62e-102 |
|
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: 308.78 E-value: 3.62e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMV 424
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 505 LDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQ 580
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-584 |
4.60e-102 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 320.90 E-value: 4.60e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 1 MKKTFSSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYvtgLPTTEISRNIANGEsinfsyifkcLIWITVVG--IG 78
Cdd:PRK10790 4 FSQLWPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPL---LISYFIDNMVAKGN----------LPLGLVAGlaAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 79 YCISQLLSGVL------MTN-----VVQSamhdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVsgalQQAFIGI 147
Cdd:PRK10790 71 YVGLQLLAAGLhyaqslLFNraavgVVQQ----LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVI----RDLYVTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 148 VNAIL-GITLAAAM---MFYIQPMMALISMIMIP---TSIWISKRVinaSQKYFQSMQNSLGELNGYVQENMTGFSVLKV 220
Cdd:PRK10790 143 VATVLrSAALIGAMlvaMFSLDWRMALVAIMIFPavlVVMVIYQRY---STPIVRRVRAYLADINDGFNEVINGMSVIQQ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 221 YGREKETLEGFKKVNHS--------LKYFGFraafisgLMMPLVQLTAYATYIGMAVLGSFYViTGAIVVGQLQAFIQYI 292
Cdd:PRK10790 220 FRQQARFGERMGEASRShymarmqtLRLDGF-------LLRPLLSLFSALILCGLLMLFGFSA-SGTIEVGVLYAFISYL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 293 WQISQPMGNVTQLSSVLQSASAATKRVFEILDEPEEKENKVDVSLPEtilGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQ 372
Cdd:PRK10790 292 GRLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQS---GRIDIDNVSFAYRDDNLVLQNINLSVPSRG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 373 TVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKlDATDYEVV 452
Cdd:PRK10790 369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVW 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 453 DAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRT 532
Cdd:PRK10790 448 QALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 533 SFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQFAEE 584
Cdd:PRK10790 528 LVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGE 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-576 |
4.99e-94 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 303.18 E-value: 4.99e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 8 LKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTGLPTTEISRNiangesinFSY-IFKCLIWI-TVVGIGYCISQLL 85
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGD--------KGPpALASAIFFmCLLSIASSVSAGL 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 86 SGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGAL-QQAFIGIVNAILGITLAAaMMFYI 164
Cdd:TIGR00958 221 RGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLsLNVNVLLRNLVMLLGLLG-FMLWL 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 165 QPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFK-KVNHSLKyFGF 243
Cdd:TIGR00958 300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKeALEETLQ-LNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 244 RAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQpmgNVTQLSSV---LQSASAATKRVF 320
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGE---AVRVLSYVysgMMQAVGASEKVF 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 321 EILDEPEEKENkvDVSL-PETILGDVTFDHVDFAY--DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDV 397
Cdd:TIGR00958 456 EYLDRKPNIPL--TGTLaPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 398 DKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINA 477
Cdd:TIGR00958 534 TGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 478 EGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRvmEGRTSFVIAHRLSTIRDADLILVMDQGQI 557
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
570
....*....|....*....
gi 488239013 558 IEKGTHESLLAQGGFYEKL 576
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHL 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
5-576 |
8.17e-87 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 281.01 E-value: 8.17e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 5 FSSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTGlpttEISRNIANGESINFSYIfkclIWItvvgiGYCISQL 84
Cdd:TIGR01192 4 FQVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFG----RIIDAISSKSDVLPTLA----LWA-----GFGVFNT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 85 LSGVLMTNVVQSAMHDLRRDIEEK----INRLPVSYFDKNQQGNILSRVTNDVDAVSGA----LQQAFIGIVNAILGITL 156
Cdd:TIGR01192 71 IAYVLVAREADRLAHGRRATLLTEafgrIISMPLSWHQQRGTSNALHTLLRATETLFGLwlefMRQHLATFVALFLLIPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 157 AAAMMFyiqpMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNH 236
Cdd:TIGR01192 151 AFAMDW----RLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 237 SLKYFGFRA----AFISGLMmplvQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQY----IWQISQPMGNVTQLSSv 308
Cdd:TIGR01192 227 NLLSAQYPVldwwALASGLN----RMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFanllIGRLDQMSGFITQIFE- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 309 lqsASAATKRVFEILDEPEEKENKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLI 388
Cdd:TIGR01192 302 ---ARAKLEDFFDLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLI 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 389 NLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMP 468
Cdd:TIGR01192 379 NLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRS 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 469 DGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADL 548
Cdd:TIGR01192 459 NGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADL 538
|
570 580
....*....|....*....|....*...
gi 488239013 549 ILVMDQGQIIEKGTHESLLAQGGFYEKL 576
Cdd:TIGR01192 539 VLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
3-576 |
3.06e-84 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 277.21 E-value: 3.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 3 KTFSSLKRLARYIRPYRGTFLLVILFTVLTVAFNVALPyvtglptteisrniangesiNFSYIF--KCLI-----WITVV 75
Cdd:TIGR03796 137 RKPSLLRALWRRLRGSRGALLYLLLAGLLLVLPGLVIP--------------------AFSQIFvdEILVqgrqdWLRPL 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 76 GIGYCISQLLSGVLmTNVVQSAMHDLRRDI--------EEKINRLPVSYFDKNQQGNILSRV-TND--VDAVSGALQQAF 144
Cdd:TIGR03796 197 LLGMGLTALLQGVL-TWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVqLNDqvAEFLSGQLATTA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 145 IGIVNAILgitlAAAMMFYIQPMMALI----SMIMIPTSIWISKRVINASQKyfqsMQNSLGELNGYVQENMTGFSVLKV 220
Cdd:TIGR03796 276 LDAVMLVF----YALLMLLYDPVLTLIgiafAAINVLALQLVSRRRVDANRR----LQQDAGKLTGVAISGLQSIETLKA 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 221 YGREKE-----------TLEGFKKVNHSLKYFGFRAAFISGLmmplvqltayaTYIGMAVLGSFYVITGAIVVGQLQAFI 289
Cdd:TIGR03796 348 SGLESDffsrwagyqakLLNAQQELGVLTQILGVLPTLLTSL-----------NSALILVVGGLRVMEGQLTIGMLVAFQ 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 290 QYIWQISQPMGNVTQLSSVLQSASAATKRVFEILDEP-----EEKENKVDVSLPETIL-GDVTFDHVDFAYDP-KKPLIQ 362
Cdd:TIGR03796 417 SLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPvdpllEEPEGSAATSEPPRRLsGYVELRNITFGYSPlEPPLIE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFg 442
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL- 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 443 kLDAT--DYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALI 520
Cdd:TIGR03796 576 -WDPTipDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII 654
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 521 QKAMDRvmEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKL 576
Cdd:TIGR03796 655 DDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARL 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
100-585 |
7.98e-80 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 261.96 E-value: 7.98e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNA-ILGITLAAAMMFYIQPMMALISMIMIPT 178
Cdd:PRK10789 70 ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlVMGCAVLIVMSTQISWQLTLLALLPMPV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 179 SIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPlvql 258
Cdd:PRK10789 150 MAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDP---- 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 259 TAYATyIGMAVL-----GSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRVFEILDEPEEKENKv 333
Cdd:PRK10789 226 TIYIA-IGMANLlaiggGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDG- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 334 DVSLPETiLGDVTFDHVDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSM 412
Cdd:PRK10789 304 SEPVPEG-RGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 413 SRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTI 492
Cdd:PRK10789 383 QLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGF 572
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGW 542
|
490
....*....|...
gi 488239013 573 YEKLYNSQFAEEA 585
Cdd:PRK10789 543 YRDMYRYQQLEAA 555
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
343-562 |
2.49e-76 |
|
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: 241.63 E-value: 2.49e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDP-KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLF 421
Cdd:cd03244 1 GDIEFKNVSLRYRPnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQGTIADNIR-FGKldATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDP 500
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
345-556 |
6.45e-76 |
|
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: 238.44 E-value: 6.45e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPK-KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGM 423
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDAWLYQGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKIL 503
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQ 556
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-580 |
9.41e-76 |
|
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: 240.47 E-value: 9.41e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLI-QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGM 423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQ 580
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
101-552 |
1.75e-74 |
|
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: 246.81 E-value: 1.75e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALI---SMIMIP 177
Cdd:TIGR02857 79 LRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLIlllTAPLIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 TSIW-ISKRVINASQKYFQSMQNslgeLNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFG---FRAAFISGLMM 253
Cdd:TIGR02857 159 IFMIlIGWAAQAAARKQWAALSR----LSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTmrvLRIAFLSSAVL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 254 PL-----VQLTAyaTYIGMAVLGSFYVITGAIVVGQL--QAFiqyiwqisQPMGNVTQLSSVLQSASAATKRVFEILDEP 326
Cdd:TIGR02857 235 ELfatlsVALVA--VYIGFRLLAGDLDLATGLFVLLLapEFY--------LPLRQLGAQYHARADGVAAAEALFAVLDAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 327 EEKEnKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG 406
Cdd:TIGR02857 305 PRPL-AGKAPVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 407 IDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQ 486
Cdd:TIGR02857 384 VPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQ 463
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 487 KQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVM 552
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
72-578 |
7.28e-74 |
|
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: 249.66 E-value: 7.28e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 72 ITVVGIG----YCISQLLSGV---LMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTND---VDAVSGALQ 141
Cdd:TIGR01193 195 LGIISIGliiaYIIQQILSYIqifLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDAssiIDALASTIL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 142 QAFIGivnaiLGITLAAAMMFYIQPM-MALISMIMIPTS---IWISKRVINASQKyfQSMQNSlGELNGYVQENMTGFSV 217
Cdd:TIGR01193 275 SLFLD-----MWILVIVGLFLVRQNMlLFLLSLLSIPVYaviIILFKRTFNKLNH--DAMQAN-AVLNSSIIEDLNGIET 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 218 LKVYGREKETlegFKKVNH--------SLKYFgfRAAFISGLMMPLVQLTayatyIGMAVL--GSFYVITGAIVVGQLQA 287
Cdd:TIGR01193 347 IKSLTSEAER---YSKIDSefgdylnkSFKYQ--KADQGQQAIKAVTKLI-----LNVVILwtGAYLVMRGKLTLGQLIT 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 288 FIQYIWQISQPMGNVTQLSSVLQSASAATKRVFEILDEPEEKENKVDVSLPETILGDVTFDHVDFAYDPKKPLIQDLNFE 367
Cdd:TIGR01193 417 FNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 368 VKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFG-KLDA 446
Cdd:TIGR01193 497 IKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENV 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 447 TDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEaliQKAMDR 526
Cdd:TIGR01193 577 SQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 527 V--MEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKLYN 578
Cdd:TIGR01193 654 LlnLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-561 |
6.52e-71 |
|
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: 227.47 E-value: 6.52e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDP-KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLF 421
Cdd:cd03245 1 GRIEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKG 561
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
8-540 |
3.66e-62 |
|
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: 214.15 E-value: 3.66e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 8 LKRLARYIRPYRGTFLLVILFTVLTVAFNVALPYVTG-LptteISRNIANGESInfsYIFKCLIWITVVGIGYCISQLLS 86
Cdd:TIGR02868 1 LLRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAwL----ISRAAEMPPVL---YLSVAAVAVRAFGIGRAVFRYLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 87 GVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVS----------------GALQQAFIGIVNA 150
Cdd:TIGR02868 74 RLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQdlyvrvivpagvalvvGAAAVAAIAVLSV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 151 ILGITLAAammfyiqpmMALISMIMIPtsiWISKRVINASQkyfQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEG 230
Cdd:TIGR02868 154 PAALILAA---------GLLLAGFVAP---LVSLRAARAAE---QALARLRGELAAQLTDALDGAAELVASGALPAALAQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 231 FKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAI--------VVGQLQAFiqyiwqisQPMGNV 302
Cdd:TIGR02868 219 VEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLapvtlavlVLLPLAAF--------EAFAAL 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 303 TQLSSVLQSASAATKRVFEILDEPEEKENKVD----VSLPETIlgDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVG 378
Cdd:TIGR02868 291 PAAAQQLTRVRAAAERIVEVLDAAGPVAEGSApaagAVGLGKP--TLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 379 PTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTA 458
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 459 NVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAH 538
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
..
gi 488239013 539 RL 540
Cdd:TIGR02868 529 HL 530
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-319 |
7.19e-60 |
|
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: 201.08 E-value: 7.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLpttEISRNIANGeSINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKR---AIDDYIVPG-QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-319 |
8.74e-59 |
|
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: 198.04 E-value: 8.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTTEIsrnIANGesiNFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV---IGGG---LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18542 75 RNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18542 155 FSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSG 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18542 235 LQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-557 |
8.15e-58 |
|
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: 193.07 E-value: 8.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 338 PETILGDVTFDHVDFAYD--PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRS 415
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 416 DVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARA 495
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 496 VVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQI 557
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
309-569 |
3.77e-57 |
|
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: 201.13 E-value: 3.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 309 LQSASAATKRVFEILDEPEEKENKVDVSLPEtilGDVTFDHVDFAYdP--KKPLIQDLNFEVKAGQTVAVVGPTGAGKTT 386
Cdd:COG4618 298 FVSARQAYRRLNELLAAVPAEPERMPLPRPK---GRLSVENLTVVP-PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKST 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 387 LINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNI-RFGklDATDYEVVDAAKTANVDHFIR 465
Cdd:COG4618 374 LARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMIL 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 466 TMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIR 544
Cdd:COG4618 452 RLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLA 531
|
250 260
....*....|....*....|....*
gi 488239013 545 DADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:COG4618 532 AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
22-319 |
9.99e-56 |
|
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: 190.07 E-value: 9.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLpttEISRNIANGesiNFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKL---LIDDVIPAG---DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd07346 75 RRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd07346 155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd07346 235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
22-319 |
1.08e-54 |
|
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: 187.29 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLpttEISRNIANGesiNFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKI---AIDEYIPNG---DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTay 261
Cdd:cd18545 156 VVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELI-- 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 262 aTYIGMAVL---GSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18545 234 -SALGTALVywyGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
324-580 |
1.14e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 195.06 E-value: 1.14e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 324 DEPEEKENKVDVSLPETILGDvtfDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRF--YdvdKGA 401
Cdd:PRK11174 333 AHPQQGEKELASNDPVTIEAE---DLEILSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 402 IRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDN 481
Cdd:PRK11174 406 LKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 482 VSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKG 561
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
|
250 260
....*....|....*....|
gi 488239013 562 THESLLAQGG-FYEKLYNSQ 580
Cdd:PRK11174 566 DYAELSQAGGlFATLLAHRQ 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
88-571 |
6.77e-53 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 195.58 E-value: 6.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 88 VLMTN---VVQSAMHDLRR---DIEEKINRLPVSYFDKNQQGNILSRVTNDVdavsGALQQAFIGIVNAILGITLAAAMM 161
Cdd:PLN03232 966 VTFTNsfwLISSSLHAAKRlhdAMLNSILRAPMLFFHTNPTGRVINRFSKDI----GDIDRNVANLMNMFMNQLWQLLST 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 162 FYIQPMMALISMIMI-PTSIwiskrVINASQKYFQSMQNSLGELNG------YVQ--ENMTGFSVLKVY----------G 222
Cdd:PLN03232 1042 FALIGTVSTISLWAImPLLI-----LFYAAYLYYQSTSREVRRLDSvtrspiYAQfgEALNGLSSIRAYkaydrmakinG 1116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 223 REKETLEGFKKVN-HSLKYFGFRAAFISGLMMPLVqltayATYigmAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGN 301
Cdd:PLN03232 1117 KSMDNNIRFTLANtSSNRWLTIRLETLGGVMIWLT-----ATF---AVLRNGNAENQAGFASTMGLLLSYTLNITTLLSG 1188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 302 VTQLSSVLQSASAATKRVFEILDEPEE-----KENKVDVSLPETilGDVTFDHVDFAYDPK-KPLIQDLNFEVKAGQTVA 375
Cdd:PLN03232 1189 VLRQASKAENSLNSVERVGNYIDLPSEataiiENNRPVSGWPSR--GSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVG 1266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 376 VVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIR-FGklDATDYEVVDA 454
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFS--EHNDADLWEA 1344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 455 AKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSF 534
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
|
490 500 510
....*....|....*....|....*....|....*..
gi 488239013 535 VIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
22-319 |
7.85e-53 |
|
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: 182.23 E-value: 7.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTTEISRNiangeSINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAG-----TLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
7-571 |
3.41e-52 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 193.42 E-value: 3.41e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 7 SLKRLARYIRPYRGTFLLVILFT--VLTVAFNVAlpyvtglPTTEISRNIANGESINFSYIFKCLIWITVVGIGYCISQL 84
Cdd:PLN03130 900 SWKVLERYKNALGGAWVVMILFLcyVLTEVFRVS-------SSTWLSEWTDQGTPKTHGPLFYNLIYALLSFGQVLVTLL 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 85 LSGVLMTNVVQSA--MHDLRRDieeKINRLPVSYFDKNQQGNILSRV---TNDVDA-----VSGALQQAF--------IG 146
Cdd:PLN03130 973 NSYWLIMSSLYAAkrLHDAMLG---SILRAPMSFFHTNPLGRIINRFakdLGDIDRnvavfVNMFLGQIFqllstfvlIG 1049
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 147 IVNAIlgiTLAAAMmfyiqPMMALISmimiptsiwiskrvinASQKYFQSMQNSLGELNG------YVQ--ENMTGFSVL 218
Cdd:PLN03130 1050 IVSTI---SLWAIM-----PLLVLFY----------------GAYLYYQSTAREVKRLDSitrspvYAQfgEALNGLSTI 1105
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 219 KVY----------GREKETLEGFKKVNHSL-KYFGFRAAFISGLMmplVQLTAyatyiGMAVLGSFYVITGAIVVGQLQA 287
Cdd:PLN03130 1106 RAYkaydrmaeinGRSMDNNIRFTLVNMSSnRWLAIRLETLGGLM---IWLTA-----SFAVMQNGRAENQAAFASTMGL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 288 FIQYIWQISQPMGNVTQLSSVLQSASAATKRVFEILDEPEE-----KENKVDVSLPETilGDVTFDHVDFAYDPK-KPLI 361
Cdd:PLN03130 1178 LLSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEaplviENNRPPPGWPSS--GSIKFEDVVLRYRPElPPVL 1255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIadniRF 441
Cdd:PLN03130 1256 HGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTV----RF 1331
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 gKLDA----TDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLE 517
Cdd:PLN03130 1332 -NLDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 518 ALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:PLN03130 1411 ALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-562 |
9.84e-52 |
|
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: 176.45 E-value: 9.84e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 338 PETilGDVTFDHVDFAYDPKKP-LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSD 416
Cdd:cd03369 2 PEH--GEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQDAWLYQGTIADNI-RFGKLDatDYEVVDAAKtanvdhfirtmpdgyempINAEGDNVSLGQKQLLTIARA 495
Cdd:cd03369 80 LRSSLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 496 VVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-580 |
4.18e-51 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 185.03 E-value: 4.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 122 QGNILSRVTNDVDA-----------------VSGALQqAFIGIVNAILGITLAAAMmfyiqpmmaLISMIMIPTSIWisk 184
Cdd:PRK11160 116 QGDLLNRLVADVDTldhlylrlisplvaalvVILVLT-IGLSFFDLTLALTLGGIL---------LLLLLLLPLLFY--- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 185 rviNASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATY 264
Cdd:PRK11160 183 ---RLGKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTV 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 265 IGMAVLGSFYV----ITGA----IVVGQLQAFiqyiwQISQPMGNVTQ-LSSVLQSAsaatKRVFEILD-EPEEKENKVd 334
Cdd:PRK11160 260 VLMLWLAAGGVggnaQPGAlialFVFAALAAF-----EALMPVAGAFQhLGQVIASA----RRINEITEqKPEVTFPTT- 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 335 vSLPETILGDVTFDHVDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS 413
Cdd:PRK11160 330 -STAAADQVSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 414 RSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTmPDGYEMPINAEGDNVSLGQKQLLTIA 493
Cdd:PRK11160 409 EAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIA 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFY 573
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRY 567
|
....*..
