|
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: 675.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 2 KHAFSSMKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTGLPTTEISRNIaagesiNFDYVIQCLIWILVVGTGYCV 81
Cdd:COG1132 3 KSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGG------DLSALLLLLLLLLGLALLRAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 82 AQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMM 161
Cdd:COG1132 77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 162 FLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGF 241
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 242 GFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFE 321
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 322 ILDEPEEELNEQDVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGA 401
Cdd:COG1132 317 LLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 402 IKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDN 481
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 VSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570 580
....*....|....*....|...
gi 488301890 562 THHELLEQGGFYEKLYNSQFAEE 584
Cdd:COG1132 557 THEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-580 |
2.52e-155 |
|
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: 462.38 E-value: 2.52e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 6 SSMKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTGLptteISRNIAAGESINFDYVIqcLIWILVVGTGYCVAQFL 85
Cdd:COG2274 142 FGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQV----VIDRVLPNQDLSTLWVL--AIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 86 SGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLIN 165
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 166 PLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKA 245
Cdd:COG2274 295 PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 246 SFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILDE 325
Cdd:COG2274 375 RRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 326 PEEELNEQDVPLPEPILGSVEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKI 404
Cdd:COG2274 455 PPEREEGRSKLSLPRLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 405 DGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSL 484
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSG 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHH 564
Cdd:COG2274 615 GQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHE 694
|
570
....*....|....*.
gi 488301890 565 ELLEQGGFYEKLYNSQ 580
Cdd:COG2274 695 ELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-583 |
3.06e-133 |
|
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: 401.02 E-value: 3.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 7 SMKRIGRYIKPYRLTFylvILFTILTVAFNAALPYLTGLpTTEISRNIAAGESINFDYVIQCLIWILVVGTGycVAQFLS 86
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGL---VLAGVAMILVAATESTLAAL-LKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRG--ICSFVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 87 GFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINP 166
Cdd:TIGR02203 75 TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 167 LMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKAS 246
Cdd:TIGR02203 155 QLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 247 FISGLMLPLVQMTAYgtyIGVAVL---GSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEIL 323
Cdd:TIGR02203 235 SAGSISSPITQLIAS---LALAVVlfiALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 324 DEPEEeLNEQDVPLPEpILGSVEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAI 402
Cdd:TIGR02203 312 DSPPE-KDTGTRAIER-ARGDVEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 403 KIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKL-DATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDN 481
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 VSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570 580
....*....|....*....|..
gi 488301890 562 THHELLEQGGFYEKLYNSQFAE 583
Cdd:TIGR02203 550 THNELLARNGLYAQLHNMQFRE 571
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
13-581 |
2.67e-120 |
|
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: 367.87 E-value: 2.67e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 13 RYIKPYRLTFYLVILFTILTVAFNAALPYLTGLpttEISRNIAAGESINFDYVIQCLIwilVVGTGYCVAQFLSGFLMTN 92
Cdd:TIGR02204 11 PFVRPYRGRVLAALVALLITAAATLSLPYAVRL---MIDHGFSKDSSGLLNRYFAFLL---VVALVLALGTAARFYLVTW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 93 VVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFS 172
Cdd:TIGR02204 85 LGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 173 VIMIPLSL----IISRTIVKISQKyfqgMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFI 248
Cdd:TIGR02204 165 LLAVPLVLlpilLFGRRVRKLSRE----SQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 249 SGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILD-EPE 327
Cdd:TIGR02204 241 RALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQaEPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 328 EELNEQDVPLPEPILGSVEFENVSFSY--DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKID 405
Cdd:TIGR02204 321 IKAPAHPKTLPVPLRGEIEFEQVNFAYpaRPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 406 GIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLG 485
Cdd:TIGR02204 401 GVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 486 QKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHE 565
Cdd:TIGR02204 481 QRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAE 560
|
570
....*....|....*.
gi 488301890 566 LLEQGGFYEKLYNSQF 581
Cdd:TIGR02204 561 LIAKGGLYARLARLQF 576
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
343-571 |
3.17e-120 |
|
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: 354.99 E-value: 3.17e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFG 422
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGG 571
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-571 |
1.88e-113 |
|
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: 349.44 E-value: 1.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 9 KRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLtglptteISRNIAA--GESINFDYVIQCLIWILVVGTGYCVAQFLS 86
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWL-------LASLLAGliIGGAPLSALLPLLGLLLAVLLLRALLAWLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 87 GFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINP 166
Cdd:COG4988 79 ERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 167 LMAI---FSVIMIPLSLI-ISRTIVKISQKYFQgmqnSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLngfg 242
Cdd:COG4988 159 LSGLillVTAPLIPLFMIlVGKGAAKASRRQWR----ALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDF---- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 243 FKA-------SFISGLMLPLVqmtaygTYIGVAVlgsyyvVAgvIVVGqlqafIQYIW-QIS---------------QP- 298
Cdd:COG4988 231 RKRtmkvlrvAFLSSAVLEFF------ASLSIAL------VA--VYIG-----FRLLGgSLTlfaalfvlllapeffLPl 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 299 ----------MGNITQLSaalqsasastmRIFEILDEPEEELNEQDVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKV 368
Cdd:COG4988 292 rdlgsfyharANGIAAAE-----------KIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 369 DAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATD 448
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 449 YEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM 528
Cdd:COG4988 441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA 520
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 488301890 529 EGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGG 571
Cdd:COG4988 521 KGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
22-303 |
5.09e-113 |
|
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: 338.99 E-value: 5.09e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLPTTEISRNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQIS 282
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-577 |
2.32e-111 |
|
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: 332.27 E-value: 2.32e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGM 423
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLY 577
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-589 |
2.77e-108 |
|
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: 337.56 E-value: 2.77e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 265 IGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILDEPEEElneQDVPLPEPIL-- 342
Cdd:COG5265 278 TAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEV---ADAPDAPPLVvg 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 -GSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:COG5265 355 gGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPK 501
Cdd:COG5265 435 GIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPP 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQF 581
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
....*...
gi 488301890 582 AEEGDYEE 589
Cdd:COG5265 595 EEEEAEEA 602
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-578 |
8.51e-106 |
|
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: 329.80 E-value: 8.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 6 SSMKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTG-LptteISRNIAAGESINFdyviqcliWILVVGTgycvaQF 84
Cdd:COG4987 1 RDLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALSGwL----IAAAALAPPILNL--------FVPIVGV-----RA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 85 LsGFLMT-----------NVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLG 153
Cdd:COG4987 64 F-AIGRTvfrylerlvshDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 154 IVMAVVMMFLINPLMA-IFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFK 232
Cdd:COG4987 143 ILAAVAFLAFFSPALAlVLALGLLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 233 QVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVI-----------------VVGQLQAFIQYIWQI 295
Cdd:COG4987 223 AAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALsgpllallvlaalalfeALAPLPAAAQHLGRV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 296 SQPMGnitqlsaalqsasastmRIFEILD-EPEEELNEQDVPLPEPilGSVEFENVSFSYDPE-KPLIRNLNFKVDAGQM 373
Cdd:COG4987 303 RAAAR-----------------RLNELLDaPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAgRPVLDGLSLTLPPGER 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 374 VAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVD 453
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWA 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 454 AAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTS 533
Cdd:COG4987 444 ALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV 523
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 488301890 534 FVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYN 578
Cdd:COG4987 524 LLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
345-580 |
8.66e-105 |
|
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: 315.71 E-value: 8.66e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 505 LDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQ 580
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
107-581 |
5.75e-104 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 325.76 E-value: 5.75e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 107 EKINRLPVSYFDKNQQGNILSRVTNDVDAVS----NAMQQSFINIVSAVLGIVMAVVM-----MFLInPLMAIFSVIMip 177
Cdd:PRK13657 97 ERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVVLLPLALFMnwrlsLVLV-VLGIVYTLIT-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 178 lSLIISRTivkisqkyfQGMQNSL----GDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLngfgFKASF--IS-- 249
Cdd:PRK13657 174 -TLVMRKT---------KDGQAAVeehyHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNL----LAAQMpvLSww 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 250 GLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQY----IWQISQPMGNITQLSAALQSASAstmrIFEILDE 325
Cdd:PRK13657 240 ALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFatllIGRLDQVVAFINQVFMAAPKLEE----FFEVEDA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 326 PEEELNEQDVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKID 405
Cdd:PRK13657 316 VPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 406 GIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLG 485
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 486 QKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHE 565
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555
|
490
....*....|....*.
gi 488301890 566 LLEQGGFYEKLYNSQF 581
Cdd:PRK13657 556 LVARGGRFAALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
345-580 |
6.83e-104 |
|
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: 313.32 E-value: 6.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYD--PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFG 422
Cdd:cd03249 1 IEFKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQ 580
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
79-583 |
8.52e-104 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 325.05 E-value: 8.52e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 79 YCVAqFLSGflmtNVVQQsmrdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAV 158
Cdd:PRK11176 87 YCIS-WVSG----KVVMT----MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLF 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 159 VMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRL 238
Cdd:PRK11176 158 IMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 239 NGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMR 318
Cdd:PRK11176 238 RQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 319 IFEILD-EPEEELNEQDVplpEPILGSVEFENVSFSYD-PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYD 396
Cdd:PRK11176 318 LFAILDlEQEKDEGKRVI---ERAKGDIEFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 397 VTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDA-TDYEVVDAAKTANVDHFIRTMPDGYEMEI 475
Cdd:PRK11176 395 IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVI 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 476 NSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQG 555
Cdd:PRK11176 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDG 554
|
490 500
....*....|....*....|....*...
gi 488301890 556 EIIEKGTHHELLEQGGFYEKLYNSQFAE 583
Cdd:PRK11176 555 EIVERGTHAELLAQNGVYAQLHKMQFGQ 582
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-584 |
1.57e-96 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 306.64 E-value: 1.57e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 1 MKHAFSSMKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTglpTTEISRNIAAGEsinfdyviqcLIWILVVG--TG 78
Cdd:PRK10790 4 FSQLWPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLI---SYFIDNMVAKGN----------LPLGLVAGlaAA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 79 YCVAQFLSGFL------MTN-----VVQQsmrdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAmqqsFINI 147
Cdd:PRK10790 71 YVGLQLLAAGLhyaqslLFNraavgVVQQ----LRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDL----YVTV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 148 VSAVLG----IVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGR 223
Cdd:PRK10790 143 VATVLRsaalIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 224 EKETLEGFKQVNH----------RLNGFgfkasfisgLMLPLVQMTAYGTYIGVAVLGSYYVVaGVIVVGQLQAFIQYIW 293
Cdd:PRK10790 223 QARFGERMGEASRshymarmqtlRLDGF---------LLRPLLSLFSALILCGLLMLFGFSAS-GTIEVGVLYAFISYLG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 294 QISQPMGNITQLSAALQSASASTMRIFEILDEPEEELNEQDVPLPEpilGSVEFENVSFSYDPEKPLIRNLNFKVDAGQM 373
Cdd:PRK10790 293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDGPRQQYGNDDRPLQS---GRIDIDNVSFAYRDDNLVLQNINLSVPSRGF 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 374 VAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKlDATDYEVVD 453
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQ 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 454 AAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTS 533
Cdd:PRK10790 449 ALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL 528
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 534 FVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQFAEE 584
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGE 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-576 |
3.45e-94 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 303.95 E-value: 3.45e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 8 MKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTGLPTTEIsrniaAGESINFDYVIQclIWILvvgTGYCVAQFLSG 87
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTL-----GGDKGPPALASA--IFFM---CLLSIASSVSA 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 88 FLMTNVVQQSM----RDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFL 163
Cdd:TIGR00958 219 GLRGGSFNYTMarinLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLW 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 164 INPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGF 243
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNK 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 244 KASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEIL 323
Cdd:TIGR00958 379 RKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 324 D-EPEEELNeqDVPLPEPILGSVEFENVSFSY--DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEG 400
Cdd:TIGR00958 459 DrKPNIPLT--GTLAPLNLEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGG 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 401 AIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGD 480
Cdd:TIGR00958 537 QVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 481 NVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRvmEGRTSFVIAHRLSTIREADLILVMKQGEIIEK 560
Cdd:TIGR00958 617 QLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEM 694
|
570
....*....|....*.
gi 488301890 561 GTHHELLEQGGFYEKL 576
Cdd:TIGR00958 695 GTHKQLMEDQGCYKHL 710
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
5-576 |
3.79e-82 |
|
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: 268.68 E-value: 3.79e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 5 FSSMKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTGlpttEISRNIAAGESInfdyviqclIWILVVGTGYCVAQF 84
Cdd:TIGR01192 4 FQVYVRALSYLNVHKNRVLLIVIANITLAAITIAEPILFG----RIIDAISSKSDV---------LPTLALWAGFGVFNT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 85 LSGFLMTNVVQQSMRDLRRDIEEK----INRLPVSYFDKNQQGNILSRVTNDVDAVSNA----MQQSFINIVSAVLGIVM 156
Cdd:TIGR01192 71 IAYVLVAREADRLAHGRRATLLTEafgrIISMPLSWHQQRGTSNALHTLLRATETLFGLwlefMRQHLATFVALFLLIPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 157 AVVMMFLINPLMAIFSVIMIPLS-LIISRTivKISQKYFQGMQNSLgdlNGYVQENMTGFSVLKLYGREKETLEGFKQVN 235
Cdd:TIGR01192 151 AFAMDWRLSIVLMVLGILYILIAkLVMQRT--KNGQAAVEHHYHNV---FKHVSDSISNVSVVHSYNRIEAETSALKQFT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 236 HRLNGFGFKA----SFISGLMlplvQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQY----IWQISQPMGNITQLSA 307
Cdd:TIGR01192 226 NNLLSAQYPVldwwALASGLN----RMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFanllIGRLDQMSGFITQIFE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 308 ALQsasasTMRIFEILDEPEEELNE-QDVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTT 386
Cdd:TIGR01192 302 ARA-----KLEDFFDLEDSVFQREEpADAPELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTT 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 387 LINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRT 466
Cdd:TIGR01192 377 LINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILK 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 467 MPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREA 546
Cdd:TIGR01192 457 RSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNA 536
|
570 580 590
....*....|....*....|....*....|
gi 488301890 547 DLILVMKQGEIIEKGTHHELLEQGGFYEKL 576
Cdd:TIGR01192 537 DLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
111-576 |
4.93e-79 |
|
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: 263.73 E-value: 4.93e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 111 RLPVSYFDKNQQGNILSRVTNDvDAVSNAMQQsfiNIVSAVLGIVMAV---VMMFLINPLMAI----FSVIMIPLSLIIS 183
Cdd:TIGR03796 239 RLPVRFFAQRHAGDIASRVQLN-DQVAEFLSG---QLATTALDAVMLVfyaLLMLLYDPVLTLigiaFAAINVLALQLVS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKyfqgMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGF-----KQVNHRLNgFGFKASFISglMLPLVQM 258
Cdd:TIGR03796 315 RRRVDANRR----LQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWagyqaKLLNAQQE-LGVLTQILG--VLPTLLT 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 259 TAygTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILDEP-----EEELNEQ 333
Cdd:TIGR03796 388 SL--NSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRNPvdpllEEPEGSA 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 334 DVPLPEPIL-GSVEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKK 411
Cdd:TIGR03796 466 ATSEPPRRLsGYVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREE 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 412 MNRSDVRSVFGMVLQDAWLYKGTIADNIRFgkLDAT--DYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQL 489
Cdd:TIGR03796 546 IPREVLANSVAMVDQDIFLFEGTVRDNLTL--WDPTipDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQR 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 490 LTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRvmEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:TIGR03796 624 LEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV 701
|
....*..
gi 488301890 570 GGFYEKL 576
Cdd:TIGR03796 702 GGAYARL 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
100-580 |
1.31e-78 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 258.87 E-value: 1.31e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIV-SAVLGIVMAVVMMFLINPLMAIFSVIMIPL 178
Cdd:PRK10789 70 ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVdSLVMGCAVLIVMSTQISWQLTLLALLPMPV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 179 -SLIISRTIVKISQKyFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQ 257
Cdd:PRK10789 150 mAIMIKRYGDQLHER-FKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIY 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 258 MTaygtyIGVAVL-----GSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILDEPEEeLNE 332
Cdd:PRK10789 229 IA-----IGMANLlaiggGSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV-VKD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 333 QDVPLPEPiLGSVEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKK 411
Cdd:PRK10789 303 GSEPVPEG-RGELDVNIRQFTYpQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 412 MNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLT 491
Cdd:PRK10789 382 LQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRIS 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGG 571
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
....*....
gi 488301890 572 FYEKLYNSQ 580
Cdd:PRK10789 542 WYRDMYRYQ 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
18-552 |
6.86e-78 |
|
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: 255.67 E-value: 6.86e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 18 YRLTFYLVILF----TILTVAFNAALPYLtglptteISRNIAAGESinfdyVIQCLIWILV---VGTGYCVAQFLSGFLM 90
Cdd:TIGR02857 1 ARRALALLALLgvlgALLIIAQAWLLARV-------VDGLISAGEP-----LAELLPALGAlalVLLLRALLGWLQERAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 91 TNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAI 170
Cdd:TIGR02857 69 ARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 171 FSVIMIPL-----SLIISRTiVKISQKYFQGMQNslgdLNGYVQENMTGFSVLKLYGREKETLEGFKQV--NHRLNGFG- 242
Cdd:TIGR02857 149 ILLLTAPLipifmILIGWAA-QAAARKQWAALSR----LSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSseEYRERTMRv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 243 FKASFISGLMLPL-----VQMTAygTYIGVAVLGSYYVVAGVIVVGQL--QAFiqyiwqisQPMGNITQLSAALQSASAS 315
Cdd:TIGR02857 224 LRIAFLSSAVLELfatlsVALVA--VYIGFRLLAGDLDLATGLFVLLLapEFY--------LPLRQLGAQYHARADGVAA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 316 TMRIFEILDEPEEELNEQdVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFY 395
Cdd:TIGR02857 294 AEALFAVLDAAPRPLAGK-APVTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 396 DVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEI 475
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPI 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 476 NSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVM 552
Cdd:TIGR02857 453 GEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
345-556 |
7.70e-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: 7.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGM 423
Cdd:cd03228 1 IEFKNVSFSYPGrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyemeinsegdnVSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488301890 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGE 556
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
343-562 |
1.18e-75 |
|
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: 239.70 E-value: 1.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVlKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKGTIADNIR-FGKldATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGT 562
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-561 |
9.68e-75 |
|
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: 237.49 E-value: 9.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:cd03245 1 GRIEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPK 501
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
345-580 |
1.25e-74 |
|
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: 237.77 E-value: 1.25e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGM 423
Cdd:cd03252 1 ITFEHVRFRYKPDGPVIlDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQ 580
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-578 |
2.56e-68 |
|
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: 234.63 E-value: 2.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 15 IKPYRLTFYLVILFTILTVAFNAALPYLTGLPTTEISRNIAAGESInfdyVIQCLIWILVVGTgycVAQFLSGFLMTNVV 94
Cdd:TIGR01193 152 TRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLGI----ISIGLIIAYIIQQ---ILSYIQIFLLNVLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 95 QQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTnDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVI 174
Cdd:TIGR01193 225 QRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 175 MIPLSLII----SRTIVKISQKYFQGmqNSLgdLNGYVQENMTGFSVLKLYGREKETlegFKQVNHRLNGF------GFK 244
Cdd:TIGR01193 304 SIPVYAVIiilfKRTFNKLNHDAMQA--NAV--LNSSIIEDLNGIETIKSLTSEAER---YSKIDSEFGDYlnksfkYQK 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 245 ASFISGLMLPLVQMTaygtyIGVAVL--GSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEI 322
Cdd:TIGR01193 377 ADQGQQAIKAVTKLI-----LNVVILwtGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEV 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 323 LDEPEEELNEQDVPLPEPILGSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAI 402
Cdd:TIGR01193 452 YLVDSEFINKKKRTELNNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 403 KIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFG-KLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDN 481
Cdd:TIGR01193 532 LLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSS 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 VSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEaliQKAMDRV--MEGRTSFVIAHRLSTIREADLILVMKQGEIIE 559
Cdd:TIGR01193 612 ISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLlnLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
570
....*....|....*....
gi 488301890 560 KGTHHELLEQGGFYEKLYN 578
Cdd:TIGR01193 689 QGSHDELLDRNGFYASLIH 707
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
338-557 |
7.75e-61 |
|
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: 201.16 E-value: 7.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 338 PEPILGSVEFENVSFSYD--PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS 415
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 DVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARA 495
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEI 557
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
22-303 |
1.08e-59 |
|
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: 200.69 E-value: 1.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLpttEISRNIAAGeSINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKR---AIDDYIVPG-QGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18544 77 RRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18544 157 ATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18544 237 LALALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLA 278
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
318-569 |
5.95e-59 |
|
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: 206.14 E-value: 5.95e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 318 RIFEILDEPEEElnEQDVPLPEPiLGSVEFENVSFSYdP--EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFY 395
Cdd:COG4618 307 RLNELLAAVPAE--PERMPLPRP-KGRLSVENLTVVP-PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVW 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 396 DVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNI-RFGklDATDYEVVDAAKTANVDHFIRTMPDGYEME 474
Cdd:COG4618 383 PPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 475 INSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIREADLILVMK 553
Cdd:COG4618 461 IGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLR 540
|
250
....*....|....*.
gi 488301890 554 QGEIIEKGTHHELLEQ 569
Cdd:COG4618 541 DGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
9-540 |
2.79e-58 |
|
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: 203.75 E-value: 2.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 9 KRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLTG-LptteISRNIAAGEsinfdyVIQCLIWILVV---GTGYCVAQF 84
Cdd:TIGR02868 2 LRILPLLKPRRRRLALAVLLGALALGSAVALLGVSAwL----ISRAAEMPP------VLYLSVAAVAVrafGIGRAVFRY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 85 LSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLI 164
Cdd:TIGR02868 72 LERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 165 NPLMAIFSVIMIPLSLI----ISRTIVKISQkyfQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNG 240
Cdd:TIGR02868 152 SVPAALILAAGLLLAGFvaplVSLRAARAAE---QALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 241 FGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAG--------VIVVGQLQAFiqyiwqisQPMGNITQLSAALQSA 312
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGrlapvtlaVLVLLPLAAF--------EAFAALPAAAQQLTRV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 313 SASTMRIFEILDePEEELNEQDVPLPEPILG---SVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLIN 389
Cdd:TIGR02868 301 RAAAERIVEVLD-AAGPVAEGSAPAAGAVGLgkpTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 390 LLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPD 469
Cdd:TIGR02868 380 TLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPD 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 470 GYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRL 540
Cdd:TIGR02868 460 GLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-562 |
3.06e-58 |
|
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: 193.78 E-value: 3.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 340 PILGSVEFENVSFSYDPEKP-LIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVR 418
Cdd:cd03369 2 PEHGEIEVENLSVRYAPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SVFGMVLQDAWLYKGTIADNI-RFGKLDatDYEVVDAaktanvdhfirtmpdgyeMEINSEGDNVSLGQKQLLTIARAVI 497
Cdd:cd03369 82 SSLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGT 562
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
22-302 |
6.45e-57 |
|
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: 193.03 E-value: 6.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLPTTEIsrnIAAGesiNFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSV---IGGG---LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18542 75 RNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18542 155 FSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18542 235 LQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQL 275
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
96-573 |
2.29e-56 |
|
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: 205.95 E-value: 2.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 96 QSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPlmaIFSVIM 175
Cdd:TIGR00957 1035 QASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATP---IAAVII 1111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 176 IPLSLI---ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYgREKETLEGFKQVNHRLNGFGFKASFISGLM 252
Cdd:TIGR00957 1112 PPLGLLyffVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF-EEQERFIHQSDLKVDENQKAYYPSIVANRW 1190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 253 LPlVQMTAYGTYIGV-----AVLGSYYVVAGVIVVGqlqafIQYIWQISQPMGNITQLSAALQSASASTMRIFEiLDEPE 327
Cdd:TIGR00957 1191 LA-VRLECVGNCIVLfaalfAVISRHSLSAGLVGLS-----VSYSLQVTFYLNWLVRMSSEMETNIVAVERLKE-YSETE 1263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 328 EE----LNEQDVPLPEPILGSVEFENVSFSYDPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAI 402
Cdd:TIGR00957 1264 KEapwqIQETAPPSGWPPRGRVEFRNYCLRYREDLDLVlRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 403 KIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIR-FGKLdaTDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDN 481
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 VSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:TIGR00957 1422 LSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501
|
490
....*....|...
gi 488301890 562 THHELLEQGG-FY 573
Cdd:TIGR00957 1502 APSNLLQQRGiFY 1514
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
319-580 |
2.53e-56 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 199.69 E-value: 2.53e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 319 IFEILDEPEEELNEQDVPLPEPILGSVEFENVS-FSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF--Y 395
Cdd:PRK11174 324 LVTFLETPLAHPQQGEKELASNDPVTIEAEDLEiLSPD-GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 396 dvtEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEI 475
Cdd:PRK11174 403 ---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPI 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 476 NSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQG 555
Cdd:PRK11174 480 GDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
|
250 260
....*....|....*....|....*.
gi 488301890 556 EIIEKGTHHELLEQGG-FYEKLYNSQ 580
Cdd:PRK11174 560 QIVQQGDYAELSQAGGlFATLLAHRQ 585
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
24-303 |
3.52e-54 |
|
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: 185.83 E-value: 3.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLpttEISRNIAAGesiNFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd07346 3 LALLLLLLATALGLALPLLTKL---LIDDVIPAG---DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIIS 183
Cdd:cd07346 77 DLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGT 263
Cdd:cd07346 157 RYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488301890 264 YIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd07346 237 TALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLA 276
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
74-587 |
5.53e-53 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 195.97 E-value: 5.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 74 VVGTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDA----VSNAMQQsFINIV- 148
Cdd:PLN03232 958 LLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDidrnVANLMNM-FMNQLw 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 149 -----SAVLGIVmAVVMMFLINPLMAIFSVIMIplsliisrtivkisqkYFQGMQNSLGDLNG------YVQ--ENMTGF 215
Cdd:PLN03232 1037 qllstFALIGTV-STISLWAIMPLLILFYAAYL----------------YYQSTSREVRRLDSvtrspiYAQfgEALNGL 1099
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 216 SVLKLY----------GREKETLEGFKQVNHRLNGF-GFKASFISGLMLPLVqmtayGTYigvAVLGSYYVVAGVIVVGQ 284
Cdd:PLN03232 1100 SSIRAYkaydrmakinGKSMDNNIRFTLANTSSNRWlTIRLETLGGVMIWLT-----ATF---AVLRNGNAENQAGFAST 1171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 285 LQAFIQYIWQISQPMGNITQLSAALQSASASTMRIFEILDEPEE--ELNEQDVPLPE-PILGSVEFENVSFSYDPE-KPL 360
Cdd:PLN03232 1172 MGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEatAIIENNRPVSGwPSRGSIKFEDVHLRYRPGlPPV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIR 440
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 441 -FGklDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEAL 519
Cdd:PLN03232 1332 pFS--EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 520 IQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLE-QGGFYEKLYNSQFAEEGDY 587
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSrDTSAFFRMVHSTGPANAQY 1478
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
22-303 |
2.72e-51 |
|
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: 178.05 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLpttEISRNIAAGesiNFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKI---AIDEYIPNG---DLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18545 76 RQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18545 156 VVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18545 236 LGTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLS 277
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
22-303 |
4.44e-50 |
|
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: 174.92 E-value: 4.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTG--LPTTEISRNIAAgesinfdyVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMR 99
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKplLDDIFVEKDLEA--------LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLS 179
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 180 LIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMT 259
Cdd:cd18552 153 ALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELL 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488301890 260 AYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18552 233 GAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLS 276
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
22-303 |
1.91e-49 |
|
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: 173.00 E-value: 1.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGlpttEISRNIAAGESINFDYVIqcLIWILVVGTgycVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVK----NLIDALSAGGSSGGLLAL--LVALFLLQA---VLSALSSYLLGRTGERVVLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18551 72 RRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18551 152 IILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQ 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18551 232 LALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLS 273
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
23-299 |
3.07e-49 |
|
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: 172.60 E-value: 3.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 23 YLV-ILFTILTVAFNAALPYLTGLPTTEISRNiaageSINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18541 1 YLLgILFLILVDLLQLLIPRIIGRAIDALTAG-----TLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270
....*....|....*....|....*....|....*...
