|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-609 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 625.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 1 MSNIKKIIPFIYPYKKYAFLNIFFNVLYALFSTLSFVALIPMLQVLFDKnkqitekpvyhgilkiQDYGQdylsyyittt 80
Cdd:COG1132 6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG----------------GDLSA---------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 81 kgthesgyvLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNE 160
Cdd:COG1132 60 ---------LLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 161 VQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGL 240
Cdd:COG1132 131 VEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGI 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 241 KVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYN 320
Cdd:COG1132 211 RVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLV-LSGSLTVGDLVAFILYLLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 321 ILTPAKAISKASYGVKRGNAAAERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDET-VLKDFSLSIKKGQTV 399
Cdd:COG1132 290 LFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 400 ALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEA 479
Cdd:COG1132 370 ALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEA 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 480 LKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSI 559
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTI 529
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1776288214 560 VIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQSFES 609
Cdd:COG1132 530 VIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-605 |
9.48e-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: 461.61 E-value: 9.48e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 2 SNIKKIIPFIYPYKKyAFLNIFfnvLYALFSTLsfVALIPML--QVLFDKnkqitekpvyhgILKIQDYgqdylsyyitt 79
Cdd:COG2274 142 FGLRWFLRLLRRYRR-LLLQVL---LASLLINL--LALATPLftQVVIDR------------VLPNQDL----------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 80 tkgthESGYVLSIMVAIIIsifLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISaDVN 159
Cdd:COG2274 193 -----STLWVLAIGLLLAL---LFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVE 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 160 EVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGG 239
Cdd:COG2274 264 SIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRG 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 240 LKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAY 319
Cdd:COG2274 344 IETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLV-IDGQLTLGQLIAFNILSG 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 320 NILTPAKAISKASYGVKRGNAAAERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDET--VLKDFSLSIKKGQ 397
Cdd:COG2274 423 RFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGE 502
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 398 TVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEII 477
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEII 582
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 478 EALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRT 557
Cdd:COG2274 583 EAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRT 662
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1776288214 558 SIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:COG2274 663 VIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
89-605 |
4.81e-153 |
|
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: 452.25 E-value: 4.81e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:TIGR02203 52 VLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:TIGR02203 132 FIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGG 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLiDKSLDGAAFIAYMGLAYNILTPAKAI 328
Cdd:TIGR02203 212 QAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQ-AGSLTAGDFTAFITAMIALIRPLKSL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 329 SKASYGVKRGNAAAERVLEILDQENPITSKPDAIVKTSFDdsIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSG 406
Cdd:TIGR02203 291 TNVNAPMQRGLAAAESLFTLLDSPPEKDTGTRAIERARGD--VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 407 SGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIE-ALKIANA 485
Cdd:TIGR02203 369 SGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIErALAAAYA 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 486 FEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRL 565
Cdd:TIGR02203 449 QDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL 528
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1776288214 566 STIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:TIGR02203 529 STIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
95-605 |
2.18e-134 |
|
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: 404.85 E-value: 2.18e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 95 AIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVK 174
Cdd:TIGR02204 62 AFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 175 EPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNT 254
Cdd:TIGR02204 142 NALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 255 VFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLIDKSLDG--AAFIAYMGLAYNILTpakAISKAS 332
Cdd:TIGR02204 222 RFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGtlGQFVFYAVMVAGSIG---TLSEVW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 333 YGVKRGNAAAERVLEILDQENPIT--SKPDAIvKTSFDDSIEVKNINFKYQ---DETVLKDFSLSIKKGQTVALVGQSGS 407
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKapAHPKTL-PVPLRGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 408 GKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFE 487
Cdd:TIGR02204 378 GKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHE 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 488 FVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLST 567
Cdd:TIGR02204 458 FISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLAT 537
|
490 500 510
....*....|....*....|....*....|....*...
gi 1776288214 568 IQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:TIGR02204 538 VLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
371-601 |
2.15e-125 |
|
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: 368.87 E-value: 2.15e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKL 601
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
89-605 |
2.54e-125 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 381.67 E-value: 2.54e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:PRK11176 63 VLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:PRK11176 143 LITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 EnyfntvfQNSTERFFNLSNSIgNRQNL----ASPASEFMgITVIAIL----LWYGGQMVLIDKSLDGAAFIAYMGLAYN 320
Cdd:PRK11176 223 Q-------EVETKRFDKVSNRM-RQQGMkmvsASSISDPI-IQLIASLalafVLYAASFPSVMDTLTAGTITVVFSSMIA 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 321 ILTPAKAISKASYGVKRGNAAAERVLEILDQEnpiTSKPDAIVK-TSFDDSIEVKNINFKYQ--DETVLKDFSLSIKKGQ 397
Cdd:PRK11176 294 LMRPLKSLTNVNAQFQRGMAACQTLFAILDLE---QEKDEGKRViERAKGDIEFRNVTFTYPgkEVPALRNINFKIPAGK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 398 TVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDA-TDDEI 476
Cdd:PRK11176 371 TVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQI 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 477 IEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR 556
Cdd:PRK11176 451 EEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1776288214 557 TSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:PRK11176 531 TSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
371-605 |
6.18e-124 |
|
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: 365.32 E-value: 6.18e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY---QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
343-606 |
6.73e-116 |
|
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: 357.98 E-value: 6.73e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 343 ERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDE-TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYD 421
Cdd:COG5265 330 ERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 422 VNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIG 501
Cdd:COG5265 410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVG 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 502 DSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGK 581
Cdd:COG5265 490 ERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGR 569
|
250 260
....*....|....*....|....*
gi 1776288214 582 IVEQGTHDELIAHNGTYNKLVTMQS 606
Cdd:COG5265 570 IVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
122-601 |
2.31e-110 |
|
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: 342.52 E-value: 2.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 122 VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFL-AILELIVKEpLTIIFTITTMLIISPKLTLFVFIF 200
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLrVLLPLLVAL-LVILAAVAFLAFFSPALALVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 201 IPVSGYIISLIGKQL-KKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASP 279
Cdd:COG4987 165 LLLAGLLLPLLAARLgRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 280 ASEF-MGITVIAILLWyGGQMVlIDKSLDGAaFIAYMGLAynILT---PAKAISKASYGVKRGNAAAERVLEILDQENPI 355
Cdd:COG4987 245 LLQLaAGLAVVAVLWL-AAPLV-AAGALSGP-LLALLVLA--ALAlfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAV 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 356 TSKPDAIVKTSFDDsIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGIN 433
Cdd:COG4987 320 TEPAEPAPAPGGPS-LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 434 IKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQ 513
Cdd:COG4987 399 LRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
....*...
gi 1776288214 594 HNGTYNKL 601
Cdd:COG4987 559 QNGRYRQL 566
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
371-605 |
1.75e-109 |
|
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: 328.42 E-value: 1.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE-TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMI 529
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 530 LDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
90-596 |
1.11e-107 |
|
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: 335.19 E-value: 1.11e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITflRNG--VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNsFLA 167
Cdd:COG4988 57 LLPLLGLLLAVLLLRALLAWLRERAAF--RAAarVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDG-YFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 ------ILELIVkePLTIIFTITTMLIISPKLTLFVFIFIPVSgyiISLIGKQLKKQStKAQQEQ-----GTFLstieET 236
Cdd:COG4988 134 rylpqlFLAALV--PLLILVAVFPLDWLSGLILLVTAPLIPLF---MILVGKGAAKAS-RRQWRAlarlsGHFL----DR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 237 IGGLKVVKGYNSENYFNTVFQNSTERFfnlsnsignRQN---------LASPASEFM---GITVIAILLWY---GGQMVL 301
Cdd:COG4988 204 LRGLTTLKLFGRAKAEAERIAEASEDF---------RKRtmkvlrvafLSSAVLEFFaslSIALVAVYIGFrllGGSLTL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 302 idksldGAAFIAYMgLAYNILTPAKAISkASYGVKR-GNAAAERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKY 380
Cdd:COG4988 275 ------FAALFVLL-LAPEFFLPLRDLG-SFYHARAnGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 381 -QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDT 459
Cdd:COG4988 347 pGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGT 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 IKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDT 539
Cdd:COG4988 427 IRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDA 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 540 ESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNG 596
Cdd:COG4988 507 ETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
371-596 |
8.00e-106 |
|
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: 318.40 E-value: 8.00e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY-QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMI 529
Cdd:cd03254 83 LQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 530 LDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNG 596
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
84-602 |
1.26e-100 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 321.29 E-value: 1.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 84 HESGYVLSIMV------AIIISIFLLKNLAdyAAMFFITFLRNG--------VLRDMRNAMYKKTLELPLAFYSEKRKGD 149
Cdd:TIGR00958 182 FYTGRVIDTLGgdkgppALASAIFFMCLLS--IASSVSAGLRGGsfnytmarINLRIREDLFRSLLRQDLGFFDENKTGE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 150 VISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTF 229
Cdd:TIGR00958 260 LTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 230 LSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFnlsnSIGNRQNLASPA----SEFMGITVIAILLWYGGQMVLIDKS 305
Cdd:TIGR00958 340 NQVAEEALSGMRTVRSFAAEEGEASRFKEALEETL----QLNKRKALAYAGylwtTSVLGMLIQVLVLYYGGQLVLTGKV 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 306 LDG--AAFIAY-MGLAYNIltpaKAISKASYGVKRGNAAAERVLEILDQ----ENPITSKPDAIVKTsfddsIEVKNINF 378
Cdd:TIGR00958 416 SSGnlVSFLLYqEQLGEAV----RVLSYVYSGMMQAVGASEKVFEYLDRkpniPLTGTLAPLNLEGL-----IEFQDVSF 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 379 KY---QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSIL 455
Cdd:TIGR00958 487 SYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 456 FNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATS 535
Cdd:TIGR00958 567 FSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 536 ALDTESEKFVQVALEnmMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLV 602
Cdd:TIGR00958 647 ALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
119-605 |
2.38e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 309.20 E-value: 2.38e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 119 RNGVLRDMrnamYKKTLELPLAFYSEKRKGDVISRISADVNEV--------QNSFLAILELIVKEPLTiiftittmLIIS 190
Cdd:PRK13657 88 RLAVLTEY----FERIIQLPLAWHSQRGSGRALHTLLRGTDALfglwlefmREHLATLVALVVLLPLA--------LFMN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 191 PKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSN-- 268
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMpv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 269 -------SIGNRqnlASPASEFMGITVIAILLWYGGQMVLIDksldgaaFIAYMGLAYNILTPAKAISKASYGVKRGNAA 341
Cdd:PRK13657 236 lswwalaSVLNR---AASTITMLAILVLGAALVQKGQLRVGE-------VVAFVGFATLLIGRLDQVVAFINQVFMAAPK 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 342 AERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFY 420
Cdd:PRK13657 306 LEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 421 DVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNI 500
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVV 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 501 GDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKG 580
Cdd:PRK13657 466 GERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
490 500
....*....|....*....|....*
gi 1776288214 581 KIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:PRK13657 546 RVVESGSFDELVARGGRFAALLRAQ 570
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
19-345 |
3.88e-87 |
|
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: 272.76 E-value: 3.88e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 19 FLNIFFNVLYALFSTLSFVALIPMLQVLFDKNKQitekpvyhgilkiqdygqdylsyyitttkgthesgYVLSIMVAIII 98
Cdd:cd18552 2 ALAILGMILVAATTAALAWLLKPLLDDIFVEKDL-----------------------------------EALLLVPLAII 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 99 SIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLT 178
Cdd:cd18552 47 GLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 179 IIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQN 258
Cdd:cd18552 127 VIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 259 STERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPAKAISKASYGVKRG 338
Cdd:cd18552 207 ANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQV-ISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRG 285
|
....*..