gi 488239013 574 EKLYNSQ 580
Cdd:PRK11160 568 YQLKQRL 574
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-573 |
1.03e-50 |
|
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: 189.00 E-value: 1.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 21 TFLLVILF---TVLTVAFNVALPYVTGLPtteisrnIANGESINFSY---IFKCL-IWITVVGIGYCISQLLSGVLMTNV 93
Cdd:TIGR00957 967 TFLSIFLFvcnHVSALASNYWLSLWTDDP-------MVNGTQNNTSLrlsVYGALgILQGFAVFGYSMAVSIGGIQASRV 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 94 vqsamhdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQ-------AFIGIVNAILGITLAAAMMFYIQP 166
Cdd:TIGR00957 1040 -------LHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPvikmfmgSLFNVIGALIVILLATPIAAVIIP 1112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 167 MMALISMIMiptsiwisKRVINASQKYFQSMQN-SLGELNGYVQENMTGFSVLKVYGREKetlegfkkvnhslkyfgfRA 245
Cdd:TIGR00957 1113 PLGLLYFFV--------QRFYVASSRQLKRLESvSRSPVYSHFNETLLGVSVIRAFEEQE------------------RF 1166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 246 AFISGLMMPLVQLTAYATYI-------GMAVLGSFYVITGAI--VVGQ--LQA-----FIQYIWQISQPMGNVTQLSSVL 309
Cdd:TIGR00957 1167 IHQSDLKVDENQKAYYPSIVanrwlavRLECVGNCIVLFAALfaVISRhsLSAglvglSVSYSLQVTFYLNWLVRMSSEM 1246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 310 QSASAATKRVFEILDEPEEKENKVDVSLPETI---LGDVTFDHVDFAYDPKKPLI-QDLNFEVKAGQTVAVVGPTGAGKT 385
Cdd:TIGR00957 1247 ETNIVAVERLKEYSETEKEAPWQIQETAPPSGwppRGRVEFRNYCLRYREDLDLVlRHINVTIHGGEKVGIVGRTGAGKS 1326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 386 TLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIR-FGKLdaTDYEVVDAAKTANVDHFI 464
Cdd:TIGR00957 1327 SLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFV 1404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 465 RTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIR 544
Cdd:TIGR00957 1405 SALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIM 1484
|
570 580 590
....*....|....*....|....*....|
gi 488239013 545 DADLILVMDQGQIIEKGTHESLLAQGG-FY 573
Cdd:TIGR00957 1485 DYTRVIVLDKGEVAEFGAPSNLLQQRGiFY 1514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
70-575 |
1.41e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 188.70 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 70 IWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFD--KNQQGNILSRVTNDVDAVSGALQQAFIGI 147
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 148 VNAILGITLAAAMMFYIQPMMA--LISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGY-------------VQENM 212
Cdd:PTZ00265 950 THFIVLFLVSMVMSFYFCPIVAavLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAF 1029
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 213 TGFSVLKVYGREK---ETLEgfKKVNHSLKYFGfRAAFISGLMMPLVQ-----LTAYATYigmavLGSFYVITGAIVVGQ 284
Cdd:PTZ00265 1030 YNMNTVIIYGLEDyfcNLIE--KAIDYSNKGQK-RKTLVNSMLWGFSQsaqlfINSFAYW-----FGSFLIRRGTILVDD 1101
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 285 -LQAFIQYIWQISQPmGNVTQLSSVLQSASAATKRVFEILDEPE----EKENKVDVSLPETILGDVTFDHVDFAY--DPK 357
Cdd:PTZ00265 1102 fMKSLFTFLFTGSYA-GKLMSLKGDSENAKLSFEKYYPLIIRKSnidvRDNGGIRIKNKNDIKGKIEIMDVNFRYisRPN 1180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDV---------------------------------------- 397
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsl 1260
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 398 --------------DKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHF 463
Cdd:PTZ00265 1261 tkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEF 1340
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 464 IRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLS 541
Cdd:PTZ00265 1341 IESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIA 1420
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 488239013 542 TIRDADLILVMDQ----GQIIE-KGTHESLL-AQGGFYEK 575
Cdd:PTZ00265 1421 SIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVYKK 1460
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
22-319 |
1.04e-49 |
|
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: 173.76 E-value: 1.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTG--LPTTEISRNIangesinfSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMH 99
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKplLDDIFVEKDL--------EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTS 179
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 180 IWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLT 259
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 260 AYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
22-319 |
2.60e-48 |
|
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: 169.92 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGlpttEISRNIANGESINFSyifkcLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVK----NLIDALSAGGSSGGL-----LALLVALFLLQAVLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-319 |
1.72e-46 |
|
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: 165.38 E-value: 1.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTTEIsrNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDV--LIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18563 79 RRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18563 159 GSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18563 239 LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-319 |
1.89e-44 |
|
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: 159.62 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTteisrNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELV-----DLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP---- 177
Cdd:cd18778 76 RSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPflal 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 TSIWISKRVinasQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQ 257
Cdd:cd18778 156 GAWLYSKKV----RPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLME 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 258 LTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18778 232 FLTSLGTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
22-319 |
4.58e-44 |
|
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: 158.72 E-value: 4.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGlptTEISRNIANGesiNFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMA---DIIDEGIANG---DLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP---- 177
Cdd:cd18548 75 RKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPilal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 TSIWISKRVInasqKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQ 257
Cdd:cd18548 155 VVFLIMKKAI----PLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMM 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 258 LTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18548 231 LIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
350-557 |
5.59e-44 |
|
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: 154.30 E-value: 5.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 350 VDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDA 428
Cdd:cd03246 6 VSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 429 WLYQGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKILILDEA 508
Cdd:cd03246 86 ELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488239013 509 TSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRDADLILVMDQGQI 557
Cdd:cd03246 124 NSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
50-580 |
9.26e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 168.28 E-value: 9.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 50 ISRNIANGESINfSYIFKcliwITVVGIGYCISQLLSGVLMTNVVQSAMHDLrrdieeKINRLPVSYFDKNQ--QGNILS 127
Cdd:PTZ00265 86 IMKNMNLGENVN-DIIFS----LVLIGIFQFILSFISSFCMDVVTTKILKTL------KLEFLKSVFYQDGQfhDNNPGS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 128 RVTNDVDAVsgaLQQAFIGIVNAILGI-TLAAAMM-FYIQPMMALISMIMIPTS----IWISKRVINASQKYfqSMQNSL 201
Cdd:PTZ00265 155 KLTSDLDFY---LEQVNAGIGTKFITIfTYASAFLgLYIWSLFKNARLTLCITCvfplIYICGVICNKKVKI--NKKTSL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 202 GELN---GYVQENMTGFSVLKVYGREKETLegfKKVNHSLKYFG---FRAAFISGLMMPLVQLTAYATYIGMAVLGSFYV 275
Cdd:PTZ00265 230 LYNNntmSIIEEALVGIRTVVSYCGEKTIL---KKFNLSEKLYSkyiLKANFMESLHIGMINGFILASYAFGFWYGTRII 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 276 IT------------GAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQsasaATKRVFEILDEPEEKENKVD-VSLPEtiL 342
Cdd:PTZ00265 307 ISdlsnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLE----ATNSLYEIINRKPLVENNDDgKKLKD--I 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDPKK--PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRI-DGIDTKSMSRSDVRS 419
Cdd:PTZ00265 381 KKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRS 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 420 LFGMVLQDAWLYQGTIADNIRFG--------------------------------------------KLDAT-------- 447
Cdd:PTZ00265 461 KIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnTTDSNeliemrkn 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 448 -----DYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQK 522
Cdd:PTZ00265 541 yqtikDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 523 AMDRVM--EGRTSFVIAHRLSTIRDADLILVMDQGQ-------------------------------------------- 556
Cdd:PTZ00265 621 TINNLKgnENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinna 700
|
650 660
....*....|....*....|....*...
gi 488239013 557 ---IIEKGTHESLLA-QGGFYEKLYNSQ 580
Cdd:PTZ00265 701 gsyIIEQGTHDALMKnKNGIYYTMINNQ 728
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
345-576 |
2.52e-43 |
|
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: 154.41 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMV 424
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAW--LYQGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAV 496
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpenlGLPREEIRerVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 497 VSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQggfYE 574
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSD---YE 226
|
..
gi 488239013 575 KL 576
Cdd:COG1122 227 LL 228
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
22-299 |
4.34e-43 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 155.49 E-value: 4.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLptteISRNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGR----ILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPM 299
Cdd:pfam00664 237 LSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
343-569 |
2.12e-42 |
|
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: 153.14 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDPK-KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLF 421
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQGTIADNIRfGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-319 |
1.05e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 146.86 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 19 RGTFLLVILFTVLTVAFNVALPYVTGLPtteISRNIANGESINFS-YIFKCLIWITVVGIGYCISQLLSGVLMTNVvqsa 97
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYA---IDHFITPGTLDGLTgFILLYLGLILIQALSVFLFIRLAGKIEMGV---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 98 MHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP 177
Cdd:cd18540 74 SYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 ----TSIWISKRVINASQKYFQsmQNSlgELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMM 253
Cdd:cd18540 154 vlavVSIYFQKKILKAYRKVRK--INS--RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFL 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 254 PLVQLtayATYIGMA---VLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18540 230 PIVLF---LGSIATAlvlWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
345-569 |
1.00e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 142.12 E-value: 1.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRsDVRSLFGMV 424
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA-EVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLYQG-TIADNIRF-GKLDATDYEVVDAA-----KTANVDHFIRTMPDGYempinaegdnvSLGQKQLLTIARAVV 497
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARLYGLPRKEARERidellELFGLTDAADRKVGTL-----------SGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 498 SDPKILILDEATSSVD--TRLE--ALIQKAMDrvmEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:COG1131 148 HDPELLILDEPTSGLDpeARRElwELLRELAA---EGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-566 |
6.04e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 150.70 E-value: 6.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 16 RPYRGTFLLVILFT-VLTVAFNVALpyvtglptteiSRNIANGESI-NFSYIFKCLIWITVVGIGYCISQLLSGVLMtNV 93
Cdd:PTZ00243 961 LHAAGFVLATFAVTeLVTVSSGVWL-----------SMWSTRSFKLsAATYLYVYLGIVLLGTFSVPLRFFLSYEAM-RR 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 94 VQSAMHdlrRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQP--MMALI 171
Cdd:PTZ00243 1029 GSRNMH---RDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPfvLVALV 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 172 SMIMIPTSIWISKRVINASQKYFQSMQNSlgELNGYVQENMTGFSVLKVYGREKETL-EGFKKV----------NHSLKY 240
Cdd:PTZ00243 1106 PCGYLYYRLMQFYNSANREIRRIKSVAKS--PVFTLLEEALQGSATITAYGKAHLVMqEALRRLdvvyscsyleNVANRW 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 241 FGFRAAFISGLMMPLVQLTAyatyIGMAVLGSFYVITGAIVVG-----QLQAFIQYIwqisqpmgnVTQLSSVlQSASAA 315
Cdd:PTZ00243 1184 LGVRVEFLSNIVVTVIALIG----VIGTMLRATSQEIGLVSLSltmamQTTATLNWL---------VRQVATV-EADMNS 1249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 316 TKRVFEILDE------PEEKEnKVD------------------------VSLPETIL-GDVTFDHVDFAYDPKKPLI-QD 363
Cdd:PTZ00243 1250 VERLLYYTDEvphedmPELDE-EVDalerrtgmaadvtgtvviepasptSAAPHPVQaGSLVFEGVQMRYREGLPLVlRG 1328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 364 LNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNIR-Fg 442
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDpF- 1407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 443 kLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILIL-DEATSSVDTRLEALIQ 521
Cdd:PTZ00243 1408 -LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQ 1486
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 488239013 522 KAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESL 566
Cdd:PTZ00243 1487 ATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
26-319 |
8.38e-38 |
|
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: 141.47 E-value: 8.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGLPTteisrNIANGESINFSYIFKCLIWITVVGIGYCISqLLSGVLMTNVVQSAMHDLRRDI 105
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAGQLI-----DAALGGGDTASLNQIALLLLGLFLLQAVFS-FFRIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP----TSIW 181
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPvvvlVAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVinasQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAY 261
Cdd:cd18576 156 FGRRI----RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLF 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 262 ATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18576 232 GAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-556 |
1.66e-37 |
|
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: 137.60 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPK----KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIridgidtkSMSRSdvrsl 420
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSV--------SVPGS----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQDAWLYQGTIADNIRFGK-LDATDYE-VVDAAkTANVDhfIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVS 498
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEERYEkVIKAC-ALEPD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 499 DPKILILDEATSSVDTRLEA-----LIQKAMdrvMEGRTSFVIAHRLSTIRDADLILVMDQGQ 556
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
22-319 |
4.50e-37 |
|
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: 139.55 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGlptTEISRNIANGesiNFSYIFK-CLIWITVVGIGYCISQLlsGVLMTNVV-QSAMH 99
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVR---YGIDSGVRAG---DLGVLLLaAAAYLAVVLAGWVAQRA--QTRLTGRTgERLLY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTS 179
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 180 IWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLT 259
Cdd:cd18546 153 ALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 260 AYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18546 233 GNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
361-510 |
1.80e-36 |
|
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: 133.16 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQG-TIADNI 439
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 440 RFGkldATDYEVVDAAKTANVDHFIRTMPDGYEM--PINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDLAdrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
22-319 |
5.47e-36 |
|
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: 136.46 E-value: 5.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPtteISRNIANGesiNFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRA---IDGPIAHG---DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILgITLAAAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLT-LVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRvinASQKYF---QSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQL 258
Cdd:cd18543 154 VARR---FRRRYFpasRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 259 TAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
346-571 |
2.00e-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: 133.44 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 346 TFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLfGMVL 425
Cdd:COG4555 3 EVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 QDAWLYQG-TIADNIRFgklDATDYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:COG4555 81 DERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 505 LDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-319 |
2.16e-35 |
|
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: 134.92 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVT------GLPTTEISRniangesinfsyifkcLIWITVVGIGYCISQLLSGVL---MTN 92
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLreiiddALPQGDLGL----------------LVLLALGMVAVAVASALLGVVqtyLSA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 93 VV-QSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALI 171
Cdd:cd18550 65 RIgQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 172 SMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQE--NMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFIS 249
Cdd:cd18550 145 SLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 250 GLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18550 225 RWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
345-559 |
4.34e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL---F 421
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQG-TIADNIRFGkLDATDYEVVDAAKTA-------NVDHFIRTMPdgyempinaegDNVSLGQKQLLTIA 493
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALP-LRVTGKSRKEIRRRVrevldlvGLSDKAKALP-----------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 494 RAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIRDADL-ILVMDQGQIIE 559
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
345-567 |
6.14e-35 |
|
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: 132.47 E-value: 6.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMV 424
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAwlyqgTIADNI---------------RFGKLDATDYEVVDAA-KTANVDHFIrtmpdgyEMPInaegDNVSLGQKQ 488
Cdd:COG1120 81 PQEP-----PAPFGLtvrelvalgryphlgLFGRPSAEDREAVEEAlERTGLEHLA-------DRPV----DELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 489 LLTIARAVVSDPKILILDEATSSVD----TRLEALIQKAMDRvmEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTH 563
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARE--RGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 488239013 564 ESLL 567
Cdd:COG1120 223 EEVL 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
347-556 |
1.17e-34 |
|
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: 130.28 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVL 425
Cdd:cd03225 2 LKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 QDA--WLYQGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVV 497
Cdd:cd03225 82 QNPddQFFGPTVEEEVAFGlenlGLPEEEIEerVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 498 SDPKILILDEATSSVD----TRLEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQ 556
Cdd:cd03225 151 MDPDILLLDEPTAGLDpagrRELLELLKKLKA---EGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-569 |
1.81e-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: 136.96 E-value: 1.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKP----LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL 420
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 ---FGMVLQDAwlYQG-----TIADNIRFGkLDAtdYEVVDAAK-TANVDHFIRT---MPDGYEMPINAegdnVSLGQKQ 488
Cdd:COG1123 341 rrrVQMVFQDP--YSSlnprmTVGDIIAEP-LRL--HGLLSRAErRERVAELLERvglPPDLADRYPHE----LSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 489 LLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHES 565
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491
|
....
gi 488239013 566 LLAQ 569
Cdd:COG1123 492 VFAN 495
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-319 |
1.27e-33 |
|
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: 130.32 E-value: 1.27e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALP--------YVTGLPTTEISRNIANGESINFSYIFkCLIWITVVGIGYC--ISQLLSGVLMT 91
Cdd:cd18564 1 LALALLALLLETALRLLEPwplkvvidDVLGDKPLPGLLGLAPLLGPDPLALL-LLAAAALVGIALLrgLASYAGTYLTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 92 NVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALI 171
Cdd:cd18564 80 LVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 172 SMIMIP----TSIWISKRVINASQKyfQSMQNslGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNH-SLKYfGFRAA 246
Cdd:cd18564 160 ALAVAPllllAARRFSRRIKEASRE--QRRRE--GALASVAQESLSAIRVVQAFGREEHEERRFARENRkSLRA-GLRAA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 247 FISGLMMPLVQ-LTAYATyigMAVL--GSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18564 235 RLQALLSPVVDvLVAVGT---ALVLwfGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
347-561 |
4.35e-33 |
|
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: 126.14 E-value: 4.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDV-----DKGAIRIDG--IDTKSMSRSDVRS 419
Cdd:cd03260 3 LRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGkdIYDLDVDVLELRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 420 LFGMVLQDAWLYQGTIADNIRFG-KL------DATDYEVVDAAKTANvdhfirtMPDgyEMPINAEGDNVSLGQKQLLTI 492
Cdd:cd03260 82 RVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAA-------LWD--EVKDRLHALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKG 561
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFG 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
359-561 |
4.71e-33 |
|
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: 126.08 E-value: 4.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS---RSDVRSLFGMVLQDA------W 429
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPmsslnpR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LyqgTIADNIRFGKLDATDYEVVDAAKTA---------NVDHFIRTMPdgYEMpinaegdnvSLGQKQLLTIARAVVSDP 500
Cdd:cd03257 99 M---TIGEQIAEPLRIHGKLSKKEARKEAvllllvgvgLPEEVLNRYP--HEL---------SGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03257 165 KLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
346-556 |
5.44e-33 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.89 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 346 TFDHVDFAYdPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVL 425
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 QdawlyqgtiadnirfgkldatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKILIL 505
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488239013 506 DEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRDA-DLILVMDQGQ 556
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-569 |
7.21e-33 |
|
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: 132.33 E-value: 7.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDP-KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD---KGAIRIDGIDTKSMSRSDVRSL 420
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQDAW--LYQGTIADNIRFGKL------DATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTI 492
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALEnlglsrAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
345-561 |
9.69e-33 |
|
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: 123.58 E-value: 9.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPK-KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSdVRSLFGM 423
Cdd:cd03247 1 LSINNVSFSYPEQeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDAWLYQGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyempinaeGDNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKG 561
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
357-557 |
1.88e-32 |
|
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: 122.89 E-value: 1.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSmSRSDVRSLFGMVLQDAWLYQG-TI 435
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYENlTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFgkldatdyevvdaaktanvdhfirtmpdgyempinaegdnvSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:cd03230 91 RENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488239013 516 LEALIQKAMDR-VMEGRTSFVIAHRLSTIRD-ADLILVMDQGQI 557
Cdd:cd03230 130 SRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
345-568 |
6.13e-32 |
|
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: 123.55 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKkPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSD---VRSLF 421
Cdd:COG1127 6 IEVRNLTKSFGDR-VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQG-TIADNIRF-----GKLDATD-YEVVDAA-KTANVDHFIRTMPdgyempinAEgdnVSLGQKQLLTIA 493
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFplrehTDLSEAEiRELVLEKlELVGLPGAADKMP--------SE---LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVD----TRLEALIQKAMDRVmeGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
345-568 |
3.24e-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: 121.45 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL---F 421
Cdd:cd03261 1 IELRGLTKSFGGRTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQG-TIADNIRF-----GKLDATDYEVVDAAKTANV--DHFIRTMPdgyempinaegDNVSLGQKQLLTIA 493
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKLEAVglRGAEDLYP-----------AELSGGMKKRVALA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVD----TRLEALIQKAMDrvMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
345-566 |
4.01e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 121.35 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKsmsrsDVRSLFGMV 424
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-----RARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDA---WLY---------QGTIADNIRFGKLDATDYEVVDAA-KTANVDHFIRTmpdgyemPINAegdnVSLGQKQLLT 491
Cdd:COG1121 81 PQRAevdWDFpitvrdvvlMGRYGRRGLFRRPSRADREAVDEAlERVGLEDLADR-------PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 492 IARAVVSDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPPEEVL 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-561 |
8.31e-31 |
|
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: 119.55 E-value: 8.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSM--SRSDVrslfG 422
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppERRNI----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLYQG-TIADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPDGyempinaegdnVSLGQKQLLTIARA 495
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 496 VVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLS-TIRDADLILVMDQGQIIEKG 561
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
345-569 |
1.38e-30 |
|
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: 119.61 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKK---PLIQDLNFEVKAGQTVAVVGPTGAGKTTL---INLLMRFydvDKGAIRIDGIDTKSMSRSDVR 418
Cdd:cd03258 2 IELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERP---TSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 419 SL---FGMVLQDAWLYQG-TIADNIRFG-KLDATDYEVVDAAktanVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIA 493
Cdd:cd03258 79 KArrrIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEER----VLELLELV--GLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVD---TR-LEALIQKAMDRVmeGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:cd03258 153 RALANNPKVLLCDEATSALDpetTQsILALLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 488239013 569 Q 569
Cdd:cd03258 231 N 231
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
81-319 |
2.08e-30 |
|
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: 121.13 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 81 ISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAM 160
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 161 MFYIQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKvnHSLKY 240
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVAD--ASEEY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 241 F--GFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVI------TGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSA 312
Cdd:cd18565 227 RdaNWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLdgpplfTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRA 306
|
....*..