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPM 273
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-580 |
4.10e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 179.64 E-value: 4.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 122 QGNILSRVTNDVDAvsnaMQQSFINIVSAVLG--IVMAVVMMFL--INPLMAIF-SVIMIPLSLIISRTIVKISQKYFQG 196
Cdd:PRK11160 116 QGDLLNRLVADVDT----LDHLYLRLISPLVAalVVILVLTIGLsfFDLTLALTlGGILLLLLLLLPLLFYRLGKKPGQD 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 197 MQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAygtyiGVAVLGSYYVV 276
Cdd:PRK11160 192 LTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQALMILAN-----GLTVVLMLWLA 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 277 A-GVIVVGQLQAFI---------------------QYIWQIsqpmgnITQlsaalqsasasTMRIFEILD-EPEEELNEQ 333
Cdd:PRK11160 267 AgGVGGNAQPGALIalfvfaalaafealmpvagafQHLGQV------IAS-----------ARRINEITEqKPEVTFPTT 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 334 DVPLPEPilGSVEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKM 412
Cdd:PRK11160 330 STAAADQ--VSLTLNNVSFTYpDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 413 NRSDVRSVFGMVLQDAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTmPDGYEMEINSEGDNVSLGQKQLLTI 492
Cdd:PRK11160 408 SEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGI 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 493 ARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGF 572
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
....*...
gi 488301890 573 YEKLYNSQ 580
Cdd:PRK11160 567 YYQLKQRL 574
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
109-571 |
4.30e-49 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 184.17 E-value: 4.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 109 INRLPVSYFDKNQQGNILSRV---TNDVD---AVSNAMqqsFINIVSAVL------GIVmAVVMMFLINPLMAIFSVIMI 176
Cdd:PLN03130 996 ILRAPMSFFHTNPLGRIINRFakdLGDIDrnvAVFVNM---FLGQIFQLLstfvliGIV-STISLWAIMPLLVLFYGAYL 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 177 plsliisrtivkisqkYFQGMQNSLGDLNG------YVQ--ENMTGFSVLKLY----------GREKETLEGFKQVNHRL 238
Cdd:PLN03130 1072 ----------------YYQSTAREVKRLDSitrspvYAQfgEALNGLSTIRAYkaydrmaeinGRSMDNNIRFTLVNMSS 1135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 239 NGF-GFKASFISGLMLPLVqmtayGTYigvAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNITQLSAALQSASASTM 317
Cdd:PLN03130 1136 NRWlAIRLETLGGLMIWLT-----ASF---AVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRLASLAENSLNAVE 1207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 318 RIFEILDEPEEE--LNEQDVPLPE-PILGSVEFENVSFSYDPE-KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMR 393
Cdd:PLN03130 1208 RVGTYIDLPSEAplVIENNRPPPGwPSSGSIKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFR 1287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 394 FYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIadniRFgKLDA----TDYEVVDAAKTANVDHFIRTMPD 469
Cdd:PLN03130 1288 IVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTV----RF-NLDPfnehNDADLWESLERAHLKDVIRRNSL 1362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 470 GYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLI 549
Cdd:PLN03130 1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRI 1442
|
490 500
....*....|....*....|..
gi 488301890 550 LVMKQGEIIEKGTHHELLEQGG 571
Cdd:PLN03130 1443 LVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
341-575 |
3.88e-48 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.38 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 341 ILGSVEFENVSFSY--DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDV--------------------- 397
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYisRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqd 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 398 ---------------------------------TEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKL 444
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 445 DATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAM 524
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 525 DRVME--GRTSFVIAHRLSTIREADLILVM----KQGEIIE-KGTHHELLE-QGGFYEK 575
Cdd:PTZ00265 1402 VDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSvQDGVYKK 1460
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-556 |
5.72e-48 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 181.00 E-value: 5.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 13 RYIKPYRLTFYLVILF------TILTVAFNAA------LPYLTGLPTTeISRNIAAGESINfdyviQCLIWILVVGTGYC 80
Cdd:PTZ00265 38 KKIKTQKIPFFLPFKClpashrKLLGVSFVCAtisggtLPFFVSVFGV-IMKNMNLGENVN-----DIIFSLVLIGIFQF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 81 VAQFLSGFLMTNVVQQSMRDLrrdieeKINRLPVSYFDKNQ--QGNILSRVTNDVD----AVSNAMQQSFINI---VSAV 151
Cdd:PTZ00265 112 ILSFISSFCMDVVTTKILKTL------KLEFLKSVFYQDGQfhDNNPGSKLTSDLDfyleQVNAGIGTKFITIftyASAF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 152 LGIVmavVMMFLINPLMAIFSVIMIPLSLI---ISRTIVKISQKYFQGMQNSLGDLngyVQENMTGFSVLKLYGREKETL 228
Cdd:PTZ00265 186 LGLY---IWSLFKNARLTLCITCVFPLIYIcgvICNKKVKINKKTSLLYNNNTMSI---IEEALVGIRTVVSYCGEKTIL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 229 EGFKQVNHRLNGFGFKASFISGLMLPLVQMTA---------YGTYIGVAVLGSYYV---VAGVIVVGQLQAFIQYIWQIS 296
Cdd:PTZ00265 260 KKFNLSEKLYSKYILKANFMESLHIGMINGFIlasyafgfwYGTRIIISDLSNQQPnndFHGGSVISILLGVLISMFMLT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 297 QPMGNITQLSAALQSasasTMRIFEILD-EPEEELNEQDVPLPEpiLGSVEFENVSFSYDPEK--PLIRNLNFKVDAGQM 373
Cdd:PTZ00265 340 IILPNITEYMKSLEA----TNSLYEIINrKPLVENNDDGKKLKD--IKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 374 VAIVGPTGAGKTTLINLLMRFYDVTEGAIKI-DGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFG---------- 442
Cdd:PTZ00265 414 YAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdleal 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 443 ----------------------------------KLDAT-------------DYEVVDAAKTANVDHFIRTMPDGYEMEI 475
Cdd:PTZ00265 494 snyynedgndsqenknkrnscrakcagdlndmsnTTDSNeliemrknyqtikDSEVVDVSKKVLIHDFVSALPDKYETLV 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 476 NSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM--EGRTSFVIAHRLSTIREADLILVMK 553
Cdd:PTZ00265 574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLS 653
|
...
gi 488301890 554 QGE 556
Cdd:PTZ00265 654 NRE 656
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
346-557 |
1.57e-47 |
|
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: 163.93 E-value: 1.57e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:cd03246 2 EVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyemeinsegdnVSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03246 82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488301890 505 LDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIREADLILVMKQGEI 557
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
24-295 |
2.02e-47 |
|
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: 167.58 E-value: 2.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGlptTEISRNIAAGesiNFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd18548 3 LAPLFKLLEVLLELLLPTLMA---DIIDEGIANG---DLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIIS 183
Cdd:cd18548 77 DLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGT 263
Cdd:cd18548 157 FLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLA 236
|
250 260 270
....*....|....*....|....*....|..
gi 488301890 264 YIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQI 295
Cdd:cd18548 237 IVAILWFGGHLINAGSLQVGDLVAFINYLMQI 268
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
345-576 |
1.90e-46 |
|
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: 162.89 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAW--LYKGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAV 496
Cdd:COG1122 81 FQNPDdqLFAPTVEEDVAFGpenlGLPREEIRerVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQggfYE 574
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSD---YE 226
|
..
gi 488301890 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 |
1.84e-45 |
|
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: 162.04 E-value: 1.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLptteISRNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGR----ILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:pfam00664 77 RRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:pfam00664 157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 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 |
4.90e-44 |
|
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: 157.38 E-value: 4.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDPE-KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:cd03288 18 GEIKIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKGTIADNIRfGKLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPK 501
Cdd:cd03288 98 SIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQ 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-556 |
9.39e-43 |
|
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: 152.24 E-value: 9.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPE----KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKidgidtkkmnrsdVRSV 420
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------------VPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 FGMVLQDAWLYKGTIADNIRFGK-LDATDYE-VVDAAkTANVDhfIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVIS 498
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEERYEkVIKAC-ALEPD--LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 499 DPKILILDEATSSVDTRLEA-----LIQKAMdrvMEGRTSFVIAHRLSTIREADLILVMKQGE 556
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-302 |
1.11e-42 |
|
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: 155.00 E-value: 1.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLPTteisrNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMtNVVQQSM-RDLR 102
Cdd:cd18778 3 LTLLCALLSTLLGLVPPWLIRELV-----DLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLN-HVAEQKVvADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 103 RDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLII 182
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 183 SRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQM-TAY 261
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFlTSL 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 488301890 262 GTyigVAVL--GSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18778 237 GT---VLVLgfGGRLVLAGELTIGDLVAFLLYLGLFYEPITSL 276
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-303 |
2.15e-42 |
|
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: 154.20 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLPTTEIsrNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd18563 3 LGFLLMLLGTALGLVPPYLTKILIDDV--LIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIIS 183
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQM-TAYG 262
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFlTSLG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 488301890 263 TYIgVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18563 241 TLI-VWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLS 280
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
345-569 |
5.74e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 5.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMV 424
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRF-GKLDATDYEVVDAA-----KTANVDHFIRTMPDGYemeinsegdnvSLGQKQLLTIARAVI 497
Cdd:COG1131 79 PQEPALYPDlTVRENLRFfARLYGLPRKEARERidellELFGLTDAADRKVGTL-----------SGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 498 SDPKILILDEATSSVD--TRLE--ALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:COG1131 148 HDPELLILDEPTSGLDpeARRElwELLRELAA---EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
26-300 |
1.38e-39 |
|
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: 146.09 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTGlptTEISRNIAAGESINFDYVIQCLIWILVVGTgycVAQFLSGFLMTNVVQQSMRDLRRDI 105
Cdd:cd18576 2 LILLLLSSAIGLVFPLLAG---QLIDAALGGGDTASLNQIALLLLGLFLLQA---VFSFFRIYLFARVGERVVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPL----SLI 181
Cdd:cd18576 76 YRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVvvlvAVL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRTIVKISQKyfqgMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAY 261
Cdd:cd18576 156 FGRRIRKLSKK----VQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLF 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 488301890 262 GTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMG 300
Cdd:cd18576 232 GAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIG 270
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
70-568 |
3.89e-38 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 151.08 E-value: 3.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 70 IWILVVGT-GYCVAQFLSGFLMtnvvQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIV 148
Cdd:PTZ00243 1005 LGIVLLGTfSVPLRFFLSYEAM----RRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 149 SAVLGIVMAVVMMFLINPLMAifsVIMIPLSLIISRTIVKIS------QKYFQGMQNSLGDLngyVQENMTGFSVLKLYG 222
Cdd:PTZ00243 1081 QCLFSICSSILVTSASQPFVL---VALVPCGYLYYRLMQFYNsanreiRRIKSVAKSPVFTL---LEEALQGSATITAYG 1154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 223 REKETLegfKQVNHRLN--------------GFGFKASFISGLMLPLVQMTAygtyIGVAVLGSYYVVAGVIvvgqlqaf 288
Cdd:PTZ00243 1155 KAHLVM---QEALRRLDvvyscsylenvanrWLGVRVEFLSNIVVTVIALIG----VIGTMLRATSQEIGLV-------- 1219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 289 iqyiwQISQPMGNITQLSAALQSASASTM--------RIFEILDE-PEEELNEQDVPL---------------------- 337
Cdd:PTZ00243 1220 -----SLSLTMAMQTTATLNWLVRQVATVeadmnsveRLLYYTDEvPHEDMPELDEEVdalerrtgmaadvtgtvviepa 1294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 338 ------PEPIL-GSVEFENVSFSYDPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDT 409
Cdd:PTZ00243 1295 sptsaaPHPVQaGSLVFEGVQMRYREGLPLVlRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREI 1374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 410 KKMNRSDVRSVFGMVLQDAWLYKGTIADNIR-FgkLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQ 488
Cdd:PTZ00243 1375 GAYGLRELRRQFSMIPQDPVLFDGTVRQNVDpF--LEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQ 1452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 489 LLTIARAVISDPKILIL-DEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PTZ00243 1453 LMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
.
gi 488301890 568 E 568
Cdd:PTZ00243 1533 M 1533
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
346-556 |
1.94e-37 |
|
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: 137.98 E-value: 1.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:cd03225 1 ELKNLSFSYpDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDA--WLYKGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAV 496
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlGLPEEEIEerVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIRE-ADLILVMKQGE 556
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
361-510 |
1.97e-37 |
|
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: 135.85 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKG-TIADNI 439
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 440 RFGkldATDYEVVDAAKTANVDHFIRTMPDGYEME--INSEGDNVSLGQKQLLTIARAVISDPKILILDEATS 510
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDLADrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
345-559 |
2.14e-37 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.26 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV---RSVF 421
Cdd:COG2884 2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKG-TIADNIRFGkLDATDYEVVDAAKTA-------NVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIA 493
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALP-LRVTGKSRKEIRRRVrevldlvGLSDKAKALP-----------HELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 494 RAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLSTIREADL-ILVMKQGEIIE 559
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
48-576 |
2.29e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 145.89 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 48 TEISRNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSgflmtNVVQQSMRdLRRDIEEKINRLPVSYFDKNQQGNILS 127
Cdd:PLN03232 325 SHLLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCESQYFQ-----NVGRVGFR-LRSTLVAAIFHKSLRLTHEARKNFASG 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 128 RVTNDVDAVSNAMQQ---SFINIVSAVLGIVMAVVMMFLINPLMAIFS----VIMIPLSLIISRTIVKISQKYFQGMQNS 200
Cdd:PLN03232 399 KVTNMITTDANALQQiaeQLHGLWSAPFRIIVSMVLLYQQLGVASLFGslilFLLIPLQTLIVRKMRKLTKEGLQWTDKR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 201 LGDLNgyvqENMTGFSVLKLYGREK-----------ETLEGFKQVnHRLNGFGfkaSFISGLMLPLVQMTAYGTYIgvaV 269
Cdd:PLN03232 479 VGIIN----EILASMDTVKCYAWEKsfesriqgirnEELSWFRKA-QLLSAFN---SFILNSIPVVVTLVSFGVFV---L 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 270 LGSYYVVAGVIVVGQLQAFIQYiwqisqPMGNITQLSAALQSASASTMRIFEILdEPEEELNEQDVPLpEPILGSVEFEN 349
Cdd:PLN03232 548 LGGDLTPARAFTSLSLFAVLRS------PLNMLPNLLSQVVNANVSLQRIEELL-LSEERILAQNPPL-QPGAPAISIKN 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 350 VSFSYDP--EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAikidgidtkkmnRSDVRSVFGMVLQD 427
Cdd:PLN03232 620 GYFSWDSktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS------------SVVIRGSVAYVPQV 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 AWLYKGTIADNIRFGkldaTDYEVVDAAKTANV---DHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:PLN03232 688 SWIFNATVRENILFG----SDFESERYWRAIDVtalQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYI 763
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 505 LDEATSSVDTRL-EALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKL 576
Cdd:PLN03232 764 FDDPLSALDAHVaHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
346-556 |
3.81e-36 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 132.37 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVL 425
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QdawlykgtiadnirfgkldatdyevvdaaktanvdhfirtmpdgyemeinsegdnVSLGQKQLLTIARAVISDPKILIL 505
Cdd:cd00267 80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488301890 506 DEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIREA-DLILVMKQGE 556
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
345-557 |
6.24e-36 |
|
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: 132.52 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMV 424
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFgkldatdyevvdaaktanvdhfirtmpdgyemeinsegdnvSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03230 79 PEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 504 ILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRE-ADLILVMKQGEI 557
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
326-569 |
9.06e-36 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 140.81 E-value: 9.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 326 PEEELNEQDVPLPEPILgsvEFENVSFSYD----PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGA 401
Cdd:COG1123 245 AARGRAAPAAAAAEPLL---EVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 402 IKIDGIDTKKMNRSDV---RSVFGMVLQDAwlY-----KGTIADNIRFGkLDAtdYEVVDAAK-TANVD----------H 462
Cdd:COG1123 322 ILFDGKDLTKLSRRSLrelRRRVQMVFQDP--YsslnpRMTVGDIIAEP-LRL--HGLLSRAErRERVAellervglppD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 463 FIRTMPdgYEMeinsegdnvSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRL 540
Cdd:COG1123 397 LADRYP--HEL---------SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDL 465
|
250 260 270
....*....|....*....|....*....|
gi 488301890 541 STIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
22-302 |
1.16e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 135.68 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLPtteISRNIAAGESINFD-YVIQCLIWILVVGTGYCVAQFLSGFLMTNVvqqsMRD 100
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYA---IDHFITPGTLDGLTgFILLYLGLILIQALSVFLFIRLAGKIEMGV----SYD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSL 180
Cdd:cd18540 77 LRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IIS----RTIVKISQKYFQgmQNSL--GDLNgyvqENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLP 254
Cdd:cd18540 157 VVSiyfqKKILKAYRKVRK--INSRitGAFN----EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLP 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 255 LVQMTAygtYIGVA---VLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18540 231 IVLFLG---SIATAlvlWYGGILVLAGAITIGTLVAFISYATQFFEPIQQL 278
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
345-567 |
2.13e-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: 133.63 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAwlykgTIADNI---------------RFGKLDATDYEVVDAA-KTANVDHFI-RTMpdgyemeinsegDNVSLGQK 487
Cdd:COG1120 81 PQEP-----PAPFGLtvrelvalgryphlgLFGRPSAEDREAVEEAlERTGLEHLAdRPV------------DELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVD----TRLEALIQKAMDRvmEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGT 562
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARE--RGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221
|
....*
gi 488301890 563 HHELL 567
Cdd:COG1120 222 PEEVL 226
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
346-571 |
2.56e-35 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 133.06 E-value: 2.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVfGMVL 425
Cdd:COG4555 3 EVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-GVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QDAWLYKG-TIADNIRFgklDATDYEVVDAAKTANVDHFIRTMpdgyEME--INSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:COG4555 81 DERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIELL----GLEefLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQGG 571
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
345-566 |
3.96e-35 |
|
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: 131.92 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDV-----TEGAIKIDG--IDTKKMNRSDV 417
Cdd:cd03260 1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGkdIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RSVFGMVLQDAWLYKGTIADNIRFG-KL------DATDYEVVDAAKTANvdhfirtMPDgyEMEINSEGDNVSLGQKQLL 490
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAA-------LWD--EVKDRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 491 TIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHEL 566
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQqAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
345-569 |
8.22e-35 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.11 E-value: 8.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVT---EGAIKIDGIDTKKMNRSDVRSV 420
Cdd:COG1123 5 LEVRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 FGMVLQDAW--LYKGTIADNIRFGKL------DATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTI 492
Cdd:COG1123 85 IGMVFQDPMtqLNPVTVGDQIAEALEnlglsrAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 493 ARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
24-299 |
8.47e-35 |
|
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: 133.00 E-value: 8.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGlptTEISRNIAAGesiNFDYVIQ-CLIWILVVGTGYcVAQFLSGFLMTNVVQQSMRDLR 102
Cdd:cd18546 3 LALLLVVVDTAASLAGPLLVR---YGIDSGVRAG---DLGVLLLaAAAYLAVVLAGW-VAQRAQTRLTGRTGERLLYDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 103 RDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLII 182
Cdd:cd18546 76 LRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 183 SRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYG 262
Cdd:cd18546 156 TRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNL 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 488301890 263 TYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18546 236 ATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPI 272
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
57-576 |
5.15e-34 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 138.72 E-value: 5.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 57 GESINFDYVIQCLIWILVVGTGYCVAQFLSgflmtNVVQQSMRdLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAV 136
Cdd:PLN03130 334 GEPAWIGYIYAFSIFVGVVLGVLCEAQYFQ-----NVMRVGFR-LRSTLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 137 SNAMQQ---SFINIVSAVLGIVMAVVMMF-------LINPLMAifsVIMIPL-SLIISRTiVKISQKYFQGMQNSLGDLN 205
Cdd:PLN03130 408 AEALQQicqQLHTLWSAPFRIIIAMVLLYqqlgvasLIGSLML---VLMFPIqTFIISKM-QKLTKEGLQRTDKRIGLMN 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 206 gyvqENMTGFSVLKLYGREKETLEGFKQV-NHRLNGFGfKASFISGL------MLP-LVQMTAYGTYigvAVLGSYYVVA 277
Cdd:PLN03130 484 ----EVLAAMDTVKCYAWENSFQSKVQTVrDDELSWFR-KAQLLSAFnsfilnSIPvLVTVVSFGVF---TLLGGDLTPA 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 278 GVIVVGQLQAFIQYiwqisqPMGNITQLSAALQSASASTMRIFEILDEPEEELneQDVPLPEPILGSVEFENVSFSYDP- 356
Cdd:PLN03130 556 RAFTSLSLFAVLRF------PLFMLPNLITQAVNANVSLKRLEELLLAEERVL--LPNPPLEPGLPAISIKNGYFSWDSk 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 -EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIdgidtkkmnrsdVRSVFGMVLQDAWLYKGTI 435
Cdd:PLN03130 628 aERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATV 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 436 ADNIRFG-KLDATDYEvvDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDT 514
Cdd:PLN03130 696 RDNILFGsPFDPERYE--RAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 515 RL-EALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEKL 576
Cdd:PLN03130 774 HVgRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
24-300 |
5.25e-34 |
|
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: 131.07 E-value: 5.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLPtteISRNIAAGesiNFDYVIQ---CLIWILVVGTGYCVAQflsGFLMTNVVQQSMRD 100
Cdd:cd18550 3 LVLLLILLSALLGLLPPLLLREI---IDDALPQG---DLGLLVLlalGMVAVAVASALLGVVQ---TYLSARIGQGVMYD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSL 180
Cdd:cd18550 74 LRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IISRTIVKISQKYFQGMQNSLGDLNGYVQE--NMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQM 258
Cdd:cd18550 154 LPTRRVGRRRRKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488301890 259 TAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMG 300
Cdd:cd18550 234 FTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLT 275
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
345-561 |
1.66e-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: 127.62 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEK---PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN---RSDVR 418
Cdd:cd03257 2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SVFGMVLQDA------WLykgTIADNIRFGKLDATDYEVVDAAKTANVDHFI-----RTMPDGYEMEinsegdnVSLGQK 487
Cdd:cd03257 82 KEIQMVFQDPmsslnpRM---TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYPHE-------LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
345-569 |
3.39e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 3.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN--------RSD 416
Cdd:COG1121 7 IELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARrrigyvpqRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VR-----SVFGMVLQDAWLYKGtiadniRFGKLDATDYEVVDAA-KTANVDHF----IRTMpdgyemeinsegdnvSLGQ 486
Cdd:COG1121 86 VDwdfpiTVRDVVLMGRYGRRG------LFRRPSRADREAVDEAlERVGLEDLadrpIGEL---------------SGGQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 487 KQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRE-ADLILVMKQGeIIEKGTHH 564
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPE 223
|
....*
gi 488301890 565 ELLEQ 569
Cdd:COG1121 224 EVLTP 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
345-575 |
3.92e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.80 E-value: 3.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGM 423
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ--DAWLYKGTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARA 495
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkKVPPKKMKdiIDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA--HRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFY 573
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
..