gi 1776288214 339 NAAAERV 345
Cdd:cd18552 286 LAAAERI 292
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
371-605 |
5.43e-84 |
|
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: 262.81 E-value: 5.43e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQ 605
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
114-602 |
1.15e-83 |
|
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: 276.44 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 114 FITFLRNGVLRDMRNAMYKKT--------LELPLAFYSEKRKGDVISRISAdvNEVQNSFLA-ILELIVKEPLTIIFTIT 184
Cdd:TIGR03796 209 VLTWLQLYYLRRLEIKLAVGMsarflwhiLRLPVRFFAQRHAGDIASRVQL--NDQVAEFLSgQLATTALDAVMLVFYAL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 185 TMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTieeTIGGLKV---VKGYNSENYFNTVFQNSTE 261
Cdd:TIGR03796 287 LMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGV---AISGLQSietLKASGLESDFFSRWAGYQA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 262 RFFNLSNSIGNR-QNLASPASEFMGITVIAILLWyGGQMVlIDKSLDGAAFIAYMGLAYNILTPAKAISKASYGVKRGNA 340
Cdd:TIGR03796 364 KLLNAQQELGVLtQILGVLPTLLTSLNSALILVV-GGLRV-MEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEG 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 341 AAERVLEILDQ------ENPITSKPDAIVKTSFDDSIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTI 412
Cdd:TIGR03796 442 DLNRLDDVLRNpvdpllEEPEGSAATSEPPRRLSGYVELRNITFGYspLEPPLIENFSLTLQPGQRVALVGGSGSGKSTI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 413 ANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLgkLDAT--DDEIIEALKIANAFEFVN 490
Cdd:TIGR03796 522 AKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTL--WDPTipDADLVRACKDAAIHDVIT 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 491 ELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVqvaLENMMQnR--TSIVIAHRLSTI 568
Cdd:TIGR03796 600 SRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII---DDNLRR-RgcTCIIVAHRLSTI 675
|
490 500 510
....*....|....*....|....*....|....
gi 1776288214 569 QKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLV 602
Cdd:TIGR03796 676 RDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
371-581 |
2.36e-81 |
|
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: 253.07 E-value: 2.36e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANIslgkldatddeiiealkianafefvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGK 581
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
122-601 |
3.82e-76 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 253.21 E-value: 3.82e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 122 VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEpLTIIFTITTML-IISPKLTLFVFIF 200
Cdd:PRK11160 91 VLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLDHLYLRLISPLVAA-LVVILVLTIGLsFFDLTLALTLGGI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 201 IPVSGYIISLIGKQLKKQSTKAQ-QEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASP 279
Cdd:PRK11160 170 LLLLLLLLPLLFYRLGKKPGQDLtHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQTEQQWLAAQRRQANLTGLSQA 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 280 ASEFM-GITVIAILlWYGGQMVLiDKSLDGA--AFIAYMGLA-YNILTP-AKAISKASYGVkrgnAAAERVLEILDQENP 354
Cdd:PRK11160 250 LMILAnGLTVVLML-WLAAGGVG-GNAQPGAliALFVFAALAaFEALMPvAGAFQHLGQVI----ASARRINEITEQKPE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 355 ITSKPDAIVKTSfDDSIEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI 432
Cdd:PRK11160 324 VTFPTTSTAAAD-QVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 433 NIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALK---IANAFEfvNELPLGIYtnIGDSGNKLSG 509
Cdd:PRK11160 403 PIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQqvgLEKLLE--DDKGLNAW--LGEGGRQLSG 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 510 GQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHD 589
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQ 558
|
490
....*....|..
gi 1776288214 590 ELIAHNGTYNKL 601
Cdd:PRK11160 559 ELLAQQGRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
90-603 |
1.33e-75 |
|
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: 255.05 E-value: 1.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISaDVNevqnsflAIL 169
Cdd:TIGR01193 195 LGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DAS-------SII 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITTMLIIS-------PKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKV 242
Cdd:TIGR01193 267 DALASTILSLFLDMWILVIVGlflvrqnMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIET 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 243 VKGYNSENyfnTVFQNSTERFFNLSNSignrqNLASPASEF--------MGITVIAILLWYGGQMVLIDKsLDGAAFIAY 314
Cdd:TIGR01193 347 IKSLTSEA---ERYSKIDSEFGDYLNK-----SFKYQKADQgqqaikavTKLILNVVILWTGAYLVMRGK-LTLGQLITF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 315 MGLAYNILTPAKAISKASYGVKRGNAAAERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQ-DETVLKDFSLSI 393
Cdd:TIGR01193 418 NALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTI 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 394 KKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLG-KLDAT 472
Cdd:TIGR01193 498 KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVS 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 473 DDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENm 552
Cdd:TIGR01193 578 QDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN- 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 553 MQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVT 603
Cdd:TIGR01193 657 LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
129-605 |
3.93e-74 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 250.64 E-value: 3.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 129 AMYKKTLELPLAFYSEKRKGDVISRISAdVNEVQNsflAILELIVKEPLTIIFTITT---MLIISPKLTLFVFIFIPVSG 205
Cdd:TIGR03797 214 AVWDRLLRLPVSFFRQYSTGDLASRAMG-ISQIRR---ILSGSTLTTLLSGIFALLNlglMFYYSWKLALVAVALALVAI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 206 YIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMG 285
Cdd:TIGR03797 290 AVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVLP 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 286 ITVIAILLWYGGQMVLIDKsLDGAAFIAYMGLAYNILTPAKAISKASYGVkrgNAAA---ERVLEILD--QENPITSKPD 360
Cdd:TIGR03797 370 VLTSAALFAAAISLLGGAG-LSLGSFLAFNTAFGSFSGAVTQLSNTLISI---LAVIplwERAKPILEalPEVDEAKTDP 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 361 AIVKtsfdDSIEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN 438
Cdd:TIGR03797 446 GKLS----GAIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 439 LQSLRGLMGLVTQDSILFNDTIKANIsLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIA 518
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIA 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFVQVALENMmqNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTY 598
Cdd:TIGR03797 601 RALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLF 678
|
....*..
gi 1776288214 599 NKLVTMQ 605
Cdd:TIGR03797 679 AQLARRQ 685
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
370-587 |
1.02e-72 |
|
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: 232.77 E-value: 1.02e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:cd03244 2 DIEFKNVSLRYRPNlpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFNDTIKANI-SLGKldATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPP 526
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLdPFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
90-609 |
4.99e-72 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 241.93 E-value: 4.99e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLadYAAMFFITFLRNGVlrDMRNAMYKK-TLELPlAFYSEKRKGDVISRISADVNEVqnSFLA- 167
Cdd:PRK10789 39 IGTMVLIAVVVYLLRYV--WRVLLFGASYQLAV--ELREDFYRQlSRQHP-EFYLRHRTGDLMARATNDVDRV--VFAAg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 --ILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKG 245
Cdd:PRK10789 112 egVLTLVDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 246 YNSENYfntvfQNSteRFFNLSNSIGnRQNL--ASPASEFMGITVIAI----LLWYGGQ--MVLIDKSLDGA--AFIAYM 315
Cdd:PRK10789 192 FGLEDR-----QSA--LFAADAEDTG-KKNMrvARIDARFDPTIYIAIgmanLLAIGGGswMVVNGSLTLGQltSFVMYL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 316 GLaynILTPAKAISKASYGVKRGNAAAERVLEILDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDETVLKDFSLSIKK 395
Cdd:PRK10789 264 GL---MIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKP 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 396 GQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDE 475
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 476 IIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQN 555
Cdd:PRK10789 421 IEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEG 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 556 RTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYNKLVTMQSFES 609
Cdd:PRK10789 501 RTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEA 554
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
371-582 |
6.51e-72 |
|
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: 230.82 E-value: 6.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQ---DETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:cd03248 12 VKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKI 582
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
165-577 |
2.06e-70 |
|
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: 236.80 E-value: 2.06e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 165 FLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVsgYIIsLIGKQLKKQSTKAQQE----QGTFLstieETIGGL 240
Cdd:TIGR02857 121 YLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPI--FMI-LIGWAAQAAARKQWAAlsrlSGHFL----DRLRGL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 241 KVVKGYNSENYFNTVFQNSTERFfnlsnsignRQN---------LASPASEF---MGITVIAILL---WYGGQMVLIdks 305
Cdd:TIGR02857 194 PTLKLFGRAKAQAAAIRRSSEEY---------RERtmrvlriafLSSAVLELfatLSVALVAVYIgfrLLAGDLDLA--- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 306 ldgAAFIAYMgLAYNILTPAKAISkASYGVKR-GNAAAERVLEILDQENPITSkPDAIVKTSFDDSIEVKNINFKYQDET 384
Cdd:TIGR02857 262 ---TGLFVLL-LAPEFYLPLRQLG-AQYHARAdGVAAAEALFAVLDAAPRPLA-GKAPVTAAPASSLEFSGVSVAYPGRR 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 385 -VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKAN 463
Cdd:TIGR02857 336 pALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAEN 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 464 ISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEK 543
Cdd:TIGR02857 416 IRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
410 420 430
....*....|....*....|....*....|....
gi 1776288214 544 FVQVALENMMQNRTSIVIAHRLSTIQKADLIVVM 577
Cdd:TIGR02857 496 EVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
73-605 |
4.17e-68 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 231.92 E-value: 4.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 73 LSYYITTTKGTHEsgYVLSIMVAIIISIFLLKNLAdyAAM-FFITFLRN----GVLRDMRNAMYKKTLELPLAFYSEKRK 147
Cdd:PRK10790 46 ISYFIDNMVAKGN--LPLGLVAGLAAAYVGLQLLA--AGLhYAQSLLFNraavGVVQQLRTDVMDAALRQPLSAFDTQPV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 148 GDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSgYIISLIGKQLkkqSTKAQQEQG 227
Cdd:PRK10790 122 GQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIFPAV-LVVMVIYQRY---STPIVRRVR 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 228 TFLSTI----EETIGGLKVVKGYNSENYFntvfqnsterffnlsnsiGNRQNLASPA--------------------SEF 283
Cdd:PRK10790 198 AYLADIndgfNEVINGMSVIQQFRQQARF------------------GERMGEASRShymarmqtlrldgfllrpllSLF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 284 MGITVIAILLWYGGQMVlidksldGA-------AFIAYMG-LAYNI--LTPAKAIskasygVKRGNAAAERVLEILDQ-- 351
Cdd:PRK10790 260 SALILCGLLMLFGFSAS-------GTievgvlyAFISYLGrLNEPLieLTTQQSM------LQQAVVAGERVFELMDGpr 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 352 ------ENPITSkpdaivktsfdDSIEVKNINFKYQ-DETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVND 424
Cdd:PRK10790 327 qqygndDRPLQS-----------GRIDIDNVSFAYRdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 425 GTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKlDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSG 504
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQG 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 505 NKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVE 584
Cdd:PRK10790 475 NNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVE 554
|
570 580
....*....|....*....|.