gi 488239013 313 SAATKRV 319
Cdd:cd18565 307 MASAKRV 313
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
347-555 |
4.03e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.63 E-value: 4.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksMSRSDVRSLFGMVLQ 426
Cdd:cd03235 2 VEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 DA---WLYQGTIADNIR---------FGKLDATDYEVVDAA-KTANVDHFIrtmpdgyEMPInaegDNVSLGQKQLLTIA 493
Cdd:cd03235 76 RRsidRDFPISVRDVVLmglyghkglFRRLSKADKAKVDEAlERVGLSELA-------DRQI----GELSGGQQQRVLLA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 494 RAVVSDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRD-ADLILVMDQG 555
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-575 |
1.10e-29 |
|
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: 125.02 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 13 RYIRPYRG-TFLLVILFTVLTV---AFNVALPYVTGLPTTEISRNIANGESINFSYIFKCLI------WITVVGIGYCIS 82
Cdd:TIGR01271 858 RYITTNRNlVFVLIFCLVIFLAevaASLLGLWLITDNPSAPNYVDQQHANASSPDVQKPVIItptsayYIFYIYVGTADS 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 83 QLLSGVL----MTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAA 158
Cdd:TIGR01271 938 VLALGFFrglpLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 159 AMMFYIQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREK--ETLegFKKV-- 234
Cdd:TIGR01271 1018 FVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSyfETL--FHKAln 1095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 235 NHSLKYFGFRAA---FISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMgnvtQLSSVLQS 311
Cdd:TIGR01271 1096 LHTANWFLYLSTlrwFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSI----DVDGLMRS 1171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 312 ASaatkRVFEILDEPEEK---ENKVDVSLPETIL--------------GDVTFDHVDFAY-DPKKPLIQDLNFEVKAGQT 373
Cdd:TIGR01271 1172 VS----RVFKFIDLPQEEprpSGGGGKYQLSTVLvienphaqkcwpsgGQMDVQGLTAKYtEAGRAVLQDLSFSVEGGQR 1247
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 374 VAVVGPTGAGKTTLINLLMRFYDVDkGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNirfgkLDA----TDY 449
Cdd:TIGR01271 1248 VGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-----LDPyeqwSDE 1321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 450 EVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME 529
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS 1401
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 488239013 530 GRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEK 575
Cdd:TIGR01271 1402 NCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
19-318 |
1.57e-29 |
|
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: 118.32 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 19 RGTFLLVILFTVLTVAFNVALPYvtglptteISRNIANG--ESINFSYIFkclIWITVVGIGYCISQLLS---------- 86
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPL--------IVRYIIDDllPSKNLRLIL---IIGAILLALYILRTLLNyfvtywghvm 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 87 GVLMTNvvqsamhDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQP 166
Cdd:cd18549 70 GARIET-------DMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 167 MMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSL-----KYF 241
Cdd:cd18549 143 PLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFleskkKAY 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 242 GFRAAFISG--LMMPLVQLTayatyigMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKR 318
Cdd:cd18549 223 KAMAYFFSGmnFFTNLLNLV-------VLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
348-561 |
1.98e-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: 114.45 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQd 427
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 awlyqgtiadnirfgkldatdyevvdAAKTANVDHFI-RTMpdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILD 506
Cdd:cd03214 81 --------------------------ALELLGLAHLAdRPF------------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 507 EATSSVD----TRLEALIQKAMDRvmEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKG 561
Cdd:cd03214 123 EPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
345-568 |
2.08e-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: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMV 424
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLY-QGTIADNIrfgKLDATDYEVVDAAKTANVDHFIRTM---PDGYempINAEGDNVSLGQKQLLTIARAVVSDP 500
Cdd:cd03295 81 IQQIGLFpHMTVEENI---ALVPKLLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 501 KILILDEATSSVD--TRLEalIQKAMDRVME--GRTSFVIAHRL-STIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:cd03295 155 PLLLMDEPFGALDpiTRDQ--LQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
345-559 |
4.33e-29 |
|
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: 114.88 E-value: 4.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPK---KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDVRslF 421
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTGPGPD--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDA----WLyqgTIADNIRFGkLDATDyeVVDAAKTANVDHFIRTMP-DGYEmpiNAEGDNVSLGQKQLLTIARAV 496
Cdd:cd03293 76 GYVFQQDallpWL---TVLDNVALG-LELQG--VPKAEARERAEELLELVGlSGFE---NAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 497 VSDPKILILDEATSSVD--TR--LEALIQKAMDRvmEGRTSFVIAHRLS-TIRDADLILVMDQ--GQIIE 559
Cdd:cd03293 147 AVDPDVLLLDEPFSALDalTReqLQEELLDIWRE--TGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-576 |
5.25e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.16 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 48 TEISRNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGV------LMTNVVQSAMHDLRRDIEEKINRLPvsyfdknq 121
Cdd:PLN03232 325 SHLLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVgrvgfrLRSTLVAAIFHKSLRLTHEARKNFA-------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 122 QGNILSRVTNDVDAVSGALQQAFiGIVNAILGITLAAAMMfYIQPMMA-----LISMIMIPTSIWISKRVINASQKYFQS 196
Cdd:PLN03232 397 SGKVTNMITTDANALQQIAEQLH-GLWSAPFRIIVSMVLL-YQQLGVAslfgsLILFLLIPLQTLIVRKMRKLTKEGLQW 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 197 MQNSLGELNgyvqENMTGFSVLKVYGREKE---TLEGFKkvNHSLKYFgfRAA--------FISGLMMPLVQLTAYATYI 265
Cdd:PLN03232 475 TDKRVGIIN----EILASMDTVKCYAWEKSfesRIQGIR--NEELSWF--RKAqllsafnsFILNSIPVVVTLVSFGVFV 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 266 gmaVLGSFYVITGAIVVGQLQAFIQYiwqisqPMGNVTQLSSVLQSASAATKRVFEILdepeEKENKVDVSLPETILG-- 343
Cdd:PLN03232 547 ---LLGGDLTPARAFTSLSLFAVLRS------PLNMLPNLLSQVVNANVSLQRIEELL----LSEERILAQNPPLQPGap 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDPK--KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRfydvdkgaiRIDGIDTKSMsrsDVRSLF 421
Cdd:PLN03232 614 AISIKNGYFSWDSKtsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSV---VIRGSV 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQGTIADNIRFGkldaTDYEVVDAAKTANV---DHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVS 498
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFG----SDFESERYWRAIDVtalQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 499 DPKILILDEATSSVDTRL-EALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKL 576
Cdd:PLN03232 758 NSDIYIFDDPLSALDAHVaHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
26-319 |
1.36e-28 |
|
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: 115.35 E-value: 1.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGLPTTEISRniangeSINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDI 105
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIK------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 106 EEKINRLPVSYFDKNQQGNILSRVTNDV----DAVSGALQQAFIGIVNAILGItlaaAMMFYIQPMMALISMIMIPTSIW 181
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTsvlqSAVTDNLSQLLRNILQVIGGL----IILFILSWKLTLVLLLVIPLLLI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGF-KKVNHSLKYfGFRAAFISGLMMPLVQLTA 260
Cdd:cd18557 152 ASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYsEALDRSYRL-ARKKALANALFQGITSLLI 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 261 YATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18557 231 YLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
361-562 |
1.58e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 114.37 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDV------RS-----LFG------- 422
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlgiaRTfqnprLFPeltvlen 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 -MVLQDAWLYQGTIADNIRFGKLDATDYEVVDAAktanvDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:COG0411 100 vLVAAHARLGRGLLAALLRLPRARREEREARERA-----EELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPK 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 502 ILILDEAT---SSVDT-RLEALIQKAMDRvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGT 562
Cdd:COG0411 173 LLLLDEPAaglNPEETeELAELIRRLRDE--RGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
26-317 |
1.78e-28 |
|
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: 114.95 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGlptTEISRNIANGESINFSYIFKCLiwiTVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDI 105
Cdd:cd18572 2 FVFLVVAALSELAIPHYTG---AVIDAVVADGSREAFYRAVLLL---LLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIWISKR 185
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 186 VINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYI 265
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488239013 266 GMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNV-TQLSSVLQSASAATK 317
Cdd:cd18572 236 LVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLgDVFSSLMQAVGAAEK 288
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-575 |
2.63e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 114.32 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAYDP-KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVL 425
Cdd:PRK13632 10 VENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 Q--DAWLYQGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVV 497
Cdd:PRK13632 90 QnpDNQFIGATVEDDIAFGlenkKVPPKKMKdiIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 498 SDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA--HRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEK 575
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
173-586 |
3.02e-28 |
|
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: 120.82 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 173 MIMIPTSIWISKRVINASQKYFQSMQNSLGELNgyvqENMTGFSVLKVYGRE---KETLEGFK----KVNHSLKYFGFRA 245
Cdd:TIGR00957 468 VLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMN----EILNGIKVLKLYAWElafLDKVEGIRqeelKVLKKSAYLHAVG 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 246 AFISGLMMPLVQLTAYATYIgmavlgsfYVITGAIVVGQlQAFIQY-IWQISQ-PMGNVTQLSSVLQSASAATKRVFEIL 323
Cdd:TIGR00957 544 TFTWVCTPFLVALITFAVYV--------TVDENNILDAE-KAFVSLaLFNILRfPLNILPMVISSIVQASVSLKRLRIFL 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 324 D----EPEEKENKvdvSLPETILGDVTFDHVDFAY---DPkkPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYD 396
Cdd:TIGR00957 615 SheelEPDSIERR---TIKPGEGNSITVHNATFTWardLP--PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 397 VDKGAIRIDGIdtksmsrsdvrslFGMVLQDAWLYQGTIADNIRFGK-LDATDYEVVDAAKTANVDhfIRTMPDGYEMPI 475
Cdd:TIGR00957 690 KVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKaLNEKYYQQVLEACALLPD--LEILPSGDRTEI 754
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 476 NAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAM---DRVMEGRTSFVIAHRLSTIRDADLILVM 552
Cdd:TIGR00957 755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVM 834
|
410 420 430
....*....|....*....|....*....|....*
gi 488239013 553 DQGQIIEKGTHESLLAQ-GGFYEKLYNSQFAEEAG 586
Cdd:TIGR00957 835 SGGKISEMGSYQELLQRdGAFAEFLRTYAPDEQQG 869
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-556 |
3.10e-28 |
|
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: 111.12 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYdPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFG 422
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLYQG-TIADNIRFGkldatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPK 501
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLS-TIRDADLILVMDQGQ 556
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
361-562 |
3.48e-28 |
|
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: 112.92 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMsRSDVRSLFGMV--LQDAWLYQG-TIAD 437
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGrtFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 NIRFG-----KLDATDYEVVDAAKTAN--VDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:cd03219 95 NVMVAaqartGSGLLLARARREEREARerAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 511 SVDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGT 562
Cdd:cd03219 173 GLN---PEETEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-578 |
7.85e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.97 E-value: 7.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTT---LINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL 420
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQ--DAWLYQGTIADNIRFGkldaTDYEVVDAAKTANVDHfiRTMPD-GYEMPINAEGDNVSLGQKQLLTIARAVV 497
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFG----LENRAVPRPEMIKIVR--DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRDADLILVMDQGQIIEKGT------HESLLAQ 569
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEMLKE 239
|
250
....*....|...
gi 488239013 570 GG----FYEKLYN 578
Cdd:PRK13640 240 IGldipFVYKLKN 252
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
345-559 |
1.26e-27 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.72 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKK---PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRsDVrslf 421
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-DR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDA----WLyqgTIADNIRFGkLDATDyeVVDAAKTANVDHFIRTMP-DGYE--MPinaegDNVSLGQKQLLTIAR 494
Cdd:COG1116 83 GVVFQEPallpWL---TVLDNVALG-LELRG--VPKAERRERARELLELVGlAGFEdaYP-----HQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 495 AVVSDPKILILDEATSSVD--TR--LEALIQKAMDRvmEGRTSFVIAH------RLstirdADLILVMDQ--GQIIE 559
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDalTRerLQDELLRLWQE--TGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-568 |
1.48e-27 |
|
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: 111.43 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDPK---KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMV 424
Cdd:COG1124 5 RNLSVSYGQGgrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDA-------WLYQGTIADNIRFGKLDATDYEVVDAAKTANVD-HFIRTMPDgyempinaegdNVSLGQKQLLTIARAV 496
Cdd:COG1124 85 FQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 497 VSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLLA 568
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-570 |
1.90e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.03 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAY-DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQ 426
Cdd:PRK13635 9 EHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 --DAWLYQGTIADNIRFG------KLDATDYEVVDAAKTANVDHFirtmpdgyempINAEGDNVSLGQKQLLTIARAVVS 498
Cdd:PRK13635 89 npDNQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDF-----------LNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 499 DPKILILDEATSSVDT--RLEAL--IQKAMDRvmEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQG 570
Cdd:PRK13635 158 QPDIIILDEATSMLDPrgRREVLetVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
361-569 |
2.01e-26 |
|
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: 108.88 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL----FGMVLQD-AWLYQGTI 435
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMPinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDtr 515
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP-----DELSGGMQQRVGLARALAVDPDILLMDEAFSALD-- 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 516 leALIQKAM-DRVME-----GRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:cd03294 193 --PLIRREMqDELLRlqaelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
348-558 |
2.31e-26 |
|
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: 106.57 E-value: 2.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDVRSLFGMVLQD 427
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 A--WLYQGTIADNIRFGKLDAtdyevvdAAKTANVDHFIRTmpdgyeMPINAEGD----NVSLGQKQLLTIARAVVSDPK 501
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKD------LDLYALKErhplSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-548 |
3.10e-26 |
|
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: 106.72 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDV---RSLF 421
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDA-WLYQGTIADNIRFGkLDATDY-------EVVDAAKTANVDHFIRTMPDGyempinaegdnVSLGQKQLLTIA 493
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFA-LEVTGVppreirkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 494 RAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-----------HRLSTIRDADL 548
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALERGKL 214
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
363-567 |
3.76e-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: 107.04 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSrSDVRSlFGMVLQDAWLY-QGTIADNIRF 441
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-PEKRD-ISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 G------KLDATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:cd03299 95 GlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 516 LEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLL 567
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
345-557 |
6.53e-26 |
|
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: 105.65 E-value: 6.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAY---DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLF 421
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 -----GMVLQDAWLYQG-TIADNI----RFGKLDATDYEVV--DAAKTANVDHFIRTMPDgyEMpinaegdnvSLGQKQL 489
Cdd:cd03255 80 rrrhiGFVFQSFNLLPDlTALENVelplLLAGVPKKERRERaeELLERVGLGDRLNHYPS--EL---------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 490 LTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLSTIRDADLILVMDQGQI 557
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
56-576 |
7.09e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 113.29 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 56 NGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNV-VQSAmhdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVD 134
Cdd:PLN03130 333 NGEPAWIGYIYAFSIFVGVVLGVLCEAQYFQNVMRVGFrLRST---LVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 135 AVSGALQQAFiGIVNAILGITLAAAMMFY----IQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNgyvqE 210
Cdd:PLN03130 410 ALQQICQQLH-TLWSAPFRIIIAMVLLYQqlgvASLIGSLMLVLMFPIQTFIISKMQKLTKEGLQRTDKRIGLMN----E 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 211 NMTGFSVLKVYGREKETLEGFKKV-NHSLKYFGfRAAFISGLMM------P-LVQLTAYATYigmAVLGSfyVITGAIVV 282
Cdd:PLN03130 485 VLAAMDTVKCYAWENSFQSKVQTVrDDELSWFR-KAQLLSAFNSfilnsiPvLVTVVSFGVF---TLLGG--DLTPARAF 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 283 GQLQAFIQyiwqISQPMGNVTQLSSVLQSASAATKRVFEILDEPEEkenkvdVSLP----ETILGDVTFDHVDFAYDPK- 357
Cdd:PLN03130 559 TSLSLFAV----LRFPLFMLPNLITQAVNANVSLKRLEELLLAEER------VLLPnpplEPGLPAISIKNGYFSWDSKa 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 -KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLmrfydvdkgairIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIA 436
Cdd:PLN03130 629 eRPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM------------LGELPPRSDASVVIRGTVAYVPQVSWIFNATVR 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRFGK-LDATDYEvvDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:PLN03130 697 DNILFGSpFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 516 L-EALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEKL 576
Cdd:PLN03130 775 VgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
353-568 |
1.10e-25 |
|
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: 105.21 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 353 AYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TKSMSRSDVRSLFGMVLQDAWLY 431
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QG-TIADNIRFGkldatdyevvdaAKTANVDHFIRTMPDGYEM-PI-----NAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:cd03224 88 PElTVEENLLLG------------AYARRRAKRKARLERVYELfPRlkerrKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 505 LDEATS----SVDTRLEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:cd03224 156 LDEPSEglapKIVEEIFEAIRELRD---EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
26-291 |
1.24e-25 |
|
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: 107.21 E-value: 1.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTG----LPTTEISRNIANGESINfsYIFKCLIWITVVGigyCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGklidVASKESGDIEIFGLSLK--TFALALLGVFVVG---AAANFGRVYLLRIAGERIVARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAF-IGIVNAILGITlAAAMMFYIQPMMALISMIMIP--- 177
Cdd:cd18573 77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLsDGLRSLVSGVG-GIGMMLYISPKLTLVMLLVVPpia 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 -TSIWISKRVINASQKyfqsMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLV 256
Cdd:cd18573 156 vGAVFYGRYVRKLSKQ----VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGST 231
|
250 260 270
....*....|....*....|....*....|....*
gi 488239013 257 QLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQY 291
Cdd:cd18573 232 GFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMY 266
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
361-559 |
2.88e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.36 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINL---LMRfydVDKGAIRIDGIDTKSMSRSDVRSL----FGMVLQDAWLYQG 433
Cdd:COG1136 24 LRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELARLrrrhIGFVFQFFNLLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 -TIADNI----RFGKLDATDYE--VVDAAKTANVDHFIRTMPDgyEMpinaegdnvSLGQKQLLTIARAVVSDPKILILD 506
Cdd:COG1136 101 lTALENValplLLAGVSRKERRerARELLERVGLGDRLDHRPS--QL---------SGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 507 EATSSVDTRLEALIQKAMDRVM-EGRTSFVIA-HRLSTIRDADLILVMDQGQIIE 559
Cdd:COG1136 170 EPTGNLDSKTGEEVLELLRELNrELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
345-561 |
2.96e-25 |
|
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: 103.87 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLfGMV 424
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLY-QGTIADNIRFG-KL-----DATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVV 497
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAH---RLSTIrdADLILVMDQGQIIEKG 561
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdqvEAMTM--ADRIAVMNDGQIQQIG 213
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
360-575 |
3.31e-25 |
|
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: 105.32 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDkGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNI 439
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 R-FGKLdaTDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEA 518
Cdd:cd03289 98 DpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 519 LIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGGFYEK 575
Cdd:cd03289 176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
345-569 |
5.79e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.93 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQ---DLNFEVKAGQTVAVVGPTGAGKTTL---INLLMRFydvDKGAIRIDGIDTKSMSRSDVR 418
Cdd:COG1135 2 IELENLSKTFPTKGGPVTaldDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 419 SL---FGMVLQDAWLYQG-TIADNIRF-----GkldatdyevVDAAKTANvdhfiRTMP-----------DGYemPinae 478
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENVALpleiaG---------VPKAEIRK-----RVAEllelvglsdkaDAY--P---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 479 gDNVSLGQKQLLTIARAVVSDPKILILDEATSSVD---TR--LEaLIQKAMDRVmeGRTSFVIAHRLSTIRD-ADLILVM 552
Cdd:COG1135 139 -SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRsiLD-LLKDINREL--GLTIVLITHEMDVVRRiCDRVAVL 214
|
250
....*....|....*..
gi 488239013 553 DQGQIIEKGTHESLLAQ 569
Cdd:COG1135 215 ENGRIVEQGPVLDVFAN 231
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
343-562 |
2.62e-24 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.38 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLfG 422
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLY-QGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARA 495
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAFPlklrKVPKAEIDrrVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 496 VVSDPKILILDEATSSVD------TRLE-ALIQKAMdrvmegRTSFVIA-HrlstirD-------ADLILVMDQGQIIEK 560
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL------GTTTIYVtH------DqveamtlADRIAVMNDGRIQQV 215
|
..
gi 488239013 561 GT 562
Cdd:COG3839 216 GT 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
358-553 |
5.42e-24 |
|
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: 99.86 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSmSRSDVRSLFGMVLQDAWLYQG-TIA 436
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYLGHADGLKPElTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRF----GKLDATDYEVVDAAKTANVDHFIRTMPDGYempinaegdnvSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:COG4133 94 ENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488239013 513 DTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIRDADLILVMD 553
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDLGD 204
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
97-319 |
7.17e-24 |
|
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: 102.11 E-value: 7.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 97 AMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMI 176
Cdd:cd18554 77 ILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 177 PTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLV 256
Cdd:cd18554 157 PFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAV 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 257 QLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18554 237 NTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-561 |
1.11e-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: 98.78 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLM--RFYDVDKGAIRIDGIdtkSMSRSDVRSLF 421
Cdd:cd03213 8 NLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLY-QGTIADNIRFgkldatdyevvdAAKtanvdhfIRtmpdgyempinaegdNVSLGQKQLLTIARAVVSDP 500
Cdd:cd03213 85 GYVPQDDILHpTLTVRETLMF------------AAK-------LR---------------GLSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLST--IRDADLILVMDQGQIIEKG 561
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
346-566 |
2.37e-23 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 99.18 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 346 TFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL---FG 422
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLY-QGTIADNIRFGKLDATdyevvdaaktanvdHFIRTMPDGY---EMPI--------------NAEGDNVSL 484
Cdd:cd03256 82 MIFQQFNLIeRLSVLENVLSGRLGRR--------------STWRSLFGLFpkeEKQRalaalervglldkaYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 485 GQKQLLTIARAVVSDPKILILDEATSSVDTR-----LEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPAssrqvMDLLKRINRE---EGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
....*...
gi 488239013 559 EKGTHESL 566
Cdd:cd03256 225 FDGPPAEL 232
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
359-567 |
8.52e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.47 E-value: 8.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSmSRSDVRSL---FGMVLQDAWLY-QGT 434
Cdd:PRK09493 15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIrqeAGMVFQQFYLFpHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADNIRFGKLDatdyevVDAAKTANVDHFIRTMPD--GYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:PRK09493 94 ALENVMFGPLR------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 513 DTRLEALIQKAM-DRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK09493 168 DPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
344-562 |
1.22e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.40 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksmsrSDVRSL--- 420
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG--------RDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 ---FGMVLQDawlYQ----GTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPDgyEMpinaegdnvSLGQK 487
Cdd:COG3842 76 krnVGMVFQD---YAlfphLTVAENVAFGlrmrGVPKAEIRarVAELLELVGLEGLADRYPH--QL---------SGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 488 QLLTIARAVVSDPKILILDEATSSVDTRL-EAL------IQKAMdrvmeGRTSFVIAHRLS---TIrdADLILVMDQGQI 557
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRI 214
|
....*
gi 488239013 558 IEKGT 562
Cdd:COG3842 215 EQVGT 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
345-562 |
1.28e-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: 96.92 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDV-RSLFGM 423
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITNLPPhKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDAWLY-QGTIADNIRFG----KLDATDY--EVVDAAKTANVDHFIRTMPDgyEMpinaegdnvSLGQKQLLTIARAV 496
Cdd:cd03300 77 VFQNYALFpHLTVFENIAFGlrlkKLPKAEIkeRVAEALDLVQLEGYANRKPS--QL---------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 497 VSDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGT 562
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-561 |
1.42e-22 |
|
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: 96.28 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQ---DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTkSMSRSDVRSLF 421
Cdd:cd03266 2 ITADALTKRFRDVKKTVQavdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDAWLYQG-TIADNIR-FGKLdatdYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSD 499
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyFAGL----YGLKGDELTARLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 500 PKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTI-RDADLILVMDQGQIIEKG 561
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
345-557 |
9.69e-22 |
|
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: 93.75 E-value: 9.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFG 422
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLY-QGTIADNIRFG-----KLDAtdyevvDAAKTANVDHFIRTmpdGYEMPINAEGDNVSLGQKQLLTIARAV 496
Cdd:cd03262 80 MVFQQFNLFpHLTVLENITLApikvkGMSK------AEAEERALELLEKV---GLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 497 VSDPKILILDEATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQI 557
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
352-562 |
1.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 95.11 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID--TKSMSRSDVRSLFGMVL 425
Cdd:PRK13637 10 HIYMEGTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 Q--DAWLYQGTIADNIRFG--KLDATDYEVVDAAKTAnvdhfIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:PRK13637 90 QypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 502 ILILDEATSSVDTR----LEALIQKAMDRvmEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGT 562
Cdd:PRK13637 165 ILILDEPTAGLDPKgrdeILNKIKELHKE--YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
19-319 |
1.54e-21 |
|
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: 95.21 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 19 RGTFLLVILFTVLTVAFNVALPYVTGLPTTEIsrnIANGESINFSYIFKCLIwitVVGIGYCISQLLSGVLMTNVVQSAM 98
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDI---IPSGDINLLNIISIGLI---LLYLFQSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 99 HDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP- 177
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPl 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 --TSIWISKRVINASQKyfQSMQNSlGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPL 255
Cdd:cd18570 154 yiLIILLFNKPFKKKNR--EVMESN-AELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSI 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 256 VQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18570 231 KGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
363-561 |
1.57e-21 |
|
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: 92.94 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLfGMVLQDAWLYQG-TIADNIRF 441
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RPV-SMLFQENNLFAHlTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 G-----KLDATDYEVVD-AAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTr 515
Cdd:cd03298 94 GlspglKLTAEDRQAIEvALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDP- 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 516 leALIQKAMDRVME-----GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03298 162 --ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
361-566 |
1.64e-21 |
|
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: 93.36 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TKSMSRSDVRSlfGMvlqdAWLYQG------ 433
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARA--GI----AYVPQGreifpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 -TIADNIRFGkLDATdyevvdAAKTANVDHFIRTM-PDGYEMpINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSS 511
Cdd:TIGR03410 90 lTVEENLLTG-LAAL------PRRSRKIPDEIYELfPVLKEM-LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 512 VDTRLEALIQKAMDRV--MEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:TIGR03410 162 IQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
100-319 |
2.00e-21 |
|
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: 94.86 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAF-IGIVNAILGITlAAAMMFYIQPMMALISMIMIPT 178
Cdd:cd18575 70 DLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLsIALRNLLLLIG-GLVMLFITSPKLTLLVLLVIPL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 179 S----IWISKRVINASQKYfqsmQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKK-VNHSLKYFGFRaAFISGLMM 253
Cdd:cd18575 149 VvlpiILFGRRVRRLSRAS----QDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATaVEAAFAAALRR-IRARALLT 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 254 PLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18575 224 ALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
349-571 |
2.09e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 349 HVDFAYDP--KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQ 426
Cdd:PRK13650 9 NLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 --DAWLYQGTIADNIRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYEmpinAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:PRK13650 89 npDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKE----REPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 505 LDEATSSVDT--RLEaLIQKAMD-RVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:PRK13650 164 LDEATSMLDPegRLE-LIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
345-567 |
2.11e-21 |
|
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: 93.61 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRF-YDVDKGAIRIDGIDTKSMSRSDVRSLFGM 423
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 V---LQDAWLYQGTIADNI---------RFGKLDATDYEVVDAA-KTANVDHF----IRTMpdgyempinaegdnvSLGQ 486
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVlsgffdsigLYREPTDEQRERARELlELLGLAHLadrpFGTL---------------SQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 487 KQLLTIARAVVSDPKILILDEATSSVDtrLEA--LIQKAMDRVM-EGRTSFV-IAHRLSTIRDA-DLILVMDQGQIIEKG 561
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLD--LGAreLLLALLDKLAaEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
|
....*.