gi 488301890 574 EK 575
Cdd:PRK13632 237 EK 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
76-589 |
2.38e-32 |
|
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: 133.53 E-value: 2.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 76 GTGYCVAQFLSGFLMTNVVQQ--------SMRdLRRDIEEKINRLPVSYFDKNQQGNILSRVTN--DVDAVSNAMQQSFI 145
Cdd:TIGR00957 357 GYFYTGLLFVCACLQTLILHQyfhicfvsGMR-IKTAVMGAVYRKALVITNSARKSSTVGEIVNlmSVDAQRFMDLATYI 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 146 NIV-SAVLGIVMAVVMMFL-INPLM---AIFSVIMIPLSliisrTIVKISQKYFQGMQNSLGDLN-GYVQENMTGFSVLK 219
Cdd:TIGR00957 436 NMIwSAPLQVILALYFLWLnLGPSVlagVAVMVLMVPLN-----AVMAMKTKTYQVAHMKSKDNRiKLMNEILNGIKVLK 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 220 LYGRE---KETLEGFKQVNHRLNGfgfKASFISglmlplvqmtAYGTY--------IGVAVLGSYYVVAGVIVVGQLQAF 288
Cdd:TIGR00957 511 LYAWElafLDKVEGIRQEELKVLK---KSAYLH----------AVGTFtwvctpflVALITFAVYVTVDENNILDAEKAF 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 289 IQY-IWQISQ-PMGNITQLSAALQSASASTMRIFEILDEpeEELNEQDV---PLPEPILGSVEFENVSFSY-DPEKPLIR 362
Cdd:TIGR00957 578 VSLaLFNILRfPLNILPMVISSIVQASVSLKRLRIFLSH--EELEPDSIerrTIKPGEGNSITVHNATFTWaRDLPPTLN 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtkkmnrsdvrSVfGMVLQDAWLYKGTIADNIRFG 442
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SV-AYVPQQAWIQNDSLRENILFG 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 443 K-LDATDYEVVDAAKTANVDhfIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQ 521
Cdd:TIGR00957 723 KaLNEKYYQQVLEACALLPD--LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIF 800
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 522 KAM---DRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQ-GGFYEKLYNSQFAE-EGDYEE 589
Cdd:TIGR00957 801 EHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRdGAFAEFLRTYAPDEqQGHLED 873
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
346-555 |
6.29e-32 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 122.64 E-value: 6.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN--------RSDV 417
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvpqRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 R-----SVFGMVLQDAWLYKGTiadnirFGKLDATDYEVVDAA-KTANVDHFIrtmpdgyEMEInsegDNVSLGQKQLLT 491
Cdd:cd03235 80 DrdfpiSVRDVVLMGLYGHKGL------FRRLSKADKAKVDEAlERVGLSELA-------DRQI----GELSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 492 IARAVISDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRE-ADLILVMKQG 555
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRT 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
345-566 |
8.46e-32 |
|
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: 123.00 E-value: 8.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV---F 421
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKG-TIADNIRF-----GKLDATDYEVVDAAKTANV--DHFIRTMPDgyemEInsegdnvSLGQKQLLTIA 493
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKLEAVglRGAEDLYPA----EL-------SGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 494 RAVISDPKILILDEATSSVD----TRLEALIQKAMDrvMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
345-568 |
8.75e-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: 123.17 E-value: 8.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSD---VRSVF 421
Cdd:COG1127 6 IEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyeLRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKG-TIADNIRF-----GKLDATD-YEVVDAA-KTANVDHFIRTMPdgyemeinSEgdnVSLGQKQLLTIA 493
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFplrehTDLSEAEiRELVLEKlELVGLPGAADKMP--------SE---LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 494 RAVISDPKILILDEATSSVD----TRLEALIQKAMDRVmeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE 568
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
345-567 |
8.88e-32 |
|
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: 123.18 E-value: 8.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIrfgKLDATDYEVVDAAKTANVDHFIRTM---PDGYEMEINSEgdnVSLGQKQLLTIARAVISDP 500
Cdd:cd03295 81 IQQIGLFPHmTVEENI---ALVPKLLKWPKEKIRERADELLALVgldPAEFADRYPHE---LSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRL-STIREADLILVMKQGEIIEKGTHHELL 567
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
346-561 |
1.53e-31 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 120.62 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVL 425
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QdawlykgtiadnirfgkldatdyevvdAAKTANVDHFI-RTMpdgyemeinsegDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03214 80 Q---------------------------ALELLGLAHLAdRPF------------NELSGGERQRVLLARALAQEPPILL 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 505 LDEATSSVD----TRLEALIQKAMDRvmEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKG 561
Cdd:cd03214 121 LDEPTSHLDiahqIELLELLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
345-561 |
1.64e-31 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 120.50 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP-EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSdVRSVFGM 423
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKGTIADNIrfgkldatdyevvdaaktanvdhfirtmpdgyemeinseGDNVSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 504 ILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
345-556 |
2.57e-31 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 119.98 E-value: 2.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV--RSVFG 422
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKG-TIADNIRFGkldatdyevvdaaktanvdhfirtmpdgyemeinsegdnVSLGQKQLLTIARAVISDPK 501
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLS-TIREADLILVMKQGE 556
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
345-561 |
3.00e-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: 120.70 E-value: 3.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKM--NRSDVrsvfG 422
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVppERRNI----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKG-TIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPDGyemeinsegdnVSLGQKQLLTIARA 495
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlklrGVPKAEIRarVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLS-TIREADLILVMKQGEIIEKG 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 ... |
345-567 |
4.68e-31 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 120.76 E-value: 4.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP---EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTL---INLLMRFydvTEGAIKIDGIDTKKMNRSDVR 418
Cdd:cd03258 2 IELKNVSKVFGDtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLERP---TSGSVLVDGTDLTLLSGKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SV---FGMVLQDAWLYKG-TIADNIRFG-KLDATDYEVVDAAktanVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIA 493
Cdd:cd03258 79 KArrrIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEER----VLELLELV--GLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 494 RAVISDPKILILDEATSSVD---TR-LEALIQKAMDRVmeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELL 567
Cdd:cd03258 153 RALANNPKVLLCDEATSALDpetTQsILALLRDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-560 |
2.35e-30 |
|
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: 127.33 E-value: 2.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 13 RYIKPYR-LTFYLVILFTILTVAFNAALP---YLTGLPTTEISRNIAAGESINFDYVIQCL--------IWILVVGTGYC 80
Cdd:TIGR01271 858 RYITTNRnLVFVLIFCLVIFLAEVAASLLglwLITDNPSAPNYVDQQHANASSPDVQKPVIitptsayyIFYIYVGTADS 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 81 VAQ--FLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAV 158
Cdd:TIGR01271 938 VLAlgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 159 VMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREK--ETLeGFKQVN- 235
Cdd:TIGR01271 1018 FVVSVLQPYIFIAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSyfETL-FHKALNl 1096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 236 HRLNGFGFKAS---FISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQpmgNITQLSAALQSA 312
Cdd:TIGR01271 1097 HTANWFLYLSTlrwFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNS---SIDVDGLMRSVS 1173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 313 sastmRIFEILDEPEEE---------LNEQDVPLPE--------PILGSVEFENVSFSYDPE-KPLIRNLNFKVDAGQMV 374
Cdd:TIGR01271 1174 -----RVFKFIDLPQEEprpsggggkYQLSTVLVIEnphaqkcwPSGGQMDVQGLTAKYTEAgRAVLQDLSFSVEGGQRV 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 375 AIVGPTGAGKTTLINLLMRFYDvTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNirfgkLDA----TDYE 450
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-----LDPyeqwSDEE 1322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 451 VVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEG 530
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
570 580 590
....*....|....*....|....*....|....*
gi 488301890 531 RTSFVIAHRLSTIREADLILV-----MKQGEIIEK 560
Cdd:TIGR01271 1403 CTVILSEHRVEALLECQQFLViegssVKQYDSIQK 1437
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
22-302 |
4.33e-30 |
|
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: 119.89 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTGLPtteISRNIAAGesiNFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRA---IDGPIAHG---DRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLgIVMAVVMMFLINPLMAIFSVIMIPLSLI 181
Cdd:cd18543 75 RTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLT-LVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 182 ISRtivKISQKYFQGM---QNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQM 258
Cdd:cd18543 154 VAR---RFRRRYFPASrraQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488301890 259 TAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRML 274
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
68-299 |
4.36e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 120.31 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 68 CLIWILV-VGTGycVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFIN 146
Cdd:cd18564 57 AAALVGIaLLRG--LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 147 IVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKE 226
Cdd:cd18564 135 LLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEH 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 227 TLEGFKQVNHRLNGFGFKASFISGLMLPLVQM-TAYGTYIgVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18564 215 EERRFARENRKSLRAGLRAARLQALLSPVVDVlVAVGTAL-VLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPV 287
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
26-302 |
5.16e-30 |
|
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: 119.59 E-value: 5.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTGLPTTEISRniaageSINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRDI 105
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIK------GGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRT 185
Cdd:cd18557 76 FSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 186 IVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYI 265
Cdd:cd18557 156 YGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLL 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 488301890 266 GVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18557 236 LVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGL 272
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
345-537 |
1.94e-29 |
|
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: 115.58 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV---RSVF 421
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDA-WLYKGTIADNIRFGkLDATDY-------EVVDAAKTANVDHFIRTMPDGyemeinsegdnVSLGQKQLLTIA 493
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVAFA-LEVTGVppreirkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488301890 494 RAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA 537
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
345-559 |
2.43e-29 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 115.91 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY---DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINL---LMRfydVTEGAIKIDGIDTKKMNRSDV- 417
Cdd:COG1136 5 LELRNLTKSYgtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSERELa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 ---RSVFGMVLQD----AWLykgTIADNI----RFGKLDATDYE--VVDAAKTANVDHFIRTMPDgyEMeinsegdnvSL 484
Cdd:COG1136 82 rlrRRHIGFVFQFfnllPEL---TALENValplLLAGVSRKERRerARELLERVGLGDRLDHRPS--QL---------SG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIA-HRLSTIREADLILVMKQGEIIE 559
Cdd:COG1136 148 GQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
348-558 |
2.82e-29 |
|
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: 115.05 E-value: 2.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRSVFGMVLQD 427
Cdd:cd03226 3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 A--WLYKGTIADNIRFGKLDAtdyevvdAAKTANVDHFIRTmpdgyeMEINSEGD----NVSLGQKQLLTIARAVISDPK 501
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKEL-------DAGNEQAETVLKD------LDLYALKErhplSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-READLILVMKQGEII 558
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
345-559 |
3.36e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 116.34 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEK---PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRsDVrsvf 421
Cdd:COG1116 8 LELRGVSKRFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-DR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDA----WLykgTIADNIRFGkLDATDyeVVDAAKTANVDHFIRTM---------PdgYEMeinsegdnvSLGQKQ 488
Cdd:COG1116 83 GVVFQEPallpWL---TVLDNVALG-LELRG--VPKAERRERARELLELVglagfedayP--HQL---------SGGMRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 489 LLTIARAVISDPKILILDEATSSVD--TR--LEALIQKAMDRvmEGRTSFVIAHrlsTIREA----DLILVMKQ--GEII 558
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDalTRerLQDELLRLWQE--TGKTVLFVTH---DVDEAvflaDRVVVLSArpGRIV 220
|
.
gi 488301890 559 E 559
Cdd:COG1116 221 E 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
345-557 |
3.97e-29 |
|
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: 114.89 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY---DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVF 421
Cdd:cd03255 1 IELKNLSKTYgggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE-LAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 -----GMVLQDAWLYKG-TIADNI----RFGKLDATDYEVV--DAAKTANVDHFIRTMPDgyEMeinsegdnvSLGQKQL 489
Cdd:cd03255 80 rrrhiGFVFQSFNLLPDlTALENVelplLLAGVPKKERRERaeELLERVGLGDRLNHYPS--EL---------SGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 490 LTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLSTIREADLILVMKQGEI 557
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
345-559 |
4.45e-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: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY---DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRsvF 421
Cdd:cd03293 1 LEVRNVSKTYgggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG---EPVTGPGPD--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDA----WLykgTIADNIRFGkLDATDyeVVDAAKTANVDHFIRTMP-DGYEmeiNSEGDNVSLGQKQLLTIARAV 496
Cdd:cd03293 76 GYVFQQDallpWL---TVLDNVALG-LELQG--VPKAEARERAEELLELVGlSGFE---NAYPHQLSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 497 ISDPKILILDEATSSVD--TR--LEALIQKAMDRvmEGRTSFVIAHRLS-TIREADLILVMKQ--GEIIE 559
Cdd:cd03293 147 AVDPDVLLLDEPFSALDalTReqLQEELLDIWRE--TGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
8-507 |
5.98e-29 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 121.06 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 8 MKRIGRYIKPYRLTFYLVILFTILTVAFNAALPYLtglptteISRNIAAGESINFDYVIQCLIWILVvgtgYCVAQFLSG 87
Cdd:COG4615 1 MNLLRLLLRESRWLLLLALLLGLLSGLANAGLIAL-------INQALNATGAALARLLLLFAGLLVL----LLLSRLASQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 88 FLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQsFINIVSAVLGIVMAVVMMFLINPL 167
Cdd:COG4615 70 LLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 168 MAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKL--------YGRE-KETLEGFKQVNHR- 237
Cdd:COG4615 149 LFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKLnrrrrrafFDEDlQPTAERYRDLRIRa 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 238 LNGFGFKASFISGLMLPLvqmtaygtyIGVAVL-------GSYYVVAGVIVVgqlqafiqyIWQISQPMGNITQLSAALQ 310
Cdd:COG4615 229 DTIFALANNWGNLLFFAL---------IGLILFllpalgwADPAVLSGFVLV---------LLFLRGPLSQLVGALPTLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 311 SASASTMRIFEI---LDEPEEELNEQDVPLPEPILGSVEFENVSFSYDPEK--------PLirNLNFKvdAGQMVAIVGP 379
Cdd:COG4615 291 RANVALRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegftlgPI--DLTIR--RGELVFIVGG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 380 TGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLykgtiadnirFGKLdatdYEVVDAAKTAN 459
Cdd:COG4615 367 NGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHL----------FDRL----LGLDGEADPAR 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 460 VDHFIRTMpdgyEME--INSEGD-----NVSLGQKQLLTIARAVISDPKILILDE 507
Cdd:COG4615 433 ARELLERL----ELDhkVSVEDGrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
346-577 |
2.34e-28 |
|
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: 113.43 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV---FG 422
Cdd:cd03256 2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrqIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKG-TIADNIRFGKLDATdyevvdaaktanvdHFIRTMPDGYEME-----------------INSEGDNVSL 484
Cdd:cd03256 82 MIFQQFNLIERlSVLENVLSGRLGRR--------------STWRSLFGLFPKEekqralaalervglldkAYQRADQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVDTR-----LEALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPAssrqvMDLLKRINRE---EGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
250
....*....|....*....
gi 488301890 559 EKGTHHELLEQggFYEKLY 577
Cdd:cd03256 225 FDGPPAELTDE--VLDEIY 241
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
26-291 |
5.05e-28 |
|
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: 114.15 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTG----LPTTEISRNIAAGESINfdYVIQCLIWILVVGtgyCVAQFLSGFLMTNVVQQSMRDL 101
Cdd:cd18573 2 LALLLVSSAVTMSVPFAIGklidVASKESGDIEIFGLSLK--TFALALLGVFVVG---AAANFGRVYLLRIAGERIVARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 102 RRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIP---- 177
Cdd:cd18573 77 RKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPpiav 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 178 LSLIISRTIVKISQKyfqgMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQ 257
Cdd:cd18573 157 GAVFYGRYVRKLSKQ----VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTG 232
|
250 260 270
....*....|....*....|....*....|....
gi 488301890 258 MTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQY 291
Cdd:cd18573 233 FSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMY 266
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
339-570 |
9.54e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 112.80 E-value: 9.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 339 EPILgsvEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV 417
Cdd:PRK13635 3 EEII---RVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RSVFGMVLQ--DAWLYKGTIADNIRFG------KLDATDYEVVDAAKTANVDHFirtmpdgyemeINSEGDNVSLGQKQL 489
Cdd:PRK13635 80 RRQVGMVFQnpDNQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDF-----------LNREPHRLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 490 LTIARAVISDPKILILDEATSSVDT--RLEAL--IQKAMDRvmEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHE 565
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPrgRREVLetVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEE 226
|
....*
gi 488301890 566 LLEQG 570
Cdd:PRK13635 227 IFKSG 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-568 |
2.94e-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: 110.66 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP---EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:COG1124 2 LEVRNLSVSYGQggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDA-------WLYKGTIADNIRFGKLDATDYEVVDAAKTANVD-HFIRTMPDgyemeinsegdNVSLGQKQLLTIA 493
Cdd:COG1124 82 QMVFQDPyaslhprHTVDRILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 494 RAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELLE 568
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
343-575 |
1.31e-26 |
|
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: 109.56 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDvTEGAIKIDGIDTKKMNRSDVRSVF 421
Cdd:cd03289 1 GQMTVKDLTAKYtEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKGTIADNIR-FGKLdaTDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGGFYEK 575
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
361-562 |
4.14e-26 |
|
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: 106.75 E-value: 4.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMnRSDVRSVFGMV--LQDAWLYKG-TIAD 437
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGL-PPHEIARLGIGrtFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 438 NIRFG-----KLDATDYEVVDAAKTAN--VDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATS 510
Cdd:cd03219 95 NVMVAaqartGSGLLLARARREEREARerAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 511 SVDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGT 562
Cdd:cd03219 173 GLN---PEETEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
361-569 |
5.23e-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: 107.73 E-value: 5.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV----FGMVLQD-AWLYKGTI 435
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSfALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 436 ADNIRFGkldatdYEVvdaaktANVDHFIRTMPD-------GYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEA 508
Cdd:cd03294 120 LENVAFG------LEV------QGVPRAEREERAaealelvGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 509 TSSVDtrleALIQKAM-DRVME-----GRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:cd03294 188 FSALD----PLIRREMqDELLRlqaelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
361-562 |
7.09e-26 |
|
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: 106.66 E-value: 7.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMnRSDVRSVFGMV--LQDAWLYKG-TIAD 437
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGL-PPHRIARLGIArtFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 438 NIRFGKLDATDYEVVDAAktANVDHFIRTMPDGYE--MEI----------NSEGDNVSLGQKQLLTIARAVISDPKILIL 505
Cdd:COG0411 99 NVLVAAHARLGRGLLAAL--LRLPRARREEREAREraEELlervgladraDEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 506 DEAT---SSVDT-RLEALIQKAMDRvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGT 562
Cdd:COG0411 177 DEPAaglNPEETeELAELIRRLRDE--RGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-578 |
7.77e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.58 E-value: 7.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTT---LINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV 420
Cdd:PRK13640 6 VEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 FGMVLQ--DAWLYKGTIADNIRFGkldaTDYEVVDAAKTANVDHfiRTMPD-GYEMEINSEGDNVSLGQKQLLTIARAVI 497
Cdd:PRK13640 86 VGIVFQnpDNQFVGATVGDDVAFG----LENRAVPRPEMIKIVR--DVLADvGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIREADLILVMKQGEIIEKGT------HHELLEQ 569
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpveifsKVEMLKE 239
|
250
....*....|...
gi 488301890 570 GG----FYEKLYN 578
Cdd:PRK13640 240 IGldipFVYKLKN 252
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
345-561 |
7.93e-26 |
|
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: 105.41 E-value: 7.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGMV 424
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFG-KL-----DATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAVI 497
Cdd:cd03301 78 FQNYALYPHmTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAH-RLSTIREADLILVMKQGEIIEKG 561
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
345-567 |
7.99e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 108.63 E-value: 7.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLI---RNLNFKVDAGQMVAIVGPTGAGKTTL---INLLMRFydvTEGAIKIDGIDTKKMNRSDVR 418
Cdd:COG1135 2 IELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SV---FGMVLQDAWLYKG-TIADNIRF-----GkldatdyevVDAAKTAN-VDHFIRTMpdGYEMEINSEGDNVSLGQKQ 488
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENVALpleiaG---------VPKAEIRKrVAELLELV--GLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 489 LLTIARAVISDPKILILDEATSSVD---TR--LEaLIQKAMDRVmeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGT 562
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDpetTRsiLD-LLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
|
....*
gi 488301890 563 HHELL 567
Cdd:COG1135 225 VLDVF 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
343-569 |
8.05e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 109.01 E-value: 8.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDtkkMNRSDV--RSV 420
Cdd:COG3839 2 ASLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD---VTDLPPkdRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 fGMVLQDAWLYKG-TIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIA 493
Cdd:COG3839 78 -AMVFQSYALYPHmTVYENIAFPlklrKVPKAEIDrrVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 494 RAVISDPKILILDEATSSVD------TRLE-ALIQKAMdrvmegRTSFVIA-HRLS---TIreADLILVMKQGEIIEKGT 562
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL------GTTTIYVtHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
....*..
gi 488301890 563 HHELLEQ 569
Cdd:COG3839 218 PEELYDR 224
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-561 |
1.12e-25 |
|
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: 104.56 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPE-----KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM--RFYDVTEGAIKIDGIDTKKmnrSD 416
Cdd:cd03213 3 TLSFRNLTVTVKSSpsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VRSVFGMVLQDAWLYKG-TIADNIRFgkldatdyevvdAAKtanvdhfIRtmpdgyemeinsegdNVSLGQKQLLTIARA 495
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAK-------LR---------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLST--IREADLILVMKQGEIIEKG 561
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
344-569 |
2.46e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 107.49 E-value: 2.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRSDVrsvf 421
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGrdVTGLPPEKRNV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQD--AW--LykgTIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPDgyEMeinsegdnvSLGQKQLLT 491
Cdd:COG3842 80 GMVFQDyaLFphL---TVAENVAFGlrmrGVPKAEIRarVAELLELVGLEGLADRYPH--QL---------SGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVDTRL-EAL------IQKAMdrvmeGRTSFVIAHRLStirEA----DLILVMKQGEIIEK 560
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLrEEMreelrrLQREL-----GITFIYVTHDQE---EAlalaDRIAVMNDGRIEQV 217
|
....*....
gi 488301890 561 GTHHELLEQ 569
Cdd:COG3842 218 GTPEEIYER 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
345-568 |
2.80e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 104.79 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPeKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTK--KMNRSDVRSVFG 422
Cdd:PRK09493 2 IEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKGTIA-DNIRFGKLDatdyevVDAAKTANVDHFIRTMPD--GYEMEINSEGDNVSLGQKQLLTIARAVISD 499
Cdd:PRK09493 81 MVFQQFYLFPHLTAlENVMFGPLR------VRGASKEEAEKQARELLAkvGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 500 PKILILDEATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE 568
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
19-303 |
2.88e-25 |
|
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: 105.99 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 19 RLTFYLVILFTILTVAFNAALPYltglptteISRNIA--AGESINFDYVIqclIWILVVGTGYCVAQFLSgFLMT---NV 93
Cdd:cd18549 1 KKLFFLDLFCAVLIAALDLVFPL--------IVRYIIddLLPSKNLRLIL---IIGAILLALYILRTLLN-YFVTywgHV 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 94 VQQSM-RDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFS 172
Cdd:cd18549 69 MGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 173 VIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNH-----RLNGFGFKASF 247
Cdd:cd18549 149 FALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDrflesKKKAYKAMAYF 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 248 ISGLMLpLVQMtaygTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18549 229 FSGMNF-FTNL----LNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLV 279
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
81-299 |
3.61e-25 |
|
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: 106.11 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 81 VAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVM 160
Cdd:cd18565 69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 161 MFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNG 240
Cdd:cd18565 149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRD 228
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 241 FGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGV------IVVGQLQAFIQYIWQISQPM 299
Cdd:cd18565 229 ANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGPplftgtLTVGTLVTFLFYTQRLLWPL 293
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
345-526 |
5.73e-25 |
|
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: 102.56 E-value: 5.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMV 424
Cdd:COG4133 3 LEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRF----GKLDATDYEVVDAAKTANVDHFIRTMPDGYemeinsegdnvSLGQKQLLTIARAVISD 499
Cdd:COG4133 81 GHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGLAGLADLPVRQL-----------SAGQKRRVALARLLLSP 149
|
170 180 190
....*....|....*....|....*....|.
gi 488301890 500 PKILILDEATSSVDT----RLEALIQKAMDR 526
Cdd:COG4133 150 APLWLLDEPFTALDAagvaLLAELIAAHLAR 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
345-568 |
5.77e-25 |
|
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: 103.57 E-value: 5.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKplIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRsvFGMV 424
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAVI 497
Cdd:cd03299 77 PQNYALFPHmTVYKNIAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE 568
Cdd:cd03299 146 VNPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
26-302 |
9.01e-25 |
|
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: 104.55 E-value: 9.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTGlptTEISRNIAAGESINFDYVIQCLIwILVVGTGycVAQFLSGFLMTNVVQQSMRDLRRDI 105
Cdd:cd18572 2 FVFLVVAALSELAIPHYTG---AVIDAVVADGSREAFYRAVLLLL-LLSVLSG--LFSGLRGGCFSYAGTRLVRRLRRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRT 185
Cdd:cd18572 76 FRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 186 IVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYI 265
Cdd:cd18572 156 YGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQV 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 488301890 266 GVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18572 236 LVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSL 272
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-569 |
2.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.20 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDP----EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGID--TKKMNRSDV 417
Cdd:PRK13637 2 SIKIENLTHIYMEgtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RSVFGMVLQ--DAWLYKGTIADNIRFG--KLDATDYEVVDAAKTAnvdhfIRTMPDGYEMEINSEGDNVSLGQKQLLTIA 493
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 494 RAVISDPKILILDEATSSVDTR----LEALIQKAMDRvmEGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELLE 568
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKgrdeILNKIKELHKE--YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
.
gi 488301890 569 Q 569
Cdd:PRK13637 235 E 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
345-567 |
3.01e-24 |
|
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: 102.08 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGA-IKIDGIDTKKMNRSDVRSVFGM 423
Cdd:COG1119 4 LELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 V---LQDAWLYKGTIADNIRFGKLDATD-YEVVDAAKTANVDHFIRtmpdgyEMEINSEGD----NVSLGQKQLLTIARA 495
Cdd:COG1119 83 VspaLQLRFPRDETVLDVVLSGFFDSIGlYREPTDEQRERARELLE------LLGLAHLADrpfgTLSQGEQRRVLIARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 496 VISDPKILILDEATSSVDtrLEA--LIQKAMDRVM-EGRTSFV-IAHRLSTIREA-DLILVMKQGEIIEKGTHHELL 567
Cdd:COG1119 157 LVKDPELLILDEPTAGLD--LGAreLLLALLDKLAaEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
346-568 |
3.36e-24 |
|
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: 100.97 E-value: 3.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSD-VRSVFGMV 424
Cdd:cd03224 2 EVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFGkldatDYEVVDAAKTANVDHFIRTMPDGYEMEiNSEGDNVSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03224 81 PEGRRIFPElTVEENLLLG-----AYARRRAKRKARLERVYELFPRLKERR-KQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 504 ILDEATS----SVDTRLEALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE 568
Cdd:cd03224 155 LLDEPSEglapKIVEEIFEAIRELRD---EGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
345-555 |
4.69e-24 |
|
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: 100.48 E-value: 4.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAI----KIDGIDTKKMNRSDVRSV 420
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 FGMVLQDAWLYKGTIADNIRFGK-LDATDYEVVDAAKTANVDhfIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISD 499
Cdd:cd03290 81 VAYAAQKPWLLNATVEENITFGSpFNKQRYKAVTDACSLQPD--IDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 500 PKILILDEATSSVDTRL-EALIQKAMDRVM--EGRTSFVIAHRLSTIREADLILVMKQG 555
Cdd:cd03290 159 TNIVFLDDPFSALDIHLsDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
321-569 |
7.91e-24 |
|
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: 101.47 E-value: 7.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 321 EILDEPEEELNEQDVPLPEPilgSVEFENVSFSYDPekpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEG 400
Cdd:cd03291 19 ELLEKAKQENNDRKHSSDDN---NLFFSNLCLVGAP---VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 401 AIKIDGidtkkmnrsdvRSVFGMvlQDAWLYKGTIADNIRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGD 480
Cdd:cd03291 93 KIKHSG-----------RISFSS--QFSWIMPGTIKENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 481 NVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALI-QKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIE 559
Cdd:cd03291 159 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYF 238
|
250
....*....|
gi 488301890 560 KGTHHELLEQ 569
Cdd:cd03291 239 YGTFSELQSL 248
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
345-568 |
1.76e-23 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 102.33 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKM--NRSDVRSVFg 422
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRHVNTVF- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 mvlQDAWLYKG-TIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARA 495
Cdd:PRK09452 93 ---QSYALFPHmTVFENVAFGlrmqKTPAAEITprVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQ---KAMDRVMeGRT-SFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLE 568
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQnelKALQRKL-GITfVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
345-569 |
1.82e-23 |
|
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: 99.23 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDV-RSVFGM 423
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITNLPPhKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIRFG----KLDATDY--EVVDAAKTANVDHFIRTMPDgyEMeinsegdnvSLGQKQLLTIARAV 496
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlrlkKLPKAEIkeRVAEALDLVQLEGYANRKPS--QL---------SGGQQQRVAIARAL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLStirEA----DLILVMKQGEIIEKGTHHELLEQ 569
Cdd:cd03300 146 VNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGITFVFVTHDQE---EAltmsDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
69-291 |
1.84e-23 |
|
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: 100.64 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 69 LIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIV 148
Cdd:cd18575 39 FLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 149 SAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLI----ISRTIVKISQKYfqgmQNSLGDLNGYVQENMTGFSVLKLYGRE 224
Cdd:cd18575 119 RNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLpiilFGRRVRRLSRAS----QDRLADLSAFAEETLSAIKTVQAFTRE 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 225 KETLEGFKQ-VNHrlngfGFKAS----FISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQY 291
Cdd:cd18575 195 DAERQRFATaVEA-----AFAAAlrriRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFY 261
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
345-557 |
2.20e-23 |
|
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: 98.37 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRSDVRSVFG 422
Cdd:cd03262 1 IEIKNLHKSFGDFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQDAWLYKG-TIADNIRFG-----KLDAtdyevvDAAKTANVDHFIRTmpdGYEMEINSEGDNVSLGQKQLLTIARAV 496
Cdd:cd03262 80 MVFQQFNLFPHlTVLENITLApikvkGMSK------AEAEERALELLEKV---GLADKADAYPAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEI 557
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
345-569 |
2.89e-23 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 100.90 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIR---NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYD---VTEGAIKIDGIDTKKMNRSDVR 418
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SV----FGMVLQDAW-----LYK-GT-IADNIR-FGKLDATDYE--VVDAAKT---ANVDHFIRTMPdgYEMeinsegdn 481
Cdd:COG0444 82 KIrgreIQMIFQDPMtslnpVMTvGDqIAEPLRiHGGLSKAEARerAIELLERvglPDPERRLDRYP--HEL-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 vSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGR-TSFV-IAHRLSTIRE-ADLILVMKQGEII 558
Cdd:COG0444 152 -SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIV 230
|
250
....*....|.