gi 1776288214 585 QGTHDELIAHNGTYNKLVTMQ 605
Cdd:PRK10790 555 QGTHQQLLAAQGRYWQMYQLQ 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
369-586 |
8.60e-68 |
|
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: 219.77 E-value: 8.60e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLM 446
Cdd:cd03245 1 GRIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPP 526
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
341-598 |
2.24e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 222.03 E-value: 2.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 341 AAERVLEILDQENPITSKPDAIVKTSFDDSIEVKN-INFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF 419
Cdd:PRK11174 320 AAESLVTFLETPLAHPQQGEKELASNDPVTIEAEDlEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 420 --YDvndGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIY 497
Cdd:PRK11174 400 lpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLD 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 498 TNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVM 577
Cdd:PRK11174 477 TPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVM 556
|
250 260
....*....|....*....|.
gi 1776288214 578 QKGKIVEQGTHDELIAHNGTY 598
Cdd:PRK11174 557 QDGQIVQQGDYAELSQAGGLF 577
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
122-565 |
1.59e-59 |
|
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: 207.60 E-value: 1.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 122 VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFL-AILELIVKEPLTIIFTITTMLIiSPKLTLFVFIF 200
Cdd:TIGR02868 84 SLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVrVIVPAGVALVVGAAAVAAIAVL-SVPAALILAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 201 IPVSGYIISLIGKQLKKQSTKAQQEQ-GTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASP 279
Cdd:TIGR02868 163 LLLAGFVAPLVSLRAARAAEQALARLrGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 280 ASE-FMGITVIAiLLWYGGQMVLiDKSLDGAAFIAYMGLAYNILTPAKAISKASYGVKRGNAAAERVLEILDQENP--IT 356
Cdd:TIGR02868 243 LTLlAAGLAVLG-ALWAGGPAVA-DGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPvaEG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 357 SKPDAIVKTSFDDSIEVKNINFKY-QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIK 435
Cdd:TIGR02868 321 SAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 436 DMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRL 515
Cdd:TIGR02868 401 SLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRL 565
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-604 |
1.45e-54 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 201.03 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 2 SNIKKIIPFIYPYKKyaflniffNVLYALFSTLSFVALIPMLQVLFDKnkqitekpvYHGILKiqdygqDYLSYYITTTK 81
Cdd:PTZ00265 811 NNLRIVYREIFSYKK--------DVTIIALSILVAGGLYPVFALLYAK---------YVSTLF------DFANLEANSNK 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 82 gthesgYVLSIMVaIIISIFLLKNLADYaamfFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRK--GDVISRISADVN 159
Cdd:PTZ00265 868 ------YSLYILV-IAIAMFISETLKNY----YNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVH 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 160 EVQNSFLAilELIVKEPLTIIFTITTML------IISPKLTLFVFIFIPVSGyIISLIGKQLKKQSTKAQQEQGTFLST- 232
Cdd:PTZ00265 937 LLKTGLVN--NIVIFTHFIVLFLVSMVMsfyfcpIVAAVLTGTYFIFMRVFA-IRARLTANKDVEKKEINQPGTVFAYNs 1013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 233 -----------IEETIGGLKVVKGYNSENYFNTVFqnstERFFNLSNSIGNRQNLASPA----SEFMGITVIAILLWYGG 297
Cdd:PTZ00265 1014 ddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLI----EKAIDYSNKGQKRKTLVNSMlwgfSQSAQLFINSFAYWFGS 1089
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 298 QMV-----LIDKSLDGAAFIAYMGLAYNILTPAKAISKasygvkRGNAAAERVLEILDQENPITSKPDAIVKTS----FD 368
Cdd:PTZ00265 1090 FLIrrgtiLVDDFMKSLFTFLFTGSYAGKLMSLKGDSE------NAKLSFEKYYPLIIRKSNIDVRDNGGIRIKnkndIK 1163
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFKYQDET---VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDV----------------------- 422
Cdd:PTZ00265 1164 GKIEIMDVNFRYISRPnvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyq 1243
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 423 -------------------------------NDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDA 471
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA 1323
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 472 TDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALEN 551
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1403
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 552 MMQ--NRTSIVIAHRLSTIQKADLIVVM----QKGKIVE-QGTHDELI-AHNGTYNKLVTM 604
Cdd:PTZ00265 1404 IKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLsVQDGVYKKYVKL 1464
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
370-594 |
9.87e-53 |
|
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: 189.57 E-value: 9.87e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:COG4618 330 RLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFNDTIKANIS-LGklDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPP 526
Cdd:COG4618 410 YLPQDVELFDGTIAENIArFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
368-587 |
3.70e-51 |
|
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: 175.29 E-value: 3.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL 445
Cdd:cd03369 4 HGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQDSILFNDTIKANislgkLDA----TDDEIIEALKIAnafefvnelplgiytnigDSGNKLSGGQKQRLSIARAV 521
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSN-----LDPfdeySDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
187-609 |
2.03e-50 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 188.70 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 187 LIISPKLTLFVFIFIPVSgYIISLI-GKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENyfnTVFQNsterfFN 265
Cdd:PTZ00265 193 LFKNARLTLCITCVFPLI-YICGVIcNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEK---TILKK-----FN 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 266 LSNSIGNRQNLASPASEFMGITVI--------AILLWYGGQMVLIDKS-------LDGAAFIA-YMGLAYNILTPAKAIS 329
Cdd:PTZ00265 264 LSEKLYSKYILKANFMESLHIGMIngfilasyAFGFWYGTRIIISDLSnqqpnndFHGGSVISiLLGVLISMFMLTIILP 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 330 KASYGVKrGNAAAERVLEILDQEnPITSKPDAIVKTSFDDSIEVKNINFKY---QDETVLKDFSLSIKKGQTVALVGQSG 406
Cdd:PTZ00265 344 NITEYMK-SLEATNSLYEIINRK-PLVENNDDGKKLKDIKKIQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESG 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 407 SGKSTIANLMTRFYDVNDGTISI-DGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANI-----SLGKLDA--------- 471
Cdd:PTZ00265 422 CGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslySLKDLEAlsnyynedg 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 472 ----------------------------TDDEIIEALKIANAFE---------------FVNELPLGIYTNIGDSGNKLS 508
Cdd:PTZ00265 502 ndsqenknkrnscrakcagdlndmsnttDSNELIEMRKNYQTIKdsevvdvskkvlihdFVSALPDKYETLVGSNASKLS 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 509 GGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMM--QNRTSIVIAHRLSTIQKADLIVVM---QKGK-- 581
Cdd:PTZ00265 582 GGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrERGStv 661
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 582 ------------------------------------------IVEQGTHDELIAH-NGTYNKLVTMQSFES 609
Cdd:PTZ00265 662 dvdiigedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNkNGIYYTMINNQKVSS 732
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
257-594 |
6.41e-48 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 176.00 E-value: 6.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 257 QNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPakaISKASYGVK 336
Cdd:TIGR01842 207 GRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLA-IDGEITPGMMIAGSILVGRALAP---IDGAIGGWK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 337 RGNAAA---ERVLEILDQEnpiTSKPDAIVKTSFDDSIEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKST 411
Cdd:TIGR01842 283 QFSGARqayKRLNELLANY---PSRDPAMPLPEPEGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKST 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 412 IANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVNE 491
Cdd:TIGR01842 360 LARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 492 LPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRLSTIQK 570
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGC 519
|
330 340
....*....|....*....|....
gi 1776288214 571 ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
89-345 |
2.10e-47 |
|
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: 168.11 E-value: 2.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:cd07346 37 LLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:cd07346 117 LLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSL---DGAAFIAYMGLAYNiltPA 325
Cdd:cd07346 197 EEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLV-LQGSLtigELVAFLAYLGMLFG---PI 272
|
250 260
....*....|....*....|
gi 1776288214 326 KAISKASYGVKRGNAAAERV 345
Cdd:cd07346 273 QRLANLYNQLQQALASLERI 292
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
371-582 |
2.70e-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: 163.54 E-value: 2.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANIslgkldatddeiiealkianafefvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 529 ILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRLSTIQKADLIVVMQKGKI 582
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
371-594 |
4.93e-47 |
|
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: 164.81 E-value: 4.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQ--DSILFNDTIKANISLG--KLDATDDEII----EALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAV 521
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRerveEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
371-594 |
1.79e-45 |
|
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: 168.54 E-value: 1.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY-----QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL 445
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 ---MGLVTQD--SILF-NDTIKANIS-----LGKLDAtdDEIIEalKIANAFEFVnELPLGIYtnigdsgNK----LSGG 510
Cdd:COG1123 341 rrrVQMVFQDpySSLNpRMTVGDIIAeplrlHGLLSR--AERRE--RVAELLERV-GLPPDLA-------DRypheLSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 511 QKQRLSIARAVLKNPPIMILDEATSALDTEsekfVQVALENMMQ------NRTSIVIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:COG1123 409 QRQRVAIARALALEPKLLILDEPTSALDVS----VQAQILNLLRdlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|.
gi 1776288214 584 EQGTHDELIAH 594
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
124-598 |
3.26e-45 |
|
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: 172.82 E-value: 3.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 124 RDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTlfvfIFIPV 203
Cdd:TIGR00957 1038 RVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAA----VIIPP 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 204 SGYIISLI-------GKQLKKQSTKAQQeqgTFLSTIEETIGGLKVVKGYNSEnyfntvfqnstERFFNLSN-SIGNRQN 275
Cdd:TIGR00957 1114 LGLLYFFVqrfyvasSRQLKRLESVSRS---PVYSHFNETLLGVSVIRAFEEQ-----------ERFIHQSDlKVDENQK 1179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 276 LASP---ASEFMGITVIAI---LLWYGGQMVLIDKSLDGAAFIAyMGLAYN--ILTPAKAISKASYGVKRGNAAAERVLE 347
Cdd:TIGR00957 1180 AYYPsivANRWLAVRLECVgncIVLFAALFAVISRHSLSAGLVG-LSVSYSlqVTFYLNWLVRMSSEMETNIVAVERLKE 1258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 348 ILDQEnpiTSKPDAIVKTSFDDS------IEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF 419
Cdd:TIGR00957 1259 YSETE---KEAPWQIQETAPPSGwpprgrVEFRNYCLRYREdlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 420 YDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANislgkLDA----TDDEIIEALKIANAFEFVNELPLG 495
Cdd:TIGR00957 1336 NESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-----LDPfsqySDEEVWWALELAHLKTFVSALPDK 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 496 IYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIV 575
Cdd:TIGR00957 1411 LDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVI 1490
|
490 500
....*....|....*....|...
gi 1776288214 576 VMQKGKIVEQGTHDELIAHNGTY 598
Cdd:TIGR00957 1491 VLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
371-602 |
1.46e-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: 159.30 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANISLGKlDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03288 100 ILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAH-NGTYNKLV 602
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQeDGVFASLV 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
371-586 |
1.26e-43 |
|
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: 155.74 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLR 443
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSI-----------LFNDTIKANISLGKLDATDDEIIEAL-KIANAFEFVNELPlgiytnigdsgNKLSGGQ 511
Cdd:cd03257 82 KEIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEAVLLLLvGVGLPEEVLNRYP-----------HELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 512 KQRLSIARAVLKNPPIMILDEATSALDTEsekfVQVALENMMQ------NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVE 584
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVS----VQAQILDLLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
|
..