gi 488239013 562 THESLL 567
Cdd:COG1119 226 PKEEVL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
355-562 |
2.61e-21 |
|
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: 92.57 E-value: 2.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 355 DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSmSRSDVRSLFGMVLQDAWLYQG- 433
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDEl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRF-GKLdatdYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:cd03263 91 TVREHLRFyARL----KGLPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 513 DTRLEALIQKAMDRVMEGRTsfVIahrLST--IRDADL----ILVMDQGQIIEKGT 562
Cdd:cd03263 165 DPASRRAIWDLILEVRKGRS--II---LTThsMDEAEAlcdrIAIMSDGKLRCIGS 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
363-558 |
2.72e-21 |
|
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: 90.95 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL-FGMVLQdawlyqgtiadnirf 441
Cdd:cd03216 18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIAMVYQ--------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 gkldatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR-LEALI 520
Cdd:cd03216 83 ----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488239013 521 qKAMDRVM-EGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:cd03216 123 -KVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
361-568 |
2.87e-21 |
|
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: 92.74 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSD-VRSLFGMVLQDAWLYQG-TIADN 438
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiARLGIGYVPEGRRIFPSlTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGKLDATDYEVVDAAKTANVDHFirtmPDGYEMpINAEGDNVSLGQKQLLTIARAVVSDPKILILDEAT-----SSVD 513
Cdd:COG0410 99 LLLGAYARRDRAEVRADLERVYELF----PRLKER-RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSlglapLIVE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 514 tRLEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:COG0410 174 -EIFEIIRRLNR---EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
362-559 |
3.99e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.63 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL-FGMVLQD----AWLyqgTIA 436
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQElnlvPNL---SVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRFGKLdATDYEVVDAAKT-ANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSS---- 511
Cdd:COG1129 98 ENIFLGRE-PRRGGLIDWRAMrRRARELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASlter 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488239013 512 -VDtRLEALIQKAMDRvmeGRTSFVIAHRLSTIRD-ADLILVMDQGQIIE 559
Cdd:COG1129 175 eVE-RLFRIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
346-569 |
5.03e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 92.13 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 346 TFDHVDFAYDPkkpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFgm 423
Cdd:COG3840 3 RLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdLTALPPAERPVSMLF-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 vlQD----AWLyqgTIADNIRFG-----KLDATDYE-VVDAAKTANVDHFIRTMPDgyempinaegdNVSLGQKQLLTIA 493
Cdd:COG3840 78 --QEnnlfPHL---TVAQNIGLGlrpglKLTAEQRAqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVDT--RLE--ALIQKAMDRvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPalRQEmlDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
.
gi 488239013 569 Q 569
Cdd:COG3840 220 G 220
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
359-569 |
1.09e-20 |
|
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: 92.61 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtkSMSRSDvrslfgmvlQDAWLYQGTIADN 438
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RISFSS---------QFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEA 518
Cdd:cd03291 118 IIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 519 LI-QKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
357-561 |
1.11e-20 |
|
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: 90.35 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSrsDVRSLFGMVLQDAWLYQG-TI 435
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI--EALRRIGALIEAPGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIR-FGKLDATDYEVVDaaKTANVDHFIrtmpdgyempiNAEGDNV---SLGQKQLLTIARAVVSDPKILILDEATSS 511
Cdd:cd03268 90 RENLRlLARLLGIRKKRID--EVLDVVGLK-----------DSAKKKVkgfSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 512 VDT----RLEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03268 157 LDPdgikELRELILSLRD---QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
359-562 |
2.71e-20 |
|
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: 90.09 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLfGMVLQDAWLYQG-TIAD 437
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNV-GFVFQHYALFRHmTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 NIRFG-KLDATDYEVVDAAKTANVDHFIRTMP-DGYEMPINAEgdnVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:cd03296 94 NVAFGlRVKPRSERPPEAEIRAKVHELLKLVQlDWLADRYPAQ---LSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 516 ----LEALIQKAMDRVmeGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGT 562
Cdd:cd03296 171 vrkeLRRWLRRLHDEL--HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
345-562 |
3.00e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 92.17 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLI---QDLNFEVKAGQTVAVVGPTGAGKTTLI---NLLMRfydVDKGAIRIDGIDTKSMSRSDVR 418
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 419 SL---FGMVLQDAWLYQG-TIADNIRFG-KLDATDYEVVDAaktanvdhfiRTMP-----------DGYemPINAEGdnv 482
Cdd:PRK11153 79 KArrqIGMIFQHFNLLSSrTVFDNVALPlELAGTPKAEIKA----------RVTEllelvglsdkaDRY--PAQLSG--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 483 slGQKQLLTIARAVVSDPKILILDEATSSVD---TR--LEAL--IQKAMdrvmeGRTSFVIAHRLSTIRD-ADLILVMDQ 554
Cdd:PRK11153 144 --GQKQRVAIARALASNPKVLLCDEATSALDpatTRsiLELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDA 216
|
....*...
gi 488239013 555 GQIIEKGT 562
Cdd:PRK11153 217 GRLVEQGT 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-568 |
3.44e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSR-SDVRSLFGM 423
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQ--DAWLYQGTIADNIRFGK----LDATDY-EVVDAAKTAnvdhfIRTMPDGYEMPINAEGdnvslGQKQLLTIARAV 496
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPenlcLPPIEIrKRVDRALAE-----IGLEKYRHRSPKTLSG-----GQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 497 VSDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
65-319 |
6.38e-20 |
|
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: 90.61 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 65 IFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDV----DAVSGAL 140
Cdd:cd18577 46 VNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTnliqDGIGEKL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 141 QQAFIGIVNAILGITLAaammFYIQPMMALISMIMIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKV 220
Cdd:cd18577 126 GLLIQSLSTFIAGFIIA----FIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 221 YGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLqafIQYIWQI---SQ 297
Cdd:cd18577 202 FGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDV---LTVFFAVligAF 278
|
250 260
....*....|....*....|..
gi 488239013 298 PMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18577 279 SLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
348-561 |
9.61e-20 |
|
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: 88.02 E-value: 9.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYdPKKPLIQDLNFEVKAGQTvAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMsRSDVRSLFGMVLQD 427
Cdd:cd03264 4 ENLTKRY-GKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQgtiadniRFGKLDATDY-----EVVDAAKTANVDHFIR--TMPDGYEMPINAegdnVSLGQKQLLTIARAVVSDP 500
Cdd:cd03264 81 FGVYP-------NFTVREFLDYiawlkGIPSKEVKARVDEVLElvNLGDRAKKKIGS----LSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 501 KILILDEATSSVD----TRLEALIQkamdRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03264 150 SILIVDEPTAGLDpeerIRFRNLLS----ELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
345-584 |
1.36e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG----IDTKSMSRSD 416
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQ--DAWLYQGTIADNIRFGKLD--ATDYEVVDAAKtanvdHFIRTMPDGYEMpINAEGDNVSLGQKQLLTI 492
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKVGLSEDL-ISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVDTR-LEALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQG 570
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEgRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
250
....*....|....*....
gi 488239013 571 GFYEKLY-----NSQFAEE 584
Cdd:PRK13641 237 EWLKKHYldepaTSRFASK 255
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-572 |
1.77e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.02 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQ----DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSD---- 416
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQ--DAWLYQGTIADNIRFG------------KLDATDYEVVDAAKtanvdHFIRTMPdgYEMpinaegdnv 482
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgipkekaeKIAAEKLEMVGLAD-----EFWEKSP--FEL--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 483 SLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEK 560
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISC 225
|
250
....*....|..
gi 488239013 561 GTHESLLAQGGF 572
Cdd:PRK13643 226 GTPSDVFQEVDF 237
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
361-561 |
2.08e-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: 86.95 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDvRSLFGMVLQDAWLYQG-TIADNI 439
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYLPEERGLYPKmKVIDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 R-FGKLdaTDYEVVDAAKtaNVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVD-TRLE 517
Cdd:cd03269 92 VyLAQL--KGLKKEEARR--RIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488239013 518 ALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03269 166 LLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
364-568 |
2.20e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.88 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 364 LNFEVKAGQTVAVVGPTGAGKTTL---INLLMRFYD--VDKGAIRIDGIDTKSMSRSDVRSL---FGMVLQDAWLY-QGT 434
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTARSLSQQKGLIRQLrqhVGFVFQNFNLFpHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADNIRFGKLdATDYEVVDAAKTANVDHFIRTMPDGYEmpiNAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDT 514
Cdd:PRK11264 102 VLENIIEGPV-IVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 515 RL--EALiqkAMDRVM--EGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK11264 178 ELvgEVL---NTIRQLaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
358-562 |
2.88e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS--RSDVRSLFgmvlQDAWLY-QGT 434
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPaeNRHVNTVF----QSYALFpHMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEA 508
Cdd:PRK09452 103 VFENVAFGlrmqKTPAAEITprVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 509 TSSVDTRLEALIQ---KAMDRVMeGRT-SFVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:PRK09452 172 LSALDYKLRKQMQnelKALQRKL-GITfVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-561 |
3.20e-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: 86.94 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 342 LGDVTFDHVDfaYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDK---GAIRIDGidtKSMSRSDVR 418
Cdd:cd03234 6 WWDVGLKAKN--WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG---QPRKPDQFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 419 SLFGMVLQ-DAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVD-----HFIRTMPDGYEMPinaegdNVSLGQKQLLTI 492
Cdd:cd03234 81 KCVAYVRQdDILLPGLTVRETLTYTAILRLPRKSSDAIRKKRVEdvllrDLALTRIGGNLVK------GISGGERRRVSI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAH--RLSTIRDADLILVMDQGQIIEKG 561
Cdd:cd03234 155 AVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
352-555 |
6.20e-19 |
|
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: 85.85 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGI--DTKSMSRSDVRSLFGMVL--QD 427
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKneSEPSFEATRSRNRYSVAYaaQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQGTIADNIRFGK-LDATDYEVVDAAKTANVDhfIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILD 506
Cdd:cd03290 88 PWLLNATVEENITFGSpFNKQRYKAVTDACSLQPD--IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 507 EATSSVDTRL-EALIQKAMDRVM--EGRTSFVIAHRLSTIRDADLILVMDQG 555
Cdd:cd03290 166 DPFSALDIHLsDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
12-326 |
7.89e-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: 87.51 E-value: 7.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 12 ARYIRPYRGTFLLVILFTVLTVAFNVALPYVTG-------LPTTEISRNIANgesinfsyiFKCLIWItVVGIGYCISQL 84
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSklisvfsLPDDDELRSEAN---------FWALMFL-VLAIVAGIAYF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 85 LSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFD--KNQQGNILSRVTNDVDAVSGA----LQQAFIGIVNAILGITLAa 158
Cdd:cd18578 71 LQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLvgdrLGLILQAIVTLVAGLIIA- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 159 ammFYIQPMMALISMIMIP---TSIWISKRVINASQKyfqSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVN 235
Cdd:cd18578 150 ---FVYGWKLALVGLATVPlllLAGYLRMRLLSGFEE---KNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEAL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 236 HSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQ----LQAFIQYIWQISQPMGNVTQLSsvlqS 311
Cdd:cd18578 224 EEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQffivFMALIFGAQSAGQAFSFAPDIA----K 299
|
330
....*....|....*
gi 488239013 312 ASAATKRVFEILDEP 326
Cdd:cd18578 300 AKAAAARIFRLLDRK 314
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
105-569 |
9.25e-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: 90.74 E-value: 9.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 105 IEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQA-FIGI----VNAILGITLAAAMMFYIQPMMALISMIMIPTs 179
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAhFVWIaplqVILLMGLIWELLEVNGFCGLGFLILLALFQA- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 180 iWISKRVInasqKYFQSMQNSLGELNGYVQENMTGFSVLKVYGRE---KETLEGFKKVNHSL-------KYFGFRAAFIS 249
Cdd:TIGR01271 240 -CLGQKMM----PYRDKRAGKISERLAITSEIIENIQSVKAYCWEeamEKIIKNIRQDELKLtrkiaylRYFYSSAFFFS 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 250 GLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVgqlqafiqyiwqisqPMGNVTQLSSVLQS---ASAATKRVFEILDEP 326
Cdd:TIGR01271 315 GFFVVFLSVVPYALIKGIILRRIFTTISYCIVL---------------RMTVTRQFPGAIQTwydSLGAITKIQDFLCKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 327 EEKENKVDVSLPETILGDVT----------FDHVDFAYDPKK------------------PLIQDLNFEVKAGQTVAVVG 378
Cdd:TIGR01271 380 EYKTLEYNLTTTEVEMVNVTaswdegigelFEKIKQNNKARKqpngddglffsnfslyvtPVLKNISFKLEKGQLLAVAG 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 379 PTGAGKTTLINLLMRFYDVDKGAIRIDGidtkSMSRSDvrslfgmvlQDAWLYQGTIADNIRFGkLDATDYEVVDAAKTA 458
Cdd:TIGR01271 460 STGSGKSSLLMMIMGELEPSEGKIKHSG----RISFSP---------QTSWIMPGTIKDNIIFG-LSYDEYRYTSVIKAC 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 459 NVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALI-QKAMDRVMEGRTSFVIA 537
Cdd:TIGR01271 526 QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVT 605
|
490 500 510
....*....|....*....|....*....|..
gi 488239013 538 HRLSTIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:TIGR01271 606 SKLEHLKKADKILLLHEGVCYFYGTFSELQAK 637
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
364-586 |
1.67e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 1.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 364 LNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDA--WLYQGTIADNIRF 441
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 GKL------DATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:PRK13647 104 GPVnmgldkDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 516 LEALIQKAMDRV-MEGRTSFVIAHRLSTIRD-ADLILVMDQGQIiekgtheslLAQGGfYEKLYNSQFAEEAG 586
Cdd:PRK13647 173 GQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRV---------LAEGD-KSLLTDEDIVEQAG 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
352-576 |
1.69e-18 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 89.84 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDgidtksmsRSdvrslFGMVLQDAWLY 431
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------RS-----IAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QGTIADNIRFgkLDATDYE-VVDAAKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:PTZ00243 734 NATVRGNILF--FDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 511 SVDTRL-EALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESlLAQGGFYEKL 576
Cdd:PTZ00243 812 ALDAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
344-562 |
1.78e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 85.91 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRS-DVRSLFG 422
Cdd:PRK13633 9 NVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIRNKAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQ--DAWLYQGTIADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIAR 494
Cdd:PRK13633 89 MVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 495 AVVSDPKILILDEATSSVDT--RLEAL--IQKAMDRvmEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPsgRREVVntIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
356-559 |
1.98e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 356 PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFG---MVLQD---AW 429
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdiqMVFQDsisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQGTIADNIRFGKLDATDYEvvDAAKTANVDHFIRTM----PDGYEMPinaegDNVSLGQKQLLTIARAVVSDPKILIL 505
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLD--KAERLARASEMLRAVdlddSVLDKRP-----PQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 506 DEATSSVDTRLEA-LIQKAMDRVMEGRTSFV-IAHRLSTI-RDADLILVMDQGQIIE 559
Cdd:PRK10419 176 DEAVSNLDLVLQAgVIRLLKKLQQQFGTACLfITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
276-556 |
2.20e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.71 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 276 ITGAIVVGQL----QAFIQYIWQISQPMGNVTQLSSVlqsaSAATKRV--FEILDEPEEKENKVDVSLPETILGDVTFDH 349
Cdd:COG4178 292 FAGEITLGGLmqaaSAFGQVQGALSWFVDNYQSLAEW----RATVDRLagFEEALEAADALPEAASRIETSEDGALALED 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 350 VDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTL---INLLMRFYDvdkGAIRIDgidtksmsrSDVRSLFgmVLQ 426
Cdd:COG4178 368 LTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLlraIAGLWPYGS---GRIARP---------AGARVLF--LPQ 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 DAWLYQGTIADNIRF--GKLDATDYEVVDAAKTANVDHFI-RtmpdgyempINAEGD--NV-SLGQKQLLTIARAVVSDP 500
Cdd:COG4178 434 RPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAeR---------LDEEADwdQVlSLGEQQRLAFARLLLHKP 504
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRDADLILVMDQGQ 556
Cdd:COG4178 505 DWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
365-569 |
2.21e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 365 NFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID--TKSMSRSDVRSLFgmvlQDAWLYQG-TIADNIRF 441
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDhtTTPPSRRPVSMLF----QENNLFSHlTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 G-----KLDATDYE-VVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:PRK10771 95 GlnpglKLNAAQREkLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 516 LEALIQKAMDRVMEGR--TSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK10771 164 LRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSG 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
362-580 |
3.32e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 84.36 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksmsrsDVRSLFGMvlqdawlyqGTI------ 435
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSALLEL---------GAGfhpelt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 -ADNIRFG-------------KLDatdyEVVDaakTANVDHFIrtmpdgyEMPINaegdNVSLGQKQLLTIARAVVSDPK 501
Cdd:COG1134 105 gRENIYLNgrllglsrkeideKFD----EIVE---FAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 502 ILILDEATSSVDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAqggFYEKL 576
Cdd:COG1134 167 ILLVDEVLAVGD---AAFQKKCLARIRElresGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEAL 240
|
....
gi 488239013 577 YNSQ 580
Cdd:COG1134 241 LAGR 244
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
359-562 |
3.72e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.97 E-value: 3.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTksMSRSDVRSL-FGMVLQDAWLYQG-TIA 436
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL--FTNLPPRERrVGFVFQHYALFPHmTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRFGkldATDYEVVDAAKTANVDHFIrtmpdgyEMpINAEG------DNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:COG1118 94 ENIAFG---LRVRPPSKAEIRARVEELL-------EL-VQLEGladrypSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 511 SVDTRLEALIQKAMDRVME--GRTS-FVI-----AHRLstirdADLILVMDQGQIIEKGT 562
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDelGGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVGT 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
357-569 |
4.04e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.93 E-value: 4.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TK-SMSRSDVrslfGMVLQDAWLY-QG 433
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvTHrSIQQRDI----CMVFQSYALFpHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRFG--KLDATDYEVVDAAKTA--NVDhfIRTMPDGYEmpinaegDNVSLGQKQLLTIARAVVSDPKILILDEAT 509
Cdd:PRK11432 94 SLGENVGYGlkMLGVPKEERKQRVKEAleLVD--LAGFEDRYV-------DQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 510 SSVDTRLealiQKAM-DRVME-----GRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK11432 165 SNLDANL----RRSMrEKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
361-583 |
4.20e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 84.50 E-value: 4.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAwlyQGTIADNIR 440
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 441 FGK-LDA-----TDYEvvDAAKTANVDHFIRT---MPDGYEMPINAegdnVSLGQKQLLTIARAVVSDPKILILDEATSS 511
Cdd:COG4167 106 IGQiLEEplrlnTDLT--AEEREERIFATLRLvglLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 512 VDTRLEALI-------QKAMDrvmegrTSFV-IAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA--QGGFYEKLYNSQ 580
Cdd:COG4167 180 LDMSVRSQIinlmlelQEKLG------ISYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAnpQHEVTKRLIESH 253
|
...
gi 488239013 581 FAE 583
Cdd:COG4167 254 FGE 256
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
361-567 |
6.78e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL----FGMVLQD-AWLYQGTI 435
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEAT 509
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 510 SSVDTRLEALIQKAMDRVM--EGRTSFVIAHRL-STIRDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
361-566 |
9.83e-18 |
|
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: 82.42 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRsDVRSLFGMVLQDAWLYQG-TIADNI 439
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIVFQDLSVDDElTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 R-FGKLdatdYEVVDAAKTANVDHFIRTMP--DGYEMPINaegdNVSLGQKQLLTIARAVVSDPKILILDEATSSVD--T 514
Cdd:cd03265 95 YiHARL----YGVPGAERRERIDELLDFVGllEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 515 RLEA--LIQKAMDRvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:cd03265 167 RAHVweYIEKLKEE--FGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
362-569 |
1.00e-17 |
|
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: 86.28 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDkGAIRIDGIDTKSMSRSDVRSL---FGMVLQDAWlyqG----- 433
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPF---Gslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 -TIADNIRFG------KLDATDYE--VVDAAKTANVDhfiRTMPDGY--EMpinaegdnvSLGQKQLLTIARAVVSDPKI 502
Cdd:COG4172 379 mTVGQIIAEGlrvhgpGLSAAERRarVAEALEEVGLD---PAARHRYphEF---------SGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 503 LILDEATSSVDtrleALIQKamdRVME---------GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:COG4172 447 LVLDEPTSALD----VSVQA---QILDllrdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
359-567 |
1.32e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLY------- 431
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSfefdvrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 ---QGTIADNIRFGKLDATDYEVVDAA-KTANVDHFIrtmpdgyEMPInaegDNVSLGQKQLLTIARAVVSDPKILILDE 507
Cdd:PRK09536 97 vveMGRTPHRSRFDTWTETDRAAVERAmERTGVAQFA-------DRPV----TSLSGGERQRVLLARALAQATPVLLLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 508 ATSSVD----TRLEALIQKAMDrvmEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK09536 166 PTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-564 |
1.36e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 1.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL-FGMVLQDAWLYQG-TIADNI 439
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQHFMLVPNlTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 RFGkLDATDYEVVDAAKTANVdhfIRTMPDGYEMPIN--AEGDNVSLGQKQLLTIARAVVSDPKILILDEATsSVDTRLE 517
Cdd:COG3845 102 VLG-LEPTKGGRLDRKAARAR---IRELSERYGLDVDpdAKVEDLSVGEQQRVEILKALYRGARILILDEPT-AVLTPQE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488239013 518 A--LIqKAMDR-VMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIekGTHE 564
Cdd:COG3845 177 AdeLF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
344-570 |
1.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.15 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRI-DGIDTKSMSRSDVR 418
Cdd:PRK13634 2 DITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 419 SL---FGMVLQ--DAWLYQGTIADNIRFGKLD--ATDYEVVDAAKTA----NVDHFIRTmpdgyEMPINAEGdnvslGQK 487
Cdd:PRK13634 82 PLrkkVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMielvGLPEELLA-----RSPFELSG-----GQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 488 QLLTIARAVVSDPKILILDEATSSVDTRLealiQKAMdrvME---------GRTSFVIAHRLSTI-RDADLILVMDQGQI 557
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKG----RKEM---MEmfyklhkekGLTTVLVTHSMEDAaRYADQIVVMHKGTV 224
|
250
....*....|...
gi 488239013 558 IEKGTHESLLAQG 570
Cdd:PRK13634 225 FLQGTPREIFADP 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-570 |
3.84e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.72 E-value: 3.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPL-IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGM 423
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQ--DAWLYQGTIADNIRFG------KLDATDYEVVDAAKtaNVDHFIRTmpdgyempiNAEGDNVSLGQKQLLTIARA 495
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALK--QVDMLERA---------DYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 496 VVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGR--TSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLAQG 570
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
357-562 |
3.86e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.36 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWL-YQGTI 435
Cdd:PRK13548 14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFGKLD-----ATDYEVVDAA-KTANVDHFirtmpdgyempinAEGDNVSL--GQKQLLTIARAVV------SDPK 501
Cdd:PRK13548 94 EEVVAMGRAPhglsrAEDDALVAAAlAQVDLAHL-------------AGRDYPQLsgGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 502 ILILDEATSSVDTR-----LEALIQKAMDRvmeGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGT 562
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvLRLARQLAHER---GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
357-564 |
5.48e-17 |
|
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: 79.49 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRF--YDVDKGAIRIDGIDTKSMSrSDVRSLFGMVLqdAWLYQGT 434
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLGIFL--AFQYPPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADnirfgkldatdyevvdaaktANVDHFIRTMPDGYempinaegdnvSLGQKQLLTIARAVVSDPKILILDEATSSVDt 514
Cdd:cd03217 89 IPG--------------------VKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 515 rLEAL--IQKAMDRVMEGRTSF-VIAH--RLSTIRDADLILVMDQGQIIEKGTHE 564
Cdd:cd03217 137 -IDALrlVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
353-561 |
5.98e-17 |
|
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: 80.27 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 353 AYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksmsrsDVRSLFGmvLQDAWLYQ 432
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---------RVSSLLG--LGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNIRF-----GKLDATDYEVVDaaktanvdhFIRT---MPDGYEMPINaegdNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:cd03220 99 LTGRENIYLngrllGLSRKEIDEKID---------EIIEfseLGDFIDLPVK----TYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 505 LDEATSSVDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:cd03220 166 IDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
363-562 |
6.42e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRslFGMVLQDAWLYQG-TIADNIRF 441
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRHmTVFDNIAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 442 G----------KLDATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSS 511
Cdd:PRK10851 98 GltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 512 VDTRLEALIQKAMDRVME--GRTS-FVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEelKFTSvFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
363-561 |
6.79e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 79.65 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKaGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG---IDT-KSMSRSDVRSLFGMVLQDAWLY-QGTIAD 437
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 NIRFG---KLDATDYEVVDAAKTA-NVDHFIRTMPDGyempinaegdnVSLGQKQLLTIARAVVSDPKILILDEATSSVD 513
Cdd:cd03297 95 NLAFGlkrKRNREDRISVDELLDLlGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488239013 514 TRLEALIQKAMDRVME--GRTSFVIAHRLSTI-RDADLILVMDQGQIIEKG 561
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-571 |
7.14e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDvRSLFGMVLQDAWLYQG-TIADNI 439
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPED-RRRIGYLPEERGLYPKmKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 R-FGKL---DATDyevvdaAKTAnvdhfIRTMPDGYEMPINAeGDNV---SLGQKQLLTIARAVVSDPKILILDEATS-- 510
Cdd:COG4152 93 VyLARLkglSKAE------AKRR-----ADEWLERLGLGDRA-NKKVeelSKGNQQKVQLIAALLHDPELLILDEPFSgl 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 511 ---SVDTRLEALIQKAmdrvMEGRTsfVI--AHRLSTI-RDADLILVMDQGQIIEKGTHESLLAQGG 571
Cdd:COG4152 161 dpvNVELLKDVIRELA----AKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-539 |
7.65e-17 |
|
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: 78.35 E-value: 7.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksmsrsDVRSLFgmV 424
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE---------GEDLLF--L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLYQGTIADNIRFgkldatdyevvdaaktanvdhfirtmpdgyempinAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:cd03223 70 PQRPYLPLGTLREQLIY-----------------------------------PWDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 488239013 505 LDEATSSVDTRLEALIqkaMDRVMEGRTSFV-IAHR 539
Cdd:cd03223 115 LDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-559 |
7.81e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.47 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGA-----IRIDGID--TKSMSRSDVRSL 420
Cdd:COG1117 15 RNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeILLDGEDiyDPDVDVVELRRR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQDAWLYQGTIADNIRFG----------KLDATdyeVVDAAKTANV-----DHfirtmpdgyempINAEGDNVSLG 485
Cdd:COG1117 94 VGMVFQKPNPFPKSIYDNVAYGlrlhgiksksELDEI---VEESLRKAALwdevkDR------------LKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 486 QKQLLTIARAVVSDPKILILDEATSSVD----TRLEALIQkamdrvmEGRTSFVIA---HRLS-TIRDADLILVMDQGQI 557
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELIL-------ELKKDYTIVivtHNMQqAARVSDYTAFFYLGEL 231
|
..