gi 488301890 559 EKGTHHELLEQ 569
Cdd:COG0444 231 EEGPVEELFEN 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
345-571 |
3.07e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.81 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDP--EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFG 422
Cdd:PRK13650 5 IEVKNLTFKYKEdqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQ--DAWLYKGTIADNIRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYEmeinSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:PRK13650 85 MVFQnpDNQFVGATVEDDVAFG-LENKGIPHEEMKERVNEALELVGMQDFKE----REPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 501 KILILDEATSSVDT--RLEaLIQKAMD-RVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQGG 571
Cdd:PRK13650 160 KIIILDEATSMLDPegRLE-LIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
345-566 |
5.85e-23 |
|
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: 97.58 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY-DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGM 423
Cdd:cd03263 1 LQIRNLTKTYkKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIRF-GKLdatdYEVVDAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPK 501
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyARL----KGLPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTsfVIahrLST--IREADL----ILVMKQGEIIEKGTHHEL 566
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRS--II---LTThsMDEAEAlcdrIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
344-569 |
9.85e-23 |
|
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: 97.41 E-value: 9.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGM 423
Cdd:cd03296 2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNV-GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIRFG-KLDATDYEVVDAAKTANVDHFIRTMP-DGYEMEINSEgdnVSLGQKQLLTIARAVISDP 500
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLKLVQlDWLADRYPAQ---LSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 501 KILILDEATSSVDTR----LEALIQKAMDRVmeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:cd03296 156 KVLLLDEPFGALDAKvrkeLRRWLRRLHDEL--HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
345-558 |
1.21e-22 |
|
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: 94.80 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRsvfgmv 424
Cdd:cd03216 1 LELRGITKRFGGVKAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPR------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 lqDAWlykgtiadniRFGkldatdyevvdaaktanvdhfIRTMpdgYEMeinsegdnvSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03216 71 --DAR----------RAG---------------------IAMV---YQL---------SVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 505 LDEATSSVDTR-LEALIqKAMDRVM-EGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:cd03216 106 LDEPTAALTPAeVERLF-KVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
98-299 |
1.61e-22 |
|
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: 98.26 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 98 MRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIP 177
Cdd:cd18554 78 LYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 178 LSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQ 257
Cdd:cd18554 158 FYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVN 237
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488301890 258 MTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18554 238 TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
345-571 |
1.81e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.50 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDA--WLYKGTIADNIRFGKL------DATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAV 496
Cdd:PRK13647 85 FQDPddQVFSSTVWDDVAFGPVnmgldkDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG-----THHELLEQ 569
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksllTDEDIVEQ 233
|
..
gi 488301890 570 GG 571
Cdd:PRK13647 234 AG 235
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
345-561 |
2.90e-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: 95.51 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLI---RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVF 421
Cdd:cd03266 2 ITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKG-TIADNIR-FGKLdatdYEVVDAAKTANVDHFIRTMpdgyEME--INSEGDNVSLGQKQLLTIARAVI 497
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyFAGL----YGLKGDELTARLEELADRL----GMEelLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTI-READLILVMKQGEIIEKG 561
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-584 |
3.38e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPEKPL----IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG----IDTKKMNRS 415
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 DVRSVFGMVLQ--DAWLYKGTIADNIRFGKLD--ATDYEVVDAAKtanvdHFIRTMPDGYEMeINSEGDNVSLGQKQLLT 491
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAL-----KWLKKVGLSEDL-ISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVDTR-LEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEgRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235
|
250 260
....*....|....*....|
gi 488301890 570 GGFYEKLY-----NSQFAEE 584
Cdd:PRK13641 236 KEWLKKHYldepaTSRFASK 255
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
345-561 |
3.70e-22 |
|
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: 94.87 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLirNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGMV 424
Cdd:cd03298 1 VRLDKIRFSYG-EQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-RPV-SML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFG-----KLDATDYEVVD-AAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAVI 497
Cdd:cd03298 76 FQENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEvALARVGLAGLEKRLP-----------GELSGGERQRVALARVLV 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 498 SDPKILILDEATSSVDTrleALIQKAMDRVME-----GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:cd03298 145 RDKPVLLLDEPFAALDP---ALRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
345-569 |
3.74e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 96.69 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS--DVRSVFG 422
Cdd:PRK13639 2 LETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQ--DAWLYKGTIADNIRFGKL------DATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIAR 494
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 495 AVISDPKILILDEATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
345-561 |
3.90e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 94.95 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYdPEKPLIRNLNFKVDAGqMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMnRSDVRSVFGMV 424
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ-PQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKgtiadniRFGKLDATDY-----EVVDAAKTANVDHFIR--TMPDGYEMEINSegdnVSLGQKQLLTIARAVI 497
Cdd:cd03264 78 PQEFGVYP-------NFTVREFLDYiawlkGIPSKEVKARVDEVLElvNLGDRAKKKIGS----LSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 498 SDPKILILDEATSSVD----TRLEALIQkamdRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:cd03264 147 GDPSILIVDEPTAGLDpeerIRFRNLLS----ELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
29-285 |
4.57e-22 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 96.77 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 29 TILTVAFNAALPYLT---GLPTTEISRNIAAGESIN--FDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd18577 5 LLAAIAAGAALPLMTivfGDLFDAFTDFGSGESSPDefLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIIS 183
Cdd:cd18577 85 RYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGT 263
Cdd:cd18577 165 GIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAM 244
|
250 260
....*....|....*....|..
gi 488301890 264 YIGVAVLGSYYVVAGVIVVGQL 285
Cdd:cd18577 245 YALAFWYGSRLVRDGEISPGDV 266
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
345-570 |
1.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPL-IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGM 423
Cdd:PRK13648 8 IVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ--DAWLYKGTIADNIRFG------KLDATDYEVVDAAKtaNVDHFIRTmpdgyemeiNSEGDNVSLGQKQLLTIARA 495
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALK--QVDMLERA---------DYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 496 VISDPKILILDEATSSVDTRLEALIQKAMDRVMEGR--TSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLEQG 570
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
345-569 |
1.45e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.33 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmnRSDVRSVFGMV 424
Cdd:PRK11432 7 VVLKNITKRFG-SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQRDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIRFG--KLDATDYEVVDAAKTA--NVDHfirtmpDGYEmeiNSEGDNVSLGQKQLLTIARAVISD 499
Cdd:PRK11432 84 FQSYALFPHmSLGENVGYGlkMLGVPKEERKQRVKEAleLVDL------AGFE---DRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 500 PKILILDEATSSVDTRLealiQKAM-DRVME-----GRTSFVIAHRLStirEA----DLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK11432 155 PKVLLFDEPLSNLDANL----RRSMrEKIRElqqqfNITSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
345-562 |
3.97e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 94.87 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLI---RNLNFKVDAGQMVAIVGPTGAGKTTLI---NLLMRfydVTEGAIKIDGIDTKKMNRSDVR 418
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhalNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SV---FGMVLQDAWLYKG-TIADNIRFG-KLDATDYEVVDAaktanvdhfiRTMP-----------DGYEMEInsegdnv 482
Cdd:PRK11153 79 KArrqIGMIFQHFNLLSSrTVFDNVALPlELAGTPKAEIKA----------RVTEllelvglsdkaDRYPAQL------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 483 SLGQKQLLTIARAVISDPKILILDEATSSVD---TR--LEAL--IQKAMdrvmeGRTSFVIAHRLSTIRE-ADLILVMKQ 554
Cdd:PRK11153 142 SGGQKQRVAIARALASNPKVLLCDEATSALDpatTRsiLELLkdINREL-----GLTIVLITHEMDVVKRiCDRVAVIDA 216
|
....*...
gi 488301890 555 GEIIEKGT 562
Cdd:PRK11153 217 GRLVEQGT 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
338-559 |
5.15e-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: 5.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 338 PEPILgsvEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV 417
Cdd:COG1129 1 AEPLL---EMRGISKSFGGVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RS--VfGMVLQD----AWLykgTIADNIRFGKLdATDYEVVDAAKT-ANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLL 490
Cdd:COG1129 77 QAagI-AIIHQElnlvPNL---SVAENIFLGRE-PRRGGLIDWRAMrRRARELLARL--GLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 491 TIARAVISDPKILILDEATSS-----VDtRLEALIQKAMDRvmeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIE 559
Cdd:COG1129 150 EIARALSRDARVLILDEPTASltereVE-RLFRIIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
344-566 |
5.46e-21 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.77 E-value: 5.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGM 423
Cdd:PRK10851 2 SIEIANIKKSFGRTQVL-NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-RKV-GF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIRFG----------KLDATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTI 492
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 493 ARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQV 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
359-576 |
1.01e-20 |
|
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: 96.90 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 359 PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtkkmnrsdvRSVFGMvlQDAWLYKGTIADN 438
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----------RISFSP--QTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 439 IRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEA 518
Cdd:TIGR01271 507 IIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 519 LI-QKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELL-EQGGFYEKL 576
Cdd:TIGR01271 586 EIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQaKRPDFSSLL 645
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
345-561 |
1.28e-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: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMnrSDVRSVFGMV 424
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN--IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIR-FGKLDATDYEVVDaaKTANVDHFIrtmpdgyemeiNSEGDNV---SLGQKQLLTIARAVISD 499
Cdd:cd03268 78 IEAPGFYPNlTARENLRlLARLLGIRKKRID--EVLDVVGLK-----------DSAKKKVkgfSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 500 PKILILDEATSSVDT----RLEALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:cd03268 145 PDLLILDEPTNGLDPdgikELRELILSLRD---QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
344-566 |
1.76e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 1.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNrsDV----RS 419
Cdd:PRK11000 3 SVTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMN--DVppaeRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 420 VfGMVLQDAWLYKG-TIADNIRFG-KLDATDYEVVD-----AAKTANVDHFIRTMPDGyemeinsegdnVSLGQKQLLTI 492
Cdd:PRK11000 77 V-GMVFQSYALYPHlSVAENMSFGlKLAGAKKEEINqrvnqVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 493 ARAVISDPKILILDEATSSVDT------RLEalIQKAMDRVmeGRTSFVIAH-RLSTIREADLILVMKQGEIIEKGTHHE 565
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAalrvqmRIE--ISRLHKRL--GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLE 220
|
.
gi 488301890 566 L 566
Cdd:PRK11000 221 L 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
346-567 |
2.57e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.20 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYdPEKPLirNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGMVL 425
Cdd:COG3840 3 RLDDLTYRY-GDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RPV-SMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QD----AWLykgTIADNIRFG-----KLDATDYE-VVDAAKTANVDHFIRTMPDgyemeinsegdNVSLGQKQLLTIARA 495
Cdd:COG3840 78 QEnnlfPHL---TVAQNIGLGlrpglKLTAEQRAqVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 496 VISDPKILILDEATSSVDT--RLE--ALIQKAMDRvmEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELL 567
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalRQEmlDLVDELCRE--RGLTVLMVTHDPEdAARIADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
345-561 |
3.51e-20 |
|
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: 89.26 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDvRSVFGMV 424
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAA-RNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLY-KGTIADNIR-FGKLdaTDYEVVDAAKtaNVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:cd03269 76 PEERGLYpKMKVIDQLVyLAQL--KGLKKEEARR--RIDEWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 503 LILDEATSSVD-TRLEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:cd03269 150 LILDEPFSGLDpVNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
339-568 |
3.64e-20 |
|
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: 89.66 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 339 EPILgsvEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMnRSD-- 416
Cdd:COG0410 1 MPML---EVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHri 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VRSVFGMVLQDAWLYKG-TIADNIRFGKLDATDYEVVDAAKTANVDHFirtmPDGYEMeINSEGDNVSLGQKQLLTIARA 495
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLERVYELF----PRLKER-RRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 496 VISDPKILILDEAT-----SSVDtRLEALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE 568
Cdd:COG0410 151 LMSRPKLLLLDEPSlglapLIVE-EIFEIIRRLNR---EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
345-569 |
8.99e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.76 E-value: 8.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY-----DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS-DVR 418
Cdd:PRK13633 5 IKCKNVSYKYesneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SVFGMVLQ--DAWLYKGTIADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLL 490
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 491 TIARAVISDPKILILDEATSSVDT--RLEAL--IQKAMDRvmEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPsgRREVVntIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 488301890 567 LEQ 569
Cdd:PRK13633 232 FKE 234
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
344-569 |
1.22e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 90.59 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPEKpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKkmnrSDV----RS 419
Cdd:COG1118 2 SIEVRNISKRFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLppreRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 420 VfGMVLQDAWLYKG-TIADNIRFGkldATDYEVVDAAKTANVDHFIRtmpdgyEMEINSEGD----NVSLGQKQLLTIAR 494
Cdd:COG1118 77 V-GFVFQHYALFPHmTVAENIAFG---LRVRPPSKAEIRARVEELLE------LVQLEGLADrypsQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 495 AVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTS-FVI-----AHRLstireADLILVMKQGEIIEKGTHHEL 566
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTvFVThdqeeALEL-----ADRVVVMNQGRIEQVGTPDEV 221
|
...
gi 488301890 567 LEQ 569
Cdd:COG1118 222 YDR 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
345-559 |
1.24e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 88.56 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDV-----TEGAIKIDGID--TKKMNRSDV 417
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLipgarVEGEILLDGEDiyDPDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RSVFGMVLQDAWLYKGTIADNIRFG----------KLDATdyeVVDAAKTAN----VDHfirtmpdgyemEINSEGDNVS 483
Cdd:COG1117 91 RRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksksELDEI---VEESLRKAAlwdeVKD-----------RLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 484 LGQKQLLTIARAVISDPKILILDEATSSVD----TRLEALIQkamdrvmEGRTSFVIA---HRLS-TIREADLILVMKQG 555
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDpistAKIEELIL-------ELKKDYTIVivtHNMQqAARVSDYTAFFYLG 229
|
....
gi 488301890 556 EIIE 559
Cdd:COG1117 230 ELVE 233
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
346-583 |
1.26e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 88.74 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDPEKPLIR--------NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV 417
Cdd:COG4167 6 EVRNLSKTFKYRTGLFRrqqfeavkPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 RSVFGMVLQDAwlyKGTIADNIRFGK-LDA-----TDYEvvDAAKTANVDHFIRT---MPDGYEMEINSegdnVSLGQKQ 488
Cdd:COG4167 86 CKHIRMIFQDP---NTSLNPRLNIGQiLEEplrlnTDLT--AEEREERIFATLRLvglLPEHANFYPHM----LSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 489 LLTIARAVISDPKILILDEATSSVDTRLEALI-------QKAMDrvmegrTSFV-IAHRLSTIRE-ADLILVMKQGEIIE 559
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDMSVRSQIinlmlelQEKLG------ISYIyVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|....*.
gi 488301890 560 KGTHHELLE--QGGFYEKLYNSQFAE 583
Cdd:COG4167 231 YGKTAEVFAnpQHEVTKRLIESHFGE 256
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
345-567 |
1.50e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.00 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPL--IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFG 422
Cdd:PRK13642 5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQ--DAWLYKGTIADNIRFGkLDATDYEVVDAAKTANVDHFIRTMPDGYemeiNSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFK----TREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGR--TSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-571 |
1.57e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.40 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRSvFGM 423
Cdd:COG4152 1 MLELKGLTKRFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG---EPLDPEDRRR-IGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIR-FGKL---DATDyevvdaAKTANVDHFIRtmpdgyeMEINS-EGDNV---SLGQKQLLTIAR 494
Cdd:COG4152 76 LPEERGLYPKmKVGEQLVyLARLkglSKAE------AKRRADEWLER-------LGLGDrANKKVeelSKGNQQKVQLIA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 495 AVISDPKILILDEATS-----SVDTRLEALIQKAmdrvMEGRTsfVI--AHRLSTI-READLILVMKQGEIIEKGTHHEL 566
Cdd:COG4152 143 ALLHDPELLILDEPFSgldpvNVELLKDVIRELA----AKGTT--VIfsSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
....*
gi 488301890 567 LEQGG 571
Cdd:COG4152 217 RRQFG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
361-567 |
1.70e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV----FGMVLQD-AWLYKGTI 435
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 436 ADNIRFG------KLDATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAVISDPKILILDEAT 509
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 510 SSVDTRLEALIQKAMDRVM--EGRTSFVIAHRL-STIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
346-566 |
1.84e-19 |
|
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: 87.58 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSD-VRSVFGMV 424
Cdd:TIGR03410 2 EVSNLNVYYG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHErARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQdawlykG-------TIADNIRFGkLDATdyevvdAAKTANVDHFIRTM-PDGYEMeINSEGDNVSLGQKQLLTIARAV 496
Cdd:TIGR03410 81 PQ------GreifprlTVEENLLTG-LAAL------PRRSRKIPDEIYELfPVLKEM-LGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
355-561 |
1.85e-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: 87.33 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 355 DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM---RFYDVTEGAIKIDGidtKKMNRSDVRSVFGMVLQDAWLY 431
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 432 KG-TIADNIRFGKLDATDYEVVDAAKTANVD-----HFIRTMPDGYEMEinsegdNVSLGQKQLLTIARAVISDPKILIL 505
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEdvllrDLALTRIGGNLVK------GISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 506 DEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAH--RLSTIREADLILVMKQGEIIEKG 561
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLArRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
358-576 |
2.51e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.53 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 358 KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDgidtkkmnRSdvrsvFGMVLQDAWLYKGTIAD 437
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--------RS-----IAYVPQQAWIMNATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 438 NIRFgkLDATDYE-VVDAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRL 516
Cdd:PTZ00243 740 NILF--FDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 517 -EALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELLeQGGFYEKL 576
Cdd:PTZ00243 818 gERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL 877
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
352-567 |
2.58e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 352 FSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGI------DTKKMNRSDVRSVFGMVL 425
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QDAWLYKG-TIADNIRFGKLDATDYEVVDAAKTanVDHFIRTMPDGYEM--EINSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:PRK14246 97 QQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVGLWKEVydRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELL 567
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
345-566 |
2.92e-19 |
|
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: 86.65 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRsDVRSVFGMV 424
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-EVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKG-TIADNIR-FGKLdatdYEVVDAAKTANVDHFIRTmpdgyeMEINSEGD----NVSLGQKQLLTIARAVIS 498
Cdd:cd03265 79 FQDLSVDDElTGWENLYiHARL----YGVPGAERRERIDELLDF------VGLLEAADrlvkTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 499 DPKILILDEATSSVD--TRLEA--LIQKAMDRvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:cd03265 149 RPEVLFLDEPTIGLDpqTRAHVweYIEKLKEE--FGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-567 |
3.13e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 88.12 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNR-SDVRSVFGM 423
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ--DAWLYKGTIADNIRFGK----LDATDyevvdaaktanvdhfIRTMPDGYEMEINSEG------DNVSLGQKQLLT 491
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGPenlcLPPIE---------------IRKRVDRALAEIGLEKyrhrspKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 492 IARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
19-302 |
3.59e-19 |
|
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: 88.27 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 19 RLTFYLVILFTILTVAFNAALPYLTGLPTTEIsrnIAAGESINFDYVIQCLIWILVVgtgYCVAQFLSGFLMTNVVQQSM 98
Cdd:cd18570 1 KKLLILILLLSLLITLLGIAGSFFFQILIDDI---IPSGDINLLNIISIGLILLYLF---QSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 99 RDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPL 178
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 179 SLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQM 258
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488301890 259 TAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-567 |
4.62e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 341 ILGSVEFENVSFSYDPEKpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVtEGAIKIDG--------IDTKKM 412
Cdd:PRK14258 4 LIPAIKVNNLSFYYDTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrveffnqnIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 413 NRSDVRSVFGMVLQDAWLYKGTIADNIRFG--------KLDATDYeVVDAAKTANvdhfirtMPDGYEMEINSEGDNVSL 484
Cdd:PRK14258 82 NLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEIDDI-VESALKDAD-------LWDEIKHKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVD----TRLEALIQKAmdRVMEGRTSFVIAHRLSTI-READLILVMKQ----- 554
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDpiasMKVESLIQSL--RLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenri 231
|
250
....*....|...
gi 488301890 555 GEIIEKGTHHELL 567
Cdd:PRK14258 232 GQLVEFGLTKKIF 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
344-577 |
6.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.53 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDP----EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGID----TKKMNRS 415
Cdd:PRK13646 2 TIRFDNVSYTYQKgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithkTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 DVRSVFGMVLQ--DAWLYKGTIADNIRFG-KLDATDYEVVDAaktanvDHFIRTMPDGYEMEINSEGD-NVSLGQKQLLT 491
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpKNFKMNLDEVKN------YAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM--EGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELLE 568
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
....*....
gi 488301890 569 QGGFYEKLY 577
Cdd:PRK13646 236 DKKKLADWH 244
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
345-569 |
9.34e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.78 E-value: 9.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMV 424
Cdd:PRK13652 4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQ--DAWLYKGTIADNIRFGKLD------ATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAV 496
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINlgldeeTVAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
344-569 |
4.55e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.65 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSdVRSVFGM 423
Cdd:PRK13536 41 AIDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL-ARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ-DAWLYKGTIADNI----RFGKLDATDYEVVdaakTANVDHFIRtmpdgYEMEINSEGDNVSLGQKQLLTIARAVIS 498
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLlvfgRYFGMSTREIEAV----IPSLLEFAR-----LESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 499 DPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
357-561 |
4.94e-18 |
|
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: 83.54 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRS---VFGMVLQDAWlyKG 433
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRigvVFGQKTQLWW--DL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 434 TIADNIRfgkLDATDYEVVDAAKTANVDHFIRTMPDGYEMeiNSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVD 513
Cdd:cd03267 111 PVIDSFY---LLAAIYDLPPARFKKRLDELSELLDLEELL--DTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 514 TRLEALIQKAMDRVMEGRTSFVI--AHRLSTI-READLILVMKQGEIIEKG 561
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLltSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
337-575 |
7.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.90 E-value: 7.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 337 LPEPILG--SVEFENVSFSYDPEKP----LIRNLNFKVDAGQMVAIVGPTGAGKTTLIN-----LLMRFYDVTEGAIKI- 404
Cdd:PRK13631 12 VPNPLSDdiILRVKNLYCVFDEKQEnelvALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 405 ---------DGIDTKKM-NRSDVRSVFGMVLQ--DAWLYKGTIADNIRFGKLdATDYEVVDAAKTANvdHFIRTMPDGYE 472
Cdd:PRK13631 92 dkknnheliTNPYSKKIkNFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAK--FYLNKMGLDDS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 473 -MEINSEGdnVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEA-LIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLI 549
Cdd:PRK13631 169 yLERSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEV 246
|
250 260
....*....|....*....|....*.
gi 488301890 550 LVMKQGEIIEKGTHHELLEQGGFYEK 575
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQHIINS 272
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
345-572 |
1.42e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPL----IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGI----DTKKMNRSD 416
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VRSVFGMVLQ--DAWLYKGTIADNIRFG------------KLDATDYEVVDAAKtanvdHFIRTMPdgYEMeinsegdnv 482
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqnfgipkekaeKIAAEKLEMVGLAD-----EFWEKSP--FEL--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 483 SLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEK 560
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISC 225
|
250
....*....|..
gi 488301890 561 GTHHELLEQGGF 572
Cdd:PRK13643 226 GTPSDVFQEVDF 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
332-569 |
1.46e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 332 EQDVPLPEPILgsvEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMrfydvteGAIKIDGidtkk 411
Cdd:COG0488 306 PPPERLGKKVL---ELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA-------GELEPDS----- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 412 mnrsdvrsvfGMVlqdawlykgTIADNIRFGKLDaTDYEVVDAAKTAnVDHFIRTMPDGYEMEINS-------EGDNV-- 482
Cdd:COG0488 370 ----------GTV---------KLGETVKIGYFD-QHQEELDPDKTV-LDELRDGAPGGTEQEVRGylgrflfSGDDAfk 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 483 -----SLGQKQLLTIARAVISDPKILILDEATSSVDTR-LEALIQkAMDRvMEGrTSFVIAH-R--LSTIreADLILVMK 553
Cdd:COG0488 429 pvgvlSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIEtLEALEE-ALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFE 503
|
250
....*....|....*..
gi 488301890 554 QGEIIEK-GTHHELLEQ 569
Cdd:COG0488 504 DGGVREYpGGYDDYLEK 520
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
336-568 |
1.78e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 83.32 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 336 PLPEPILgsvEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS 415
Cdd:PRK13537 2 PMSVAPI---DFRNVEKRYG-DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 dVRSVFGMVLQ-DAWLYKGTIADNIR-FGKldatdYEVVDAAKTAnvdhfiRTMPDGYEM-EINSEGD----NVSLGQKQ 488
Cdd:PRK13537 78 -ARQRVGVVPQfDNLDPDFTVRENLLvFGR-----YFGLSAAAAR------ALVPPLLEFaKLENKADakvgELSGGMKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 489 LLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHEL 566
Cdd:PRK13537 146 RLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHAL 225
|
..