gi 1776288214 585 QG 586
Cdd:cd03257 227 EG 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
371-586 |
1.40e-43 |
|
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: 153.62 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLMGL 448
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANIslgkldatddeiiealkianafefvnelplgiytnigdsGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
371-593 |
2.49e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.22 E-value: 2.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDmNLQSLRGLMGLVT 450
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFND-TIKANISL-GKLDATDDEIIEAlKIANAFEFVNelplgiytnIGDSGNK----LSGGQKQRLSIARAVLKN 524
Cdd:COG1131 80 QEPALYPDlTVRENLRFfARLYGLPRKEARE-RIDELLELFG---------LTDAADRkvgtLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 525 PPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
371-594 |
1.60e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.84 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI--KDMNLQSLRGLMGL 448
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLG-----KLDATddeiiEALKIANAF-------EFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:COG1126 82 VFQQFNLFPHlTVLENVTLApikvkKMSKA-----EAEERAMELlervglaDKADAYP-----------AQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFV-----QVALENMmqnrTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHD 589
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPELVGEVldvmrDLAKEGM----TMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPE 221
|
....*
gi 1776288214 590 ELIAH 594
Cdd:COG1126 222 EFFEN 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
371-594 |
1.89e-42 |
|
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: 152.66 E-value: 1.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLMG 447
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFND-TIKANISL-----GKLDATDDEIIEALKIanafEFVnelplgiytNIGDSGNK----LSGGQKQRLSI 517
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKL----EAV---------GLRGAEDLypaeLSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALD-TESEKFVQVALE-NMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
371-591 |
6.40e-42 |
|
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: 150.79 E-value: 6.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN-----DGTISIDGINI--KDMNLQSLR 443
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIydLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSILFNDTIKANISLG------KLDATDDEIIE-ALKIANAFEFVNELPlgiytnigdSGNKLSGGQKQRLS 516
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEeALRKAALWDEVKDRL---------HALGLSGGQQQRLC 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
124-597 |
1.04e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.45 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 124 RDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISpklTLFVFIFIPV 203
Cdd:PLN03232 983 KRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS---TISLWAIMPL 1059
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 204 sgyIISLIGKQLKKQSTKAQQEQ------GTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSterffnLSNSIgnRQNLA 277
Cdd:PLN03232 1060 ---LILFYAAYLYYQSTSREVRRldsvtrSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKS------MDNNI--RFTLA 1128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 278 SPASE-FMGITVIAIllwyGGQMVLIDKSL---------DGAAFIAYMGLaynILTPAKAISKASYGVKRGNAAAERVLE 347
Cdd:PLN03232 1129 NTSSNrWLTIRLETL----GGVMIWLTATFavlrngnaeNQAGFASTMGL---LLSYTLNITTLLSGVLRQASKAENSLN 1201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 348 ILDQEN---PITSKPDAIVKTS-------FDDSIEVKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANL 415
Cdd:PLN03232 1202 SVERVGnyiDLPSEATAIIENNrpvsgwpSRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 416 MTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANISLGKlDATDDEIIEALKIANAFEFVNELPLG 495
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFS-EHNDADLWEALERAHIKDVIDRNPFG 1360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 496 IYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIV 575
Cdd:PLN03232 1361 LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440
|
490 500
....*....|....*....|..
gi 1776288214 576 VMQKGKIVEQGTHDELIAHNGT 597
Cdd:PLN03232 1441 VLSSGQVLEYDSPQELLSRDTS 1462
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
371-594 |
2.58e-41 |
|
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: 149.95 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNIN----FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLM 446
Cdd:COG1124 2 LEVRNLSvsygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSIL-FN------DTIKANISLGKLDATDDEIIEALKIAN-----AFEFVNElplgiytnigdsgnkLSGGQKQR 514
Cdd:COG1124 82 QMVFQDPYAsLHprhtvdRILAEPLRIHGLPDREERIAELLEQVGlppsfLDRYPHQ---------------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESEKFVqVALENMMQ---NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDE 590
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEI-LNLLKDLReerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225
|
....
gi 1776288214 591 LIAH 594
Cdd:COG1124 226 LLAG 229
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
372-581 |
4.08e-41 |
|
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: 148.38 E-value: 4.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQ--DSILFNDTIKANI--SLGKLDATDDEIIEalKIANAFEFVNELPLG---IYTnigdsgnkLSGGQKQRLSIARAVL 522
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVafGLENLGLPEEEIEE--RVEEALELVGLEGLRdrsPFT--------LSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 523 KNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTI-QKADLIVVMQKGK 581
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
371-594 |
4.91e-41 |
|
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: 156.22 E-value: 4.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN---DGTISIDGINIKDMNLQSLRGL 445
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQD--SILFNDTIKANI--SLGKLDATDDEIIEalKIANAFEFVnelplGIYTNIGDSGNKLSGGQKQRLSIARAV 521
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIaeALENLGLSRAEARA--RVLELLEAV-----GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTI-QKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
371-582 |
8.15e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 147.27 E-value: 8.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFNDTIKANI----SLGKLDATDDEIIEALKianAFEFvNELPLGiyTNIGDsgnkLSGGQKQRLSIARAVLKNPP 526
Cdd:COG4619 81 QEPALWGGTVRDNLpfpfQLRERKFDRERALELLE---RLGL-PPDILD--KPVER----LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKI 582
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
371-581 |
1.73e-40 |
|
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: 146.08 E-value: 1.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE-----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIdginikdmnlqslRGL 445
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV-------------PGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQDSILFNDTIKANISLGK-LDATD-DEIIEA------LKIanafefvneLPLGIYTNIGDSGNKLSGGQKQRLSI 517
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKpFDEERyEKVIKAcalepdLEI---------LPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEK--FVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGK 581
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRhiFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
372-581 |
7.00e-40 |
|
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: 142.77 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQ 451
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 dsilfndtikanislgkldatddeiiealkianafefvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:cd00267 81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 532 EATSALDTESEKFVQVALENMMQ-NRTSIVIAHRLSTIQKA-DLIVVMQKGK 581
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
371-592 |
1.86e-39 |
|
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: 145.19 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSIL-FNDTIKANISLG---------KLDATDDEII-EALKIANAFEF----VNELplgiytnigdsgnklSGGQKQRL 515
Cdd:COG1120 82 QEPPApFGLTVRELVALGryphlglfgRPSAEDREAVeEALERTGLEHLadrpVDEL---------------SGGERQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDtesekfV--QVALENMM------QNRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQG 586
Cdd:COG1120 147 LIARALAQEPPLLLLDEPTSHLD------LahQLEVLELLrrlareRGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
....*.
gi 1776288214 587 THDELI 592
Cdd:COG1120 221 PPEEVL 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
124-602 |
2.20e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 155.28 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 124 RDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSflaiLELIVKEPLTIIFT-ITTMLIISPKLTLFVFIFIP 202
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRN----VAVFVNMFLGQIFQlLSTFVLIGIVSTISLWAIMP 1061
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 203 VsgyIISLIGKQLKKQSTKAQQEQgtfLSTIE---------ETIGGLKVVKGYNSENYFNTVFQNS--TERFFNLSNSIG 271
Cdd:PLN03130 1062 L---LVLFYGAYLYYQSTAREVKR---LDSITrspvyaqfgEALNGLSTIRAYKAYDRMAEINGRSmdNNIRFTLVNMSS 1135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 272 NRqnlaspaseFMGI---TVIAILLWYGGQMVLID--KSLDGAAFIAYMGL----AYNILTPAKAISK-ASYGVKRGNAA 341
Cdd:PLN03130 1136 NR---------WLAIrleTLGGLMIWLTASFAVMQngRAENQAAFASTMGLllsyALNITSLLTAVLRlASLAENSLNAV 1206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 342 aERVLEILD--QENPI---TSKPDAIVKTSfdDSIEVKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIAN 414
Cdd:PLN03130 1207 -ERVGTYIDlpSEAPLvieNNRPPPGWPSS--GSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLN 1283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 415 LMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANislgkLDA----TDDEIIEALKIANAFEFVN 490
Cdd:PLN03130 1284 ALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN-----LDPfnehNDADLWESLERAHLKDVIR 1358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 491 ELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK 570
Cdd:PLN03130 1359 RNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID 1438
|
490 500 510
....*....|....*....|....*....|...
gi 1776288214 571 ADLIVVMQKGKIVEQGTHDELIAH-NGTYNKLV 602
Cdd:PLN03130 1439 CDRILVLDAGRVVEFDTPENLLSNeGSAFSKMV 1471
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
371-595 |
3.94e-39 |
|
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: 143.58 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLMG 447
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFND-TIKANISLG---KLDATDDEIIE--ALKIanafEFVNeLPlgiytnigDSGNK----LSGGQKQRLSI 517
Cdd:COG1127 86 MLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRElvLEKL----ELVG-LP--------GAADKmpseLSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALD--TeSEKFVQVALEnmMQNR---TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDpiT-SAVIDELIRE--LRDElglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
....
gi 1776288214 592 IAHN 595
Cdd:COG1127 230 LASD 233
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
386-535 |
1.12e-38 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 139.32 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFND-TIKANI 464
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 465 SLGKLDATDDEIIEALKIANAFEFVNeLPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATS 535
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
371-596 |
1.46e-38 |
|
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: 142.30 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQsLRGLMGLVT 450
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-NDTIKANIS-LGKLDATDDEIIEAlKIANAFEFVnELPLGIYTNIGdsgnKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:COG4555 81 DERGLYdRLTVRENIRyFAELYGLFDEELKK-RIEELIELL-GLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAHNG 596
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
371-595 |
1.61e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 143.23 E-value: 1.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY--QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQ--DSILFNDTIKANISLGkLD---ATDDEIIE----ALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIAR 519
Cdd:PRK13635 86 VFQnpDNQFVGATVQDDVAFG-LEnigVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHN 595
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
371-586 |
4.27e-38 |
|
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: 139.96 E-value: 4.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQsLRGLmGLVT 450
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNI-GMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-NDTIKANISLG------KLDATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVLK 523
Cdd:cd03259 79 QDYALFpHLTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
371-594 |
7.18e-38 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.03 E-value: 7.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDM-NLQSLRGLMG 447
Cdd:TIGR04520 1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQ--DSILFNDTIKANISLG----KLDAtdDEII----EALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSI 517
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDVAFGlenlGVPR--EEMRkrvdEALKLVGMEDFRDREP-----------HLLSGGQKQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEKFV-QVALE-NMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVlETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
371-581 |
8.03e-37 |
|
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: 135.39 E-value: 8.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQS--LRGLMGL 448
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILF-NDTIKANISLGkldatddeiiealkianafefvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03229 81 VFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQN--RTSIVIAHRLSTIQK-ADLIVVMQKGK 581
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
371-594 |
1.69e-36 |
|
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: 138.65 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNIN--FKYQDETV--LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN---DGTISIDGINIKDMN---LQ 440
Cdd:COG0444 2 LEVRNLKvyFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGL-MGLVTQDSIL-FN----------DTIKANISLGKLDAtDDEIIEALK---IANAFEFVNELPlgiytnigdsgN 505
Cdd:COG0444 82 KIRGReIQMIFQDPMTsLNpvmtvgdqiaEPLRIHGGLSKAEA-RERAIELLErvgLPDPERRLDRYP-----------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 506 KLSGGQKQRLSIARAVLKNPPIMILDEATSALD-TesekfVQVALENMMQN-----RTSIV-IAHRLSTIQK-ADLIVVM 577
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQILNLLKDlqrelGLAILfITHDLGVVAEiADRVAVM 224
|
250
....*....|....*..