gi 488239013 558 IE 559
Cdd:COG1117 232 VE 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
360-569 |
9.02e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 81.55 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLN---FEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL---FGMVLQDAWlyqG 433
Cdd:PRK11308 27 LVKALDgvsFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqkIQIVFQNPY---G 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRFG-----------KLDAtdyevvdAAKTANVDHFIRTM---PDGYE----MpinaegdnVSLGQKQLLTIARA 495
Cdd:PRK11308 104 SLNPRKKVGqileepllintSLSA-------AERREKALAMMAKVglrPEHYDryphM--------FSGGQRQRIAIARA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 496 VVSDPKILILDEATSSVDTRLEA-LIQKAMDRVMEGRTSFV-IAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK11308 169 LMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
358-561 |
9.76e-17 |
|
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: 79.68 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL---FGMVLQDAWlyQGT 434
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIgvvFGQKTQLWW--DLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADNIRfgkLDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEgdNVSLGQKQLLTIARAVVSDPKILILDEATSSVDT 514
Cdd:cd03267 112 VIDSFY---LLAAIYDLPPARFKKRLDELSELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488239013 515 RLEALIQKAMDRVMEGRTSFVI--AHRLSTI-RDADLILVMDQGQIIEKG 561
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
345-568 |
1.08e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSdVRSLFGMV 424
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQ-DAWLYQGTIADNIR-----FGKLDATDYEVVdaaktANVDHFIRtmpdgYEMPINAEGDNVSLGQKQLLTIARAVVS 498
Cdd:PRK13537 86 PQfDNLDPDFTVRENLLvfgryFGLSAAAARALV-----PPLLEFAK-----LENKADAKVGELSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 499 DPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
344-561 |
1.53e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 81.61 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 344 DVTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGI---DTKSMSRSdvrsl 420
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAERG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 FGMVLQDAWLY-QGTIADNIRFG-KLDATDYEVVD-----AAKTANVDHFIRTMPDGyempinaegdnVSLGQKQLLTIA 493
Cdd:PRK11000 77 VGMVFQSYALYpHLSVAENMSFGlKLAGAKKEEINqrvnqVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 494 RAVVSDPKILILDEATSSVDT------RLEalIQKAMDRVmeGRTSFVIAH-RLSTIRDADLILVMDQGQIIEKG 561
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAalrvqmRIE--ISRLHKRL--GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
352-562 |
2.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 79.74 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFGMVLQ--D 427
Cdd:PRK13639 9 YSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepIKYDKKSLLEVRKTVGIVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQGTIADNIRFGKL------DATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPK 501
Cdd:PRK13639 89 DQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 502 ILILDEATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGT 562
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGT 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
358-567 |
2.39e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 80.65 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSdVRSLFGMVLQ-DAWLYQGTIA 436
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGVVPQfDNLDLEFTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNI----RFGKLDATDYEVVdaakTANVDHFIRtmpdgYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:PRK13536 133 ENLlvfgRYFGMSTREIEAV----IPSLLEFAR-----LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 513 DTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK13536 204 DPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
357-568 |
2.42e-16 |
|
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: 78.35 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID--TKSMSRsdvRSLFGMVL--QDAWLYQ 432
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDitKLPMHK---RARLGIGYlpQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 G-TIADNIR-----FGKLDATDYEVVDAA-KTANVDHFIRTMpdgyempinaeGDNVSLGQKQLLTIARAVVSDPKILIL 505
Cdd:cd03218 89 KlTVEENILavleiRGLSKKEREEKLEELlEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 506 DEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLS-TIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
346-560 |
3.12e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.59 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 346 TFDHVDFAYdPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRsdvrslfGM 423
Cdd:PRK11248 3 QISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAER-------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQ-DAWLYQGTIADNIRFG----KLDATDYEVVDAAKTANVD------HFIRTMpdgyempinaegdnvSLGQKQLLTI 492
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFGlqlaGVEKMQRLEIAHQMLKKVGlegaekRYIWQL---------------SGGQRQRVGI 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHrlsTIRDA-----DLILVM-DQGQIIEK 560
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEAvfmatELVLLSpGPGRVVER 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
345-577 |
3.15e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.44 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID----TKSMSRSD 416
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQ--DAWLYQGTIADNIRFG----KLDatdyevVDAAKTanvDHFIRTMPDGYEMPINAEGD-NVSLGQKQL 489
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGpknfKMN------LDEVKN---YAHRLLMDLGFSRDVMSQSPfQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 490 LTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVM--EGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESL 566
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
250
....*....|.
gi 488239013 567 LAQGGFYEKLY 577
Cdd:PRK13646 234 FKDKKKLADWH 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
312-559 |
4.72e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 312 ASAATKRV--FE--ILDEPEEKENKVDVSLPETI-LGD--VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGK 384
Cdd:COG0488 276 AKQAQSRIkaLEklEREEPPRRDKTVEIRFPPPErLGKkvLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 385 TTLINLLMRFYDVDKGAIRidgidtksmsrsdvrslfgmvlqdawlyqgtIADNIRFGKLDaTDYEVVDAAKTAnVDHFI 464
Cdd:COG0488 355 STLLKLLAGELEPDSGTVK-------------------------------LGETVKIGYFD-QHQEELDPDKTV-LDELR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 465 RTMPDGYEMPINA-------EGDNV-------SLGQKQLLTIARAVVSDPKILILDEATSSVDTR-LEALIQkAMDRvME 529
Cdd:COG0488 402 DGAPGGTEQEVRGylgrflfSGDDAfkpvgvlSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIEtLEALEE-ALDD-FP 479
|
250 260 270
....*....|....*....|....*....|...
gi 488239013 530 GrTSFVIAH-R--LSTIrdADLILVMDQGQIIE 559
Cdd:COG0488 480 G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
365-564 |
1.79e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.57 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 365 NFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG----------IDTKSMSRS--DVRsLFG--------MV 424
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGqhieglpghqIARMGVVRTfqHVR-LFRemtvienlLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLYQGTIAdnirfGKLDATDYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:PRK11300 104 AQHQQLKTGLFS-----GLLKTPAFRRAESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 505 LDEATSSVDTR----LEALIQKAmdRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHE 564
Cdd:PRK11300 177 LDEPAAGLNPKetkeLDELIAEL--RNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPE 239
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
337-569 |
3.41e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.04 E-value: 3.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 337 LPETILgdvTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSR 414
Cdd:PRK13636 1 MEDYIL---KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 415 SDVRSLFGMVLQ--DAWLYQGTIADNIRFGKL------DATDYEVVDAAKTANVDHfIRTMPDGYempinaegdnVSLGQ 486
Cdd:PRK13636 78 MKLRESVGMVFQdpDNQLFSASVYQDVSFGAVnlklpeDEVRKRVDNALKRTGIEH-LKDKPTHC----------LSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 487 KQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIR-DADLILVMDQGQIIEKGTH 563
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNP 226
|
....*.
gi 488239013 564 ESLLAQ 569
Cdd:PRK13636 227 KEVFAE 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
343-562 |
3.87e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 3.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 343 GDVTFDHVDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAI-----RIDGIDTKSMS 413
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyAIPANLKKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 414 RSDVRSLFGMVLQ--DAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVDHFIrTMPDGY--EMPINAEGdnvslGQKQL 489
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDYvkRSPFELSG-----GQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 490 LTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGT 562
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-562 |
4.68e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 75.46 E-value: 4.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDkGAIRIDG--------IDTKSMSRSD 416
Cdd:PRK14258 8 IKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGrveffnqnIYERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQDAWLYQGTIADNIRFG--------KLDATDYeVVDAAKTANvdhfirtMPDGYEMPINAEGDNVSLGQKQ 488
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEIDDI-VESALKDAD-------LWDEIKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 489 LLTIARAVVSDPKILILDEATSSVD----TRLEALIQKAmdRVMEGRTSFVIAHRLSTI-RDADLILVMDQ-----GQII 558
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLV 235
|
....
gi 488239013 559 EKGT 562
Cdd:PRK14258 236 EFGL 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
348-583 |
5.18e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 75.05 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDPKKPLIqDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--------IDTKSMS--RSDV 417
Cdd:PRK11124 6 NGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRelRRNV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 418 rslfGMVLQDAWLY-QGTIADN-----IRFGKLDAtdyevvDAAKTANVDHFIRTMPDGY--EMPINAEGdnvslGQKQL 489
Cdd:PRK11124 85 ----GMVFQQYNLWpHLTVQQNlieapCRVLGLSK------DQALARAEKLLERLRLKPYadRFPLHLSG-----GQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 490 LTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESll 567
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDASC-- 227
|
250
....*....|....*.
gi 488239013 568 aqggfYEKLYNSQFAE 583
Cdd:PRK11124 228 -----FTQPQTEAFKN 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
332-562 |
7.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.66 E-value: 7.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 332 KVDVSLPETILGD--VTFDHVDFAYDPKKP----LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRID 405
Cdd:PRK13631 7 KKKLKVPNPLSDDiiLRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 406 GI---------------DTKSMSR-SDVRSLFGMVLQ--DAWLYQGTIADNIRFGKLdATDYEVVDAAKTANvdHFIRTM 467
Cdd:PRK13631 87 DIyigdkknnhelitnpYSKKIKNfKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAK--FYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 468 PDGYEM----PINAEGdnvslGQKQLLTIARAVVSDPKILILDEATSSVDTRLEA-LIQKAMDRVMEGRTSFVIAHRLST 542
Cdd:PRK13631 164 GLDDSYlersPFGLSG-----GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEH 238
|
250 260
....*....|....*....|.
gi 488239013 543 IRD-ADLILVMDQGQIIEKGT 562
Cdd:PRK13631 239 VLEvADEVIVMDKGKILKTGT 259
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
363-569 |
1.24e-14 |
|
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: 75.52 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINL---LMRfydVDKGAIRIDG---IDTKSmsRSDV----RSLfGMVLQDAWL-- 430
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSAR--GIFLpphrRRI-GYVFQEARLfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 431 -YqgTIADNIRFG-----------KLDatdyEVVDaakTANVDHFIRTMPDgyempinaegdNVSLGQKQLLTIARAVVS 498
Cdd:COG4148 91 hL--SVRGNLLYGrkrapraerriSFD----EVVE---LLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 499 DPKILILDEATSSVDTR--------LEALIQK----------AMDRVMegrtsfviahRLstirdADLILVMDQGQIIEK 560
Cdd:COG4148 151 SPRLLLMDEPLAALDLArkaeilpyLERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVAS 215
|
....*....
gi 488239013 561 GTHESLLAQ 569
Cdd:COG4148 216 GPLAEVLSR 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
352-569 |
1.61e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 74.07 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQ--DAW 429
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQGTIADNIRFGKLD------ATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:PRK13652 91 IFSPTVEQDIAFGPINlgldeeTVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-567 |
1.74e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.54 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGI------DTKSMSRSDVRSLFGMVL 425
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 QDAWLY-QGTIADNIRFGKLDATDYEVVDAAKTanVDHFIRTMPDGYEM--PINAEGDNVSLGQKQLLTIARAVVSDPKI 502
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLWKEVydRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
352-568 |
2.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.59 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 352 FAYDPKKPLIQ--DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQ--D 427
Cdd:PRK13642 12 FKYEKESDVNQlnGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQnpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQGTIADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPDgyempinaegdNVSLGQKQLLTIARAVVSDPK 501
Cdd:PRK13642 92 NQFVGATVEDDVAFGmenqgiPREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRVMEGR--TSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-565 |
2.56e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRsdvRSLFGMV 424
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---KNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDA---WLYQGTIADNI---RFGKL------DATDYEVVDAAkTANVDhfirtMPDGYEMPINaegdNVSLGQKQLLTI 492
Cdd:PRK15056 84 PQSEevdWSFPVLVEDVVmmgRYGHMgwlrraKKRDRQIVTAA-LARVD-----MVEFRHRQIG----ELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHES 565
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
358-537 |
2.98e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TKSMSRSDVRSLfGMvlQDAWLYQGTIA 436
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiDDPDVAEACHYL-GH--RNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRF--GKLDATDYEVVDAAKTANVDHfIRTMPDGYempinaegdnVSLGQKQLLTIARAVVSDPKILILDEATSSVDT 514
Cdd:PRK13539 92 ENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|...
gi 488239013 515 RLEALIQKAMDRVMEGRTSFVIA 537
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAA 183
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
362-566 |
3.02e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDVRSLF--GMvlqdAWLYQG------ 433
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAALaaGV----AIIYQElhlvpe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 -TIADNIRFGKLDATdYEVVDAaKTANVDHFIRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:PRK11288 94 mTVAENLYLGQLPHK-GGIVNR-RLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 513 DTR----LEALIQKAMDrvmEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEkgTHESL 566
Cdd:PRK11288 172 SAReieqLFRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
361-555 |
3.20e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL-FGMVLQD-AWLYQGTIADN 438
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGKLDATDY---EVVDAAKTANVDHFIrTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:PRK09700 101 LYIGRHLTKKVcgvNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488239013 516 LEALIQKAMDRVM-EGRTSFVIAHRLSTIRD-ADLILVMDQG 555
Cdd:PRK09700 180 EVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
348-570 |
3.66e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 72.74 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS-RSDVRSLF----- 421
Cdd:PRK11231 6 ENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLARRLAllpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 -----GMVLQDAWLYqGTIADNIRFGKLDATDYEVVDAA--KTaNVDHFIrtmpdgyEMPInaegDNVSLGQKQLLTIAR 494
Cdd:PRK11231 85 hltpeGITVRELVAY-GRSPWLSLWGRLSAEDNARVNQAmeQT-RINHLA-------DRRL----TDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 495 AVVSDPKILILDEATSSVDTRLEALIQKAMdRVM--EGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLAQG 570
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLM-RELntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
356-566 |
4.81e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.59 E-value: 4.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 356 PKKPL--IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS---RSDVRSLFGMVLQD--A 428
Cdd:PRK15079 30 PPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDplA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 429 WLY-QGTIADNI----RFGKLDATDYEVVDAAKTAnvdhfirTMPDGYeMP--INAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:PRK15079 110 SLNpRMTIGEIIaeplRTYHPKLSRQEVKDRVKAM-------MLKVGL-LPnlINRYPHEFSGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 502 ILILDEATSSVDTRLEALI---QKAMDRVMeGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVvnlLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
359-526 |
5.95e-14 |
|
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: 71.31 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRidgidtksmsrsdVRSLFGMVlqdawlyqgTIADn 438
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL-------------VRHDGGWV---------DLAQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 irfgkldATDYEVVDAAKTA--NVDHFIRTMP-----DGYEMPINAEGD----------------NV------------S 483
Cdd:COG4778 82 -------ASPREILALRRRTigYVSQFLRVIPrvsalDVVAEPLLERGVdreearararellarlNLperlwdlppatfS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488239013 484 LGQKQLLTIARAVVSDPKILILDEATSSVDT----RLEALIQKAMDR 526
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAanraVVVELIEEAKAR 201
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
354-561 |
9.37e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 71.50 E-value: 9.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 354 YDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG-----IDTKSMSRSDVRSLF----GMV 424
Cdd:PRK11701 16 YGPRKGC-RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLrtewGFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAwlyqgtiADNIRFGkldatdyevVDAAktANVDHfiRTMPDG---Y--------------EMPINAEGD---NVSL 484
Cdd:PRK11701 95 HQHP-------RDGLRMQ---------VSAG--GNIGE--RLMAVGarhYgdiratagdwlervEIDAARIDDlptTFSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 485 GQKQLLTIARAVVSDPKILILDEATS----SVDTRLEALIQKAmdrVMEGRTSFVI-AHRLSTIRD-ADLILVMDQGQII 558
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGL---VRELGLAVVIvTHDLAVARLlAHRLLVMKQGRVV 231
|
...
gi 488239013 559 EKG 561
Cdd:PRK11701 232 ESG 234
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-562 |
1.28e-13 |
|
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: 74.28 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 310 QSASAATKRVFEILDEPEEKENKVDV----SLPETILGDVTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKT 385
Cdd:TIGR01257 891 ERALEKTEPLTEEMEDPEHPEGINDSfferELPGLVPGVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKT 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 386 TLINLLMRFYDVDKGAIRIDGIDTKSmSRSDVRSLFGMVLQDAWLYQG-TIADNIRF-GKLDATDYEVVDAAKTANVDHf 463
Cdd:TIGR01257 971 TTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyAQLKGRSWEEAQLEMEAMLED- 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 464 irtmpDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSti 543
Cdd:TIGR01257 1049 -----TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD-- 1121
|
250 260
....*....|....*....|...
gi 488239013 544 rDADL----ILVMDQGQIIEKGT 562
Cdd:TIGR01257 1122 -EADLlgdrIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
19-319 |
1.36e-13 |
|
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: 71.77 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 19 RGTFLLVILFTVLTVAFNVALPYVTGLPTTEISrniangESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTnVVQSAM 98
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNVI------VPGNLNLLNVLGIGILILFLLYGLFSFLRGYIII-KLQTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 99 -HDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFI-GIVNAILGITLaAAMMFYIQPMMALI----S 172
Cdd:cd18555 74 dKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVIsLIIDLLLLVIY-LIYMLYYSPLLTLIvlllG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 173 MIMIPTSIWISKRVINASQKYFQSMqnslGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLM 252
Cdd:cd18555 152 LLIVLLLLLTRKKIKKLNQEEIVAQ----TKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNIL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 253 MPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18555 228 NSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
111-319 |
1.59e-13 |
|
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: 71.44 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 111 RLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIP----TSIWISKRV 186
Cdd:cd18568 87 SLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlyvlLTLLSSPKL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 187 INASQKYFQSmqnsLGELNGYVQENMTGFSVLKVYGREKET-LEGFKKVNHSLK--YFGFRAAFISGLMMPLVQltaYAT 263
Cdd:cd18568 166 KRNSREIFQA----NAEQQSFLVEALTGIATIKALAAERPIrWRWENKFAKALNtrFRGQKLSIVLQLISSLIN---HLG 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 264 YIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18568 239 TIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
22-292 |
2.33e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 71.00 E-value: 2.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGlptteisrniANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSA---M 98
Cdd:cd18580 5 LLLLLLLAFLSQFSNIWLDWWSS----------DWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRAsrrL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 99 HD--LRRdieekINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMI 176
Cdd:cd18580 75 HDklLRS-----VLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 177 PTSIWISKRVINASQ--KYFQSMQNSlgELNGYVQENMTGFSVLKVYGREKETLEGF-KKVNHSLKYF----------GF 243
Cdd:cd18580 150 VVYYLLQRYYLRTSRqlRRLESESRS--PLYSHFSETLSGLSTIRAFGWQERFIEENlRLLDASQRAFylllavqrwlGL 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 244 R-----AAFISGLMMPLVQLTAY--ATYIGMAVLgsfYVITgaiVVGQLQAFIQYI 292
Cdd:cd18580 228 RldllgALLALVVALLAVLLRSSisAGLVGLALT---YALS---LTGSLQWLVRQW 277
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
361-579 |
2.70e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAiRIDG--------IDTKSMSRSDVRSLFGMVLQDAWLYQ 432
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGkvtfhgknLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNIRFG--------KLDatdyEVVDAAKTANVdhfirtMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILI 504
Cdd:PRK14243 105 KSIYDNIAYGaringykgDMD----ELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 505 LDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRL-STIRDADLILVMDQgQIIEKGTHESLLAQGGFYEKLYNS 579
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFNV-ELTEGGGRYGYLVEFDRTEKIFNS 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
360-524 |
4.05e-13 |
|
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: 68.29 E-value: 4.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADNI 439
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 RFGKLDATDYEVVDAAKTANVdhfirtmpDGYE-MPINaegdNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEA 518
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGL--------NGFEdRPVA----QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 488239013 519 LIQKAM 524
Cdd:cd03231 163 RFAEAM 168
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
26-319 |
4.90e-13 |
|
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: 69.97 E-value: 4.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGLPTTEISRNIANGESINFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDI 105
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 106 EEKINRLPVSYFDKNQQGNILSRVTNDV----DAVSGALQQAFIGIVNAILGITlaaaMMFYIQPMMALISMIMIP---- 177
Cdd:cd18780 82 FSAIIAQEIAFFDVTRTGELLNRLSSDTqvlqNAVTVNLSMLLRYLVQIIGGLV----FMFTTSWKLTLVMLSVVPplsi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 TSIWISKRVINASQKyfqsMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGF-KKVNHSLKYfGFRAAFISGLMMPLV 256
Cdd:cd18780 158 GAVIYGKYVRKLSKK----FQDALAAASTVAEESISNIRTVRSFAKETKEVSRYsEKINESYLL-GKKLARASGGFNGFM 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 257 QLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18780 233 GAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-578 |
5.05e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.00 E-value: 5.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 356 PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMrFY---DVDK-GAIRIDG--IDTKSMSRsdvRSlfgmvlqdAW 429
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRspkGVKGsGSVLLNGmpIDAKEMRA---IS--------AY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQgtiaDNIRFGKLDATDYEVVDA-----------AKTANVDHFIRTMP--DGYEMPINAEGD--NVSLGQKQLLTIAR 494
Cdd:TIGR00955 104 VQQ----DDLFIPTLTVREHLMFQAhlrmprrvtkkEKRERVDEVLQALGlrKCANTRIGVPGRvkGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 495 AVVSDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLST--IRDADLILVMDQGQIIEKGTHE---SLLA 568
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDqavPFFS 259
|
250
....*....|.