gi 488301890 567 LE 568
Cdd:PRK13537 226 IE 227
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
363-561 |
2.46e-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: 80.80 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDA-GQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG---IDT-KKMNRSDVRSVFGMVLQDAWLYKG-TIA 436
Cdd:cd03297 14 TLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFPHlNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 DNIRFG---KLDATDYEVVDAAKTA-NVDHFIRTMPDGyemeinsegdnVSLGQKQLLTIARAVISDPKILILDEATSSV 512
Cdd:cd03297 94 ENLAFGlkrKRNREDRISVDELLDLlGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488301890 513 DTRLEALIQKAMDRVME--GRTSFVIAHRLSTI-READLILVMKQGEIIEKG 561
Cdd:cd03297 163 DRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
13-289 |
3.51e-17 |
|
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: 82.88 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 13 RYIKPYRLTFYLVILFTILTVAFNAALPYLTG-------LPTTEISRniaagESINFdyviQCLIWiLVVGTGYCVAQFL 85
Cdd:cd18578 2 KLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSklisvfsLPDDDELR-----SEANF----WALMF-LVLAIVAGIAYFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 86 SGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFD--KNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFL 163
Cdd:cd18578 72 QGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 164 INPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGF 243
Cdd:cd18578 152 YGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGL 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488301890 244 KASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQ-LQAFI 289
Cdd:cd18578 232 RRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQfFIVFM 278
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
363-569 |
4.11e-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: 84.35 E-value: 4.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDvTEGAIKIDGIDTKKMNRSD---VRSVFGMVLQDAWlykG------ 433
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQDPF---Gslsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 434 TIADNIRFG------KLDATDYE--VVDAAKTANVDhfiRTMPDGYEMEinsegdnVSLGQKQLLTIARAVISDPKILIL 505
Cdd:COG4172 380 TVGQIIAEGlrvhgpGLSAAERRarVAEALEEVGLD---PAARHRYPHE-------FSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 506 DEATSSVDtrleALIQKamdRVME---------GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:COG4172 450 DEPTSALD----VSVQA---QILDllrdlqrehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
346-577 |
5.73e-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: 5.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF--YDVTEGAIKIDGIDTKKMNrSDVRSVFGM 423
Cdd:cd03217 2 EIKDLHVSVG-GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLqdAWLYKGTIADnirfgkldatdyevvdaaktANVDHFIRTMPDGYemeinsegdnvSLGQKQLLTIARAVISDPKIL 503
Cdd:cd03217 80 FL--AFQYPPEIPG--------------------VKNADFLRYVNEGF-----------SGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 504 ILDEATSSVDtrLEAL--IQKAMDRVMEGRTSF-VIAH--RLSTIREADLILVMKQGEIIEKGThHELLEQggFYEKLY 577
Cdd:cd03217 127 ILDEPDSGLD--IDALrlVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE--IEKKGY 200
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
345-555 |
5.81e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 5.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSV-FGM 423
Cdd:PRK09700 6 ISMAGIGKSFGPVHAL-KSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQD-AWLYKGTIADNIRFGKLDATDY---EVVDAAKTANVDHFIrTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISD 499
Cdd:PRK09700 85 IYQElSVIDELTVLENLYIGRHLTKKVcgvNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 500 PKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRE-ADLILVMKQG 555
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
348-567 |
8.31e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.01 E-value: 8.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDPekpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGMVLQD 427
Cdd:PRK10771 5 TDITWLYHH---LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR-RPV-SMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 AWLYKG-TIADNIRFG-----KLDATDYE-VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAVISDP 500
Cdd:PRK10771 80 NNLFSHlTVAQNIGLGlnpglKLNAAQREkLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGR--TSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-539 |
2.08e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 76.81 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtkkmnrsDVRSVFgmV 424
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE---------GEDLLF--L 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKGTIADNIRFgkldatdyevvdaaktanvdhfirtmPdgyemeinsEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03223 70 PQRPYLPLGTLREQLIY--------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*.
gi 488301890 505 LDEATSSVDTRLEALIqkaMDRVMEGRTSFV-IAHR 539
Cdd:cd03223 115 LDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
348-568 |
3.57e-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: 77.97 E-value: 3.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNrSDVRSVFGMVL-- 425
Cdd:cd03218 4 ENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP-MHKRARLGIGYlp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QDAWLYKG-TIADNIRfgkLDATDYEVVDAAKTANVDHFIRtmpdgyEMEI----NSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:cd03218 82 QEASIFRKlTVEENIL---AVLEIRGLSKKEREEKLEELLE------EFHIthlrKSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA-HRLS-TIREADLILVMKQGEIIEKGTHHELLE 568
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
343-555 |
3.78e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.78 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKI-DGIDTkkmnrsdvrsvf 421
Cdd:COG4178 361 GALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV------------ 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 gMVL-QDAWLYKGTIADNIRF--GKLDATDYEVVDAAKTANVDHFIrtmpDGYEMEINSegDNV-SLGQKQLLTIARAVI 497
Cdd:COG4178 429 -LFLpQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLA----ERLDEEADW--DQVlSLGEQQRLAFARLLL 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVMKQG 555
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
365-566 |
5.03e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 79.37 E-value: 5.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 365 NFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN---RSDVRSVFGMVLQD--AWLY-KGTIADN 438
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKddeWRAVRSDIQMIFQDplASLNpRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 439 I----RFGKLDATDYEVVDAAKTANVDhfIRTMPDgyemEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDT 514
Cdd:PRK15079 121 IaeplRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 515 RLEALI---QKAMDRVMeGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK15079 195 SIQAQVvnlLQQLQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
361-561 |
6.60e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 6.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAWLYKGTIADNI- 439
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLVEDVVm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 440 --RFGKL------DATDYEVVDAAkTANVDhfirtMPDGYEMEINSegdnVSLGQKQLLTIARAVISDPKILILDEATSS 511
Cdd:PRK15056 103 mgRYGHMgwlrraKKRDRQIVTAA-LARVD-----MVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 512 VDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIREADLILVMKQGEIIEKG 561
Cdd:PRK15056 173 VDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
356-578 |
9.21e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.48 E-value: 9.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 356 PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMrFYDVT----EGAIKIDGidtKKMNRSDVRSVFGMVLQDawly 431
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQD---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 432 kgtiadNIRFGKLDATDYEVVDA-----------AKTANVDHFIRTMP--DGYEMEINSEGD--NVSLGQKQLLTIARAV 496
Cdd:TIGR00955 108 ------DLFIPTLTVREHLMFQAhlrmprrvtkkEKRERVDEVLQALGlrKCANTRIGVPGRvkGLSGGERKRLAFASEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 497 ISDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLST--IREADLILVMKQGEIIEKGTHHEL---LEQG 570
Cdd:TIGR00955 182 LTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAvpfFSDL 261
|
....*....
gi 488301890 571 GFY-EKLYN 578
Cdd:TIGR00955 262 GHPcPENYN 270
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
366-569 |
1.32e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 78.08 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 366 FKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV---RSVFGMVLQDAWlykGTIADNIRFG 442
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQkllRQKIQIVFQNPY---GSLNPRKKVG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 443 -----------KLDAtdyevvdAAKTANVDHFIRTM---PDGYE----MeinsegdnVSLGQKQLLTIARAVISDPKILI 504
Cdd:PRK11308 113 qileepllintSLSA-------AERREKALAMMAKVglrPEHYDryphM--------FSGGQRQRIAIARALMLDPDVVV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 505 LDEATSSVDTRLEA-LIQKAMDRVMEGRTSFV-IAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK11308 178 ADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
362-558 |
1.34e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 362 RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSD----VRSVFGMVLQDAWLYKG-TIA 436
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 DNIRFGkLDATDYEVVDAAKTANVdhfIRTMPDGYEMEINSE---GDnVSLGQKQLLTIARAVISDPKILILDEATsSVD 513
Cdd:COG3845 99 ENIVLG-LEPTKGGRLDRKAARAR---IRELSERYGLDVDPDakvED-LSVGEQQRVEILKALYRGARILILDEPT-AVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488301890 514 TRLEA--LIqKAMDR-VMEGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:COG3845 173 TPQEAdeLF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKVV 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-568 |
1.62e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.80 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVT-----EGAIKIDGID--TKKMNRSD 416
Cdd:PRK14267 4 AIETVNLRVYYG-SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiySPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VRSVFGMVLQDAWLYKG-TIADNIRFG-KL-------DATDYEVVDAAKTAnvdhfirTMPDGYEMEINSEGDNVSLGQK 487
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHlTIYDNVAIGvKLnglvkskKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHR-LSTIREADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKV 235
|
..
gi 488301890 567 LE 568
Cdd:PRK14267 236 FE 237
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
348-562 |
1.83e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQD 427
Cdd:PRK13548 6 RNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 AWL-YKGTIADNIRFGKLD-----ATDYEVVDAA-KTANVDHF----IRTMpdgyemeinsegdnvSLGQKQLLTIARA- 495
Cdd:PRK13548 85 SSLsFPFTVEEVVAMGRAPhglsrAEDDALVAAAlAQVDLAHLagrdYPQL---------------SGGEQQRVQLARVl 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 496 -----VISDPKILILDEATSSVDTR-----LEALIQKAMDRvmeGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGT 562
Cdd:PRK13548 150 aqlwePDGPPRWLLLDEPTSALDLAhqhhvLRLARQLAHER---GLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
344-580 |
1.88e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.27 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSY---------------------DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAI 402
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 403 KIDGidtkkmnrsDVRSVFGMvlqdawlykGTI-------ADNIRFG-------------KLDatdyEVVDaakTANVDH 462
Cdd:COG1134 84 EVNG---------RVSALLEL---------GAGfhpeltgRENIYLNgrllglsrkeideKFD----EIVE---FAELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 463 FI----RTmpdgYemeinsegdnvSLGQKQLLTIARAVISDPKILILDEATSSVDtrlEALIQKAMDRVME----GRTSF 534
Cdd:COG1134 139 FIdqpvKT----Y-----------SSGMRARLAFAVATAVDPDILLVDEVLAVGD---AAFQKKCLARIRElresGRTVI 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488301890 535 VIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEqggFYEKLYNSQ 580
Cdd:COG1134 201 FVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGR 244
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
363-566 |
2.47e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKID-----GIDTKKMNRSDVRSVFgmvlQDAWLYKG-TIA 436
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRgqhieGLPGHQIARMGVVRTF----QHVRLFREmTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 DNIR-----------FGKLDAT-DYEVVDAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:PRK11300 99 ENLLvaqhqqlktglFSGLLKTpAFRRAESEALDRAATWLERV--GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 505 LDEATSSVDTR----LEALIQKAmdRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK11300 177 LDEPAAGLNPKetkeLDELIAEL--RNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
345-566 |
2.88e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.60 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIR----NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKI--DGIDTKKMNRS--D 416
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgeRVITAGKKNKKlkP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 417 VRSVFGMVLQ--DAWLYKGTIADNIRFGKLDATDYEvVDAAKTAnvdhfiRTMPD--GYEMEINSEGD-NVSLGQKQLLT 491
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKA------REMIElvGLPEELLARSPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVDTRLealiQKAMdrvME---------GRTSFVIAHRLSTI-READLILVMKQGEIIEKG 561
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKG----RKEM---MEmfyklhkekGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
|
....*
gi 488301890 562 THHEL 566
Cdd:PRK13634 229 TPREI 233
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
357-524 |
3.30e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.53 E-value: 3.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRSVFGmvlqdawlYKG--- 433
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACH--------YLGhrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 434 ------TIADNIRF--GKLDATDYEVVDAAKTANVDHfIRTMPDGYemeinsegdnVSLGQKQLLTIARAVISDPKILIL 505
Cdd:PRK13539 83 amkpalTVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170
....*....|....*....
gi 488301890 506 DEATSSVDTRLEALIQKAM 524
Cdd:PRK13539 152 DEPTAALDAAAVALFAELI 170
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
345-561 |
3.32e-15 |
|
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: 74.88 E-value: 3.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSY---------------------DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIK 403
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 404 IDGidtkkmnrsDVRSVFGmvLQDAWLYKGTIADNIRF-----GKLDATDYEVVDaaktanvdhFIrtmpdgYEMeinSE 478
Cdd:cd03220 81 VRG---------RVSSLLG--LGGGFNPELTGRENIYLngrllGLSRKEIDEKID---------EI------IEF---SE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 479 -GD-------NVSLGQKQLLTIARAVISDPKILILDEATSSVDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRE- 545
Cdd:cd03220 132 lGDfidlpvkTYSSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRl 208
|
250
....*....|....*.
gi 488301890 546 ADLILVMKQGEIIEKG 561
Cdd:cd03220 209 CDRALVLEKGKIRFDG 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
339-566 |
3.67e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 75.58 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 339 EPILgsvEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDV-----TEGAIKIDG--IDTKK 411
Cdd:PRK14239 3 EPIL---QVSDLSVYYNKKKAL-NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGhnIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 412 MNRSDVRSVFGMVLQDAWLYKGTIADNIRFG-KLDAT-DYEVVDAA-----KTANVdhfirtmPDGYEMEINSEGDNVSL 484
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFPMSIYENVVYGlRLKGIkDKQVLDEAvekslKGASI-------WDEVKDRLHDSALGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLSTI-READLILVMKQGEIIEKGTH 563
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDT 231
|
...
gi 488301890 564 HEL 566
Cdd:PRK14239 232 KQM 234
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
346-551 |
4.02e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 75.51 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRsdvrsvfGM 423
Cdd:PRK11248 3 QISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpVEGPGAER-------GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ-DAWLYKGTIADNIRFG----KLDATDYEVVDAAKTANVD------HFIRTMpdgyemeinsegdnvSLGQKQLLTI 492
Cdd:PRK11248 75 VFQnEGLLPWRNVQDNVAFGlqlaGVEKMQRLEIAHQMLKKVGlegaekRYIWQL---------------SGGQRQRVGI 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 493 ARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHrlsTIREA-----DLILV 551
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH---DIEEAvfmatELVLL 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
335-568 |
6.38e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 76.80 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 335 VPLPEPILGSV-----EFENVSFSYDPEkPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDT 409
Cdd:PRK11607 5 IPRPQAKTRKAltpllEIRNLTKSFDGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 410 KKMnrSDVRSVFGMVLQDAWLYKG-TIADNIRFG----KL--DATDYEVVDAAKTANVDHFIRTMPdgyemeinsegDNV 482
Cdd:PRK11607 84 SHV--PPYQRPINMMFQSYALFPHmTVEQNIAFGlkqdKLpkAEIASRVNEMLGLVHMQEFAKRKP-----------HQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 483 SLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAH-RLSTIREADLILVMKQGEIIE 559
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQ 230
|
....*....
gi 488301890 560 KGTHHELLE 568
Cdd:PRK11607 231 IGEPEEIYE 239
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
343-567 |
6.63e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 75.43 E-value: 6.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 343 GSVEFENVSFSYDPEKPL----IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYdVTEGAIKIDG-----IDTKKMN 413
Cdd:PRK13645 5 KDIILDNVSYTYAKKTPFefkaLNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLI-ISETGQTIVGdyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 414 R-SDVRSVFGMVLQ--DAWLYKGTIADNIRFGKLDATDYEVVDAAKTANVDHFIrTMPDGYEMEINSEgdnVSLGQKQLL 490
Cdd:PRK13645 84 EvKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDYVKRSPFE---LSGGQKRRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 491 TIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTI-READLILVMKQGEIIEKGTHHELL 567
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
356-559 |
8.84e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 74.72 E-value: 8.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 356 PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFG---MVLQD---AW 429
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRdiqMVFQDsisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 LYKGTIADNIRFGKLDATDYEvvDAAKTANVDHFIRTMpdGYEMEINSE-GDNVSLGQKQLLTIARAVISDPKILILDEA 508
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLD--KAERLARASEMLRAV--DLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488301890 509 TSSVDTRLEA-LIQKAMDRVMEGRTSFV-IAHRLSTI-READLILVMKQGEIIE 559
Cdd:PRK10419 179 VSNLDLVLQAgVIRLLKKLQQQFGTACLfITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
348-570 |
9.12e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN-RSDVRSVF----- 421
Cdd:PRK11231 6 ENLTVGYG-TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSsRQLARRLAllpqh 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 -----GMVLQDAWLYkGTIADNIRFGKLDATDYEVVDAA--KTaNVDHFirtmpdgyemeINSEGDNVSLGQKQLLTIAR 494
Cdd:PRK11231 85 hltpeGITVRELVAY-GRSPWLSLWGRLSAEDNARVNQAmeQT-RINHL-----------ADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 495 AVISDPKILILDEATSSVDTRLEALIQKAMdRVM--EGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELLEQG 570
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLM-RELntQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
364-567 |
1.04e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.02 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 364 LNFKVDAGQMVAIVGPTGAGKTTL---INLLMRFYD--VTEGAIKIDGIDTKKMNRSDVRSV---FGMVLQDAWLY-KGT 434
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQPEAgtIRVGDITIDTARSLSQQKGLIRQLrqhVGFVFQNFNLFpHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 435 IADNIRFGKLdATDYEVVDAAKTANVDHFIRTMPDGYEmeiNSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDT 514
Cdd:PRK11264 102 VLENIIEGPV-IVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 515 RL--EALiqkAMDRVM--EGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK11264 178 ELvgEVL---NTIRQLaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALF 232
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
316-562 |
1.13e-14 |
|
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: 77.75 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 316 TMRIFEILDEPE--EELN----EQDVPLPEPilgSVEFENVSFSYDPE-KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLI 388
Cdd:TIGR01257 897 TEPLTEEMEDPEhpEGINdsffERELPGLVP---GVCVKNLVKIFEPSgRPAVDRLNITFYENQITAFLGHNGAGKTTTL 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 389 NLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMVLQDAWLYKG-TIADNIRF-GKLDATDYEVVDAAKTANVDHfirt 466
Cdd:TIGR01257 974 SILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFyAQLKGRSWEEAQLEMEAMLED---- 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 467 mpDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRLStirEA 546
Cdd:TIGR01257 1049 --TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EA 1123
|
250 260
....*....|....*....|
gi 488301890 547 DL----ILVMKQGEIIEKGT 562
Cdd:TIGR01257 1124 DLlgdrIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
26-303 |
2.02e-14 |
|
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: 74.21 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTGLPTTEISRNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRDI 105
Cdd:cd18780 2 TIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 106 EEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRT 185
Cdd:cd18780 82 FSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 186 IVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGF-KQVNHRLnGFGFKASFISGLMLPLVQMTAYGTY 264
Cdd:cd18780 162 YGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYsEKINESY-LLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 488301890 265 IGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLS 279
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
336-561 |
2.17e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 336 PLPEPILgSVEfeNVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG-----IDTK 410
Cdd:PRK11701 1 MMDQPLL-SVR--GLTKLYGPRKGC-RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 411 KMNRSDVRSVF----GMVLQDAwlykgtiADNIRFGkldatdyevVDAAktANVDHfiRTMPDG---Y------------ 471
Cdd:PRK11701 77 ALSEAERRRLLrtewGFVHQHP-------RDGLRMQ---------VSAG--GNIGE--RLMAVGarhYgdiratagdwle 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 472 EMEINSEG-DNV----SLGQKQLLTIARAVISDPKILILDEATS----SVDTRLEALIQKAmdrVMEGRTSFVI-AHRLS 541
Cdd:PRK11701 137 RVEIDAARiDDLpttfSGGMQQRLQIARNLVTHPRLVFMDEPTGgldvSVQARLLDLLRGL---VRELGLAVVIvTHDLA 213
|
250 260
....*....|....*....|.
gi 488301890 542 TIRE-ADLILVMKQGEIIEKG 561
Cdd:PRK11701 214 VARLlAHRLLVMKQGRVVESG 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
345-567 |
2.74e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.73 E-value: 2.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRSDVRSVFG 422
Cdd:PRK13636 6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 MVLQ--DAWLYKGTIADNIRFGKL------DATDYEVVDAAKTANVDHfIRTMPDGYemeinsegdnVSLGQKQLLTIAR 494
Cdd:PRK13636 86 MVFQdpDNQLFSASVYQDVSFGAVnlklpeDEVRKRVDNALKRTGIEH-LKDKPTHC----------LSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 495 AVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIR-EADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
350-567 |
2.77e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.88 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 350 VSFSydpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAW 429
Cdd:PRK09536 11 VEFG---DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 LY----------KGTIADNIRFGKLDATDYEVVDAA-KTANVDHFirtmpdgyemeINSEGDNVSLGQKQLLTIARAVIS 498
Cdd:PRK09536 88 LSfefdvrqvveMGRTPHRSRFDTWTETDRAAVERAmERTGVAQF-----------ADRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488301890 499 DPKILILDEATSSVD----TRLEALIQKAMDrvmEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK09536 157 ATPVLLLDEPTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
331-539 |
3.37e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.91 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 331 NEQDVPLPEPILGSVEFENVSFSyDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDgidtk 410
Cdd:COG2401 17 YSSVLDLSERVAIVLEAFGVELR-VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 411 kmnrsdvrsvfgmVLQDAWLYKGTIADNI--RFGKLDATdyEVVDAAKTANVDHFIRTMpdgyemeinsegDNVSLGQKQ 488
Cdd:COG2401 91 -------------VPDNQFGREASLIDAIgrKGDFKDAV--ELLNAVGLSDAVLWLRRF------------KELSTGQKF 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488301890 489 LLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIA-HR 539
Cdd:COG2401 144 RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArRAGITLVVAtHH 196
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
318-569 |
4.19e-14 |
|
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: 74.84 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 318 RIFEILDEPEEElneQDVPLPEPILgsvEFENVSFSY-DPEKPLIR---NLNFKVDAGQMVAIVGPTGAGKTTLINLLMR 393
Cdd:TIGR03269 259 VFMEGVSEVEKE---CEVEVGEPII---KVRNVSKRYiSVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAG 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 394 FYDVTEGAIKI----DGID-TKK--MNRSDVRSVFGMVLQDAWLY-KGTIADNIRfgklDATDYEVVDAAKTANVDHFIR 465
Cdd:TIGR03269 333 VLEPTSGEVNVrvgdEWVDmTKPgpDGRGRAKRYIGILHQEYDLYpHRTVLDNLT----EAIGLELPDELARMKAVITLK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 466 TMpdGYEME-----INSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVD--TRLEAL--IQKAmdRVMEGRTSFVI 536
Cdd:TIGR03269 409 MV--GFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpiTKVDVThsILKA--REEMEQTFIIV 484
|
250 260 270
....*....|....*....|....*....|....
gi 488301890 537 AHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:TIGR03269 485 SHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
361-540 |
4.79e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.51 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAiKIDG--------IDTKKMNRSDVRSVFGMVLQDAWLYK 432
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGF-RVEGkvtfhgknLYAPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 433 GTIADNIRFG--------KLDatdyEVVDAAKTANVdhfirtMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:PRK14243 105 KSIYDNIAYGaringykgDMD----ELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 488301890 505 LDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHRL 540
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
25-303 |
6.25e-14 |
|
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: 72.59 E-value: 6.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 25 VILFTILTVAFNAALPYLTGLptteISRNIAAGESINFDYVIqcLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRD 104
Cdd:cd18568 7 ILLASLLLQLLGLALPLFTQI----ILDRVLVHKNISLLNLI--LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 105 IEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIP----LSL 180
Cdd:cd18568 81 FYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPlyvlLTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IISRTIVKISQKYFQgmqnSLGDLNGYVQENMTGFSVLKLYGREKETL----EGF-KQVNHRLNG--FGFKASFISGLML 253
Cdd:cd18568 160 LSSPKLKRNSREIFQ----ANAEQQSFLVEALTGIATIKALAAERPIRwrweNKFaKALNTRFRGqkLSIVLQLISSLIN 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488301890 254 PLvqmtaygTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18568 236 HL-------GTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALV 278
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
328-566 |
6.57e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 328 EELNEQDVPlpepilgSVEFENVSFSYD-PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG 406
Cdd:PRK10261 5 DELDARDVL-------AVENLNIAFMQEqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 407 IDTKKMNR----------SDVRSVFG----MVLQD-------AWLYKGTIADNIRFGKLDATDYEVVDAAKTANVdhfIR 465
Cdd:PRK10261 78 MLLRRRSRqvielseqsaAQMRHVRGadmaMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQ---VR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 466 tMPDGYEMeINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQ---KAMDRVMEGRTSFvIAHRLST 542
Cdd:PRK10261 155 -IPEAQTI-LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMSMGVIF-ITHDMGV 231
|
250 260
....*....|....*....|....*
gi 488301890 543 IRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK10261 232 VAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
344-564 |
7.36e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 7.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPEKPLIrNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--------IDTKKMN-- 413
Cdd:PRK11124 2 SIQLNGINCFYGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 414 RSDVrsvfGMVLQDAWLYKG-TIADN-----IRFGKLDAtdyevvDAAKTANVDHFIR----TMPDGYEMEInsegdnvS 483
Cdd:PRK11124 81 RRNV----GMVFQQYNLWPHlTVQQNlieapCRVLGLSK------DQALARAEKLLERlrlkPYADRFPLHL-------S 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 484 LGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQG 223
|
...
gi 488301890 562 THH 564
Cdd:PRK11124 224 DAS 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
357-524 |
8.57e-14 |
|
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: 70.21 E-value: 8.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAwlYKGTIA 436
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPG--IKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 --DNIRFGKLDATDYEVVDAAKTANVDHFiRTMPDGYemeinsegdnVSLGQKQLLTIARAVISDPKILILDEATSSVDT 514
Cdd:cd03231 90 vlENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170
....*....|
gi 488301890 515 RLEALIQKAM 524
Cdd:cd03231 159 AGVARFAEAM 168
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
357-567 |
9.59e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 9.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSD-------------VRSVFGM 423
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQ--DAWLYKgTIADNIrfgkLDATdYEVVDAAKTANVDHFIRTMpDGYEMEINSEGD---NVSLGQKQLLTIARAVIS 498
Cdd:PRK10619 97 VFQhfNLWSHM-TVLENV----MEAP-IQVLGLSKQEARERAVKYL-AKVGIDERAQGKypvHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 499 DPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
335-561 |
1.63e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 335 VPLPEPILGSVEFENVSFSYDPEKPLIR----------NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDvTEGAIKI 404
Cdd:PRK15134 266 VPLPEPASPLLDVEQLQVAFPIRKGILKrtvdhnvvvkNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 405 DGIDTKKMNRSD---VRSVFGMVLQDAWL-------YKGTIADNIRFGK--LDATDYE--VVDAAKTANVDHFIRTMpdg 470
Cdd:PRK15134 345 DGQPLHNLNRRQllpVRHRIQVVFQDPNSslnprlnVLQIIEEGLRVHQptLSAAQREqqVIAVMEEVGLDPETRHR--- 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 471 YEMEInsegdnvSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEG-RTSFV-IAHRLSTIRE-AD 547
Cdd:PRK15134 422 YPAEF-------SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLfISHDLHVVRAlCH 494
|
250
....*....|....
gi 488301890 548 LILVMKQGEIIEKG 561
Cdd:PRK15134 495 QVIVLRQGEVVEQG 508
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
332-559 |
2.00e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 332 EQDVPLPEPILG--SVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDT 409
Cdd:PRK10522 308 KAEFPRPQAFPDwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 410 KKMNRSDVRSVFGMVLQDAWLykgtiadnirFGKLDATDYEVVDAAKtanVDHFIRT--MPDGYEMEINSEGD-NVSLGQ 486
Cdd:PRK10522 388 TAEQPEDYRKLFSAVFTDFHL----------FDQLLGPEGKPANPAL---VEKWLERlkMAHKLELEDGRISNlKLSKGQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 487 KQLLTIARAVISDPKILILDEATSSVD--------TRLEALIQKAmdrvmeGRTSFVIAHRLSTIREADLILVMKQGEII 558
Cdd:PRK10522 455 KKRLALLLALAEERDILLLDEWAADQDphfrrefyQVLLPLLQEM------GKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
.