gi 1776288214 578 QKGKIVEQGTHDELIAH 594
Cdd:COG0444 225 YAGRIVEEGPVEELFEN 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
371-594 |
1.75e-36 |
|
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: 136.17 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQD----ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLR 443
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSILFND-TIKANISLG-KLDATDDEIIEAlKIANAFEFVnelplGIYTNIGDSGNKLSGGQKQRLSIARAV 521
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE-RVLELLELV-----GLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
372-586 |
4.38e-36 |
|
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: 133.33 E-value: 4.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQ 451
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 dsilfndtikanislgkldatddeIIEALKIAN-AFEFVNElplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPIMIL 530
Cdd:cd03214 81 ------------------------ALELLGLAHlADRPFNE---------------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 531 DEATSALD--TESEKFVQVALENMMQNRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQG 586
Cdd:cd03214 122 DEPTSHLDiaHQIELLELLRRLARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
371-594 |
7.19e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 134.74 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQD-ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILF-NDTIKANISL-GKLDATDDEIIEAlKIANAFEFVNelpLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03295 81 IQQIGLFpHMTVEENIALvPKLLKWPKEKIRE-RADELLALVG---LDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRL-STIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
371-585 |
7.35e-36 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 7.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLR 443
Cdd:COG1136 5 LELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 G-LMGLVTQDSILFND-TIKANISL----GKLDATDD-----EIIEALKIAnafEFVNELPlgiytnigdsgNKLSGGQK 512
Cdd:COG1136 85 RrHIGFVFQFFNLLPElTALENVALplllAGVSRKERrerarELLERVGLG---DRLDHRP-----------SQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQKADLIVVMQKGKIVEQ 585
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
371-582 |
7.64e-36 |
|
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: 133.77 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLR 443
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GL-MGLVTQDSILFND-TIKANISL-----GKLDATDDE-IIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:cd03255 81 RRhIGFVFQSFNLLPDlTALENVELplllaGVPKKERRErAEELLERVGLGDRLNHYP-----------SELSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFVQVALENM--MQNRTSIVIAHRLSTIQKADLIVVMQKGKI 582
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-598 |
9.75e-36 |
|
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: 144.32 E-value: 9.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 23 FFNVLYALFSTlSFvalipMLQVLFdknKQITEKPVYHG--ILKIqdygqdyLSYYITTTKGTHESGYVLSIMVaIIISI 100
Cdd:TIGR00957 307 LFKVLYKTFGP-YF-----LMSFCF---KAIHDLMMFIGpqILSL-------LIRFVNDPMAPDWQGYFYTGLL-FVCAC 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 101 FLLKNLADYAAMFFITFLR--NGVLrdmrNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNsFLAILELIVKEPLT 178
Cdd:TIGR00957 370 LQTLILHQYFHICFVSGMRikTAVM----GAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMD-LATYINMIWSAPLQ 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 179 IIFTITTM-LIISPKL---TLFVFIFIPVSGyiisLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYF-N 253
Cdd:TIGR00957 445 VILALYFLwLNLGPSVlagVAVMVLMVPLNA----VMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAFlD 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 254 TVFQNSTERFFNLSNS-----IGNRQNLASPaseFMgitVIAILLWYggqMVLIDKS--LDgaAFIAYMGLA-YNILT-P 324
Cdd:TIGR00957 521 KVEGIRQEELKVLKKSaylhaVGTFTWVCTP---FL---VALITFAV---YVTVDENniLD--AEKAFVSLAlFNILRfP 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 325 AKAISKASYGVKRGNAAAERVLEILDQENpitSKPDAI----VKTSFDDSIEVKNINFKY--QDETVLKDFSLSIKKGQT 398
Cdd:TIGR00957 590 LNILPMVISSIVQASVSLKRLRIFLSHEE---LEPDSIerrtIKPGEGNSITVHNATFTWarDLPPTLNGITFSIPEGAL 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 399 VALVGQSGSGKSTIANLMTRFYDVNDGTISIdginikdmnlqslRGLMGLVTQDSILFNDTIKANISLGKL--DATDDEI 476
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-------------KGSVAYVPQQAWIQNDSLRENILFGKAlnEKYYQQV 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 477 IEALKIANAFEFvneLPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFV---QVALENMM 553
Cdd:TIGR00957 734 LEACALLPDLEI---LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfehVIGPEGVL 810
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1776288214 554 QNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTY 598
Cdd:TIGR00957 811 KNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
86-345 |
1.53e-35 |
|
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: 135.30 E-value: 1.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 86 SGYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSF 165
Cdd:cd18576 31 DTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 166 LAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKG 245
Cdd:cd18576 111 TTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 246 YNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNIltpA 325
Cdd:cd18576 191 FTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLV-LAGELTAGDLVAFLLYTLFI---A 266
|
250 260
....*....|....*....|...
gi 1776288214 326 KAISKAS--YG-VKRGNAAAERV 345
Cdd:cd18576 267 GSIGSLAdlYGqLQKALGASERV 289
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
371-582 |
1.69e-35 |
|
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: 132.65 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI--KDMNLQSLRGLMGL 448
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILF-NDTIKANISLGKL-------DATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARA 520
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLAPIkvkgmskAEAEERALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 521 VLKNPPIMILDEATSALDTESEKFV-----QVALENMmqnrTSIVIAHRLSTIQK-ADLIVVMQKGKI 582
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVldvmkDLAEEGM----TMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
85-345 |
7.41e-35 |
|
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: 133.33 E-value: 7.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 85 ESGYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNS 164
Cdd:cd18551 30 SAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLREL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 165 FLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVK 244
Cdd:cd18551 110 ITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 245 GYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTP 324
Cdd:cd18551 190 ASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV-ASGALTVGTLVAFLLYLFQLITP 268
|
250 260
....*....|....*....|.
gi 1776288214 325 AKAISKASYGVKRGNAAAERV 345
Cdd:cd18551 269 LSQLSSFFTQLQKALGALERI 289
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
371-582 |
1.30e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 129.05 E-value: 1.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDmNLQSLRGLMGLVT 450
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFND-TIKANIslgkldatddeiiealkianafefvnelplgiytnigdsgnKLSGGQKQRLSIARAVLKNPPIMI 529
Cdd:cd03230 80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 530 LDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKI 582
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
88-345 |
2.17e-34 |
|
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: 132.15 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSIMVAIIISifllknladYAAMFF--ITFLRNGVL--RDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQN 163
Cdd:cd18541 42 YALLILLLALLI---------GIFRFLwrYLIFGASRRieYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 164 SF----LAILELIVkeplTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGG 239
Cdd:cd18541 113 ALgpgiLYLVDALF----LGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSG 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 240 LKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSL---DGAAFIAYMG 316
Cdd:cd18541 189 IRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLV-IRGTItlgDLVAFNSYLG 267
|
250 260 270
....*....|....*....|....*....|
gi 1776288214 317 LayniLT-PAKAISKASYGVKRGNAAAERV 345
Cdd:cd18541 268 M----LIwPMMALGWVINLIQRGAASLKRI 293
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
89-345 |
3.57e-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: 350008 [Multi-domain] Cd Length: 307 Bit Score: 131.87 E-value: 3.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:cd18564 52 LLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:cd18564 132 VLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGR 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlidksLDGA-------AFIAYMGLAYni 321
Cdd:cd18564 212 EEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLV-----LAGRltpgdllVFLAYLKNLY-- 284
|
250 260
....*....|....*....|....
gi 1776288214 322 lTPAKAISKASYGVKRGNAAAERV 345
Cdd:cd18564 285 -KPVRDLAKLTGRIAKASASAERV 307
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
371-591 |
3.66e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.88 E-value: 3.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQ--DSILFNDTIKANISLG------KLDATDDEIIEALKIANAFEFVNELPLgiytnigdsgnKLSGGQKQRLSIARA 520
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 521 VLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
90-345 |
7.77e-34 |
|
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: 130.63 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAIL 169
Cdd:cd18542 38 LWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSE 249
Cdd:cd18542 118 VELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFARE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 250 NYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPAKAIS 329
Cdd:cd18542 198 DYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLV-INGEITLGELVAFISYLWMLIWPVRQLG 276
|
250
....*....|....*.
gi 1776288214 330 KASYGVKRGNAAAERV 345
Cdd:cd18542 277 RLINDMSRASASAERI 292
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
368-591 |
1.06e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.00 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVND-----GTISIDGINI--KDMNLQ 440
Cdd:COG1117 9 EPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPgarveGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQDSILFNDTIKANISLG-----KLDATD-DEIIE-ALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQ 513
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSElDEIVEeSLRKAALWDEVKD-------RLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKfvqvALENMMQ---NRTSIVI-------AHRLStiqkaDLIVVMQKGKIV 583
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTA----KIEELILelkKDYTIVIvthnmqqAARVS-----DYTAFFYLGELV 232
|
....*...
gi 1776288214 584 EQGTHDEL 591
Cdd:COG1117 233 EFGPTEQI 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
5.95e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 5.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:PRK13648 8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQ--DSILFNDTIKANISLG------KLDATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARA 520
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAGV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 521 VLKNPPIMILDEATSALDTESEK--FVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQnlLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
370-591 |
6.80e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 129.45 E-value: 6.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNlqSL----RGl 445
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVT--GLppekRN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQDSILF-NDTIKANISLG-KLDATDDEIIEAlKIANAFEFVnelplgiytNIGDSGNK----LSGGQKQRLSIAR 519
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRA-RVAELLELV---------GLEGLADRyphqLSGGQQQRVALAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLS---TIqkADLIVVMQKGKIVEQGTHDEL 591
Cdd:COG3842 149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
372-583 |
1.15e-32 |
|
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: 124.68 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNLQSLRGLMGLVT 450
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDS--ILFNDTIKANISLGKLDATDD-EIIEA-LKIANAFEFVNELPLgiytnigdsgnKLSGGQKQRLSIARAVLKNPP 526
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAGnEQAETvLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 527 IMILDEATSALDTE-----SEKFVQVALenmmQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:cd03226 147 LLIFDEPTSGLDYKnmervGELIRELAA----QGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
371-584 |
2.48e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.39 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY-QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLM 446
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFND-TIKANISLGkLDAT--DDEIIEAlKIANAFEFVnelplgiytNIGDSGNK----LSGGQKQRLSIAR 519
Cdd:COG2884 82 GVVFQDFRLLPDrTVYENVALP-LRVTgkSRKEIRR-RVREVLDLV---------GLSDKAKAlpheLSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 520 AVLKNPPIMILDEATSALDTE-SEKFVQVaLENMMQNRTSIVIA-HRLSTIQKADL-IVVMQKGKIVE 584
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
371-591 |
2.63e-32 |
|
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: 124.66 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIkdMNLQSLRGLMGLVT 450
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFND-TIKANISLG-KLDATDDEII-----EALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVLK 523
Cdd:cd03300 79 QNYALFPHlTVFENIAFGlRLKKLPKAEIkervaEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:cd03300 148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
371-595 |
5.98e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.33 E-value: 5.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETvlKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLmglvt 450
Cdd:COG3840 2 LRLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-PAERPV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 qdSILFND-------TIKANISLG-----KLDATD-DEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSI 517
Cdd:COG3840 74 --SMLFQEnnlfphlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALD----TESEKFV-QVALEnmmQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVdELCRE---RGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
....