gi 488239013 569 QGGFY-EKLYN 578
Cdd:TIGR00955 260 DLGHPcPENYN 270
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-557 |
5.25e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.75 E-value: 5.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDV---RSLF 421
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQD-AWLYQGTIADNIRFGKLDA-TDYEVVDAAKTANVDHfIRTMPDGYEMPINAEGdnvslGQKQLLTIARAVVSD 499
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIPLIIAgASGDDIRRRVSAALDK-VGLLDKAKNFPIQLSG-----GEQQRVGIARAVVNK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 500 PKILILDEATSSVDTRLEALIQK---AMDRVmeGRTSFVIAHRLSTI-RDADLILVMDQGQI 557
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRlfeEFNRV--GVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
357-507 |
6.65e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 68.52 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TK-SMSRsdvRSLFGM--VLQDAWLYQ 432
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDiTHlPMHK---RARLGIgyLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 G-TIADNIR----FGKLDATDYEvvdaAKTA------NVDHFIRTMpdgyempinaeGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:COG1137 92 KlTVEDNILavleLRKLSKKERE----ERLEelleefGITHLRKSK-----------AYSLSGGERRRVEIARALATNPK 156
|
....*.
gi 488239013 502 ILILDE 507
Cdd:COG1137 157 FILLDE 162
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
360-569 |
6.65e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.84 E-value: 6.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSD-------------VRSLFGMVLQ 426
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 --DAWLYQgTIADNIRFGKLDATDYEVVDAAKTAnVDHFIRTMPDGY---EMPINAEGdnvslGQKQLLTIARAVVSDPK 501
Cdd:PRK10619 100 hfNLWSHM-TVLENVMEAPIQVLGLSKQEARERA-VKYLAKVGIDERaqgKYPVHLSG-----GQQQRVSIARALAMEPE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 502 ILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-561 |
7.13e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD-----KGAIRIDGIDTKS--MSRSDVRSLFGMVLQDAWLY- 431
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QGTIADNIRFG-KL-------DATDYEVVDAAKTAnvdhfirTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:PRK14267 99 HLTIYDNVAIGvKLnglvkskKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHR-LSTIRDADLILVMDQGQIIEKG 561
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
347-568 |
7.73e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 71.16 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQ 426
Cdd:PRK10522 325 LRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 DAWLYQGTIADnirfgKLDATDYEVVDA--------AKTANVDHFIRTMpdgyempinaegdNVSLGQKQLLTIARAVVS 498
Cdd:PRK10522 405 DFHLFDQLLGP-----EGKPANPALVEKwlerlkmaHKLELEDGRISNL-------------KLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 499 DPKILILDEATSSVD--------TRLEALIQKAmdrvmeGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK10522 467 ERDILLLDEWAADQDphfrrefyQVLLPLLQEM------GKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAA 538
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
357-555 |
8.26e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDgidtksmsrsdvrslfgmVLQDAWLYQGTIA 436
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNI--RFGKLDATdyEVVDAAKTANVDHFIRTMpdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDT 514
Cdd:COG2401 104 DAIgrKGDFKDAV--ELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488239013 515 RLEALIQKAMDRVM-EGRTSFVIA-HRLSTIRD--ADLILVMDQG 555
Cdd:COG2401 170 QTAKRVARNLQKLArRAGITLVVAtHHYDVIDDlqPDLLIFVGYG 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
361-557 |
8.61e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.55 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIrIDGIDTKSMSRSDVRSLFgmvlQDAWLYQ-GTIADNI 439
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMF----QDARLLPwKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 RFG-----KLDATD-YEVVDAAKTANvdhfirtmpdgyEMPINAEGdnvslGQKQLLTIARAVVSDPKILILDEATSSVD 513
Cdd:PRK11247 103 GLGlkgqwRDAALQaLAAVGLADRAN------------EWPAALSG-----GQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488239013 514 --TRLEalIQKAMDRVME--GRTSFVIAHRLS-TIRDADLILVMDQGQI 557
Cdd:PRK11247 166 alTRIE--MQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
356-566 |
1.40e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 356 PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG----------IDTKSMSRSDVRSLFG--- 422
Cdd:PRK10261 27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRGadm 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 -MVLQD-------AWLYQGTIADNIRFGKLDATDYEVVDAAKTANVdhfIRtMPDGYEMpINAEGDNVSLGQKQLLTIAR 494
Cdd:PRK10261 107 aMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQ---VR-IPEAQTI-LSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 495 AVVSDPKILILDEATSSVDTRLEALIQ---KAMDRVMEGRTSFvIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMSMGVIF-ITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
349-569 |
2.26e-12 |
|
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: 69.71 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 349 HVDFA-YDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKT----TLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL--- 420
Cdd:COG4172 13 SVAFGqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 421 -FGMVLQDAW-----LYqgTIADNIrfgkldatdYEVV--------DAAKTANVDHFIRT-MPDGyEMPINAEGDNVSLG 485
Cdd:COG4172 93 rIAMIFQEPMtslnpLH--TIGKQI---------AEVLrlhrglsgAAARARALELLERVgIPDP-ERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 486 QKQLLTIARAVVSDPKILILDEATSSVDTRLEALI-------QKAMDRVMegrtsFVIAHRLSTIRD-ADLILVMDQGQI 557
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIldllkdlQRELGMAL-----LLITHDLGVVRRfADRVAVMRQGEI 235
|
250
....*....|..
gi 488239013 558 IEKGTHESLLAQ 569
Cdd:COG4172 236 VEQGPTAELFAA 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
359-525 |
2.59e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.84 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDAWLYQGTIADN 438
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGK--LDATDYEVVDAAKTANVDHFIRTmpdgyemPINAegdnVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRL 516
Cdd:TIGR01189 94 LHFWAaiHGGAQRTIEDALAAVGLTGFEDL-------PAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
....*....
gi 488239013 517 EALIQKAMD 525
Cdd:TIGR01189 163 VALLAGLLR 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-509 |
3.10e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.94 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 347 FDHVDFAYdPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIdgidtksmsRSDVRslFGMVLQ 426
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 DAWLYQG-TIADNIR--FGKLDA--TDYEVV---------DAAKTANVDHFIRTMpDGYEMPINAEG------------- 479
Cdd:COG0488 69 EPPLDDDlTVLDTVLdgDAELRAleAELEELeaklaepdeDLERLAELQEEFEAL-GGWEAEARAEEilsglgfpeedld 147
|
170 180 190
....*....|....*....|....*....|...
gi 488239013 480 ---DNVSLGQKQLLTIARAVVSDPKILILDEAT 509
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
358-566 |
3.16e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.32 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMsrSDVRSLFGMVLQDAWLY-QGTIA 436
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFpHMTVE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRFG----KL--DATDYEVVDAAKTANVDHFIRTMPdgyempinaegDNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:PRK11607 110 QNIAFGlkqdKLpkAEIASRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 511 SVDTRLEALIQKAMDRVME--GRTSFVIAH-RLSTIRDADLILVMDQGQIIEKGTHESL 566
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
338-557 |
3.76e-12 |
|
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: 68.70 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 338 PETIlGDVTFD--HVDfAYDPKKPLIQ---DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD-KGAIRIDG--IDT 409
Cdd:TIGR02633 250 PHEI-GDVILEarNLT-CWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 410 KSMSRSdVRSLFGMVLQDAwLYQGTIAD-----NIRFGKLD--ATDYEVVDAAKTANVDHFIRTM------PDgyeMPIN 476
Cdd:TIGR02633 328 RNPAQA-IRAGIAMVPEDR-KRHGIVPIlgvgkNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvktasPF---LPIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 477 aegdNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRD-ADLILVMDQ 554
Cdd:TIGR02633 403 ----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGE 478
|
...
gi 488239013 555 GQI 557
Cdd:TIGR02633 479 GKL 481
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
361-583 |
3.99e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDVR---SLFGMVLQDAwlyQGTIAD 437
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD---HPLHFGDYSyrsQRIRMIFQDP---STSLNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 NIRFGKLdatdyevVDAAKTANVDhfirTMPDGYEMPINAEGDNVSL--------------GQKQLLTIARAVVSDPKIL 503
Cdd:PRK15112 103 RQRISQI-------LDFPLRLNTD----LEPEQREKQIIETLRQVGLlpdhasyyphmlapGQKQRLGLARALILRPKVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 504 ILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA--QGGFYEKLYN 578
Cdd:PRK15112 172 IADEALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAspLHELTKRLIA 251
|
....*
gi 488239013 579 SQFAE 583
Cdd:PRK15112 252 GHFGE 256
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
368-558 |
4.79e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 368 VKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTK-SMSRSDVRSLFGMVLQDAWLY-QGTIADNI------ 439
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIpQLTIAENIflgref 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 --RFGKLDATD-YEVVDA-AKTANVDHFIRTMPdgyempinaeGDnVSLGQKQLLTIARAVVSDPKILILDEATSSV-DT 514
Cdd:PRK10762 107 vnRFGRIDWKKmYAEADKlLARLNLRFSSDKLV----------GE-LSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488239013 515 RLEALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
361-568 |
4.79e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 4.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDvDKGAIRIDGIDTKSMSRSD---VRSLFGMVLQDAWL------- 430
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPNSslnprln 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 431 YQGTIADNIRFGK--LDATDYE--VVDAAKTANVDHFIRtmpdgYEMPINAEGdnvslGQKQLLTIARAVVSDPKILILD 506
Cdd:PRK15134 381 VLQIIEEGLRVHQptLSAAQREqqVIAVMEEVGLDPETR-----HRYPAEFSG-----GQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 507 EATSSVDTRLEALIQKAMDRVMEG-RTSFV-IAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
358-568 |
9.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGaIRIDGiDTKSMSRS--------DVRSLFGMVLQDAW 429
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSG-DVLLGGRSifnyrdvlEFRRRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQGTIADNIRFGK-----LDATDYEVVDAAKTANVDHFIRTMPDGYEMPINAEGdnvslGQKQLLTIARAVVSDPKILI 504
Cdd:PRK14271 112 PFPMSIMDNVLAGVrahklVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSG-----GQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 505 LDEATSSVD----TRLEALIQKAMDRVmegrTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK14271 187 LDEPTSALDptttEKIEEFIRSLADRL----TVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
357-555 |
9.77e-12 |
|
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: 64.19 E-value: 9.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYD--VDKGAIRIDGID-TKSMSRSdvrslFGMVLQ-DAWLYQ 432
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPlDKNFQRS-----TGYVEQqDVHSPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNIRFgkldatdyevvdaakTANvdhfIRtmpdgyempinaegdNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:cd03232 94 LTVREALRF---------------SAL----LR---------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488239013 513 DTRLEALIQKAMDRV-MEGRTSFVIAHRLS--TIRDADLILVMDQG 555
Cdd:cd03232 140 DSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-561 |
1.00e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.32 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD-----KGAIRIDGIDTKSMSRSDVRSLFGMVLQ-DAWLYQG 433
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRFG----KLDATDYEVVDAAKTANVDhfiRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEAT 509
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488239013 510 SSVDTRLEALIQKAMDRVMEGRTSFVIAH-RLSTIRDADLILVMDQGQIIEKG 561
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
354-567 |
1.05e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 65.18 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 354 YDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD-----KGAIRIDGIDTKSmSRSD---VRSLFGMVL 425
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYS-PRTDtvdLRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 426 QDAWLYQGTIADNIRFG-KLDAT-DYEVVDAA-----KTANV-DHFIRTMPDgyempiNAEGdnVSLGQKQLLTIARAVV 497
Cdd:PRK14239 93 QQPNPFPMSIYENVVYGlRLKGIkDKQVLDEAvekslKGASIwDEVKDRLHD------SALG--LSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 498 SDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTI-RDADLILVMDQGQIIEKG-THESLL 567
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTKQMFM 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
353-568 |
1.18e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 353 AYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMS-RSDVRSLFGMVLQDAWLY 431
Cdd:PRK10895 12 AYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QG-TIADNIRFG---KLDATDYEVVDAAKTANVDHFIRTMPDGYempinaeGDNVSLGQKQLLTIARAVVSDPKILILDE 507
Cdd:PRK10895 91 RRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 508 ATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRL-STIRDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
355-568 |
2.03e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.34 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 355 DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKT----TLINLLMRFYDVDKGAIRIDGidtKSMSRSDVRS-LFGMVLQD-- 427
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDG---KPVAPCALRGrKIATIMQNpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 -AWLYQGTIADNIR-----FGKL--DATDYEVVDAAKTANVDHFIRTMPdgYEMpinaegdnvSLGQKQLLTIARAVVSD 499
Cdd:PRK10418 90 sAFNPLHTMHTHARetclaLGKPadDATLTAALEAVGLENAARVLKLYP--FEM---------SGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 500 PKILILDEATSSVDTRLEALIQKAMDRVMEGRTS--FVIAHRLSTI-RDADLILVMDQGQIIEKGTHESLLA 568
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-569 |
2.14e-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: 66.36 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIR-------IDGIDTKSMSRSDVRSLFGMVLQDAWLY-Q 432
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYpH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNI----------RFGKLDAtdyevVDAAKTANVDHfirtmpDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKI 502
Cdd:TIGR03269 380 RTVLDNLteaiglelpdELARMKA-----VITLKMVGFDE------EKAEEILDKYPDELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 503 LILDEATSSVD--TRLEAL--IQKAmdRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQ 569
Cdd:TIGR03269 449 VILDEPTGTMDpiTKVDVThsILKA--REEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
345-575 |
2.29e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 64.77 E-value: 2.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRS----D 416
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 417 VRSLFGMVLQ--DAWLYQGTIADNIRFGK----LDATDYEVVDAAKTANV----DHFIRTmpdgyemPINAEGdnvslGQ 486
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPqnfgVSQEEAEALAREKLALVgiseSLFEKN-------PFELSG-----GQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 487 KQLLTIARAVVSDPKILILDEATSSVDTR----LEALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKgrkeLMTLFKKLHQ---SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
250
....*....|....
gi 488239013 562 THESLLAQGGFYEK 575
Cdd:PRK13649 228 KPKDIFQDVDFLEE 241
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
302-553 |
3.17e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 66.31 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 302 VTQLSSVL---QSASAATKRVFEILDEPEEKENKVDVSLPETILGD---VTFDHVDFAYDPKKPLIQDLNFEVKAGQTVA 375
Cdd:TIGR00954 403 VDTLLQVLddvKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQdngIKFENIPLVTPNGDVLIESLSFEVPSGNNLL 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 376 VVGPTGAGKTTLINLLMRFYDVDKGAIRIDgiDTKSMSRSDVRSLFGM-VLQDAWLYQGTIADNIRFGKLDATDYEVVDa 454
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGELWPVYGGRLTKP--AKGKLFYVPQRPYMTLgTLRDQIIYPDSSEDMKRRGLSDKDLEQILD- 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 455 aktaNVD-HFIRTMPDGYEMpINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVmeGRTS 533
Cdd:TIGR00954 560 ----NVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITL 632
|
250 260
....*....|....*....|
gi 488239013 534 FVIAHRLSTIRDADLILVMD 553
Cdd:TIGR00954 633 FSVSHRKSLWKYHEYLLYMD 652
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
348-513 |
3.85e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 348 DHVDFAYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQD 427
Cdd:PRK10247 11 QNVGYLAGDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQGTIADNIRFgkldatDYEVvdAAKTANVDHFIRTMpDGYEMPINAEGDNV---SLGQKQLLTIARAVVSDPKILI 504
Cdd:PRK10247 90 PTLFGDTVYDNLIF------PWQI--RNQQPDPAIFLDDL-ERFALPDTILTKNIaelSGGEKQRISLIRNLQFMPKVLL 160
|
....*....
gi 488239013 505 LDEATSSVD 513
Cdd:PRK10247 161 LDEITSALD 169
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
100-280 |
4.60e-11 |
|
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: 64.04 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAvsgaLQQAFIGIVN----AILGITLAAAMMFYIQPMMALI-SMI 174
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDT----LDNLYLRVLSppvvALLVILATILFLAFFSPALALIlLAG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 175 MIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMP 254
Cdd:cd18585 145 LLLAGVVIPLLFYRLGKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQA 224
|
170 180
....*....|....*....|....*.
gi 488239013 255 LVQLTAYATYIGMAVLGSFYVITGAI 280
Cdd:cd18585 225 LMILLSGLTVWLVLWLGAPLVQNGAL 250
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-557 |
5.20e-11 |
|
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: 61.68 E-value: 5.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSL-FGMV----LQDAWLYQ 432
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVpedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNIRFGKLdatdyevvdaaktanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:cd03215 93 LSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488239013 513 D--TRLE--ALIQKAMDrvmEGRTSFVIAHRLSTIRD-ADLILVMDQGQI 557
Cdd:cd03215 136 DvgAKAEiyRLIRELAD---AGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
356-558 |
8.23e-11 |
|
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: 61.51 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 356 PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLL---MRFYDVDKGAIRIDGIDTKSMSRSdvrslfgmvlqdawlYQ 432
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---------------YP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTI----ADNIRFGKLdaTDYEVVDAAKTANVDHFIRtmpdgyempinaegdNVSLGQKQLLTIARAVVSDPKILILDEA 508
Cdd:cd03233 83 GEIiyvsEEDVHFPTL--TVRETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 509 TSSVD--TRLEAL-IQKAMDRVMEGrTSFVIAHRLS-TIRDA-DLILVMDQGQII 558
Cdd:cd03233 146 TRGLDssTALEILkCIRTMADVLKT-TTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-557 |
8.83e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.57 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 338 PETIlGDVTF--DHVDfAYDPKKPLIQ---DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYD-VDKGAIRIDG--IDT 409
Cdd:PRK13549 252 PHTI-GEVILevRNLT-AWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 410 KSmSRSDVRSLFGMVLQDAWLY----QGTIADNIRFGKLDA-TDYEVVD-AAKTANVDHFIRTM------PdgyEMPINa 477
Cdd:PRK13549 330 RN-PQQAIAQGIAMVPEDRKRDgivpVMGVGKNITLAALDRfTGGSRIDdAAELKTILESIQRLkvktasP---ELAIA- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 478 egdNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRD-ADLILVMDQG 555
Cdd:PRK13549 405 ---RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEG 481
|
..
gi 488239013 556 QI 557
Cdd:PRK13549 482 KL 483
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-538 |
8.83e-11 |
|
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: 62.10 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFGMVlqdAWLyqgTIADN 438
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqITEPGPDRMVVFQNYSLL---PWL---TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGkLDATDYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVD--TRl 516
Cdd:TIGR01184 75 IALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalTR- 150
|
170 180
....*....|....*....|...
gi 488239013 517 EALIQKAMDRVMEGR-TSFVIAH 538
Cdd:TIGR01184 151 GNLQEELMQIWEEHRvTVLMVTH 173
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
350-584 |
9.69e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 9.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 350 VDFAYDPKKPL----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRS---------- 415
Cdd:PRK13651 8 IVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvlekl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 416 --------------DVRSLFGMVLQDA--WLYQGTIADNIRFGKLD-ATDYEvvDAAKTANVDHFIRTMPDGY--EMPIN 476
Cdd:PRK13651 88 viqktrfkkikkikEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmGVSKE--EAKKRAAKYIELVGLDESYlqRSPFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 477 AEGdnvslGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRL-STIRDADLILVMDQ 554
Cdd:PRK13651 166 LSG-----GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKD 240
|
250 260 270
....*....|....*....|....*....|
gi 488239013 555 GQIIEkgthesllaQGGFYEKLYNSQFAEE 584
Cdd:PRK13651 241 GKIIK---------DGDTYDILSDNKFLIE 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-566 |
1.33e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLfGMVL--QDAWLYQG-TI 435
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL-GIYLvpQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFGkLDATdyevvdAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSS---V 512
Cdd:PRK15439 104 KENILFG-LPKR------QASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASltpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 513 DTrlEALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:PRK15439 175 ET--ERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
354-562 |
1.41e-10 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 62.94 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 354 YDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLfGMVLQDAWLY-Q 432
Cdd:PRK11650 13 YDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RDI-AMVFQNYALYpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 433 GTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyempinAEgdnVSLGQKQLLTIARAVVSDPKILILD 506
Cdd:PRK11650 91 MSVRENMAYGlkirGMPKAEIEerVAEAARILELEPLLDRKP--------RE---LSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 507 EATSSVDT------RLEalIQKAMDRVmeGRTSFVIAH-RLSTIRDADLILVMDQGQIIEKGT 562
Cdd:PRK11650 160 EPLSNLDAklrvqmRLE--IQRLHRRL--KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
111-291 |
1.64e-10 |
|
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: 62.48 E-value: 1.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 111 RLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFI-GIVNAILGItLAAAMMFYIQPMMALISMIMipTSIWISKRVIna 189
Cdd:cd18567 87 RLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVeALLDGLMAI-LTLVMMFLYSPKLALIVLAA--VALYALLRLA-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 190 sqkYFQSMQNSLGEL-------NGYVQENMTGFSVLKVYGREKETLEGF-----KKVNHSLKYFGFRAAFISglmmpLVQ 257
Cdd:cd18567 161 ---LYPPLRRATEEQivasakeQSHFLETIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQILFSA-----ANG 232
|
170 180 190
....*....|....*....|....*....|....
gi 488239013 258 LTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQY 291
Cdd:cd18567 233 LLFGLENILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-568 |
1.95e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.28 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLL--MRFYDVDKGAI-------------------- 402
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 403 -------------RIDGIDTKSMSRSDVRSLFGMVLQDAW-LY-QGTIADNIrFGKLDATDYEVVDAAKTAnVDhFIRTM 467
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFaLYgDDTVLDNV-LEALEEIGYEGKEAVGRA-VD-LIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 468 PDGYEMPINAEgdNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVI-AHRLSTIRD 545
Cdd:TIGR03269 157 QLSHRITHIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLtSHWPEVIED 234
|
250 260
....*....|....*....|....
gi 488239013 546 -ADLILVMDQGQIIEKGTHESLLA 568
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
19-319 |
2.11e-10 |
|
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: 62.11 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 19 RGTFLLVILFTVLTVAFNVALPyvtglptteisrniangesiNFSYIF--KCLI-----WITVVGIGYCISQLLSGVLmt 91
Cdd:cd18569 1 RSALLFVVLAGLLLVIPGLVIP--------------------VFSRIFidDILVgglpdWLRPLLLGMALTALLQGLL-- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 92 NVVQSamHDLRRdIEEKIN------------RLPVSYFDKNQQGNILSRV-TND--VDAVSGALQQAFIGIVNAIlgitL 156
Cdd:cd18569 59 TWLQQ--YYLLR-LETKLAlssssrffwhvlRLPVEFFSQRYAGDIASRVqSNDrvANLLSGQLATTVLNLVMAV----F 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 157 AAAMMFYIQPMMALI----SMIMIPTSIWISKRVINASQKyfqsMQNSLGELNGYVqenMTGFSV---LKVYGREKETLE 229
Cdd:cd18569 132 YALLMLQYDVPLTLIgiaiALLNLLVLRLVSRKRVDLNRR----LLQDSGKLTGTT---MSGLQMietLKASGAESDFFS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 230 ---GFK-KVNHSLKYFGFRAAFISGLMMPLVQLTayatyiGMAVL--GSFYVITGAIVVGQLQAFIQYIWQISQPMGNVT 303
Cdd:cd18569 205 rwaGYQaKVLNAQQELGRTNQLLGALPTLLSALT------NAAILglGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLV 278
|
330
....*....|....*.