gi 488301890 559 E 559
Cdd:PRK10522 529 E 529
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
20-238 |
2.05e-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: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 20 LTFYLVILFTILTVAFNAALPYLTglptteiSRNIAAGESINFDYVIqclIWILVVGTGYCVAQFLSGFLMTNVVQQSMR 99
Cdd:cd18580 3 LLLLLLLLLAFLSQFSNIWLDWWS-------SDWSSSPNSSSGYYLG---VYAALLVLASVLLVLLRWLLFVLAGLRASR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLS 179
Cdd:cd18580 73 RLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVY 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 180 LIISRTIVKISQ--KYFQGMQNSlgDLNGYVQENMTGFSVLKLYGREKEtlegFKQVNHRL 238
Cdd:cd18580 153 YLLQRYYLRTSRqlRRLESESRS--PLYSHFSETLSGLSTIRAFGWQER----FIEENLRL 207
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
345-572 |
2.08e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPL----IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS----- 415
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 -------------------DVRSVFGMVLQDA--WLYKGTIADNIRFGKLD-ATDYEvvDAAKTANVDHFIRTMPDGYem 473
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmGVSKE--EAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 474 eINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLSTIRE-ADLILV 551
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEwTKRTIF 237
|
250 260
....*....|....*....|.
gi 488301890 552 MKQGEIIEKGTHHELLEQGGF 572
Cdd:PRK13651 238 FKDGKIIKDGDTYDILSDNKF 258
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
365-567 |
2.58e-13 |
|
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: 71.67 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 365 NFKVDAGQMVAIVGPTGAGKTTLINL---LMRfydVTEGAIKIDG---IDTKKmnRSDV----RSVfGMVLQDAWL---Y 431
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQDSAR--GIFLpphrRRI-GYVFQEARLfphL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 432 kgTIADNIRFG-----------KLDatdyEVVDaakTANVDHFIRTMPDgyemeinsegdNVSLGQKQLLTIARAVISDP 500
Cdd:COG4148 93 --SVRGNLLYGrkrapraerriSFD----EVVE---LLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 501 KILILDEATSSVDTR--------LEALIQK----------AMDRVMegrtsfviahRLstireADLILVMKQGEIIEKGT 562
Cdd:COG4148 153 RLLLMDEPLAALDLArkaeilpyLERLRDEldipilyvshSLDEVA----------RL-----ADHVVLLEQGRVVASGP 217
|
....*
gi 488301890 563 HHELL 567
Cdd:COG4148 218 LAEVL 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
360-569 |
2.67e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 69.94 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 360 LIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDV-----TEGAIKIDGIDTKKMNRSDVRSVFGMVLQ-DAWLYKG 433
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 434 TIADNIRFG----KLDATDYEVVDAAKTANVDhfiRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEAT 509
Cdd:PRK14247 98 SIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 510 SSVDTRLEALIQKAMDRVMEGRTSFVIAH-RLSTIREADLILVMKQGEIIEKGT--------HHELLEQ 569
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPtrevftnpRHELTEK 243
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
99-288 |
2.78e-13 |
|
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: 70.70 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 99 RDLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPL 178
Cdd:cd18782 75 LELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 179 SLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEgfkQVNHRLNGF---GFKASFISGLMLPL 255
Cdd:cd18782 154 QLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARW---RWQNRYARSlgeGFKLTVLGTTSGSL 230
|
170 180 190
....*....|....*....|....*....|...
gi 488301890 256 VQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAF 288
Cdd:cd18782 231 SQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAF 263
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
347-509 |
3.63e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 347 FENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIdgidtkkmnRSDVRsvFGMVLQ 426
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI---------PKGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 427 DAWLYKG-TIADNIR--FGKLDA--TDYEVV---------DAAKTANVDHFIRTMpDGYEMEINSEG------------- 479
Cdd:COG0488 69 EPPLDDDlTVLDTVLdgDAELRAleAELEELeaklaepdeDLERLAELQEEFEAL-GGWEAEARAEEilsglgfpeedld 147
|
170 180 190
....*....|....*....|....*....|...
gi 488301890 480 ---DNVSLGQKQLLTIARAVISDPKILILDEAT 509
Cdd:COG0488 148 rpvSELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
348-557 |
4.11e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.71 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIkIDGIDTKKMNRSDVRsvfgMVLQD 427
Cdd:PRK11247 16 NAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTR----LMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 AWL--YKGTIaDNIRFG-----KLDATD-YEVVDAAKTANvdhfirTMPDGyemeinsegdnVSLGQKQLLTIARAVISD 499
Cdd:PRK11247 90 ARLlpWKKVI-DNVGLGlkgqwRDAALQaLAAVGLADRAN------EWPAA-----------LSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 500 PKILILDEATSSVD--TRLEalIQKAMDRVME--GRTSFVIAHRLS-TIREADLILVMKQGEI 557
Cdd:PRK11247 152 PGLLLLDEPLGALDalTRIE--MQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-569 |
5.36e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 71.48 E-value: 5.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSDVRSVFG--- 422
Cdd:PRK11288 6 SFDGIGKTFPGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAALAagv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 423 -MVLQDAWLY-KGTIADNIRFGKLDATdYEVVDAaKTANvdHFIRTMPDGYEMEINSEG--DNVSLGQKQLLTIARAVIS 498
Cdd:PRK11288 82 aIIYQELHLVpEMTVAENLYLGQLPHK-GGIVNR-RLLN--YEAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 499 DPKILILDEATSSVDTR----LEALIQKAMDrvmEGRTSFVIAHRLSTI-READLILVMKQGEIIEkgtHHELLEQ 569
Cdd:PRK11288 158 NARVIAFDEPTSSLSAReieqLFRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVA---TFDDMAQ 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
359-526 |
6.05e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 68.61 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 359 PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIkidgidtkkmnrsDVRSVFGMVlqdawlykgTIADn 438
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-------------LVRHDGGWV---------DLAQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 439 irfgkldATDYEVVDAAKTA--NVDHFIRTMP--------------DGYEMEINSE--GD-----NV------------S 483
Cdd:COG4778 82 -------ASPREILALRRRTigYVSQFLRVIPrvsaldvvaeplleRGVDREEARAraREllarlNLperlwdlppatfS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488301890 484 LGQKQLLTIARAVISDPKILILDEATSSVDT----RLEALIQKAMDR 526
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAanraVVVELIEEAKAR 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
344-569 |
6.18e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.26 E-value: 6.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDvRSVfGM 423
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RDI-AM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIRFG----KLDATDYE--VVDAAKTANVDHFIRTMPdgyemeinsegDNVSLGQKQLLTIARAV 496
Cdd:PRK11650 81 VFQNYALYPHmSVRENMAYGlkirGMPKAEIEerVAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 497 ISDPKILILDEATSSVDT------RLEalIQKAMDRVmeGRTSFVIAH-RLSTIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrvqmRLE--IQRLHRRL--KTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
345-568 |
6.75e-13 |
|
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: 71.37 E-value: 6.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLL--MRFYDVTEGAI-------------------- 402
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVL-KNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 403 -------------KIDGIDTKKMNRSDVRSVFGMVLQDAW-LY-KGTIADNIrFGKLDATDYEVVDAAKTA-------NV 460
Cdd:TIGR03269 80 epcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFaLYgDDTVLDNV-LEALEEIGYEGKEAVGRAvdliemvQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 461 DHFIrtmpdgyeMEINSEgdnVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHR 539
Cdd:TIGR03269 159 SHRI--------THIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 488301890 540 LSTIRE--ADLILVMKQGEIIEKGTHHELLE 568
Cdd:TIGR03269 228 WPEVIEdlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
361-583 |
7.48e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 7.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQDAwlyKGTIADNIR 440
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 441 FGKLdatdyevVDAAKTANVDhfirTMPDGYEMEINSEGDNVSL--------------GQKQLLTIARAVISDPKILILD 506
Cdd:PRK15112 106 ISQI-------LDFPLRLNTD----LEPEQREKQIIETLRQVGLlpdhasyyphmlapGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 507 EATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE--QGGFYEKLYNSQF 581
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEkqGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLAspLHELTKRLIAGHF 254
|
..
gi 488301890 582 AE 583
Cdd:PRK15112 255 GE 256
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
345-567 |
9.07e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGID-----TKKMNRSDV-- 417
Cdd:PRK11614 6 LSFDKVSAHYGKIQAL-HEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwqTAKIMREAVai 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 ----RSVFG-MVLQDAWLYKGTIADNIRFGKLDATDYEVvdaaktanvdhfirtMPDGYEMEINSEGdNVSLGQKQLLTI 492
Cdd:PRK11614 85 vpegRRVFSrMTVEENLAMGGFFAERDQFQERIKWVYEL---------------FPRLHERRIQRAG-TMSGGEQQMLAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 493 ARAVISDPKILILDEATSSVdtrLEALIQKAMDRVM----EGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
19-288 |
1.67e-12 |
|
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: 68.31 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 19 RLTFYLVILFTILTVAFNAALPYLTGLPTTEIsrnIAAGESINFDYVIqclIWILVVGTGYCVAQFLSGFLMTnVVQQSM 98
Cdd:cd18555 1 KKLLISILLLSLLLQLLTLLIPILTQYVIDNV---IVPGNLNLLNVLG---IGILILFLLYGLFSFLRGYIII-KLQTKL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 99 -RDLRRDIEEKINRLPVSYFDKNQQGNILSRvtndvdAVSNAMQQSFI--NIVSAVLGIVMAVV---MMFLINPLMA--- 169
Cdd:cd18555 74 dKSLMSDFFEHLLKLPYSFFENRSSGDLLFR------ANSNVYIRQILsnQVISLIIDLLLLVIyliYMLYYSPLLTliv 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 170 -IFSVIMIPLSLIISRTIVKISQKYFQgmqnSLGDLNGYVQENMTGFSVLKLYGREKET-----------LEGFKQVNHR 237
Cdd:cd18555 148 lLLGLLIVLLLLLTRKKIKKLNQEEIV----AQTKVQSYLTETLYGIETIKSLGSEKNIykkwenlfkkqLKAFKKKERL 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 238 LNGFGFKASFISgLMLPLVqmtaygtyigVAVLGSYYVVAGVIVVGQLQAF 288
Cdd:cd18555 224 SNILNSISSSIQ-FIAPLL----------ILWIGAYLVINGELTLGELIAF 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
338-569 |
1.71e-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: 70.10 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 338 PEPILgSVEFENVSF-SYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKT----TLINLLMRFYDVTEGAIKIDGIDTKKM 412
Cdd:COG4172 3 SMPLL-SVEDLSVAFgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 413 NRSDVRSV----FGMVLQDAW-----LYkgTIADNIrfgkldatdYEVV--------DAAKTANVDHFIRT-MPDGyEME 474
Cdd:COG4172 82 SERELRRIrgnrIAMIFQEPMtslnpLH--TIGKQI---------AEVLrlhrglsgAAARARALELLERVgIPDP-ERR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 475 INSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALI-------QKAMDRVMegrtsFVIAHRLSTIRE-A 546
Cdd:COG4172 150 LDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQIldllkdlQRELGMAL-----LLITHDLGVVRRfA 224
|
250 260
....*....|....*....|...
gi 488301890 547 DLILVMKQGEIIEKGTHHELLEQ 569
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
347-555 |
1.72e-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: 66.50 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 347 FENVSFSYD---PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYD--VTEGAIKIDGidtkKMNRSDVRSVF 421
Cdd:cd03232 6 WKNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILING----RPLDKNFQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQ-DAWLYKGTIADNIRFgkldatdyevvdaakTANvdhfIRtmpdgyemeinsegdNVSLGQKQLLTIARAVISDP 500
Cdd:cd03232 82 GYVEQqDVHSPNLTVREALRF---------------SAL----LR---------------GLSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRV-MEGRTSFVIAHRLS--TIREADLILVMKQG 555
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
357-525 |
1.73e-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: 66.61 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVfgmvlqdAWL-----Y 431
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENI-------LYLghlpgL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 432 KG--TIADNIRFGK--LDATDYEVVDAAKTANVDHFIRTmPDGYemeinsegdnVSLGQKQLLTIARAVISDPKILILDE 507
Cdd:TIGR01189 85 KPelSALENLHFWAaiHGGAQRTIEDALAAVGLTGFEDL-PAAQ----------LSAGQQRRLALARLWLSRRPLWILDE 153
|
170
....*....|....*...
gi 488301890 508 ATSSVDTRLEALIQKAMD 525
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLR 171
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
345-564 |
2.30e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV---RSVF 421
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQD-AWLYKGTIADNIRFGKldatdyeVVDAAKTANVDHFIRTMPD--GYEMEINSEGDNVSLGQKQLLTIARAVIS 498
Cdd:PRK10908 82 GMIFQDhHLLMDRTVYDNVAIPL-------IIAGASGDDIRRRVSAALDkvGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 499 DPKILILDEATSSVDTRLEALIQK---AMDRVmeGRTSFVIAHRLSTI-READLILVMKQGEIIekGTHH 564
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRlfeEFNRV--GVTVLMATHDIGLIsRRSYRMLTLSDGHLH--GGVG 220
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
111-291 |
2.34e-12 |
|
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: 67.87 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 111 RLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFiniVSAVLGIVMAV---VMMFLINPLMAIFSVIMIPLSLIISRTIV 187
Cdd:cd18567 87 RLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGF---VEALLDGLMAIltlVMMFLYSPKLALIVLAAVALYALLRLALY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 188 KISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGF-----KQVNHRLN------GFGFKASFISGLMlplv 256
Cdd:cd18567 163 PPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWlnllvDAINADIRlqrlqiLFSAANGLLFGLE---- 238
|
170 180 190
....*....|....*....|....*....|....*
gi 488301890 257 qmtaygtYIGVAVLGSYYVVAGVIVVGQLQAFIQY 291
Cdd:cd18567 239 -------NILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
348-577 |
2.90e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVLQD 427
Cdd:PRK10253 11 EQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 A----------WLYKGTIADNIRFGKLDATDYEVVDAAKTANvdhfirtmpdGYEMEINSEGDNVSLGQKQLLTIARAVI 497
Cdd:PRK10253 90 AttpgditvqeLVARGRYPHQPLFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 498 SDPKILILDEATSSVDTR-----LEALIQkaMDRVmEGRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELLeQGG 571
Cdd:PRK10253 160 QETAIMLLDEPTTWLDIShqidlLELLSE--LNRE-KGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV-TAE 235
|
....*.
gi 488301890 572 FYEKLY 577
Cdd:PRK10253 236 LIERIY 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
356-558 |
4.68e-12 |
|
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: 65.36 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 356 PEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLL---MRFYDVTEGAIKIDGIDTKKMNRSdvrsvfgmvlqdawlYK 432
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFAEK---------------YP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 433 GTI----ADNIRFGKLdaTDYEVVDAAKTANVDHFIRtmpdgyemeinsegdNVSLGQKQLLTIARAVISDPKILILDEA 508
Cdd:cd03233 83 GEIiyvsEEDVHFPTL--TVRETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 509 TSSVD--TRLEAL-IQKAMDRVMEGrTSFVIAHRLS-TIREA-DLILVMKQGEII 558
Cdd:cd03233 146 TRGLDssTALEILkCIRTMADVLKT-TTFVSLYQASdEIYDLfDKVLVLYEGRQI 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
345-521 |
4.98e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 63.62 E-value: 4.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMrfydvteGAIKIDgidtkkmnrsdvrsvfgmv 424
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------GELEPD------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 lqdawlyKGTIadnirfgkldatdyEVVDAAKTANVDHFirtmpdgyemeinsegdnvSLGQKQLLTIARAVISDPKILI 504
Cdd:cd03221 54 -------EGIV--------------TWGSTVKIGYFEQL-------------------SGGEKMRLALAKLLLENPNLLL 93
|
170
....*....|....*...
gi 488301890 505 LDEATSSVDTR-LEALIQ 521
Cdd:cd03221 94 LDEPTNHLDLEsIEALEE 111
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
346-558 |
5.13e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.60 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSY---DPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV----R 418
Cdd:PRK10535 6 ELKDIRRSYpsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 SVFGMVLQDAWLYKG-TIADNIrfgKLDATDYEVVDAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVI 497
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNV---EVPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 498 SDPKILILDEATSSVDTR----LEALIQKAMDRvmeGRTSFVIAHRLSTIREADLILVMKQGEII 558
Cdd:PRK10535 161 NGGQVILADEPTGALDSHsgeeVMAILHQLRDR---GHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
111-299 |
8.49e-12 |
|
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: 66.37 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 111 RLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIV--- 187
Cdd:cd18588 87 RLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTpil 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 188 --KISQKYFQGMQNslgdlNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYI 265
Cdd:cd18588 166 rrRLEEKFQRGAEN-----QSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTL 240
|
170 180 190
....*....|....*....|....*....|....
gi 488301890 266 GVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18588 241 AILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPV 274
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
363-558 |
1.03e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVT--EGAIKIDGIDTKKMNRSDV-RSVFGMVLQDAWLYKG-TIADN 438
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKElSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 439 I-------RFGKLDatdyevvDAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSS 511
Cdd:PRK13549 103 IflgneitPGGIMD-------YDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488301890 512 VdTRLEA--LIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:PRK13549 174 L-TESETavLLDIIRDLKAHGIACIYISHKLNEVKAiSDTICVIRDGRHI 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-567 |
1.18e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.50 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 334 DVPLPEPILGSVefeNVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGA-----IKIDGID 408
Cdd:PRK14271 14 DVDAAAPAMAAV---NLTLGF-AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 409 TkkMNRSDV---RSVFGMVLQDAWLYKGTIADNIRFGK-----LDATDYEVVDAAKTANVDhfirtMPDGYEMEINSEGD 480
Cdd:PRK14271 90 I--FNYRDVlefRRRVGMLFQRPNPFPMSIMDNVLAGVrahklVPRKEFRGVAQARLTEVG-----LWDAVKDRLSDSPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 481 NVSLGQKQLLTIARAVISDPKILILDEATSSVD----TRLEALIQKAMDRVmegrTSFVIAHRLS-TIREADLILVMKQG 555
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDptttEKIEEFIRSLADRL----TVIIVTHNLAqAARISDRAALFFDG 238
|
250
....*....|..
gi 488301890 556 EIIEKGTHHELL 567
Cdd:PRK14271 239 RLVEEGPTEQLF 250
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
38-297 |
1.34e-11 |
|
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: 65.57 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 38 ALPYLTGLPTTEISRNIAAGESINfdyviqcLIWILV-VGTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSY 116
Cdd:cd18589 14 AIPYYTGRMTDWIMNKDAPEAFTA-------AITVMSlLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 117 FDKNQQGNILSRVTNDVDAVSNAMQQSfiniVSAVLGIVMAVVMMFLI----NPLMAIFSVIMIPLSLIISRTIVKISQK 192
Cdd:cd18589 87 FDSNQTGDIVSRVTTDTEDMSESLSEN----LSLLMWYLARGLFLFIFmlwlSPKLALLTALGLPLLLLVPKFVGKFQQS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 193 YFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFK---QVNHRLN-------GFGFKASFISGLMLPlvqmtayg 262
Cdd:cd18589 163 LAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRqrlQKTYRLNkkeaaayAVSMWTSSFSGLALK-------- 234
|
250 260 270
....*....|....*....|....*....|....*
gi 488301890 263 tyIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQ 297
Cdd:cd18589 235 --VGILYYGGQLVTAGTVSSGDLVTFVLYELQFTS 267
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-575 |
1.76e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 65.15 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 344 SVEFENVSFSYDP----EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGI----DTKKMNRS 415
Cdd:PRK13649 2 GINLQNVSYTYQAgtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 DVRSVFGMVLQ--DAWLYKGTIADNIRFGK----LDATDYEVVDAAKTANV---DHFIRTMPdgYEMeinsegdnvSLGQ 486
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPqnfgVSQEEAEALAREKLALVgisESLFEKNP--FEL---------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 487 KQLLTIARAVISDPKILILDEATSSVDTR----LEALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG 561
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKgrkeLMTLFKKLHQ---SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
|
250
....*....|....
gi 488301890 562 THHELLEQGGFYEK 575
Cdd:PRK13649 228 KPKDIFQDVDFLEE 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
348-568 |
2.47e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.89 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGID-TKK-MNRsdvRSVFGM-- 423
Cdd:COG1137 7 ENLVKSYG-KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDiTHLpMHK---RARLGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKG-TIADNIR----FGKLDATDYEvvdaAKTA------NVDHfIRtmpdgyemeiNSEGDNVSLGQKQLLTI 492
Cdd:COG1137 83 LPQEASIFRKlTVEDNILavleLRKLSKKERE----ERLEelleefGITH-LR----------KSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 493 ARAVISDPKILILDEATSSVD----TRLEALIQKAMDRVMegrtSFVIA-HRlstIREA----DLILVMKQGEIIEKGTH 563
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKERGI----GVLITdHN---VRETlgicDRAYIISEGKVLAEGTP 220
|
....*
gi 488301890 564 HELLE 568
Cdd:COG1137 221 EEILN 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
345-403 |
3.08e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 3.08e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIK 403
Cdd:PRK15064 320 LEVENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
348-577 |
3.64e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 3.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYdPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG-----IDTKKMNR-------- 414
Cdd:PRK10575 15 RNVSFRV-PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqplesWSSKAFARkvaylpqq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 415 ---SDVRSVFGMVLQDAWLYKGTIAdniRFGkldATDYEVVDAAKTanvdhFIRTMPDGYEMEinsegDNVSLGQKQLLT 491
Cdd:PRK10575 94 lpaAEGMTVRELVAIGRYPWHGALG---RFG---AADREKVEEAIS-----LVGLKPLAHRLV-----DSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 492 IARAVISDPKILILDEATSSVD----TRLEALIQkamdRVMEGRTSFVIA--HRLS-TIREADLILVMKQGEIIEKGTHH 564
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDiahqVDVLALVH----RLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPA 233
|
250
....*....|...
gi 488301890 565 ELLeQGGFYEKLY 577
Cdd:PRK10575 234 ELM-RGETLEQIY 245
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
100-280 |
4.08e-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: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDavsnAMQQSFINI----VSAVLGIVMAVVMMFLINPLMA-----I 170
Cdd:cd18585 69 NLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADID----TLDNLYLRVlsppVVALLVILATILFLAFFSPALAlillaG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 171 FSVIMIPLSLIISRTIVKISQKyfqgMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISG 250
Cdd:cd18585 145 LLLAGVVIPLLFYRLGKKIGQQ----LVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSG 220
|
170 180 190
....*....|....*....|....*....|
gi 488301890 251 LMLPLVQMTAYGTYIGVAVLGSYYVVAGVI 280
Cdd:cd18585 221 LSQALMILLSGLTVWLVLWLGAPLVQNGAL 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
346-569 |
5.52e-11 |
|
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: 65.23 E-value: 5.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSfSYDPEKPLIR---NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYD-VTEGAIKIDG--IDTKKMNRSdVRS 419
Cdd:TIGR02633 259 EARNLT-CWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGkpVDIRNPAQA-IRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 420 VFGMVLQDAwLYKGTIAD-----NIRFGKLD--ATDYEVVDAAKTANVDHFIRTM------PDgyeMEINSegdnVSLGQ 486
Cdd:TIGR02633 337 GIAMVPEDR-KRHGIVPIlgvgkNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvktasPF---LPIGR----LSGGN 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 487 KQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHH 564
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNH 488
|
....*
gi 488301890 565 ELLEQ 569
Cdd:TIGR02633 489 ALTQE 493
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
357-562 |
7.42e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.74 E-value: 7.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF--YDVTEGAIKIDGIDTKKMNrSDVRSVFGMVLqdAWLYKGT 434
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFL--AFQYPIE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 435 IA--DNIRF--------------GKLDATD-YEVV-DAAKTANVD-HFI-RTMPDGYemeinsegdnvSLGQKQLLTIAR 494
Cdd:CHL00131 96 IPgvSNADFlrlaynskrkfqglPELDPLEfLEIInEKLKLVGMDpSFLsRNVNEGF-----------SGGEKKRNEILQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 495 AVISDPKILILDEATSSVDtrLEAL--IQKAMDRVMEGRTSFV-IAH--RLSTIREADLILVMKQGEIIEKGT 562
Cdd:CHL00131 165 MALLDSELAILDETDSGLD--IDALkiIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
359-566 |
7.43e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 359 PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSvFGMVL--QDAWLYKG-TI 435
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQ-LGIYLvpQEPLLFPNlSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 436 ADNIRFGkLDATdyevvdAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSS---V 512
Cdd:PRK15439 104 KENILFG-LPKR------QASMQKMKQLLAAL--GCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASltpA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 513 DTrlEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHEL 566
Cdd:PRK15439 175 ET--ERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
352-572 |
7.75e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.10 E-value: 7.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 352 FSYDPEkPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRSDVRSVFGMVLQDA- 428
Cdd:PRK13638 9 FRYQDE-PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 429 -WLYKGTIADNIRFG--KLDATDYEV---VDAAKT-ANVDHFiRTMPdgyemeINSegdnVSLGQKQLLTIARAVISDPK 501
Cdd:PRK13638 88 qQIFYTDIDSDIAFSlrNLGVPEAEItrrVDEALTlVDAQHF-RHQP------IQC----LSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 502 ILILDEATSSVD----TRLEALIQKAmdrVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKG------THHELLEQG 570
Cdd:PRK13638 157 YLLLDEPTAGLDpagrTQMIAIIRRI---VAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
..