gi 1776288214 592 IAHN 595
Cdd:COG3840 218 LDGE 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
370-590 |
1.34e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.00 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI--KDMNLQSL 442
Cdd:PRK13637 2 SIKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQ--DSILFNDTIKANISLG--KLDATDDEIIEalKIANAFEFVnelplGI-YTNIGD-SGNKLSGGQKQRLS 516
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIEN--RVKRAMNIV-----GLdYEDYKDkSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 517 IARAVLKNPPIMILDEATSALD--TESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDE 590
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
390-594 |
1.66e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.84 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 390 SLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL---MGLVTQDSilfndtikanisL 466
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP------------Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 467 GKLDA--TDDEII-EALKI------ANAFEFVNEL-------PlgiytnigDSGNK----LSGGQKQRLSIARAVLKNPP 526
Cdd:COG4608 106 ASLNPrmTVGDIIaEPLRIhglaskAERRERVAELlelvglrP--------EHADRypheFSGGQRQRIGIARALALNPK 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 527 IMILDEATSALDteseKFVQVALENMM---QNR---TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG4608 178 LIVCDEPVSALD----VSIQAQVLNLLedlQDElglTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
90-345 |
6.91e-31 |
|
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: 122.51 E-value: 6.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAIL 169
Cdd:cd18547 44 LLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSE 249
Cdd:cd18547 124 TQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 250 NYFNTVFQNSTERFFNLS---NSIGnrqNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPAK 326
Cdd:cd18547 204 EEAIEEFDEINEELYKASfkaQFYS---GLLMPIMNFINNLGYVLVAVVGGLLV-INGALTVGVIQAFLQYSRQFSQPIN 279
|
250
....*....|....*....
gi 1776288214 327 AISKASYGVKRGNAAAERV 345
Cdd:cd18547 280 QISQQINSLQSALAGAERV 298
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
371-595 |
7.03e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.96 E-value: 7.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdMNLQSLRGLMGLVT 450
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-----KPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QdSILFNDTIKAN----ISLG---------KLDATDDEII-EALKIANAFEFVNelplgiyTNIGDsgnkLSGGQKQRLS 516
Cdd:COG1121 82 Q-RAEVDWDFPITvrdvVLMGrygrrglfrRPSRADREAVdEALERVGLEDLAD-------RPIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEK-FVQVaLENM-MQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEaLYEL-LRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAHGPPEEVLTP 228
|
..
gi 1776288214 594 HN 595
Cdd:COG1121 229 EN 230
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
90-345 |
7.42e-31 |
|
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: 122.26 E-value: 7.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAIL 169
Cdd:cd18778 39 LLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSE 249
Cdd:cd18778 119 PQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGRE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 250 NYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLIDK-SL-DGAAFIAYMGLAYnilTPAKA 327
Cdd:cd18778 199 EEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGElTIgDLVAFLLYLGLFY---EPITS 275
|
250
....*....|....*...
gi 1776288214 328 ISKASYGVKRGNAAAERV 345
Cdd:cd18778 276 LHGLNEMLQRALAGAERV 293
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
372-586 |
8.10e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 119.56 E-value: 8.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTRFydvnDGTISIDGINIKDMnlqslRGLMG 447
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTllkaILGLLKPT----SGSIRVFGKPLEKE-----RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSIL---FNDTIKANISLG---------KLDATDDEII-EALKIANAFEFVNElplgiytNIGdsgnKLSGGQKQR 514
Cdd:cd03235 72 YVPQRRSIdrdFPISVRDVVLMGlyghkglfrRLSKADKAKVdEALERVGLSELADR-------QIG----ELSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
371-594 |
1.59e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 122.49 E-value: 1.59e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY----QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIA---NLMTRFydvNDGTISIDGINIKDMNLQSLR 443
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLERP---TSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GL---MGLVTQDSILFND-TIKANISLG-KLDATDDEIIEAlKIANAFEFVNelplgiytnIGDSGNK----LSGGQKQR 514
Cdd:COG1135 79 AArrkIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEIRK-RVAELLELVG---------LSDKADAypsqLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALD---TES---------EKFvqvalenmmqNRTSIVIAHRLSTIQK-ADLIVVMQKGK 581
Cdd:COG1135 149 VGIARALANNPKVLLCDEATSALDpetTRSildllkdinREL----------GLTIVLITHEMDVVRRiCDRVAVLENGR 218
|
250
....*....|...
gi 1776288214 582 IVEQGTHDELIAH 594
Cdd:COG1135 219 IVEQGPVLDVFAN 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
371-594 |
2.02e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.43 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD--MNLQSLRGLMGL 448
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLGKLDatddeiIEALKIANAFEFVNEL--PLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNP 525
Cdd:PRK09493 82 VFQQFYLFPHlTALENVMFGPLR------VRGASKEEAEKQARELlaKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 526 PIMILDEATSALDTESEKFV-----QVALENMmqnrTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVlkvmqDLAEEGM----TMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
371-585 |
2.48e-30 |
|
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: 118.34 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlQSLRGL- 445
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 --MGLVTQDSILFN-DTIKANISLGkLDATDDEIIEALKIANAF-------EFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:cd03293 73 pdRGYVFQQDALLPwLTVLDNVALG-LELQGVPKAEARERAEELlelvglsGFENAYP-----------HQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLS-TIQKADLIVVMQK--GKIVEQ 585
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
371-591 |
3.37e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.01 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLM 446
Cdd:COG3638 3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDsilFN-----DTIKaNISLGKLDAT-----------DDEIIEALKianAFEFVNelplgiytnIGDSGNK---- 506
Cdd:COG3638 83 GMIFQQ---FNlvprlSVLT-NVLAGRLGRTstwrsllglfpPEDRERALE---ALERVG---------LADKAYQradq 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 507 LSGGQKQRLSIARAVLKNPPIMILDEATSALDTES-----EKFVQVALEnmmQNRTSIVIAHRLSTIQK-ADLIVVMQKG 580
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARE---DGITVVVNLHQVDLARRyADRIIGLRDG 223
|
250
....*....|.
gi 1776288214 581 KIVEQGTHDEL 591
Cdd:COG3638 224 RVVFDGPPAEL 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
122-582 |
3.87e-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: 126.95 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 122 VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSF-LAILELIvKEPLTIIFTITTMLIISPKLTL----F 196
Cdd:TIGR01271 956 VSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLpLTLFDFI-QLTLIVLGAIFVVSVLQPYIFIaaipV 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 197 VFIFIPVSGYIISlIGKQLKKQSTKAQQEQGTFLSTieeTIGGLKVVKGYNSENYFNTVFQNSterfFNLSNSIGNRQnL 276
Cdd:TIGR01271 1035 AVIFIMLRAYFLR-TSQQLKQLESEARSPIFSHLIT---SLKGLWTIRAFGRQSYFETLFHKA----LNLHTANWFLY-L 1105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 277 ASPASEFMGITVIAILLWYGGQMVLIDKSLDGAAFIAY-MGLAYNILTPAKAISKASYGVKRGNAAAERVLEILD--QEN 353
Cdd:TIGR01271 1106 STLRWFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIiLTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDlpQEE 1185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 354 PITSKPDAIVKTSFDDSIE---------------VKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLM 416
Cdd:TIGR01271 1186 PRPSGGGGKYQLSTVLVIEnphaqkcwpsggqmdVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 417 TRFYDVnDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTIKANislgkLDA----TDDEIIEALKIANAFEFVNEL 492
Cdd:TIGR01271 1266 LRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN-----LDPyeqwSDEEIWKVAEEVGLKSVIEQF 1339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 493 PLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKAD 572
Cdd:TIGR01271 1340 PDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQ 1419
|
490
....*....|
gi 1776288214 573 LIVVMQKGKI 582
Cdd:TIGR01271 1420 QFLVIEGSSV 1429
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
371-591 |
5.81e-30 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 118.05 E-value: 5.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY-QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI---KDMNLQSLRGLM 446
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFND-TIKANISLGKLDA-----------TDDEIIEALKianAFEFVNELPLgIYTNIGdsgnKLSGGQKQR 514
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALA---ALERVGLLDK-AYQRAD----QLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESEKFVQVALE--NMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
368-591 |
8.62e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.65 E-value: 8.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDE------TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDM-NLQ 440
Cdd:PRK13633 2 NEMIKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQ--DSILFNDTIKANISLG--KLDATDDEII----EALKIANAFEFVNELPlgiytnigdsgNKLSGGQK 512
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIRervdESLKKVGMYEYRRHAP-----------HLLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALE--NMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDE 590
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 1776288214 591 L 591
Cdd:PRK13633 231 I 231
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
386-594 |
1.27e-29 |
|
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: 118.13 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL----MGLVTQDSILF-NDTI 460
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLGKLDATDDEIIEALKIANAFEFVNelplgiytnIGDSGNK----LSGGQKQRLSIARAVLKNPPIMILDEATSA 536
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVG---------LEGWEHKypdeLSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 537 LDTESEKFVQ---VALENMMQnRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03294 191 LDPLIRREMQdelLRLQAELQ-KTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
368-593 |
1.65e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.91 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKY---QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRG 444
Cdd:PRK13650 2 SNIIEVKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 LMGLVTQ--DSILFNDTIKANISLG------KLDATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLS 516
Cdd:PRK13650 82 KIGMVFQnpDNQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
89-345 |
1.95e-29 |
|
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: 118.05 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:cd18557 34 VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:cd18557 114 LSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLiDKSLDGAAFIAYMGLAYNILTPAKAI 328
Cdd:cd18557 194 EEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASSVGGL 272
|
250
....*....|....*..
gi 1776288214 329 SKASYGVKRGNAAAERV 345
Cdd:cd18557 273 SSLLADIMKALGASERV 289
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
371-591 |
2.49e-29 |
|
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: 115.68 E-value: 2.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNIN--FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKdMNLQSLRGLMGL 448
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISL-----GKLDATDDEIIEALKianafefvnelplgIYTNIGDSGNK----LSGGQKQRLSIA 518
Cdd:cd03263 80 CPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLL--------------RVLGLTDKANKrartLSGGMKRKLSLA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHrlsTIQKADL----IVVMQKGKIVEQGTHDEL 591
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAEAlcdrIAIMSDGKLRCIGSPQEL 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
370-589 |
2.98e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 2.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKST---IANLMTRfydVNDGTISIDG--------INIKDMn 438
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGnhfdfsktPSDKAI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 439 lQSLRGLMGLVTQDSILF------NDTIKANISLGKLDATD-----DEIIEALKIAnafEFVNELPLgiytnigdsgnKL 507
Cdd:PRK11124 78 -RELRRNVGMVFQQYNLWphltvqQNLIEAPCRVLGLSKDQalaraEKLLERLRLK---PYADRFPL-----------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 508 SGGQKQRLSIARAVLKNPPIMILDEATSALDTE-SEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQ 585
Cdd:PRK11124 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222
|
....
gi 1776288214 586 GTHD 589
Cdd:PRK11124 223 GDAS 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
129-602 |
3.16e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.93 E-value: 3.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 129 AMYKKTLELPlafySEKRK----GDVISRISADVNEVQNSFLaILELIVKEPLTIIftiTTMLIISPKL-------TLFV 197
Cdd:PLN03232 379 AIFHKSLRLT----HEARKnfasGKVTNMITTDANALQQIAE-QLHGLWSAPFRII---VSMVLLYQQLgvaslfgSLIL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 198 FIFIPVSGYIISligkQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTerffNLSNSIGNRQNLA 277
Cdd:PLN03232 451 FLLIPLQTLIVR----KMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIR----NEELSWFRKAQLL 522
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 278 SPASEFM--GITVIAILLWYGgQMVLIDKSLDGAAFIAYMGLAYNILTPAKAISKASYGVKRGNAAAERVLEILDQENPI 355
Cdd:PLN03232 523 SAFNSFIlnSIPVVVTLVSFG-VFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERI 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 356 TSKPDAIVKTSfdDSIEVKNINFKYQDET---VLKDFSLSIKKGQTVALVGQSGSGK-STIANLMTRFYDVNDGTISIdg 431
Cdd:PLN03232 602 LAQNPPLQPGA--PAISIKNGYFSWDSKTskpTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVI-- 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 432 inikdmnlqslRGLMGLVTQDSILFNDTIKANISLGKlDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQ 511
Cdd:PLN03232 678 -----------RGSVAYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQ 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 512 KQRLSIARAVLKNPPIMILDEATSALDTE-SEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDE 590
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
490
....*....|..