gi 488239013 304 QLSSVLQSASAATKRV 319
Cdd:cd18569 279 GLGGTLQEMRGDMERL 294
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
361-561 |
2.55e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSR-SDVRSLFGMVLQDAWLY---QGT 434
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGKlQALRRDIQFIFQDPYASldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 435 IADNIR-----FGKLDATdyevVDAAKTANVDHFIRTMPD-GYEMPINAEGdnvslGQKQLLTIARAVVSDPKILILDEA 508
Cdd:PRK10261 420 VGDSIMeplrvHGLLPGK----AAAARVAWLLERVGLLPEhAWRYPHEFSG-----GQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 509 TSSVDTRLEA-LIQKAMDRVMEGRTSFV-IAHRLSTI-RDADLILVMDQGQIIEKG 561
Cdd:PRK10261 491 VSALDVSIRGqIINLLLDLQRDFGIAYLfISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
357-577 |
2.56e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.54 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 357 KKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDA-------- 428
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAttpgditv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 429 --WLYQGTIADNIRFGKLDATDYEVVDAAKTANvdhfirtmpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILD 506
Cdd:PRK10253 99 qeLVARGRYPHQPLFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 507 EATSSVDTR-----LEALIQkaMDRVmEGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLLAqGGFYEKLY 577
Cdd:PRK10253 169 EPTTWLDIShqidlLELLSE--LNRE-KGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-AELIERIY 241
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
345-568 |
2.91e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLIQdLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-----TKSMSRSDV-- 417
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHE-VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwqTAKIMREAVai 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 418 ----RSLFG-MVLQDAWLYQGTIADNIRFGKLDATDYEVvdaaktanvdhfirtMPDGYEMPINAEGdNVSLGQKQLLTI 492
Cdd:PRK11614 85 vpegRRVFSrMTVEENLAMGGFFAERDQFQERIKWVYEL---------------FPRLHERRIQRAG-TMSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVdtrLEALIQKAMDRVM----EGRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
.
gi 488239013 568 A 568
Cdd:PRK11614 226 A 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
345-521 |
4.43e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 58.23 E-value: 4.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIridgidtksmsrsdvrslfgmv 424
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 lqdawlyqgTIADNIRFGkldatdYevvdaaktanVDHFirtmpdgyempinaegdnvSLGQKQLLTIARAVVSDPKILI 504
Cdd:cd03221 58 ---------TWGSTVKIG------Y----------FEQL-------------------SGGEKMRLALAKLLLENPNLLL 93
|
170
....*....|....*...
gi 488239013 505 LDEATSSVDTR-LEALIQ 521
Cdd:cd03221 94 LDEPTNHLDLEsIEALEE 111
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
100-319 |
5.57e-10 |
|
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: 60.68 E-value: 5.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTS 179
Cdd:cd18782 76 ELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 180 I---WISKRVInasQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFK-KVNHSLKYfGFRAAFISGLMMPL 255
Cdd:cd18782 155 LlltFLFGPIL---RRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQnRYARSLGE-GFKLTVLGTTSGSL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 256 VQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18782 231 SQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-558 |
9.57e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD--KGAIRIDGIDTKSMSRSDVRSLfGMVL--QDAWLYQG-TIAD 437
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERA-GIAIihQELALVKElSVLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 NI-------RFGKLDatdyevvDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATS 510
Cdd:PRK13549 102 NIflgneitPGGIMD-------YDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488239013 511 SVdTRLEA--LIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:PRK13549 173 SL-TESETavLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
111-319 |
1.22e-09 |
|
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: 59.82 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 111 RLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPT----SIWISKRV 186
Cdd:cd18588 87 RLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLyallSLLVTPIL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 187 INASQKYFQ-SMQNslgelNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYI 265
Cdd:cd18588 166 RRRLEEKFQrGAEN-----QSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 266 GMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18588 241 AILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
363-565 |
1.76e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.50 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKA-----GQTvAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtksmsrsdvRSLF---------------G 422
Cdd:PRK11144 12 DLCLTVNLtlpaqGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-----------RVLFdaekgiclppekrriG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 423 MVLQDAWLY-QGTIADNIRFGkldatdyevvdaAKTANVDHF--------IRTMPDGYemPINAEGdnvslGQKQLLTIA 493
Cdd:PRK11144 80 YVFQDARLFpHYKVRGNLRYG------------MAKSMVAQFdkivallgIEPLLDRY--PGSLSG-----GEKQRVAIG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 494 RAVVSDPKILILDEATSSVD--------TRLEALIQkamdrvmEGRTSFV-IAHRLSTI-RDADLILVMDQGQIIEKGTH 563
Cdd:PRK11144 141 RALLTAPELLLMDEPLASLDlprkrellPYLERLAR-------EINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPL 213
|
..
gi 488239013 564 ES 565
Cdd:PRK11144 214 EE 215
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
364-567 |
1.93e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 364 LNFEVKAGQTVAVVGPTGAGKTTLINLL--MRFYdvdKGAIRIDGIDTKSMSRSD-----------VRSLFGM-VLQDAW 429
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMagLLPG---SGSIQFAGQPLEAWSAAElarhraylsqqQTPPFAMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQgtiADNIRFGKLDATDYEVVDAAKtanvdhfirtMPDGYEMPINAegdnVSLGQKQ-------LLTIARAVVSDPKI 502
Cdd:PRK03695 92 LHQ---PDKTRTEAVASALNEVAEALG----------LDDKLGRSVNQ----LSGGEWQrvrlaavVLQVWPDINPAGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 503 LILDEATSSVDTRLEAliqkAMDRVME-----GRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGTHESLL 567
Cdd:PRK03695 155 LLLDEPMNSLDVAQQA----ALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
363-558 |
2.21e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSmSRSDVRSLFGMVLQDAWLY-QGTIADNI 439
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKS-SKEALENGISMVHQELNLVlQRSVMDNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 440 RFGKLDATDYeVVDAAKTANVdhfIRTMPDGYEMPIN--AEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR-- 515
Cdd:PRK10982 95 WLGRYPTKGM-FVDQDKMYRD---TKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKev 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488239013 516 --LEALIQKAMDRvmeGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:PRK10982 171 nhLFTIIRKLKER---GCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
38-297 |
2.25e-09 |
|
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: 58.64 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 38 ALPYVTGLPTTEIsrnIANGESINFSYifkCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYF 117
Cdd:cd18589 14 AIPYYTGRMTDWI---MNKDAPEAFTA---AITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 118 DKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIWISKRVINASQKYFQSM 197
Cdd:cd18589 88 DSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 198 QNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVIT 277
Cdd:cd18589 168 QKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTA 247
|
250 260
....*....|....*....|
gi 488239013 278 GAIVVGQLQAFIQYIWQISQ 297
Cdd:cd18589 248 GTVSSGDLVTFVLYELQFTS 267
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
359-568 |
2.29e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSR---------SDVRSLFGMVLqd 427
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDglangivyiSEDRKRDGLVL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 awlyqG-TIADNIRFGKLDATDYEVVD---AAKTANVDHFIRTM----PdGYEMPINaegdNVSLGQKQLLTIARAVVSD 499
Cdd:PRK10762 344 -----GmSVKENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 500 PKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRD-ADLILVMDQGQI-----IEKGTHESLLA 568
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFkAEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
362-559 |
2.37e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 362 QDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRF-----YDvdkGAIRIDGidtKSMSRSDVRS--LFGMVL--QD-AWLY 431
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsYE---GEILFDG---EVCRFKDIRDseALGIVIihQElALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QGTIADNIRFGKLDATdYEVVDAAKTanvdhFIRTM-----------PDgyeMPInaegDNVSLGQKQLLTIARAVVSDP 500
Cdd:NF040905 92 YLSIAENIFLGNERAK-RGVIDWNET-----NRRARellakvgldesPD---TLV----TDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488239013 501 KILILDEATSSV-DTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIE 559
Cdd:NF040905 159 KLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
371-562 |
2.92e-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: 55.84 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 371 GQTVAVVGPTGAGKTTLINLLMRFYDVD-KGAIRIDGIDTKSMSRSDVRslfgmvlqdawlyqgtiadnirfgkldatdy 449
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPgGGVIYIDGEDILEEVLDQLL------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 450 evvdaaktanvdhfirtmpdgyEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMD---- 525
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488239013 526 ---RVMEGRTSFVIAHRLSTIRDADLILVMDQGQIIEKGT 562
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
358-558 |
3.18e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.65 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDV--------------RSLFGM 423
Cdd:COG1129 265 GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPrdairagiayvpedRKGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 424 VLQDawlyqgTIADNI---------RFGKLDatdyevvDAAKTANVDHFIRTM---PDGYEMPINaegdNVSLG--QKQL 489
Cdd:COG1129 342 VLDL------SIRENItlasldrlsRGGLLD-------RRRERALAEEYIKRLrikTPSPEQPVG----NLSGGnqQKVV 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488239013 490 ltIARAVVSDPKILILDEATSSVD--TRLEalIQKAMDR-VMEGRTSFVIahrlST-----IRDADLILVMDQGQII 558
Cdd:COG1129 405 --LAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
315-524 |
3.41e-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: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 315 ATKRVFEILDEPEEKENKVDVSLPETILGDVTFDHVDFAYD-----PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLIN 389
Cdd:TIGR00956 728 EAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEvkikkEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 390 LLMRfyDVDKGAIRID-------GIDTkSMSRSdvrslFGMVLQ-DAWLYQGTIADNIRFGKLDATDYEVVDAAKTANVD 461
Cdd:TIGR00956 808 VLAE--RVTTGVITGGdrlvngrPLDS-SFQRS-----IGYVQQqDLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVE 879
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 462 HFIR--TMPDGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILI-LDEATSSVDTRLEALIQKAM 524
Cdd:TIGR00956 880 EVIKllEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLM 945
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
358-575 |
4.12e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG--IDTKSMSRSDVRSLFGMVLQDA--WLYQG 433
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRFG--KLDATDYEV---VDAAKT-ANVDHFirtmpdgYEMPINAegdnVSLGQKQLLTIARAVVSDPKILILDE 507
Cdd:PRK13638 94 DIDSDIAFSlrNLGVPEAEItrrVDEALTlVDAQHF-------RHQPIQC----LSHGQKKRVAIAGALVLQARYLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 508 ATSSVD----TRLEALIQKAmdrVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQGGFYEK 575
Cdd:PRK13638 163 PTAGLDpagrTQMIAIIRRI---VAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
358-566 |
4.17e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRS---DVRSLFGMVLQDAWLYQG- 433
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSMLFQSGALFTDm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 TIADNIRFGKLDATD-------------YEVVDAAKTANVdhfirtmpdgyeMPINAEGdnvslGQKQLLTIARAVVSDP 500
Cdd:PRK11831 100 NVFDNVAYPLREHTQlpapllhstvmmkLEAVGLRGAAKL------------MPSELSG-----GMARRAALARAIALEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESL 566
Cdd:PRK11831 163 DLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
358-569 |
4.51e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLM--RFYDVDKGAIRIDGIDTKSMSRSDvRSLFGMVLqdAWLYQGTI 435
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFM--AFQYPVEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 --ADNIRF--GKLDAT-DYEVVDAAKTANVDHFIRTMPDGYEMPINAEGDNV----SLGQKQLLTIARAVVSDPKILILD 506
Cdd:PRK09580 91 pgVSNQFFlqTALNAVrSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 507 EATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRD---ADLILVMDQGQIIEKGTHeSLLAQ 569
Cdd:PRK09580 171 ESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSGDF-TLVKQ 235
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
342-404 |
4.56e-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: 4.56e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 342 LGD--VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRI 404
Cdd:TIGR03719 318 LGDkvIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
39-319 |
5.66e-09 |
|
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: 57.71 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 39 LPYVTGLptteisrnIANGESI--NFSYIFKCLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSY 116
Cdd:cd18784 15 IPYYTGQ--------VIDGIVIekSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 117 FDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIWISKRVINASQKYFQS 196
Cdd:cd18784 87 FDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 197 MQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFK-KVNHSLKYFGFRAAFISGLMMpLVQLTAYATYIGMAVLGSFYV 275
Cdd:cd18784 167 VQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSeKLKDTYKLKIKEALAYGGYVW-SNELTELALTVSTLYYGGHLV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488239013 276 ITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18784 246 ITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
101-285 |
5.78e-09 |
|
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: 57.67 E-value: 5.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSI 180
Cdd:cd18561 71 LRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 181 ----WISKRVINASQKYFQSMqnslGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSlkyfgFRAAFISGLMMPLV 256
Cdd:cd18561 151 lspaLWDRLAKDTGRRHWAAY----GRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAED-----LRQATMKVLAVSLL 221
|
170 180 190
....*....|....*....|....*....|....
gi 488239013 257 QL--TAYATYIG---MAVLGSFYVITGAIVVGQL 285
Cdd:cd18561 222 SSgiMGLATALGtalALGVGALRVLGGQLTLSSL 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
358-580 |
7.43e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD-----KGAIRIDGidtKSMSRSDVRSLFGMV-LQDAWLY 431
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHG---ESLLHASEQTLRGVRgNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 432 QGTIADNIRFGKLDATDYEVV--------DAAKTANVDHFIRTmpdGYEMPINAEGD---NVSLGQKQLLTIARAVVSDP 500
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQLYEVLslhrgmrrEAARGEILNCLDRV---GIRQAAKRLTDyphQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 501 KILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLA--QGGFYEK 575
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSapTHPYTQK 255
|
....*
gi 488239013 576 LYNSQ 580
Cdd:PRK15134 256 LLNSE 260
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
99-319 |
1.04e-08 |
|
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: 56.82 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 99 HDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAV----SGALQQAFIGIVNAILGITLaaamMFYIQPMMALISMI 174
Cdd:cd18566 75 HRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIreflTGQALLALLDLPFVLIFLGL----IWYLGGKLVLVPLV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 175 MIPTSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMP 254
Cdd:cd18566 150 LLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQT 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 255 LVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18566 230 LGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPLQRAFGLWTRFQQVRVAVRRL 294
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
358-569 |
1.29e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.19 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRF--YDVDKGAIRIDGIDTKSMSrSDVRSLFGMVLqdAWLYQGTI 435
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFL--AFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 A--DNIRF--------------GKLDATD-YEVV-DAAKTANVD-HFI-RTMPDGYempinaegdnvSLGQKQLLTIARA 495
Cdd:CHL00131 97 PgvSNADFlrlaynskrkfqglPELDPLEfLEIInEKLKLVGMDpSFLsRNVNEGF-----------SGGEKKRNEILQM 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 496 VVSDPKILILDEATSSVDtrLEAL--IQKAMDRVMEGRTSFV-IAH--RLSTIRDADLILVMDQGQIIEKGTHEslLAQ 569
Cdd:CHL00131 166 ALLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE--LAK 240
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
114-317 |
1.48e-08 |
|
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: 56.19 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 114 VSYFDKNQQGNILSRVTNDVDAVSGALQQAfigiVNAILGITLAA----AMMFYIQPMMALISMIMIPTSIWISKRVINA 189
Cdd:cd18590 84 IGFFEKTKTGDLTSRLSTDTTLMSRSVALN----ANVLLRSLVKTlgmlGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 190 SQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKV---NHSLKYfgfRAAFISGLMMPLVQLTAYATYIG 266
Cdd:cd18590 160 HQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEAlerTYNLKD---RRDTVRAVYLLVRRVLQLGVQVL 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 267 MAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGN-VTQLSSVLQSASAATK 317
Cdd:cd18590 237 MLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTlVYIYGDMLSNVGAAAK 288
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
26-301 |
1.53e-08 |
|
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: 56.35 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGLPTTEISRNIANGESINFSYIfkcliwitvvgIGYCISQLLS-------GVLMTNVVQSAM 98
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAVPLLLL-----------LAYGLARILSslfnelrDALFARVSQRAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 99 HDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQ-PMMALISMIMIP 177
Cdd:cd18582 71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYgWSYALITLVTVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 178 TSIWISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREK-------ETLEGFK----KVNHSLKYFGFRAA 246
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEyeaerydKALAKYEkaavKSQTSLALLNIGQA 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 247 FISGLMMplvqltayatyIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGN 301
Cdd:cd18582 231 LIISLGL-----------TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNF 274
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
361-574 |
1.93e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.27 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKT----TLINLLMRFYDVDkGAIRIDGIDTKSMSRSDVRSL----FGMVLQDAW--- 429
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPEKELNKLraeqISMIFQDPMtsl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 ---------------LYQGtiadnirFGKLDATDYEV--VDAAKTANVDHFIRTMPDGYempinaegdnvSLGQKQLLTI 492
Cdd:PRK09473 111 npymrvgeqlmevlmLHKG-------MSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 493 ARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFV-IAHRLSTIRD-ADLILVMDQGQIIEKGTHESLlaq 569
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV--- 249
|
....*
gi 488239013 570 ggFYE 574
Cdd:PRK09473 250 --FYQ 252
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
326-547 |
2.06e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 326 PEEKENKVDVSLPET----ILGDVTFDHVDfaydpkKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLlmrfydvdkga 401
Cdd:PRK10938 243 PEPDEPSARHALPANepriVLNNGVVSYND------RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL----------- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 402 irIDGIDTKSMSrSDVrSLFGMvlqdawlYQG---TIADNIR-FGKLDAT---DYEVVDAAKTANVDHFI------RTMP 468
Cdd:PRK10938 306 --ITGDHPQGYS-NDL-TLFGR-------RRGsgeTIWDIKKhIGYVSSSlhlDYRVSTSVRNVILSGFFdsigiyQAVS 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 469 D-------------GYEMPI-NAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTS 533
Cdd:PRK10938 375 DrqqklaqqwldilGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQ 454
|
250 260
....*....|....*....|....*.
gi 488239013 534 --FV----------IAHRLSTIRDAD 547
Cdd:PRK10938 455 llFVshhaedapacITHRLEFVPDGD 480
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
364-562 |
2.86e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.85 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 364 LNFEVKAGQTVAVVGPTGAGKTTlinLLMRFYDV--DKGAIRIDGIDTKSMS-------RS----DVRSLFGM-VLQDAW 429
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMAGLlpGQGEILLNGRPLSDWSaaelarhRAylsqQQSPPFAMpVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 430 LYQgtiADNIRFGKLDATDYEVVDAAKTAnvdhfirtmpDGYEMPINAegdnVSLGQKQ-------LLTIARAVVSDPKI 502
Cdd:COG4138 92 LHQ---PAGASSEAVEQLLAQLAEALGLE----------DKLSRPLTQ----LSGGEWQrvrlaavLLQVWPTINPEGQL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 503 LILDEATSSVDTRLEAliqkAMDRVME-----GRTSFVIAHRLS-TIRDADLILVMDQGQIIEKGT 562
Cdd:COG4138 155 LLLDEPMNSLDVAQQA----ALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
361-558 |
3.16e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.37 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFY---DVDkGAIRIDGIDTKSMSRSDV-RSLFGMVLQDAWLYQG-TI 435
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWD-GEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIRFG-KLDATDYEVVDAAKTANVDHFIR--TMPDgyeMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSV 512
Cdd:TIGR02633 96 AENIFLGnEITLPGGRMAYNAMYLRAKNLLRelQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488239013 513 -DTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRD-ADLILVMDQGQII 558
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
358-520 |
3.73e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 358 KPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMsRSDvrslfgmvLQDAWLYQG---- 433
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDE--------YHQDLLYLGhqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 434 -----TIADNIRF-GKL--DATDYEVVDAAKTANVdhfirtmpDGYEM-PINAegdnVSLGQKQLLTIARAVVSDPKILI 504
Cdd:PRK13538 85 iktelTALENLRFyQRLhgPGDDEALWEALAQVGL--------AGFEDvPVRQ----LSAGQQRRVALARLWLTRAPLWI 152
|
170 180
....*....|....*....|
gi 488239013 505 LDEATSSVDT----RLEALI 520
Cdd:PRK13538 153 LDEPFTAIDKqgvaRLEALL 172
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
355-564 |
5.41e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 5.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 355 DPKKPL--IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYD----VDKGAIRIDGIDTKSMSRSDVRSLFG----MV 424
Cdd:PRK11022 15 DESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLVGaevaMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWL---------YQGTIADNIRFGKLDATDYE-VVDAAKTANVdhfirtmPDGyEMPINAEGDNVSLGQKQLLTIAR 494
Cdd:PRK11022 95 FQDPMTslnpcytvgFQIMEAIKVHQGGNKKTRRQrAIDLLNQVGI-------PDP-ASRLDVYPHQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 495 AVVSDPKILILDEATSSVDTRLEALI---------QKAMDRVMegrtsfvIAHRLSTIRD-ADLILVMDQGQIIEKGTHE 564
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDVTIQAQIielllelqqKENMALVL-------ITHDLALVAEaAHKIIVMYAGQVVETGKAH 239
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-404 |
5.88e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 5.88e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488239013 342 LGDVT--FDHVDFAYDPKKpLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRI 404
Cdd:PRK11819 320 LGDKVieAENLSKSFGDRL-LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
345-403 |
8.23e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.90 E-value: 8.23e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488239013 345 VTFDHVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIR 403
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-585 |
1.28e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 53.55 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGID-TKsmSRSDVRSLFGMV------------LQD 427
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFK--RRKEFARRIGVVfgqrsqlwwdlpAID 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 428 AWLYQGTIadnirfgkldatdYEVVDAAKTANVDHFIrtmpdgyEM---------PINaegdNVSLGQKQLLTIARAVVS 498
Cdd:COG4586 116 SFRLLKAI-------------YRIPDAEYKKRLDELV-------ELldlgelldtPVR----QLSLGQRMRCELAAALLH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 499 DPKILILDEATSSVD----TRLEALIqKAMDRVmEGRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQGGfY 573
Cdd:COG4586 172 RPKILFLDEPTIGLDvvskEAIREFL-KEYNRE-RGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG-P 248
|
250
....*....|..
gi 488239013 574 EKLYNSQFAEEA 585
Cdd:COG4586 249 YKTIVLELAEPV 260
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
363-557 |
1.82e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 363 DLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDvRSLFGMVL-----QDAWLYqgtiad 437
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVYlpedrQSSGLY------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 438 nirfgkLDATDYEVVDAAKTANVDHFIRTMPD-----GYEMPIN---AEGDN----VSLGQKQLLTIARAVVSDPKILIL 505
Cdd:PRK15439 354 ------LDAPLAWNVCALTHNRRGFWIKPAREnavleRYRRALNikfNHAEQaartLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 506 DEATSSVDTRLEALIQKAMDRVMEGRTSFV-IAHRLSTIRD-ADLILVMDQGQI 557
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-547 |
1.83e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 349 HVDFAYDpKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDVRSLFGMVLQDA 428
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 429 WLYQGTIADNIRFG-KLDATDYEVVDAAKTANVDHFIrTMPDGYempinaegdnVSLGQKQLLTIARAVVSDPKILILDE 507
Cdd:PRK13540 85 INPYLTLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488239013 508 ATSSVDTR-LEALIQKAMDRVMEGRTSFVIAHRLSTIRDAD 547
Cdd:PRK13540 154 PLVALDELsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
360-557 |
1.96e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 360 LIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLmrfYDVDK---GAIRIDG--IDTKSmSRSDVRSlfGMVL------QDA 428
Cdd:PRK11288 268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLL---YGATRrtaGQVYLDGkpIDIRS-PRDAIRA--GIMLcpedrkAEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 429 WLYQGTIADNI---------RFGKLdatdyeVVDAAKTANVDHFIRTM----PDGyEMPINaegdNVSLGQKQLLTIARA 495
Cdd:PRK11288 342 IIPVHSVADNInisarrhhlRAGCL------INNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 496 VVSDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRL-STIRDADLILVMDQGQI 557
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGRI 474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
324-562 |
2.23e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 324 DEPEEKENKVDVS----LPETILGdVTFDHVDFAYD-PKK-----------PLIQDLNFEVKAGQTVAVVGPTGAGKTTL 387
Cdd:PLN03140 844 DSSLEAANGVAPKrgmvLPFTPLA-MSFDDVNYFVDmPAEmkeqgvtedrlQLLREVTGAFRPGVLTALMGVSGAGKTTL 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 388 INLLM--RFYDVDKGAIRIDGIDTKSMS---------RSDVRSLfGMVLQDAWLYQGTIADNIRFGKLDATDY--EVVDA 454
Cdd:PLN03140 923 MDVLAgrKTGGYIEGDIRISGFPKKQETfarisgyceQNDIHSP-QVTVRESLIYSAFLRLPKEVSKEEKMMFvdEVMEL 1001
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 455 AKTANVDHFIRTMPdgyempiNAEGdnVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAM-DRVMEGRTS 533
Cdd:PLN03140 1002 VELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTV 1072
|
250 260 270
....*....|....*....|....*....|..