gi 488301890 571 GF 572
Cdd:PRK13638 234 GL 235
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
361-559 |
8.02e-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: 62.48 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG--IDTKKMNRSDVRSVFGMVlqdAWLykgTIADN 438
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqITEPGPDRMVVFQNYSLL---PWL---TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 439 IRFGkLDATDYEVVDAAKTANVDHFIRTMpdGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVD--TRl 516
Cdd:TIGR01184 75 IALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDalTR- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488301890 517 EALIQKAMDRVMEGR-TSFVIAHrlsTIREADLI---LVM-------KQGEIIE 559
Cdd:TIGR01184 151 GNLQEELMQIWEEHRvTVLMVTH---DVDEALLLsdrVVMltngpaaNIGQILE 201
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
79-298 |
1.05e-10 |
|
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: 63.01 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 79 YCVAQFLSGFL--MTNV----VQQSM-RDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAV 151
Cdd:cd18560 44 YALLRFSSKLLkeLRSLlyrrVQQNAyRELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 152 LGIVMA-VVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEG 230
Cdd:cd18560 124 LELIVVsVVFAFHFGAWLALIVFLSVLLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDR 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 231 FKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQP 298
Cdd:cd18560 204 YGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
328-411 |
1.14e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 328 EELNEQD-----------VPlPEPILGS--VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF 394
Cdd:PRK11819 296 EELLSEEyqkrnetneifIP-PGPRLGDkvIEAENLSKSFG-DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQ 373
|
90 100 110
....*....|....*....|....*....|
gi 488301890 395 YDVTEGAIKI-------------DGIDTKK 411
Cdd:PRK11819 374 EQPDSGTIKIgetvklayvdqsrDALDPNK 403
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
328-404 |
1.15e-10 |
|
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: 64.19 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 328 EELNEQD-----------VPlPEPILGS--VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF 394
Cdd:TIGR03719 294 EELLSQEfqkrnetaeiyIP-PGPRLGDkvIEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQ 371
|
90
....*....|
gi 488301890 395 YDVTEGAIKI 404
Cdd:TIGR03719 372 EQPDSGTIEI 381
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
345-566 |
1.44e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.02 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFsyDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKT----TLINLLMRFYDVTEGAIKIDGI-----DTKKMNRS 415
Cdd:PRK10418 5 IELRNIAL--QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKpvapcALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 416 DV----RSVFGMVLqdawlykgTIADNIR-----FGKL--DATDYEVVDAAKTANVDHFIRTMPdgYEMeinsegdnvSL 484
Cdd:PRK10418 83 TImqnpRSAFNPLH--------TMHTHARetclaLGKPadDATLTAALEAVGLENAARVLKLYP--FEM---------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 485 GQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVMEGRTS--FVIAHRLSTI-READLILVMKQGEIIEKG 561
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVaRLADDVAVMSHGRIVEQG 223
|
....*
gi 488301890 562 THHEL 566
Cdd:PRK10418 224 DVETL 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
360-557 |
1.49e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 360 LIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKM---NRSDVRS-VFGMVLQDAWLYKG-T 434
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 435 IADNIRFGKLdatdyevVDAAKTANVDHFIRTM--PDGYEMEINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSV 512
Cdd:PRK11629 104 ALENVAMPLL-------IGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488301890 513 DTRLEALIQKAMDR--VMEGRTSFVIAHRLSTIREADLILVMKQGEI 557
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
357-520 |
2.01e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.59 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmnrsdVRSVFGMVLqdawLYKG--- 433
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYHQDL----LYLGhqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 434 ------TIADNIRF-GKL--DATDYEVVDAAKTANVdhfirtmpDGYEmeinsegD----NVSLGQKQLLTIARAVISDP 500
Cdd:PRK13538 84 giktelTALENLRFyQRLhgPGDDEALWEALAQVGL--------AGFE-------DvpvrQLSAGQQRRVALARLWLTRA 148
|
170 180
....*....|....*....|....
gi 488301890 501 KILILDEATSSVDT----RLEALI 520
Cdd:PRK13538 149 PLWILDEPFTAIDKqgvaRLEALL 172
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
348-567 |
2.23e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDPEKpLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMN-RSDVRSVFGMVLQ 426
Cdd:PRK10895 7 KNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 427 DAWLYKG-TIADNIrFGKLDATDyevvDAAKTANVDHFIRTMPDGYEMEI-NSEGDNVSLGQKQLLTIARAVISDPKILI 504
Cdd:PRK10895 86 EASIFRRlSVYDNL-MAVLQIRD----DLSAEQREDRANELMEEFHIEHLrDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 505 LDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRL-STIREADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-558 |
3.60e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTK-KMNRSDVRSVFGMVLQDAWLYKG-TIADNI- 439
Cdd:PRK10762 22 GAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAENIf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 440 -------RFGKLDATD-YEVVDA-AKTANVDHFIRTMPdgyemeinseGDnVSLGQKQLLTIARAVISDPKILILDEATS 510
Cdd:PRK10762 102 lgrefvnRFGRIDWKKmYAEADKlLARLNLRFSSDKLV----------GE-LSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488301890 511 SV-DTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:PRK10762 171 ALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEiCDDVTVFRDGQFI 220
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
368-555 |
4.11e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 368 VDAGQMVAIVGPTGAGKTTLINLLMRFYD---VTEGAIKIDGIdtkKMNRSDVRSVFGMVLQDAWLYKGTIADNIRFGKL 444
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGR---PLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 445 DATDYEVVDAAKTANVDHFIRTMpdgyEME------INSEGDNVSLGQKQLLTIARAVISDPKILI-LDEATSSVDTRLE 517
Cdd:TIGR00956 863 LRQPKSVSKSEKMEYVEEVIKLL----EMEsyadavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488301890 518 ALIQKAMDRVME-GRTSFVIAHRLSTI--READLILVMKQG 555
Cdd:TIGR00956 939 WSICKLMRKLADhGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
346-513 |
5.07e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 59.73 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDVRSVFGMVL 425
Cdd:PRK10247 9 QLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QDAWLYKGTIADNIRFgkldatDYEVvdAAKTANVDHFIRTMpDGYEMEINSEGDNV---SLGQKQLLTIARAVISDPKI 502
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF------PWQI--RNQQPDPAIFLDDL-ERFALPDTILTKNIaelSGGEKQRISLIRNLQFMPKV 158
|
170
....*....|.
gi 488301890 503 LILDEATSSVD 513
Cdd:PRK10247 159 LLLDEITSALD 169
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-589 |
5.26e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 60.87 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMV------------LQDA 428
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrsqlwwdlpAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 429 WLYKGTIadnirfgkldatdYEVVDAAKTANVDHFIRTMpdgyEME--INSEGDNVSLGQKQLLTIARAVISDPKILILD 506
Cdd:COG4586 117 FRLLKAI-------------YRIPDAEYKKRLDELVELL----DLGelLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 507 EATSSVD----TRLEALIqKAMDRVmEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQGGfYEKLYNSQF 581
Cdd:COG4586 180 EPTIGLDvvskEAIREFL-KEYNRE-RGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFG-PYKTIVLEL 256
|
....*...
gi 488301890 582 AEEGDYEE 589
Cdd:COG4586 257 AEPVPPLE 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
361-558 |
9.52e-10 |
|
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: 60.99 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFY--DVTEGAIKIDGIDTKKMNRSDV-RSVFGMVLQDAWLYKG-TIA 436
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPElSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 DNIRFG-KLDATDYEVVDAAKTANVDHFIRtmpdgyemEINSEGDNVS-------LGQKQLLTIARAVISDPKILILDEA 508
Cdd:TIGR02633 97 ENIFLGnEITLPGGRMAYNAMYLRAKNLLR--------ELQLDADNVTrpvgdygGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488301890 509 TSSV-DTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:TIGR02633 169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
325-558 |
9.62e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 61.19 E-value: 9.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 325 EPEEELNEQDVPLPEPILgsvEFENVSFsydpeKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKI 404
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVL---EVEGLSV-----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 405 DGidtKKMNRSDVRS------VF--------GMVLQDawlykgTIADNI---------RFGKLDatdyevvDAAKTANVD 461
Cdd:COG1129 312 DG---KPVRIRSPRDairagiAYvpedrkgeGLVLDL------SIRENItlasldrlsRGGLLD-------RRRERALAE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 462 HFIRTM---PDGYEMEINsegdNVSLG--QKQLltIARAVISDPKILILDEATSSVD--TRLEalIQKAMDR-VMEGRTS 533
Cdd:COG1129 376 EYIKRLrikTPSPEQPVG----NLSGGnqQKVV--LAKWLATDPKVLILDEPTRGIDvgAKAE--IYRLIRElAAEGKAV 447
|
250 260
....*....|....*....|....*....
gi 488301890 534 FVIAhrlSTIRE----ADLILVMKQGEII 558
Cdd:COG1129 448 IVIS---SELPEllglSDRILVMREGRIV 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
346-557 |
1.03e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.10 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSfSYDPEKPLIR---NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYD-VTEGAIKIDGIDTKKMNRSD-VRSV 420
Cdd:PRK13549 261 EVRNLT-AWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQaIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 421 FGMVLQDAWLYkGTIAD-----NIRFGKLDA-TDYEVVD-AAKTANVDHFIRTM------PdgyEMEINsegdNVSLGQK 487
Cdd:PRK13549 340 IAMVPEDRKRD-GIVPVmgvgkNITLAALDRfTGGSRIDdAAELKTILESIQRLkvktasP---ELAIA----RLSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTSFVIAHRLSTIRE-ADLILVMKQGEI 557
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
339-557 |
1.09e-09 |
|
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: 57.83 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 339 EPILgsvEFENVSFsydpeKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV- 417
Cdd:cd03215 2 EPVL---EVRGLSV-----KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 418 ----------RSVFGMVLQdawlykGTIADNIRFGKLdatdyevvdaaktanvdhfirtmpdgyemeinsegdnVSLGQK 487
Cdd:cd03215 74 ragiayvpedRKREGLVLD------LSVAENIALSSL-------------------------------------LSGGNQ 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVD--TRLE--ALIQKAMDrvmEGRTSFVIAHRLSTIRE-ADLILVMKQGEI 557
Cdd:cd03215 111 QKVVLARWLARDPRVLILDEPTRGVDvgAKAEiyRLIRELAD---AGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
361-574 |
2.88e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 58.97 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKT----TLINLLMRfYDVTEGAIKIDGID-----TKKMNRsdVRS-VFGMVLQDAW- 429
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREilnlpEKELNK--LRAeQISMIFQDPMt 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 -----------------LYKGtiadnirFGKLDATDYEV--VDAAKTANVDHFIRTMPDGYemeinsegdnvSLGQKQLL 490
Cdd:PRK09473 109 slnpymrvgeqlmevlmLHKG-------MSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 491 TIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFV-IAHRLSTIRE-ADLILVMKQGEIIEKGTHHELl 567
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV- 249
|
....*..
gi 488301890 568 eqggFYE 574
Cdd:PRK09473 250 ----FYQ 252
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
348-558 |
2.95e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 348 ENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTK-KMNRSDVRSVFGMVLQ 426
Cdd:PRK10982 2 SNISKSFPGVKAL-DNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 427 DAWLYKG-TIADNIRFGKLDATDYeVVDAAKTANVdhfIRTMPDGYEMEIN--SEGDNVSLGQKQLLTIARAVISDPKIL 503
Cdd:PRK10982 81 ELNLVLQrSVMDNMWLGRYPTKGM-FVDQDKMYRD---TKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 504 ILDEATSSVDTR----LEALIQKAMDRvmeGRTSFVIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:PRK10982 157 IMDEPTSSLTEKevnhLFTIIRKLKER---GCGIVYISHKMEEIFQlCDEITILRDGQWI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
345-566 |
2.96e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 58.10 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFY---DVTEGAIKIDGIDTKKMNR--SDVR- 418
Cdd:PRK09984 5 IRVEKLAKTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRlaRDIRk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 419 --SVFGMVLQDAWLY-KGTIADNIRFGKLDATDY--------------EVVDAAKTANVDHFIrtmpdgyemeiNSEGDN 481
Cdd:PRK09984 84 srANTGYIFQQFNLVnRLSVLENVLIGALGSTPFwrtcfswftreqkqRALQALTRVGMVHFA-----------HQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 482 VSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRV--MEGRTSFVIAHRLS-TIREADLILVMKQGEII 558
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHVF 232
|
....*...
gi 488301890 559 EKGTHHEL 566
Cdd:PRK09984 233 YDGSSQQF 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
363-559 |
3.32e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFY--DVTEGAIKIDGidtKKMNRSDVRS--VFGMVL--QDAWLYKG-TI 435
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYphGSYEGEILFDG---EVCRFKDIRDseALGIVIihQELALIPYlSI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 436 ADNIRFGKLDATdYEVVDAAKTanvdhFIRTM-----------PDGYEMEInsegdnvSLGQKQLLTIARAVISDPKILI 504
Cdd:NF040905 96 AENIFLGNERAK-RGVIDWNET-----NRRARellakvgldesPDTLVTDI-------GVGKQQLVEIAKALSKDVKLLI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 505 LDEATSSV-DTRLEALIQKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGEIIE 559
Cdd:NF040905 163 LDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
349-547 |
5.03e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 349 NVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmNRSDVRSVFGMVLQDA 428
Cdd:PRK13540 6 ELDFDYH-DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 429 WLYKG-TIADNIRFG-KLDATDYEVVDAAKTANVDHFIrTMPDGYemeinsegdnVSLGQKQLLTIARAVISDPKILILD 506
Cdd:PRK13540 84 GINPYlTLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488301890 507 EATSSVDTR-LEALIQKAMDRVMEGRTSFVIAHRLSTIREAD 547
Cdd:PRK13540 153 EPLVALDELsLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
357-570 |
5.99e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM--RFYDVTEGAIKIDGIDTKKMNRSDvRSVFGMVLQDAW----- 429
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFMAFQYpveip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 -----LYKGTIADNIRFGK----LDATDYEVVDAAKTANVDhfirtMPDgyEMEINSEGDNVSLGQKQLLTIARAVISDP 500
Cdd:PRK09580 92 gvsnqFFLQTALNAVRSYRgqepLDRFDFQDLMEEKIALLK-----MPE--DLLTRSVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488301890 501 KILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIA---HRLSTIREADLILVMKQGEIIEKGTH---HELLEQG 570
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQG 240
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
70-238 |
6.45e-09 |
|
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: 57.48 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 70 IWILVV-GTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIV 148
Cdd:cd18606 38 IGIYAGlGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 149 SAVLGIVMAVVMMFLINPLMAIfsvIMIPLSLI----------ISRTIvkisqKYFQGMQNSLgdLNGYVQENMTGFSVL 218
Cdd:cd18606 118 YTLSSIIGTFILIIIYLPWFAI---ALPPLLVLyyfianyyraSSREL-----KRLESILRSF--VYANFSESLSGLSTI 187
|
170 180
....*....|....*....|
gi 488301890 219 KLYGREKEtlegFKQVNHRL 238
Cdd:cd18606 188 RAYGAQDR----FIKKNEKL 203
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
26-302 |
7.00e-09 |
|
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: 57.51 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 26 ILFTILTVAFNAALPYLTGLPTTEISRNIAAGESInfdyviqcLIWILVvgtGYCVAQFLSGF-------LMTNVVQQSM 98
Cdd:cd18582 2 LLLLVLAKLLNVAVPFLLKYAVDALSAPASALLAV--------PLLLLL---AYGLARILSSLfnelrdaLFARVSQRAV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 99 RDLRRDIEEKINRLPVSYFDKNQQG---NILSRVTNDVDAVSNAMqqsFINIVSAVLGIVMAVVMMF-LINPLMAIFSVI 174
Cdd:cd18582 71 RRLALRVFRHLHSLSLRFHLSRKTGalsRAIERGTRGIEFLLRFL---LFNILPTILELLLVCGILWyLYGWSYALITLV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 175 MIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKaSFISGLMLP 254
Cdd:cd18582 148 TVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVK-SQTSLALLN 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488301890 255 LVQMTAYGT-YIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18582 227 IGQALIISLgLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFL 275
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
371-550 |
8.14e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 8.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 371 GQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIdgidtkkmnrsdvrsvfgmvlqdawlykgtiadnirfgkldatdye 450
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 451 vVDAAKTANVDHFIRTMPDGYEMEINSEGdnvslGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMD----- 525
Cdd:smart00382 36 -IDGEDILEEVLDQLLLIIVGGKKASGSG-----ELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlll 109
|
170 180
....*....|....*....|....*..
gi 488301890 526 --RVMEGRTSFVIAHRLSTIREADLIL 550
Cdd:smart00382 110 llKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
101-285 |
8.45e-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: 56.90 E-value: 8.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSL 180
Cdd:cd18561 71 LRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIP 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYG---REKETL----EGFKQVNHRLNGFGFKASFISGLml 253
Cdd:cd18561 151 LSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGaskRRGNELaaraEDLRQATMKVLAVSLLSSGIMGL-- 228
|
170 180 190
....*....|....*....|....*....|....*
gi 488301890 254 plvqmtayGTYIGVA---VLGSYYVVAGVIVVGQL 285
Cdd:cd18561 229 --------ATALGTAlalGVGALRVLGGQLTLSSL 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
325-568 |
9.01e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 9.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 325 EPEEELNEQDVPLP-EPILG-----------SVEFENVSfsydPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM 392
Cdd:PRK10261 296 AKQEPPIEQDTVVDgEPILQvrnlvtrfplrSGLLNRVT----REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 393 RFYDVTEGAIKIDG--IDT---KKMN--RSDVRSVFgmvlQDAWLY---KGTIADNI-------RFGKLDATDYEVVDAA 455
Cdd:PRK10261 372 RLVESQGGEIIFNGqrIDTlspGKLQalRRDIQFIF----QDPYASldpRQTVGDSImeplrvhGLLPGKAAAARVAWLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 456 KTANV--DHFIRtmpdgYEMEInsegdnvSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEA-LIQKAMDRVMEGRT 532
Cdd:PRK10261 448 ERVGLlpEHAWR-----YPHEF-------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDFGI 515
|
250 260 270
....*....|....*....|....*....|....*...
gi 488301890 533 SFV-IAHRLSTI-READLILVMKQGEIIEKGTHHELLE 568
Cdd:PRK10261 516 AYLfISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
345-566 |
1.15e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 56.31 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRS---DVRSVF 421
Cdd:PRK11831 8 VDMRGVSFTRG-NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 422 GMVLQDAWLYKG-TIADNIRFGKLDATD-------------YEVVDAAKTANVdhfirtMPdgyemeinSEgdnVSLGQK 487
Cdd:PRK11831 87 SMLFQSGALFTDmNVFDNVAYPLREHTQlpapllhstvmmkLEAVGLRGAAKL------MP--------SE---LSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 488 QLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHH 564
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
|
..
gi 488301890 565 EL 566
Cdd:PRK11831 230 AL 231
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
345-552 |
1.45e-08 |
|
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: 57.84 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDgiDTKKMNRSDVRSVFGM- 423
Cdd:TIGR00954 452 IKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--AKGKLFYVPQRPYMTLg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 424 VLQDAWLYKGTIADNIRFGKLDATDYEVVDaaktaNVD-HFIRTMPDGYEMeINSEGDNVSLGQKQLLTIARAVISDPKI 502
Cdd:TIGR00954 530 TLRDQIIYPDSSEDMKRRGLSDKDLEQILD-----NVQlTHILEREGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVmeGRTSFVIAHRLSTIREADLILVM 552
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKSLWKYHEYLLYM 651
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
24-253 |
2.18e-08 |
|
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: 55.88 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLtglptteISRNIAAGESinFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd18584 4 LGLLAALLIIAQAWLLARI-------IAGVFLEGAG--LAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVI---MIPLSL 180
Cdd:cd18584 75 RLLARLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVtapLIPLFM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 I-ISRTIVKISQKYFQgmqnSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNgfgfKAS-------FISGLM 252
Cdd:cd18584 155 IlIGKAAQAASRRQWA----ALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYR----RRTmkvlrvaFLSSAV 226
|
.
gi 488301890 253 L 253
Cdd:cd18584 227 L 227
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
114-291 |
2.20e-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: 55.81 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 114 VSYFDKNQQGNILSRVTNDVDAVSNAMQQSfINIVSAVLGIVMAVV-MMFLINPLMAIFSVIMIPLSLIISRTIVKISQK 192
Cdd:cd18590 84 IGFFEKTKTGDLTSRLSTDTTLMSRSVALN-ANVLLRSLVKTLGMLgFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQK 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 193 YFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGS 272
Cdd:cd18590 163 LSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGR 242
|
170
....*....|....*....
gi 488301890 273 YYVVAGVIVVGQLQAFIQY 291
Cdd:cd18590 243 QLIQSGHLTTGSLVSFILY 261
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
326-547 |
4.58e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 326 PEEELNEQDVPLPEPIlGSVEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLlmrfydvtegaikID 405
Cdd:PRK10938 243 PEPDEPSARHALPANE-PRIVLNNGVVSYN-DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSL-------------IT 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 406 GiDTKKMNRSDVrSVFGMvlqdawlYKG---TIADNIR-FGKLDAT---DYEVVDAAKTANVDHFI------RTMPD--- 469
Cdd:PRK10938 308 G-DHPQGYSNDL-TLFGR-------RRGsgeTIWDIKKhIGYVSSSlhlDYRVSTSVRNVILSGFFdsigiyQAVSDrqq 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 470 ----------GYEMEI-NSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDTRLEALIQKAMDR-VMEGRTS--FV 535
Cdd:PRK10938 379 klaqqwldilGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQllFV 458
|
250 260
....*....|....*....|..
gi 488301890 536 ----------IAHRLSTIREAD 547
Cdd:PRK10938 459 shhaedapacITHRLEFVPDGD 480
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
364-581 |
8.39e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.69 E-value: 8.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 364 LNFKVDAGQMVAIVGPTGAGKTTlinLLMRFYDVT--EGAIKIDGIDTKKMN-------RS----DVRSVFGM-VLQDAW 429
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMAGLLpgQGEILLNGRPLSDWSaaelarhRAylsqQQSPPFAMpVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 LYkgtIADNIRFGKLDATDYEVVDAAKTAnvdhfirtmpDGYEMEINsegdNVSLGQKQLLTIARAVI-------SDPKI 502
Cdd:COG4138 92 LH---QPAGASSEAVEQLLAQLAEALGLE----------DKLSRPLT----QLSGGEWQRVRLAAVLLqvwptinPEGQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 503 LILDEATSSVDTRLEAliqkAMDRVME-----GRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELLEQGGFyEKL 576
Cdd:COG4138 155 LLLDEPMNSLDVAQQA----ALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPENL-SEV 229
|
....*
gi 488301890 577 YNSQF 581
Cdd:COG4138 230 FGVKF 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
321-513 |
8.93e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 321 EILDEPEEELNEQDV-------------PLPEPILGSVEFE----NVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAG 383
Cdd:NF040905 219 ETLDCRADEVTEDRIirgmvgrdledryPERTPKIGEVVFEvknwTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAG 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 384 KTTL-INLLMRFYDV-TEGAIKIDG--IDTKKMNR---------SDVRSVFGMVLQDawlykgTIADNIRFGKLDA-TDY 449
Cdd:NF040905 299 RTELaMSVFGRSYGRnISGTVFKDGkeVDVSTVSDaidaglayvTEDRKGYGLNLID------DIKRNITLANLGKvSRR 372
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 450 EVVDAAKTANV-DHFIRTM----PDgyemeINSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVD 513
Cdd:NF040905 373 GVIDENEEIKVaEEYRKKMniktPS-----VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
360-562 |
1.03e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.24 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 360 LIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM--RFYDVTEGAIKIDGIDTKKMNRSDVRsvfGMVLQ-DAWLYKGTIA 436
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQETFARIS---GYCEQnDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 437 DNIRFGKLDATDYEVVDAAKTANVDHFIRTMpdgyemEINSEGDNV---------SLGQKQLLTIARAVISDPKILILDE 507
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMFVDEVMELV------ELDNLKDAIvglpgvtglSTEQRKRLTIAVELVANPSIIFMDE 1045
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 508 ATSSVDTRLEALIQKAM-DRVMEGRTSFVIAHRLST-IREA-DLILVMKQ-GEIIEKGT 562
Cdd:PLN03140 1046 PTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSIdIFEAfDELLLMKRgGQVIYSGP 1104
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
362-557 |
1.31e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 362 RNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKM---NRSDV--------RSVFGMVLqDAWL 430
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALstaQRLARglvylpedRQSSGLYL-DAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 431 YKGTIA---DNIRF---GKLDATDYEVVDAA---KTANVDHFIRTMpdgyemeinsegdnvSLGQKQLLTIARAVISDPK 501
Cdd:PRK15439 359 AWNVCAlthNRRGFwikPARENAVLERYRRAlniKFNHAEQAARTL---------------SGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVMEGRTSFV-IAHRLSTIRE-ADLILVMKQGEI 557
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
357-580 |
1.58e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.33 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 357 EKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRF-------YdvTEGAIKIDGIDTKKMNRSDVRSVFG----MVL 425
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvY--PSGDIRFHGESLLHASEQTLRGVRGnkiaMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 426 QDAWLYKGTIADnirfgkLDATDYEVV--------DAAKTANVDHFIRTMPDGYEMEINSEGDNVSLGQKQLLTIARAVI 497
Cdd:PRK15134 99 QEPMVSLNPLHT------LEKQLYEVLslhrgmrrEAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 498 SDPKILILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLE--QGGF 572
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSapTHPY 252
|
....*...
gi 488301890 573 YEKLYNSQ 580
Cdd:PRK15134 253 TQKLLNSE 260
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
76-181 |
2.72e-07 |
|
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: 52.48 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 76 GTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIV 155
Cdd:cd18603 51 GLGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVI 130
|
90 100
....*....|....*....|....*.
gi 488301890 156 MAVVMMFLINPlmaIFSVIMIPLSLI 181
Cdd:cd18603 131 STLVVISISTP---IFLVVIIPLAIL 153
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
363-561 |
4.09e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 363 NLNFKVDA---GQMV-AIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG---IDT-KKMNRSDVRSVFGMVLQDAWL---Y 431
Cdd:PRK11144 12 DLCLTVNLtlpAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAeKGICLPPEKRRIGYVFQDARLfphY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 432 kgTIADNIRFGKLDATDYEVVDAAKTANVDHFIRTMPDgyemeinsegdNVSLGQKQLLTIARAVISDPKILILDEATSS 511
Cdd:PRK11144 92 --KVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPG-----------SLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 512 VD--------TRLEALIQkamdrvmEGRTSFV-IAHRLSTI-READLILVMKQGEIIEKG 561
Cdd:PRK11144 159 LDlprkrellPYLERLAR-------EINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
361-584 |
4.23e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 4.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtkkmnrsdvrSVFGMVLQDAWLYKGTIADNIR 440
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 441 FG---------KLDATDYEVVDaakTANVDHFIRTMPDGYemeinsegdnvSLGQKQLLTIARAVISDPKILILDEATSS 511
Cdd:PRK13545 108 LKglmmgltkeKIKEIIPEIIE---FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 512 VDtrlEALIQKAMDRVME----GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQGGFYEKLYNSQFAEE 584
Cdd:PRK13545 174 GD---QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEE 248
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
39-303 |
4.77e-07 |
|
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: 51.54 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 39 LPYLTGLPTTEISRNIAAgESINFDYVIQCLIWIlvvGTGYCvAQFLSGFLMTNVVQQSMRdLRRDIEEKINRLPVSYFD 118
Cdd:cd18784 15 IPYYTGQVIDGIVIEKSQ-DKFSRAIIIMGLLAI---ASSVA-AGIRGGLFTLAMARLNIR-IRNLLFRSIVSQEIGFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 119 KNQQGNILSRVTNDVDAVSNAMQQSfINI-VSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGM 197
Cdd:cd18784 89 TVKTGDITSRLTSDTTTMSDTVSLN-LNIfLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 198 QNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVA 277
Cdd:cd18784 168 QDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVIT 247
|
250 260
....*....|....*....|....*.