gi 1776288214 591 LIAHNGTYNKLV 602
Cdd:PLN03232 826 LSKSGSLFKKLM 837
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
370-591 |
4.88e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 4.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNlqSL----RGl 445
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVT--DLppkdRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQDSILF-NDTIKANISLG----KLDATD-----DEIIEALKIAnafEFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPKAEidrrvREAAELLGLE---DLLDRKP-----------KQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDtesekfvqVALENMMqnRTSIVIAHR---LSTI-----QK-----ADLIVVMQKGKI 582
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLD--------AKLRVEM--RAEIKRLHRrlgTTTIyvthdQVeamtlADRIAVMNDGRI 212
|
....*....
gi 1776288214 583 VEQGTHDEL 591
Cdd:COG3839 213 QQVGTPEEL 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
370-589 |
9.07e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.72 E-value: 9.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--------INIKDMnlQS 441
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAI--RL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRGLMGLVTQDSILF------NDTIKANI---SLGKLDATD--DEIIEALKIAnafEFVNELPLgiytnigdsgnKLSGG 510
Cdd:COG4161 80 LRQKVGMVFQQYNLWphltvmENLIEAPCkvlGLSKEQAREkaMKLLARLRLT---DKADRFPL-----------HLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 511 QKQRLSIARAVLKNPPIMILDEATSALDTE-SEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTH 588
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
.
gi 1776288214 589 D 589
Cdd:COG4161 226 S 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
371-584 |
1.75e-28 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 114.42 E-value: 1.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQslrglM 446
Cdd:COG1116 8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFN-DTIKANISLGkLDATDDEIIEALKIANAF-------EFVNELPlgiytnigdsgNKLSGGQKQRLSIA 518
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERARELlelvglaGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 519 RAVLKNPPIMILDEATSALDtesekfvqvAL--ENMMQ---------NRTSIVIAH------RLstiqkADLIVVMQK-- 579
Cdd:COG1116 151 RALANDPEVLLMDEPFGALD---------ALtrERLQDellrlwqetGKTVLFVTHdvdeavFL-----ADRVVVLSArp 216
|
....*
gi 1776288214 580 GKIVE 584
Cdd:COG1116 217 GRIVE 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
371-594 |
2.07e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 114.08 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI---KDMNLQ-----SL 442
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQkglirQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILF-NDTIKANISLGKLdatddeIIEALKIANAFEFVNELplgiYTNIGDSGN------KLSGGQKQRL 515
Cdd:PRK11264 84 RQHVGFVFQNFNLFpHRTVLENIIEGPV------IVKGEPKEEATARAREL----LAKVGLAGKetsyprRLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ-NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
.
gi 1776288214 594 H 594
Cdd:PRK11264 234 D 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
366-586 |
2.17e-28 |
|
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: 112.26 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 366 SFDD-SIEVKNINFKYQdETVLKDFSLSIKKGQTVALVGQSGSGKSTIAN-LMTRFYDVND-GTISIDGINIKdmnLQSL 442
Cdd:cd03213 5 SFRNlTVTVKSSPSKSG-KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGVsGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILFndtikanislgkldatddeiiEALKIANAFEFVNELplgiytnigdsgNKLSGGQKQRLSIARAVL 522
Cdd:cd03213 81 RKIIGYVPQDDILH---------------------PTLTVRETLMFAAKL------------RGLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 523 KNPPIMILDEATSALDTESEKFVQVALENMMQ-NRTSIVIAHRLST--IQKADLIVVMQKGKIVEQG 586
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
370-594 |
2.18e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.40 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTrfydVNDGTISIDGiniKDM--NLQSL- 442
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLET----PDSGRIVLNG---RDLftNLPPRe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGlMGLVTQDSILF-NDTIKANISLG----KLDATD-----DEIIEALKIAnafEFVNELPlgiytnigdsgNKLSGGQK 512
Cdd:COG1118 75 RR-VGFVFQHYALFpHMTVAENIAFGlrvrPPSKAEirarvEELLELVQLE---GLADRYP-----------SQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTesekFVQVALENMM------QNRTSIVIAH------RLstiqkADLIVVMQKG 580
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEPFGALDA----KVRKELRRWLrrlhdeLGGTTVFVTHdqeealEL-----ADRVVVMNQG 210
|
250
....*....|....
gi 1776288214 581 KIVEQGTHDELIAH 594
Cdd:COG1118 211 RIEQVGTPDEVYDR 224
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
77-345 |
2.22e-28 |
|
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: 115.30 E-value: 2.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 77 ITTTKGTHESGYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISA 156
Cdd:cd18563 29 VLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 157 DVNEVQNsFLA--ILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIE 234
Cdd:cd18563 109 DTDRLQD-FLSdgLPDFLT-NILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLN 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 235 ETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEF-MGITVIaILLWYGGQMVLIDK-SLdGA--A 310
Cdd:cd18563 187 DTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFlTSLGTL-IVWYFGGRQVLSGTmTL-GTlvA 264
|
250 260 270
....*....|....*....|....*....|....*
gi 1776288214 311 FIAYMGLAYnilTPAKAISKASYGVKRGNAAAERV 345
Cdd:cd18563 265 FLSYLGMFY---GPLQWLSRLNNWITRALTSAERI 296
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
370-592 |
2.53e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 121.42 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:PTZ00243 1308 SLVFEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFNDTIKANISlGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSG 1466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 528 MIL-DEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELI 592
Cdd:PTZ00243 1467 FILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
87-584 |
5.81e-28 |
|
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: 118.36 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 87 GYVLSIMVAIIISIfllknladyAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFL 166
Cdd:COG4615 53 LFAGLLVLLLLSRL---------ASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 167 AILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVK-- 244
Cdd:COG4615 124 RLPELLQ-SVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKln 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 245 GYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLIDKS-LDGAAFIAYMglaynILT 323
Cdd:COG4615 203 RRRRRAFFDEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWADPAvLSGFVLVLLF-----LRG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 324 PAKAISKASYGVKRGNAAAERVLEI---LDQENPITSKPDAIVKTSFDDSIEVKNINFKYQDET-----VLKDFSLSIKK 395
Cdd:COG4615 278 PLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRR 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 396 GQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSILFNDTikanisLGKLDATDDE 475
Cdd:COG4615 358 GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPA 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 476 IIEA----LKIANAFEFVNelplGIYTNIgdsgnKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTE-SEKFVQVALE 550
Cdd:COG4615 432 RAREllerLELDHKVSVED----GRFSTT-----DLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfRRVFYTELLP 502
|
490 500 510
....*....|....*....|....*....|....*
gi 1776288214 551 NMM-QNRTSIVIAHRLSTIQKADLIVVMQKGKIVE 584
Cdd:COG4615 503 ELKaRGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
370-597 |
2.04e-27 |
|
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: 110.89 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlRGLmGLV 449
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RNV-GFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISLG------KLDATDDEIIEalKIANAFEFVNelplgiYTNIGDS-GNKLSGGQKQRLSIARAV 521
Cdd:cd03296 80 FQHYALFRHmTVFDNVAFGlrvkprSERPPEAEIRA--KVHELLKLVQ------LDWLADRyPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDELIAHNGT 597
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
368-587 |
2.30e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.02 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD------ 436
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 437 ----------MNLQSLRGLMGLVTQ--DSILFNDTIKANISLGKLdATDDEIIEALKIAnAFeFVNELPLGiYTNIGDSG 504
Cdd:PRK13631 99 litnpyskkiKNFKELRRRVSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLA-KF-YLNKMGLD-DSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 505 NKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEK-FVQVALENMMQNRTSIVIAHRLSTI-QKADLIVVMQKGKI 582
Cdd:PRK13631 175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKI 254
|
....*
gi 1776288214 583 VEQGT 587
Cdd:PRK13631 255 LKTGT 259
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
371-586 |
2.31e-27 |
|
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: 109.98 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTvALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLMGLVT 450
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDsILFNDTIKA-----------NISLGKLDAtddEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIAR 519
Cdd:cd03264 79 QE-FGVYPNFTVrefldyiawlkGIPSKEVKA---RVDEVLELVNLGDRAKKKI-----------GSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 520 AVLKNPPIMILDEATSALDTESekfvQVALENMMQ----NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEE----RIRFRNLLSelgeDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
368-591 |
2.63e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFY---DVNDGTISIDGINIKDMNLQSL 442
Cdd:PRK13640 3 DNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQ--DSILFNDTIKANISLGkLDATDDEIIEALKIANafEFVNELplGIYTNIGDSGNKLSGGQKQRLSIARA 520
Cdd:PRK13640 83 REKVGIVFQnpDNQFVGATVGDDVAFG-LENRAVPRPEMIKIVR--DVLADV--GMLDYIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 521 VLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
109-301 |
3.42e-27 |
|
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: 111.20 E-value: 3.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 109 YAAMFFITFLRNGVL--------RDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTII 180
Cdd:pfam00664 51 GLAQFILSFLQSYLLnhtgerlsRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 181 FTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNST 260
Cdd:pfam00664 131 GGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKAL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776288214 261 ERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVL 301
Cdd:pfam00664 211 EEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVI 251
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
368-596 |
5.11e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLM 446
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQ--DSILFNDTIKANISLG--KLDATDDEII----EALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIA 518
Cdd:PRK13647 82 GLVFQdpDDQVFSSTVWDDVAFGpvNMGLDKDEVErrveEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLS-TIQKADLIVVMQKGKIVEQG-----THDEL 591
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDI 230
|
....*
gi 1776288214 592 IAHNG 596
Cdd:PRK13647 231 VEQAG 235
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
194-601 |
5.41e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 117.15 E-value: 5.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 194 TLFVFIFIPVSGYIISligkQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTerffNLSNSIGNR 273
Cdd:PLN03130 447 SLMLVLMFPIQTFIIS----KMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVR----DDELSWFRK 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 274 QNLASPASEFM--GITVIAILLWYGgqmvlidksldgaaFIAYMGlayNILTPAKAISKAS-YGVKR------------- 337
Cdd:PLN03130 519 AQLLSAFNSFIlnSIPVLVTVVSFG--------------VFTLLG---GDLTPARAFTSLSlFAVLRfplfmlpnlitqa 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 338 --GNAAAERVLEILDQENPITSkPDAIVKTSFDdSIEVKNINFKYQ---DETVLKDFSLSIKKGQTVALVGQSGSGK-ST 411
Cdd:PLN03130 582 vnANVSLKRLEELLLAEERVLL-PNPPLEPGLP-AISIKNGYFSWDskaERPTLSNINLDVPVGSLVAIVGSTGEGKtSL 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 412 IANLMTRFYDVNDGTISIdginikdmnlqslRGLMGLVTQDSILFNDTIKANISLGK-LDATDDEiiEALKIANAFEFVN 490
Cdd:PLN03130 660 ISAMLGELPPRSDASVVI-------------RGTVAYVPQVSWIFNATVRDNILFGSpFDPERYE--RAIDVTALQHDLD 724
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 491 ELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFV-QVALENMMQNRTSIVIAHRLSTIQ 569
Cdd:PLN03130 725 LLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLS 804
|
410 420 430
....*....|....*....|....*....|..