gi 488239013 534 FVIAHRLST-IRDA--DLILVMDQGQIIEKGT 562
Cdd:PLN03140 1073 VCTIHQPSIdIFEAfdELLLMKRGGQVIYSGP 1104
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
22-238 |
5.87e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 51.32 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYvtglpTTEISRNIANGEsinfsYIfkcliWITVV-GIGYCISQLLSGVLMTNVVQSAMHD 100
Cdd:cd18606 5 LLLLILSQFAQVFTNLWLSF-----WTEDFFGLSQGF-----YI-----GIYAGlGVLQAIFLFLFGLLLAYLGIRASKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSI 180
Cdd:cd18606 70 LHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488239013 181 WIskrvinasQKYFQ----------SMQNSLgeLNGYVQENMTGFSVLKVYGREKEtlegFKKVNHSL 238
Cdd:cd18606 150 FI--------ANYYRassrelkrleSILRSF--VYANFSESLSGLSTIRAYGAQDR----FIKKNEKL 203
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
359-513 |
6.46e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 359 PLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGidtKSMSRSDvRSLFgmvlqdawlyqgtIADN 438
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGD-RSRF-------------MAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 439 IRFGKLDAtdyevvDAAKTANVdHFIRTMpDGY---EMPINAEG------------DNVSLGQKQLLTIARAVVSDPKIL 503
Cdd:PRK13543 88 GHLPGLKA------DLSTLENL-HFLCGL-HGRrakQMPGSALAivglagyedtlvRQLSAGQKKRLALARLWLSPAPLW 159
|
170
....*....|
gi 488239013 504 ILDEATSSVD 513
Cdd:PRK13543 160 LLDEPYANLD 169
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
361-584 |
7.36e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDG----IDTKSMSRSDVRSLFGMVLQDawLYQGTIA 436
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsaalIAISSGLNGQLTGIENIELKG--LMMGLTK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 437 DNIRfgkldATDYEVVDaakTANVDHFIRTMPDGYempinaegdnvSLGQKQLLTIARAVVSDPKILILDEATSSVDtrl 516
Cdd:PRK13545 118 EKIK-----EIIPEIIE---FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD--- 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488239013 517 EALIQKAMDRVME----GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKGTHESLLAQGGFYEKLYNSQFAEE 584
Cdd:PRK13545 176 QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEE 248
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
361-558 |
9.21e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 9.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 361 IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRIDGIDTKSMSRSDV----RSLFGMVLQDAWLYQG-TI 435
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRYHLLSHlTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 436 ADNIrfgKLDATDYEVVDAAKTANVDHFIRTMpdGYEMPINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTR 515
Cdd:PRK10535 104 AQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488239013 516 ----LEALIQKAMDRvmeGRTSFVIAHRLSTIRDADLILVMDQGQII 558
Cdd:PRK10535 179 sgeeVMAILHQLRDR---GHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
325-558 |
1.18e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 325 EPEEKENKVDVSLPETILgdvTFDHVDFAYDPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRI 404
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVL---EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 405 DGIDTKSMSRSDVRSL-----------FGMVLqdawlyQGTIADNIRFGKLDATDY---------EVVDAAKTAnVDHF- 463
Cdd:COG3845 318 DGEDITGLSPRERRRLgvayipedrlgRGLVP------DMSVAENLILGRYRRPPFsrggfldrkAIRAFAEEL-IEEFd 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 464 IRTmPDgyempINAEGDNVSLGQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKA-MDRVMEGRTSFVIAHRLST 542
Cdd:COG3845 391 VRT-PG-----PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRlLELRDAGAAVLLISEDLDE 464
|
250
....*....|....*..
gi 488239013 543 IRD-ADLILVMDQGQII 558
Cdd:COG3845 465 ILAlSDRIAVMYEGRIV 481
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
24-319 |
1.57e-06 |
|
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: 50.18 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 24 LVILFTVLTVAFNVALPYVTGLptteISRNIANGESINFSYIFKCLIWITVVGIGYCISQ-------LLSGVLMTNVVQS 96
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGL----LISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLhqyfflsFRLGMRVRSALSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 97 AMHdlrrdieEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIgIVNAILGITLAAAMMFY---IQPMMALISM 173
Cdd:cd18579 77 LIY-------RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHY-LWSAPLQIIVALYLLYRllgWAALAGLGVL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 174 I-MIPTSIWISKRVINASQKYFQSMQNSLGELNgyvqENMTGFSVLKVYGREKETLegfKKVNH-------SLKYFGFRA 245
Cdd:cd18579 149 LlLIPLQAFLAKLISKLRKKLMKATDERVKLTN----EILSGIKVIKLYAWEKPFL---KRIEElrkkelkALRKFGYLR 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488239013 246 AFISGLMMPLVQLTAYATYIGMAVLGSfyVITGAIVvgqlqaF--IQYIWQISQPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18579 222 ALNSFLFFSTPVLVSLATFATYVLLGN--PLTAAKV------FtaLSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
355-513 |
1.70e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 355 DPKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTL-INLLMRFYDVD-KGAIRIDG--IDTKSMSR---------SDVRSLF 421
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGRSYGRNiSGTVFKDGkeVDVSTVSDaidaglayvTEDRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 422 GMVLQDawlyqgTIADNIRFGKLDA-TDYEVVDAAKTANV-DHFIRTM----PDgyempINAEGDNVSLGQKQLLTIARA 495
Cdd:NF040905 350 GLNLID------DIKRNITLANLGKvSRRGVIDENEEIKVaEEYRKKMniktPS-----VFQKVGNLSGGNQQKVVLSKW 418
|
170
....*....|....*...
gi 488239013 496 VVSDPKILILDEATSSVD 513
Cdd:NF040905 419 LFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
69-271 |
1.89e-06 |
|
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: 49.72 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 69 LIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIV 148
Cdd:cd18584 40 LLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 149 NAILGITLAAAMMFYIQPMMALISMIMIPT----SIWISKRVINASQKYFQSMQnslgELNGYVQENMTGFSVLKVYGRE 224
Cdd:cd18584 120 LAAIVPLLILVAVFPLDWVSALILLVTAPLiplfMILIGKAAQAASRRQWAALS----RLSGHFLDRLRGLPTLKLFGRA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 225 KETLEGFKKVNHSlkyfgFRA--------AFISGLMMPLvqLTAYAT-----YIGMAVLG 271
Cdd:cd18584 196 RAQAARIARASED-----YRRrtmkvlrvAFLSSAVLEF--FATLSIalvavYIGFRLLG 248
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
345-513 |
4.02e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 48.57 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 345 VTFDHVDFAYDPKKPLiQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIridgidtksmsRSDVRSLFGMV 424
Cdd:PRK09544 5 VSLENVSVSFGQRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 425 LQDAWLyQGTIADNI-RFGKL--DATDYEVVDAAKTANVDHFirtmpdgyempINAEGDNVSLGQKQLLTIARAVVSDPK 501
Cdd:PRK09544 73 PQKLYL-DTTLPLTVnRFLRLrpGTKKEDILPALKRVQAGHL-----------IDAPMQKLSGGETQRVLLARALLNRPQ 140
|
170
....*....|..
gi 488239013 502 ILILDEATSSVD 513
Cdd:PRK09544 141 LLVLDEPTQGVD 152
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
22-251 |
4.51e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 48.62 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTT---EISRNIANGESINFsyifkcliWITV---VGIGYCISQLLSGVLMTNVVQ 95
Cdd:cd18604 1 WALLLLLFVLSQLLSVGQSWWLGIWASayeTSSALPPSEVSVLY--------YLGIyalISLLSVLLGTLRYLLFFFGSL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 96 SAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIM 175
Cdd:cd18604 73 RASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 176 IPTSIWISKRVINASQ--KYFQSmqNSLGELNGYVQENMTGFSVLKVYGREKE-TLEGFKKVNHSLKYF----------G 242
Cdd:cd18604 153 AALYVYIGRLYLRASRelKRLES--VARSPILSHFGETLAGLVTIRAFGAEERfIEEMLRRIDRYSRAFrylwnlnrwlS 230
|
....*....
gi 488239013 243 FRAAFISGL 251
Cdd:cd18604 231 VRIDLLGAL 239
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
23-284 |
5.54e-06 |
|
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: 48.43 E-value: 5.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 23 LLVILFTVLTVAF-NVALPYVTGLPTTEISR----NIANGESINFSYIFkcliwiTVVGIGYCISQLLSGVLMTNVVQSA 97
Cdd:cd18558 17 AFMVIFGDMTDSFtNGGMTNITGNSSGLNSSagpfEKLEEEMTLYAYYY------LIIGAIVLITAYIQGSFWGLAAGRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 98 MHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNA--------ILGITLAAAMMFYIqpmMA 169
Cdd:cd18558 91 TKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNiatfgtgfIIGFIRGWKLTLVI---LA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 170 LISMIMIPTSIWISKRVINASQKyfqsmQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFIS 249
Cdd:cd18558 168 ISPVLGLSAVVWAKILSGFTDKE-----KKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488239013 250 GLMMPLVQLTAYATY-----------------IGMAVLGSFYVITGAIVVGQ 284
Cdd:cd18558 243 NISMGAAFLLIYASYalafwygtylvtqqeysIGEVLTVFFSVLIGAFSAGQ 294
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
354-559 |
1.07e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 354 YDPKKplIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLmrfYDVDK---GAIRIDGIDTKSMSRSD-VRSLFGMVLQ--- 426
Cdd:PRK09700 274 RDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCL---FGVDKragGEIRLNGKDISPRSPLDaVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 427 -DAWLYQGTIADNI---RFGKLDATD-----YEVVDAAKTANVDhfiRTMPDGYEMPINAEGDNVSLGQKQLLTIARAVV 497
Cdd:PRK09700 349 dNGFFPNFSIAQNMaisRSLKDGGYKgamglFHEVDEQRTAENQ---RELLALKCHSVNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488239013 498 SDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRDA-DLILVMDQGQIIE 559
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
26-298 |
2.10e-05 |
|
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: 46.45 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 26 ILFTVLTVAFNVALPYVTGLPTTEISRNIAN-GESINFSYIFKCLIWITVVGIGYcisqlLSGVLMTNVVQSAMHDLRRD 104
Cdd:cd18560 2 LLLLILGKACNVLAPLFLGRAVNALTLAKVKdLESAVTLILLYALLRFSSKLLKE-----LRSLLYRRVQQNAYRELSLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 105 IEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAFIGIVNAILGITLAAAM-MFYIQPMMALISMIMIPTSIWIS 183
Cdd:cd18560 77 TFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVfAFHFGAWLALIVFLSVLLYGVFT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 184 KRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYAT 263
Cdd:cd18560 157 IKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270
....*....|....*....|....*....|....*
gi 488239013 264 YIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQP 298
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
25-311 |
3.80e-05 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 45.98 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 25 VILFTVLTVAFNVALPYVTGLPTTEISRNiaNGESINFSYIfkclIWITVVGI-GYCISQLLSGVLMTNVVQSAMHDLRR 103
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSGG--SGKSPWKEIG----LYVLLRFLqSGGGLGLLRSWLWIPVEQYSYRALST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 104 DIEEKINRLPVSYFDKNQQGNILsRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMmFYIQ--PMMALISMIMIPTSIW 181
Cdd:cd18583 75 AAFNHVMNLSMDFHDSKKSGEVL-KAIEQGSSINDLLEQILFQIVPMIIDLVIAIVY-LYYLfdPYMGLIVAVVMVLYVW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 182 ISKRVINASQKYFQSMQNSLGELNGYVQENMTGFSVLKVYGREKETLEGFK-KVNHSLKyfGFRAAFISGLMMPLVQ--- 257
Cdd:cd18583 153 STIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYReAVKNYQK--AERKYLFSLNLLNAVQsli 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488239013 258 LTayATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQS 311
Cdd:cd18583 231 LT--LGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQS 282
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-513 |
5.07e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 5.07e-05
10 20 30
....*....|....*....|....*....|....
gi 488239013 480 DNVSLGQKQLLTIARAVVSDPKILILDEATSSVD 513
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
47-291 |
6.21e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 45.21 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 47 TTEISRNIANGESINFSYIFKCLIWITVVGIGYCisqLLSGVLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNIL 126
Cdd:cd18605 26 VSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFT---LLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRIL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 127 SRVTNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSIWISK--RVINASQKYFQSMqnSLGEL 204
Cdd:cd18605 103 NRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFIYYRIQRyyRATSRELKRLNSV--NLSPL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 205 NGYVQENMTGFSVLKVYGREKETLEGF-KKVNHSLK----------YFGFRAAFISGLMMPLVQLTA----------YAT 263
Cdd:cd18605 181 YTHFSETLKGLVTIRAFRKQERFLKEYlEKLENNQRaqlasqaasqWLSIRLQLLGVLIVTFVALTAvvqhffglsiDAG 260
|
250 260
....*....|....*....|....*...
gi 488239013 264 YIGMAVLgsfYVITgaiVVGQLQAFIQY 291
Cdd:cd18605 261 LIGLALS---YALP---ITGLLSGLLNS 282
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
485-568 |
6.53e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 6.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 485 GQKQLLTIARAVVSDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRD-ADLILVMDQGQIIEKG 561
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVETA 241
|
....*..
gi 488239013 562 THESLLA 568
Cdd:PRK15093 242 PSKELVT 248
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
25-182 |
6.93e-05 |
|
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: 44.84 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 25 VILFTVLTVAFNVALPYVTGLPTTEISRNIANGESINFSYIFK-----CLIWITVVGIGYCISQLLSgVLMTNVVQsamh 99
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKpalklLGLYLLQSLLTFAYISLLS-VVGERVAA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQAF-IGIVNAILgITLAAAMMFYIQPMMALISMIMIPT 178
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVsQGLRSVTQ-TVGCVVSLYLISPKLTLLLLVIVPV 154
|
....
gi 488239013 179 SIWI 182
Cdd:cd18574 155 VVLV 158
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
368-398 |
8.50e-05 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 43.68 E-value: 8.50e-05
10 20 30
....*....|....*....|....*....|.
gi 488239013 368 VKAGQTVAVVGPTGAGKTTLINLLMRFYDVD 398
Cdd:cd01130 9 VRARKNILISGGTGSGKTTLLNALLSFIPPD 39
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
22-246 |
9.26e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 44.86 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNV--------------ALPYVTGLPTTEISRNIANGESINFsYIFKCLIWITVVGIGYCISqllsG 87
Cdd:cd18599 5 FLFVLLLFILSVGSTVfsdwwlsywlkqgsGNTTNNVDNSTVDSGNISDNPDLNF-YQLVYGGSILVILLLSLIR----G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 88 VLMTNVVQSAMHDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVS--------GALQQAFIgivnaILGITLAAA 159
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDvrlpftleNFLQNVLL-----VVFSLIIIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 160 MMF-YIQPMMALISMIMiptsIWISKrVINASQKYFQSMQN-SLGELNGYVQENMTGFSVLKVYGREKETLEGFKKV--N 235
Cdd:cd18599 155 IVFpWFLIALIPLAIIF----VFLSK-IFRRAIRELKRLENiSRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLldQ 229
|
250
....*....|.
gi 488239013 236 HSLKYFGFRAA 246
Cdd:cd18599 230 NSSAFFLFNCA 240
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
368-405 |
1.16e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.54 E-value: 1.16e-04
10 20 30
....*....|....*....|....*....|....*...
gi 488239013 368 VKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIRID 405
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEEVQKTGAVRED 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
343-403 |
1.52e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 1.52e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 343 GDVTFDHVDFAYD-PKKPLIQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVDKGAIR 403
Cdd:PRK11147 316 GKIVFEMENVNYQiDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
22-241 |
1.74e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 43.62 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 22 FLLVILFTVLTVAFNVALPYVTGLPTTEISRNIANGESINFSYifkcLIWITVVGIGYCISQLLSGVLMTNVVQSAMHDL 101
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYR----LGVYGALGLGQAIFVFLGSLALALGCVRASRNL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSGALQQ-------AFIGIVNAILGITLAAAMMFYIQPMMALISMI 174
Cdd:cd18603 77 HNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQnirsflnCLFQVISTLVVISISTPIFLVVIIPLAILYFF 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488239013 175 M----IPTSIWIsKRvINASQKyfqSMQNSlgelngYVQENMTGFSVLKVYGREKE-TLEGFKKVNHSLKYF 241
Cdd:cd18603 157 IqrfyVATSRQL-KR-LESVSR---SPIYS------HFSETLQGASTIRAYGVQERfIRESDRRVDENQRAY 217
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
370-391 |
2.63e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.39 E-value: 2.63e-04
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
368-394 |
5.66e-04 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 42.46 E-value: 5.66e-04
10 20
....*....|....*....|....*..
gi 488239013 368 VKAGQTVAVVGPTGAGKTTLINLLMRF 394
Cdd:COG4962 179 VRARLNILVSGGTGSGKTTLLNALSGF 205
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
108-312 |
6.15e-04 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC 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: 350015 [Multi-domain] Cd Length: 294 Bit Score: 42.04 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 108 KINRLPVSYFDKNQQGNILSRVtNDVDAVSGALQQAFIGIVNAILGITLAAAMMFYIQPMMALISMIMIPTSI-WIS--- 183
Cdd:cd18571 84 KLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGSVLYIlWILlfl 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 184 --KRVINasQKYFQSM---QNSLGELNGYVQEnmtgfsvLKVYGREKETLEGFKKVNHSLkyfgFRAAfISGLMMPLVQL 258
Cdd:cd18571 163 kkRKKLD--YKRFDLSsenQSKLIELINGMQE-------IKLNNSERQKRWEWERIQAKL----FKIN-IKSLKLDQYQQ 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 259 TAY-----ATYIGMAVLGSFYVITGAIVVGQLQAfIQYIW-QISQPMGNVTQLSSVLQSA 312
Cdd:cd18571 229 IGAlfinqLKNILITFLAAKLVIDGEITLGMMLA-IQYIIgQLNSPIEQLIGFIQSLQDA 287
|
|
| PRK13898 |
PRK13898 |
type IV secretion system ATPase VirB4; Provisional |
365-409 |
1.38e-03 |
|
type IV secretion system ATPase VirB4; Provisional
Pssm-ID: 172418 Cd Length: 800 Bit Score: 41.68 E-value: 1.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 365 NFEVK-AGQTvAVVGPTGAGKTTLINLL----------MRFYDVDKGA---IR-IDGIDT 409
Cdd:PRK13898 440 NFHVRdVGHT-LIIGPTGAGKTVLMNFLcaqamkfsprMFFFDKDRGAeifIRaLNGVYT 498
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
69-319 |
1.72e-03 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 40.66 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 69 LIWITVVGIGYCISQLLSGVLMTNVVQSAMHDLRR---DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVsgalqQAFI 145
Cdd:cd18559 38 QVYLSVLGALAILQGITVFQYSMAVSIGGIFASRAvhlDLYHKALRSPISFFERTPSGELVNLFSKDLDRV-----DSMA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 146 GIVNAILGITLAAAMMFYI-----QPMMALI---SMIMIPTSIWISKRVINASQKYFQSMQNSLGELNgyvqENMTGFSV 217
Cdd:cd18559 113 PQVIKMWMGPLQNVIGLYLlillaGPMAAVGiplGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFN----ETLLGISV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 218 LKVYGREKE-------TLEGFKKVNHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMavlGSFYVITGAIVVGQLQAFIQ 290
Cdd:cd18559 189 IKAFEWEEAfirqvdaKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSR---HSLAGLVALKVFYSLALTTY 265
|
250 260
....*....|....*....|....*....
gi 488239013 291 YIWqisqPMGNVTQLSSVLQSASAATKRV 319
Cdd:cd18559 266 LNW----PLNMSPEVITNIVAAEVSLERS 290
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
306-521 |
2.58e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 306 SSVLQSASAATKR---VFEILDEPEEKenkVDVSLPETILGD--VTFDHVDFAYdPKKPLI-QDLNFEVKAGQTVAVVGP 379
Cdd:PLN03073 468 ASLVQSRIKALDRlghVDAVVNDPDYK---FEFPTPDDRPGPpiISFSDASFGY-PGGPLLfKNLNFGIDLDSRIAMVGP 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 380 TGAGKTTLINLLMRFYDVDKGAI--------------RIDGIDTKS-----MSRSdvrslfgmvlqdawlYQGTIADNIR 440
Cdd:PLN03073 544 NGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLDLSSnpllyMMRC---------------FPGVPEQKLR 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 441 --FGKLDATDYEVVDAAKTanvdhfirtmpdgyempinaegdnVSLGQKQLLTIARAVVSDPKILILDEATSSVD-TRLE 517
Cdd:PLN03073 609 ahLGSFGVTGNLALQPMYT------------------------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVE 664
|
....
gi 488239013 518 ALIQ 521
Cdd:PLN03073 665 ALIQ 668
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
374-418 |
2.82e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 38.09 E-value: 2.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488239013 374 VAVVGPTGAGKTTLINLLMRFYD-VDKGAIRIDgiDTKSMSRSDVR 418
Cdd:pfam13401 8 LVLTGESGTGKTTLLRRLLEQLPeVRDSVVFVD--LPSGTSPKDLL 51
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
370-391 |
3.31e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 38.68 E-value: 3.31e-03
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
355-398 |
4.30e-03 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 40.15 E-value: 4.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488239013 355 DPKKPL-----IQDLNFEVKAGQTVAVVGPTGAGKTTLINLLMRFYDVD 398
Cdd:PRK04192 206 PPVEPLitgqrVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
487-583 |
6.60e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.23 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 487 KQLLtiARAVVSDPKILILDEATSSVDT--------RLEALIQKAMDRVMegrtsfvIAHRLSTIRD-ADLILVMDQGQI 557
Cdd:PRK10938 143 KTLL--CQALMSEPDLLILDEPFDGLDVasrqqlaeLLASLHQSGITLVL-------VLNRFDEIPDfVQFAGVLADCTL 213
|
90 100 110
....*....|....*....|....*....|.
gi 488239013 558 IEKGT-----HESLLAQGGFYEKLYNSQFAE 583
Cdd:PRK10938 214 AETGEreeilQQALVAQLAHSEQLEGVQLPE 244
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
159-317 |
9.41e-03 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB 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 LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 38.19 E-value: 9.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 159 AMMFYIQPMMALISMIMIP----TSIWISKRVINASQkyfQSMQNSlGELNGYVQENMTGFSVLKVYGREKETLEGFKKV 234
Cdd:cd18587 133 AVIALIGGPLALVPLVAIPlvllYGLLLQKPLRRLVE---ESMRES-AQKNALLVESLSGLETIKALGAEGRMQRRWEEA 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488239013 235 NHSLKYFGFRAAFISGLMMPLVQLTAYATYIGMAVLGSFYVITGAIVVGQLQAFIQYIWQISQPMGNVTQLSSVLQSASA 314
Cdd:cd18587 209 VAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIACVILSGRALAPLGQIAGLLTRYQQART 288
|
...
gi 488239013 315 ATK 317
Cdd:cd18587 289 ALK 291
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
374-395 |
9.55e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 38.09 E-value: 9.55e-03
|
| |