gi 488301890 278 GVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18784 248 GQISGGNLISFILYQLELGSCLESVG 273
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
359-567 |
5.21e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 359 PLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKMNRSDV-----------RSVFGMVLqd 427
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGlangivyisedRKRDGLVL-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 awlykG-TIADNIRFGKLDATDYEVVD---AAKTANVDHFIRTM----PdGYEMEINsegdNVSLGQKQLLTIARAVISD 499
Cdd:PRK10762 344 -----GmSVKENMSLTALRYFSRAGGSlkhADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTR 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 500 PKILILDEATSSVDTRLEALIQKAMDRVMEGRTSFVIAHrlSTIRE----ADLILVMKQGEI-----IEKGTHHELL 567
Cdd:PRK10762 414 PKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS--SEMPEvlgmSDRILVMHEGRIsgeftREQATQEKLM 488
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
22-302 |
5.51e-07 |
|
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: 51.67 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNAALPYLTglptteisRNIA----AGESINFDYVIqcLIWILVVGTGYCVAQFLSGFLMTNVvqqS 97
Cdd:cd18571 4 ILQLLLGLLLGSLLQLIFPFLT--------QSIVdkgiNNKDLNFIYLI--LIAQLVLFLGSTSIEFIRSWILLHI---S 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 98 MR---DLRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSA-----VLGIVMAV--VMMFLINPL 167
Cdd:cd18571 71 SRiniSIISDFLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSllnliVFSIVLAYynLTIFLIFLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 168 MAIFSVIMIPLSLIISRtivKISQKYFQGMQNSlgdlNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLngfgFKASf 247
Cdd:cd18571 150 GSVLYILWILLFLKKRK---KLDYKRFDLSSEN----QSKLIELINGMQEIKLNNSERQKRWEWERIQAKL----FKIN- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 248 ISGLMLPLVQMTAY-----GTYIGVAVLGSYYVVAGVIVVGQLQAfIQYIW-QISQPMGNI 302
Cdd:cd18571 218 IKSLKLDQYQQIGAlfinqLKNILITFLAAKLVIDGEITLGMMLA-IQYIIgQLNSPIEQL 277
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
364-569 |
6.68e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 364 LNFKVDAGQMVAIVGPTGAGKTTLinlLMRFYDVT--EGAIKIDGIDTKKMNRSD-----------VRSVFGM-VLQDAW 429
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTL---LARMAGLLpgSGSIQFAGQPLEAWSAAElarhraylsqqQTPPFAMpVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 LYKgtiADNIRFGKLDATDYEVVDAAKtanvdhfirtMPDGYEMEINsegdNVSLGQKQ-------LLTIARAVISDPKI 502
Cdd:PRK03695 92 LHQ---PDKTRTEAVASALNEVAEALG----------LDDKLGRSVN----QLSGGEWQrvrlaavVLQVWPDINPAGQL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488301890 503 LILDEATSSVDTRLEAliqkAMDRVME-----GRTSFVIAHRLS-TIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK03695 155 LLLDEPMNSLDVAQQA----ALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
325-558 |
8.50e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 325 EPEEELNEQDVPLPEPILgsvEFENVSFSYDPEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKI 404
Cdd:COG3845 241 EVLLRVEKAPAEPGEVVL---EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 405 DGIDTKKMNRSDV-----------RSVFGMVLQdawlykGTIADNI-----------RFGKLD---ATDY--EVVDAA-- 455
Cdd:COG3845 318 DGEDITGLSPRERrrlgvayipedRLGRGLVPD------MSVAENLilgryrrppfsRGGFLDrkaIRAFaeELIEEFdv 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 456 KTANVDHFIRTMpdgyemeinSeGDNVslgQKqlLTIARAVISDPKILILDEATSSVDTRLEALIQKA-MDRVMEGRTSF 534
Cdd:COG3845 392 RTPGPDTPARSL---------S-GGNQ---QK--VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRlLELRDAGAAVL 456
|
250 260
....*....|....*....|....*
gi 488301890 535 VIAHRLSTIRE-ADLILVMKQGEII 558
Cdd:COG3845 457 LISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
346-392 |
8.79e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 8.79e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488301890 346 EFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLM 392
Cdd:PRK11147 321 EMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLML 366
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
24-184 |
8.80e-07 |
|
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: 50.93 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLPTT---EISRNIAAGESINFdYviqclIWI-LVVGTGYCVAQFLSGFLMTNVVQQSMR 99
Cdd:cd18604 3 LLLLLFVLSQLLSVGQSWWLGIWASayeTSSALPPSEVSVLY-Y-----LGIyALISLLSVLLGTLRYLLFFFGSLRASR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 DLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLS 179
Cdd:cd18604 77 KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALY 156
|
....*
gi 488301890 180 LIISR 184
Cdd:cd18604 157 VYIGR 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
365-569 |
1.17e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.45 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 365 NFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMN----RSDVRSvfGMVL------QDAWLYKGT 434
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDirspRDAIRA--GIMLcpedrkAEGIIPVHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 435 IADNI---------RFGKLdatdyeVVDAAKTANVDHFIRTM----PDGYEMEINSEGDNvslGQKQLLtiARAVISDPK 501
Cdd:PRK11288 348 VADNInisarrhhlRAGCL------INNRWEAENADRFIRSLniktPSREQLIMNLSGGN---QQKAIL--GRWLSEDMK 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 502 ILILDEATSSVDTRLEALIQKAMDRVME-GRTSFVIAHRL-STIREADLILVMKQGEIIEKGTHHELLEQ 569
Cdd:PRK11288 417 VILLDEPTRGIDVGAKHEIYNVIYELAAqGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATER 486
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
350-513 |
1.84e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.08 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 350 VSFSYDPEkPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtkKMNRSDVRSVFgmvlqdaw 429
Cdd:PRK13543 17 LAFSRNEE-PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG----KTATRGDRSRF-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 430 lykgtIADNIRFGKLDAtdyevvDAAKTANVdHFI--------RTMPD---------GYEMEINSEgdnVSLGQKQLLTI 492
Cdd:PRK13543 84 -----MAYLGHLPGLKA------DLSTLENL-HFLcglhgrraKQMPGsalaivglaGYEDTLVRQ---LSAGQKKRLAL 148
|
170 180
....*....|....*....|.
gi 488301890 493 ARAVISDPKILILDEATSSVD 513
Cdd:PRK13543 149 ARLWLSPAPLWLLDEPYANLD 169
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
345-513 |
1.95e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.34 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDpEKPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKidgidtkkmnRSDVRSVfGMV 424
Cdd:PRK09544 5 VSLENVSVSFG-QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK----------RNGKLRI-GYV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQDAWLYKGTIADNIRFGKL--DATDYEVVDAAKTANVDHFIRtmpdgYEMEinsegdNVSLGQKQLLTIARAVISDPKI 502
Cdd:PRK09544 73 PQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGHLID-----APMQ------KLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 488301890 503 LILDEATSSVD 513
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
321-521 |
2.58e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 321 EILDEPEEELneqDVPLPE--PILGSVEFENVSFSYdPEKPLI-RNLNFKVDAGQMVAIVGPTGAGKTTLINLlmrfydv 397
Cdd:PLN03073 486 AVVNDPDYKF---EFPTPDdrPGPPIISFSDASFGY-PGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKL------- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 398 tegaikIDGidtkkmnrsDVRSVFGMVLQDAwlykgtiadNIRFGKLDATDYEVVDAAKTANVdHFIRTMPDGYEMEINS 477
Cdd:PLN03073 555 ------ISG---------ELQPSSGTVFRSA---------KVRMAVFSQHHVDGLDLSSNPLL-YMMRCFPGVPEQKLRA 609
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 478 E------GDNVSL--------GQKQLLTIARAVISDPKILILDEATSSVD-TRLEALIQ 521
Cdd:PLN03073 610 HlgsfgvTGNLALqpmytlsgGQKSRVAFAKITFKKPHILLLDEPSNHLDlDAVEALIQ 668
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
346-559 |
4.68e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.40 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 346 EFENVSfSYDPEKplIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGIDTKKmnRSDVRSV-FGMV 424
Cdd:PRK09700 267 EVRNVT-SRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVkKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 L------QDAWLYKGTIADNI---RFGKLDATD-----YEVVDAAKTANVDhfiRTMPDGYEMEINSEGDNVSLGQKQLL 490
Cdd:PRK09700 342 YitesrrDNGFFPNFSIAQNMaisRSLKDGGYKgamglFHEVDEQRTAENQ---RELLALKCHSVNQNITELSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488301890 491 TIARAVISDPKILILDEATSSVDTRLEALIQKAMDRVM-EGRTSFVIAHRLSTIREA-DLILVMKQGEIIE 559
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
24-192 |
5.47e-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: 48.25 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGLptteISRNIAAGESINFDYviqclIWILVVGtgYCVAQFLSGFLMTNVVQQSMR---- 99
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGL----LISYLSSYPDEPLSE-----GYLLALA--LFLVSLLQSLLLHQYFFLSFRlgmr 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 100 ------DLrrdIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQsFINIVSAVLGIVMAVVMMF-LINPLM---A 169
Cdd:cd18579 70 vrsalsSL---IYRKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLF-LHYLWSAPLQIIVALYLLYrLLGWAAlagL 145
|
170 180
....*....|....*....|...
gi 488301890 170 IFSVIMIPLSLIISRTIVKISQK 192
Cdd:cd18579 146 GVLLLLIPLQAFLAKLISKLRKK 168
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-571 |
1.15e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.58 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 480 DNVSLGQKQLLTIARAVISDPKILILDEATSSVDT-------RLeaLIQKAM-DRVmegrTSFVIAHRLStirEA---DL 548
Cdd:NF033858 396 DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPvardmfwRL--LIELSReDGV----TIFISTHFMN---EAercDR 466
|
90 100
....*....|....*....|...
gi 488301890 549 ILVMKQGEIIEKGTHHELLEQGG 571
Cdd:NF033858 467 ISLMHAGRVLASDTPAALVAARG 489
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
371-567 |
1.43e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.49 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 371 GQMVAIVGPTGAGKTTLINLLMRF----YDVTEGAIKIDGIDTKKMNRSDVRSVFG----MVLQD--------------- 427
Cdd:PRK15093 33 GEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhnvsMIFQEpqscldpservgrql 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 -----AWLYKGTIADNIRFGKLDAtdYEVVDAAKTANVDHFIRTMPdgYEMeinsegdnvSLGQKQLLTIARAVISDPKI 502
Cdd:PRK15093 113 mqnipGWTYKGRWWQRFGWRKRRA--IELLHRVGIKDHKDAMRSFP--YEL---------TEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 503 LILDEATSSVDTRLEALIQKAMDRVME--GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELL 567
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
67-224 |
1.82e-05 |
|
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: 46.82 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 67 QCLIWILVVGTGYC---VAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNaMQQS 143
Cdd:cd18559 36 HGQVYLSVLGALAIlqgITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDS-MAPQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 144 FINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGR 223
Cdd:cd18559 115 VIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEW 194
|
.
gi 488301890 224 E 224
Cdd:cd18559 195 E 195
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
25-182 |
3.45e-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: 46.00 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 25 VILFTILTVAFNAALPYLTGLPTTEISRNIAAGESINFDYVIQCLIWILVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRD 104
Cdd:cd18574 1 AVLSALAAALVNIQIPLLLGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRND 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 105 IEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSLII 182
Cdd:cd18574 81 LFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLV 158
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
73-284 |
4.58e-05 |
|
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: 45.73 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 73 LVVGTGYCVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVL 152
Cdd:cd18558 66 LIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 153 GIVMAVVMMFLINPLMAIFSVIMIPLSLIISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFK 232
Cdd:cd18558 146 TFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYA 225
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488301890 233 QVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQ 284
Cdd:cd18558 226 QNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGE 277
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
47-193 |
4.66e-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: 45.60 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 47 TTEISRNIAAGESINFDYVIQCLIWILVVGTgycVAQFLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNIL 126
Cdd:cd18605 26 VSHSNNSFFNFINDSFNFFLTVYGFLAGLNS---LFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRIL 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 127 SRVTNDVDAVSNAMqQSFINIVSA-VLGIVMAVVMMFLINPLMAIFsviMIPLSLIISRtivkISQKY 193
Cdd:cd18605 103 NRFSSDVYTIDDSL-PFILNILLAqLFGLLGYLVVICYQLPWLLLL---LLPLAFIYYR----IQRYY 162
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
345-571 |
5.76e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.27 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 345 VEFENVSFSYDPEKPLiRNLNFKVDAGQMVAIVGPTGAGKTTLINLLmrfydvtEGAikidgidtKKMNRSDVRsVFGMV 424
Cdd:NF033858 2 ARLEGVSHRYGKTVAL-DDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGA--------RKIQQGRVE-VLGGD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 425 LQD-----------AWLYKG---------TIADNIRF-GKL---DATDYE--VVDAAKTANVDHFiRTMPDGyemeinse 478
Cdd:NF033858 65 MADarhrravcpriAYMPQGlgknlyptlSVFENLDFfGRLfgqDAAERRrrIDELLRATGLAPF-ADRPAG-------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 479 gdNVSLGQKQLLTIARAVISDPKILILDEATSSVD--TRLE--ALIqkamDRVMEGRTSF-VIahrLST--IREA---DL 548
Cdd:NF033858 136 --KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwELI----DRIRAERPGMsVL---VATayMEEAerfDW 206
|
250 260
....*....|....*....|...
gi 488301890 549 ILVMKQGEIIEKGTHHELLEQGG 571
Cdd:NF033858 207 LVAMDAGRVLATGTPAELLARTG 229
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
22-233 |
6.72e-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: 45.25 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 22 FYLVILFTILTVAFNA--------------ALPYLTGLPTTEISRNIAAGESINFdYVIQCLIWILVVgtgyCVAQFLSG 87
Cdd:cd18599 5 FLFVLLLFILSVGSTVfsdwwlsywlkqgsGNTTNNVDNSTVDSGNISDNPDLNF-YQLVYGGSILVI----LLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 88 FLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVS--------NAMQQSFinIVSAVLGIVMAVV 159
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDvrlpftleNFLQNVL--LVVFSLIIIAIVF 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488301890 160 MMFLIN--PLMAIFSVIMIplsliisrtIVKISQKYFQGMQN-SLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQ 233
Cdd:cd18599 158 PWFLIAliPLAIIFVFLSK---------IFRRAIRELKRLENiSRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKK 225
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
101-299 |
1.21e-04 |
|
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: 44.11 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAIFSVIMIPLSL 180
Cdd:cd18566 77 LSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IISRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFISGLMLPLVQMTA 260
Cdd:cd18566 156 LVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFS 235
|
170 180 190
....*....|....*....|....*....|....*....
gi 488301890 261 YGTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPM 299
Cdd:cd18566 236 QVSMVAVVAFGALLVINGDLTVGALIACTMLSGRVLQPL 274
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
358-573 |
3.01e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 358 KPLIRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDGidtKKMNRSD----VRSVFGMVLQD------ 427
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG---KKINNHNaneaINHGFALVTEErrstgi 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 428 -AWLYKG--TIADNIR-----FGKLDATDYE-----VVDAaktanvdhfIRTMPDGYEMEINSegdnVSLGQKQLLTIAR 494
Cdd:PRK10982 338 yAYLDIGfnSLISNIRnyknkVGLLDNSRMKsdtqwVIDS---------MRVKTPGHRTQIGS----LSGGNQQKVIIGR 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 495 AVISDPKILILDEATSSVDTRLEALI-QKAMDRVMEGRTSFVIAHRLSTIRE-ADLILVMKQGE---IIE--KGTHHELL 567
Cdd:PRK10982 405 WLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDtkTTTQNEIL 484
|
....*.
gi 488301890 568 EQGGFY 573
Cdd:PRK10982 485 RLASLH 490
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
25-303 |
4.13e-04 |
|
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: 42.52 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 25 VILFTILTVAFNAALPYLTGLPTTEISRNiaAGESInfdyVIQCLIWI-LVVGTGYCVAQFLSGFLMTNVVQQSMRDLRR 103
Cdd:cd18583 1 CFLCLLAERVLNVLVPRQLGIIVDSLSGG--SGKSP----WKEIGLYVlLRFLQSGGGLGLLRSWLWIPVEQYSYRALST 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 104 DIEEKINRLPVSYFDKNQQGNILsRVTNDVDAVSNAMQQSFINIVSAVLGIVMA-VVMMFLINPLMAIFSVIMIPLSLII 182
Cdd:cd18583 75 AAFNHVMNLSMDFHDSKKSGEVL-KAIEQGSSINDLLEQILFQIVPMIIDLVIAiVYLYYLFDPYMGLIVAVVMVLYVWS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 183 SRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLNGFGFKASFiSGLMLPLVQ---MT 259
Cdd:cd18583 154 TIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLF-SLNLLNAVQsliLT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 488301890 260 AygTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNIT 303
Cdd:cd18583 233 L--GLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFA 274
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
101-302 |
6.90e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 41.73 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 101 LRRDIEEKINRLPVSYFDKNQQGNILSRVtNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFLINPLMAifsVIMIPLSL 180
Cdd:cd18783 77 LALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLA---LVVLAFSA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 181 IISRTI---VKISQKYFQGMQNSLGDLNGYVQENMTGFSVLK---LYGREKETLE--GFKQVNHRLNgFGFKASFISGLM 252
Cdd:cd18783 153 LIALIIlafLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKslaLEPRQRREWDerVARAIRARFA-VGRLSNWPQTLT 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488301890 253 LPLVQMtaygTYIGVAVLGSYYVVAGVIVVGQLQAFIQYIWQISQPMGNI 302
Cdd:cd18783 232 GPLEKL----MTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQL 277
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
368-399 |
6.98e-04 |
|
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: 40.99 E-value: 6.98e-04
10 20 30
....*....|....*....|....*....|..
gi 488301890 368 VDAGQMVAIVGPTGAGKTTLINLLMRFYDVTE 399
Cdd:cd01130 9 VRARKNILISGGTGSGKTTLLNALLSFIPPDE 40
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
111-288 |
7.69e-04 |
|
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: 41.69 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 111 RLPVSYFDKNQQGNILSRV-TND--VDAVSNAMQQSFINIVSAVLgivmAVVMMFLINPLMA----IFSVIMIPLSLIIS 183
Cdd:cd18569 87 RLPVEFFSQRYAGDIASRVqSNDrvANLLSGQLATTVLNLVMAVF----YALLMLQYDVPLTligiAIALLNLLVLRLVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 184 RTIVKISQKyfqgMQNSLGDLNGYVqenMTGFSV---LKLYGREketlegfkqvnhrlNGF-----GFKASFIS------ 249
Cdd:cd18569 163 RKRVDLNRR----LLQDSGKLTGTT---MSGLQMietLKASGAE--------------SDFfsrwaGYQAKVLNaqqelg 221
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488301890 250 ------GLMLPLVQMTaygTYIGVAVLGSYYVVAGVIVVGQLQAF 288
Cdd:cd18569 222 rtnqllGALPTLLSAL---TNAAILGLGGLLVMDGALTIGMLVAF 263
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
361-561 |
1.52e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 40.00 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINllmrfydvtegaikiDGIDTKKMNR-SDVRSVFGmvlqdawlYKGTIadni 439
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------EGLYASGKARlISFLPKFS--------RNKLI---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 440 RFGKLdatdyevvdaaktanvdHFIRTMPDGYeMEINSEGDNVSLGQKQLLTIARAVISDPK--ILILDEATSSVDTR-L 516
Cdd:cd03238 64 FIDQL-----------------QFLIDVGLGY-LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQdI 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488301890 517 EALIQKAMDRVMEGRTSFVIAHRLSTIREADLILVM-----KQ-GEIIEKG 561
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFgpgsgKSgGKVVFSG 176
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
118-192 |
1.66e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 40.94 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 118 DKNQQGNILSRVTNDVDAVSNAMQQSFInIVSAVLGIVMAVVmmFLINpLM-------AIFSVIMIPLSLIISRTIVKIS 190
Cdd:cd18596 110 SSASVGKINNLMSVDANRISEFAAFLHL-LVSAPLQIVIAIV--FLYR-LLgwsalvgLAVMVLLLPLNGYLAKRYSRAQ 185
|
..
gi 488301890 191 QK 192
Cdd:cd18596 186 KE 187
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
107-289 |
1.94e-03 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 40.69 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 107 EKINRLPVSYFDKNQQGNILSRVTNDVDAVS----NAMQQSFINIVSAVLGIVMAvvmmFLINPLMAIFSVIMIPLSLII 182
Cdd:cd18562 77 EHVITLPLSFHSQRGSGRLLRIMLRGTDALFglwlGFFREHLAALVSLIVLLPVA----LWMNWRLALLLVVLAAVYAAL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 183 SRTIVKISQKYFQGMQNSLGDLNGYVQENMTGFSVLKLYGREKETLEGFKQVNHRLngfgFKASFIS----GLMLPLVQM 258
Cdd:cd18562 153 NRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRL----LAAQYPVlnwwALASVLTRA 228
|
170 180 190
....*....|....*....|....*....|.
gi 488301890 259 TAYGTYIGVAVLGSYYVVAGVIVVGQLQAFI 289
Cdd:cd18562 229 ASTLTMVAIFALGAWLVQRGELTVGEIVSFV 259
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
24-289 |
1.94e-03 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 40.61 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 24 LVILFTILTVAFNAALPYLTGlptteisrniaagesINFDYVI----QCLIWILVVGTG-YCVAQFLSGFLMTNVVQQsm 98
Cdd:cd18779 6 QILLASLLLQLLGLALPLLTG---------------VLVDRVIprgdRDLLGVLGLGLAaLVLTQLLAGLLRSHLLLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 99 rdLRRDIEEKIN--------RLPVSYFDKNQQGNILSRVTndvdavSNAMQQSFI--NIVSAVLGIVMAVV---MMFLIN 165
Cdd:cd18779 69 --LRTRLDTQLTlgflehllRLPYRFFQQRSTGDLLMRLS------SNATIRELLtsQTLSALLDGTLVLGylaLLFAQS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 166 PLMAI----FSVIMIPLSLIISRTIVKISQKYFQGMqnslGDLNGYVQENMTGFSVLKLYGREKETLEG-----FKQVNH 236
Cdd:cd18779 141 PLLGLvvlgLAALQVALLLATRRRVRELMARELAAQ----AEAQSYLVEALSGIETLKASGAEDRALDRwsnlfVDQLNA 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488301890 237 RLNGfGFKASFISGLMLpLVQMtayGTYIGVAVLGSYYVVAGVIVVGQLQAFI 289
Cdd:cd18779 217 SLRR-GRLDALVDALLA-TLRL---AAPLVLLWVGAWQVLDGQLSLGTMLALN 264
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
370-391 |
2.26e-03 |
|
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: 39.69 E-value: 2.26e-03
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
84-181 |
2.39e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 40.38 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 84 FLSGFLMTNVVQQSMRDLRRDIEEKINRLPVSYFDKNQQGNILSRVTNDVDAVSNAMQQSFINIVSAVLGIVMAVVMMFL 163
Cdd:cd18601 77 FLRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVV 156
|
90
....*....|....*...
gi 488301890 164 INPLMAIFsviMIPLSLI 181
Cdd:cd18601 157 VNPWVLIP---VIPLVIL 171
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
75-265 |
3.96e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 39.38 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 75 VGTGYCVAQFLSGFLMTNVVQQSMRDLRRD-----------IEEKINRLpvSYFDKNQ--QGNILSRVTNDVDAVSNAMQ 141
Cdd:cd18595 36 KGYLYAVLLFLVSIIQSLLLHQYFHRCFRLgmrirtaltsaIYRKALRL--SNSARKKstVGEIVNLMSVDAQRIQDLVP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 142 qsFINIV-SAVLGIVMAVVMMF-LINPlmAIFS-----VIMIPLSLIISRTIvkisqKYFQGMQNSLGD-----LNgyvq 209
Cdd:cd18595 114 --YLNMLwSAPLQIILALYFLWqTLGP--SVLAglgvmILLIPLNAVLARKI-----KKLQVKQMKLKDeriklMN---- 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 210 ENMTGFSVLKLYG------------REKEtLEGFKQVNHrLNGFgfkASFISGLMLPLVQMTAYGTYI 265
Cdd:cd18595 181 EILNGIKVLKLYAweesfekkilkiREKE-LKLLKKAAY-LNAV---SSFLWTCAPFLVSLATFATYV 243
|
|
| Gem1 |
COG1100 |
GTPase SAR1 family domain [General function prediction only]; |
374-408 |
5.55e-03 |
|
GTPase SAR1 family domain [General function prediction only];
Pssm-ID: 440717 [Multi-domain] Cd Length: 177 Bit Score: 38.04 E-value: 5.55e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488301890 374 VAIVGPTGAGKTTLINLLMR------FYDVTEGA------IKIDGID 408
Cdd:COG1100 6 IVVVGTGGVGKTSLVNRLVGdifsleKYLSTNGVtidkkeLKLDGLD 52
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
368-399 |
5.84e-03 |
|
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: 39.38 E-value: 5.84e-03
10 20 30
....*....|....*....|....*....|..
gi 488301890 368 VDAGQMVAIVGPTGAGKTTLINLLMRFYDVTE 399
Cdd:COG4962 179 VRARLNILVSGGTGSGKTTLLNALSGFIPPDE 210
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
361-578 |
6.29e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 361 IRNLNFKVDAGQMVAIVGPTGAGKTTLINLLMRFYDVTEGAIKIDG-IDTKKMNRSDVRSVFGMvlqdawlykgtiaDNI 439
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAISAGLSGQLTGI-------------ENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 440 RFgKLDATDYEVVDAAKTanvdhfirtMPDGYEME-----INSEGDNVSLGQKQLLTIARAVISDPKILILDEATSSVDt 514
Cdd:PRK13546 107 EF-KMLCMGFKRKEIKAM---------TPKIIEFSelgefIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488301890 515 rlEALIQKAMDRVME----GRTSFVIAHRLSTIRE-ADLILVMKQGEIIEKGTHHELLEQggfYEKLYN 578
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLN 239
|
|
| FlhF |
COG1419 |
Flagellar biosynthesis GTPase FlhF [Cell motility]; |
360-388 |
6.52e-03 |
|
Flagellar biosynthesis GTPase FlhF [Cell motility];
Pssm-ID: 441029 [Multi-domain] Cd Length: 361 Bit Score: 39.08 E-value: 6.52e-03
10 20 30
....*....|....*....|....*....|...
gi 488301890 360 LIRNLNFK----VDAGQMVAIVGPTGAGKTTLI 388
Cdd:COG1419 149 LARRLPVAedplLDEGGVIALVGPTGVGKTTTI 181
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
154-287 |
7.59e-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: 38.57 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488301890 154 IVMAVVMMFLINPLMAIFSVIMIPLSLIIS----RTIVKISQkyfQGMQNSlGDLNGYVQENMTGFSVLKLYGREKETLE 229
Cdd:cd18587 128 VLLFLAVIALIGGPLALVPLVAIPLVLLYGlllqKPLRRLVE---ESMRES-AQKNALLVESLSGLETIKALGAEGRMQR 203
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 488301890 230 GFKQVNHRLNGFGFKASFISGLMLPLVQMTAYGTYIGVAVLGSYYVVAGVIVVGQLQA 287
Cdd:cd18587 204 RWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLIA 261
|
|
| |