gi 1776288214 570 KADLIVVMQKGKIVEQGTHDELIAHNGTYNKL 601
Cdd:PLN03130 805 QVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
90-345 |
5.55e-27 |
|
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: 111.00 E-value: 5.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISaDVNEVQNSF-LAI 168
Cdd:cd18570 41 LNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAIsSTT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:cd18570 120 ISLFL-DLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPAKAI 328
Cdd:cd18570 199 EEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLV-IKGQLSLGQLIAFNALLGYFLGPIENL 277
|
250
....*....|....*..
gi 1776288214 329 SKASYGVKRGNAAAERV 345
Cdd:cd18570 278 INLQPKIQEAKVAADRL 294
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
371-586 |
8.21e-27 |
|
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: 108.35 E-value: 8.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVlkDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQslRGLMGLVT 450
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFND-TIKANISLG-----KLDATDDEIIE-ALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVLK 523
Cdd:cd03298 77 QENNLFAHlTVEQNVGLGlspglKLTAEDRQAIEvALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03298 146 DKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
371-582 |
8.39e-27 |
|
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: 109.94 E-value: 8.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQD--ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVnDGTISIDGINIKDMNLQSLRGLMGL 448
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANIS-LGKLdaTDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03289 82 IPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKI 582
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
376-594 |
8.74e-27 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 109.89 E-value: 8.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 376 INFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL---MGLVTQD 452
Cdd:TIGR02769 17 LFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 453 SI-LFN--DTIKANIS-----LGKLDATDDE--IIEALKIAN-AFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAV 521
Cdd:TIGR02769 97 SPsAVNprMTVRQIIGeplrhLTSLDESEQKarIAELLDMVGlRSEDADKLP-----------RQLSGGQLQRINIARAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQ--GTHDELIAH 594
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEEcdVAQLLSFKH 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
371-593 |
9.44e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.18 E-value: 9.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET---VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMG 447
Cdd:PRK13642 5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQ--DSILFNDTIKANISLGKLDA--TDDEII----EALKIANAFEFVNELPLgiytnigdsgnKLSGGQKQRLSIAR 519
Cdd:PRK13642 85 MVFQnpDNQFVGATVEDDVAFGMENQgiPREEMIkrvdEALLAVNMLDFKTREPA-----------RLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
89-345 |
9.91e-27 |
|
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: 110.26 E-value: 9.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAI 168
Cdd:cd18550 37 LLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEET--IGGLKVVKGY 246
Cdd:cd18550 117 LTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLF 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 247 NSENYFntvfqnsTERFFNLSN---SIGNRQNLASpASEFMGITVI-----AILLWYGGQMVlIDKSLD-GA--AFIAYM 315
Cdd:cd18550 197 GREDDE-------AARFARRSRelrDLGVRQALAG-RWFFAALGLFtaigpALVYWVGGLLV-IGGGLTiGTlvAFTALL 267
|
250 260 270
....*....|....*....|....*....|
gi 1776288214 316 GlayNILTPAKAISKASYGVKRGNAAAERV 345
Cdd:cd18550 268 G---RLYGPLTQLLNIQVDLMTSLALFERI 294
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
386-594 |
1.08e-26 |
|
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: 114.40 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDvNDGTISIDGINIKDMN---LQSLRGLMGLVTQD---SilFND- 458
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgS--LSPr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 459 -TIKANISLG------KLDAT--DDEIIEALK-------IANAF--EFvnelplgiytnigdsgnklSGGQKQRLSIARA 520
Cdd:COG4172 379 mTVGQIIAEGlrvhgpGLSAAerRARVAEALEevgldpaARHRYphEF-------------------SGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 521 VLKNPPIMILDEATSALD-TesekfVQ---VALENMMQNR---TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELI 592
Cdd:COG4172 440 LILEPKLLVLDEPTSALDvS-----VQaqiLDLLRDLQREhglAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVF 514
|
..
gi 1776288214 593 AH 594
Cdd:COG4172 515 DA 516
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
91-301 |
1.45e-26 |
|
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: 109.88 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 91 SIMVAIIISIFLlkNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILE 170
Cdd:cd18575 38 AFLLLLAVALVL--ALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 171 LIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSEN 250
Cdd:cd18575 116 IALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTRED 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 251 YFNTVFQNSTERFFNLSNS-IGNRQNLASPASeFMGITVIAILLWYGGQMVL 301
Cdd:cd18575 196 AERQRFATAVEAAFAAALRrIRARALLTALVI-FLVFGAIVFVLWLGAHDVL 246
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
90-345 |
1.86e-26 |
|
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: 109.49 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNsFLAIL 169
Cdd:cd18543 38 LWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQR-FLAFG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSE 249
Cdd:cd18543 117 PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 250 NYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPAKAIS 329
Cdd:cd18543 197 RRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLV-ANGSLTLGTLVAFSAYLTMLVWPVRMLG 275
|
250
....*....|....*.
gi 1776288214 330 KASYGVKRGNAAAERV 345
Cdd:cd18543 276 WLLAMAQRARAAAERV 291
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
93-316 |
1.98e-26 |
|
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: 109.48 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 93 MVAIIISIFLLKNLADYAAMF----FITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSF-LA 167
Cdd:cd18545 38 GLLIIALLFLALNLVNWVASRlriyLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLsNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 ILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYN 247
Cdd:cd18545 118 LINLIP-DLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 248 SENYfntvfqnSTERFFNLSNSigNRQ---------NLASPASEFMGITVIAILLWYGGQMVLIDKSLDG--AAFIAYMG 316
Cdd:cd18545 197 REDE-------NEEIFDELNRE--NRKanmravrlnALFWPLVELISALGTALVYWYGGKLVLGGAITVGvlVAFIGYVG 267
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
371-586 |
2.93e-26 |
|
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: 106.53 E-value: 2.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDmnLQSLRGLMGLVT 450
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-------NDTIKANIsLGKLDATDDEIIEalkianafefvnelplgiYTNIGDSGNK----LSGGQKQRLSIAR 519
Cdd:cd03268 79 EAPGFYpnltareNLRLLARL-LGIRKKRIDEVLD------------------VVGLKDSAKKkvkgFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
371-562 |
3.34e-26 |
|
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: 106.41 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTRFydvnDGTISIDGINIKDmNLQSLRGLM 446
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLPPS----AGEVLWNGEPIRD-AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFND-TIKANI----SLGKLDATDDEIIEALKIAN--AFEfvnELPLGiytnigdsgnKLSGGQKQRLSIAR 519
Cdd:COG4133 78 AYLGHADGLKPElTVRENLrfwaALYGLRADREAIDEALEAVGlaGLA---DLPVR----------QLSAGQKRRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA 562
Cdd:COG4133 145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLT 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
370-593 |
3.76e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.71 E-value: 3.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI----KDMNLQ 440
Cdd:PRK13646 2 TIRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQ--DSILFNDTIKANISLGKLDATDDeiIEALKiANAFEFVneLPLGIYTNI-GDSGNKLSGGQKQRLSI 517
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVK-NYAHRLL--MDLGFSRDVmSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEKFVQVALENMM--QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
371-562 |
4.22e-26 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 106.34 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETV-LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI---KDMNLQSLRGLM 446
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDS-ILFNDTIKANI--SLGKLDATDDEIIEalKIANAFEFVnelplGIYTNIGDSGNKLSGGQKQRLSIARAVLK 523
Cdd:cd03292 81 GVVFQDFrLLPDRNVYENVafALEVTGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIVN 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA 562
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
386-586 |
4.31e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 106.23 E-value: 4.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIK---KGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD----MNLQSLRGLMGLVTQDSILF-N 457
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 458 DTIKANISLG---KLDATD----DEIIEALKIanafefvnelplgiyTNIGDSG-NKLSGGQKQRLSIARAVLKNPPIMI 529
Cdd:cd03297 90 LNVRENLAFGlkrKRNREDrisvDELLDLLGL---------------DHLLNRYpAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 530 LDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
70-345 |
5.04e-26 |
|
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: 108.24 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 70 QDYLSYYITTTKGTHESgyvLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGD 149
Cdd:cd18544 23 KRAIDDYIVPGQGDLQG---LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 150 VISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLigkqLKKQSTKAQQEQGTF 229
Cdd:cd18544 100 LVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL----FRKKSRKAYREVREK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 230 LSTI----EETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSnsigNRQNLAS----PASEFMGITVIAILLWYGGQMVl 301
Cdd:cd18544 176 LSRLnaflQESISGMSVIQLFNREKREFEEFDEINQEYRKAN----LKSIKLFalfrPLVELLSSLALALVLWYGGGQV- 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 302 idksLDGA-------AFIAYMG--------LA--YNILtpakaiskasygvKRGNAAAERV 345
Cdd:cd18544 251 ----LSGAvtlgvlyAFIQYIQrffrpirdLAekFNIL-------------QSAMASAERI 294
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
371-592 |
5.40e-26 |
|
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: 107.09 E-value: 5.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDG-TISIDGINIKDMNLQSLRGLMGLV 449
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 T---QDSILFNDTIK--------ANISLGKlDATDDEIIEALKIANAFEfVNEL---PLGiytnigdsgnKLSGGQKQRL 515
Cdd:COG1119 84 SpalQLRFPRDETVLdvvlsgffDSIGLYR-EPTDEQRERARELLELLG-LAHLadrPFG----------TLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTES-EKFVQVaLENMMQN--RTSIVIAHRL----STIQKAdliVVMQKGKIVEQGTH 588
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKLAAEgaPTLVLVTHHVeeipPGITHV---LLLKDGRVVAAGPK 227
|
....
gi 1776288214 589 DELI 592
Cdd:COG1119 228 EEVL 231
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
372-587 |
5.98e-26 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 106.69 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIAN-LMTR-FYDVNDGTISIDGINIKDMNLQSlRGLMGL- 448
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDILELSPDE-RARAGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 -----------VTQDSILfnDTIKANISLGKLDATD-----DEIIEALKIANAFefvnelpLGIYTNIGdsgnkLSGGQK 512
Cdd:COG0396 81 lafqypveipgVSVSNFL--RTALNARRGEELSAREflkllKEKMKELGLDEDF-------LDRYVNEG-----FSGGEK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMM-QNRTSIVIAH--RLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:COG0396 147 KRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
371-593 |
6.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.77 E-value: 6.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN-LQSLRGLMGL 448
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQ--DSILFNDTIKANISLG--KLDATDDEIIEALKIANAfefvnELPLGIYTNigDSGNKLSGGQKQRLSIARAVLKN 524
Cdd:PRK13644 82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALA-----EIGLEKYRH--RSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 525 PPIMILDEATSALDTESEKFVQVALENMMQNRTSIV-IAHRLSTIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
85-609 |
1.18e-25 |
|
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: 112.70 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 85 ESGYVLSIMVAIIisiFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNS 164
Cdd:TIGR01271 119 EIAYYLALGLCLL---FIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEG 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 165 fLAILELIVKEPLTIIFTittMLIISPKLTLFVFI---FIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLK 241
Cdd:TIGR01271 196 -LALAHFVWIAPLQVILL---MGLIWELLEVNGFCglgFLILLALFQACLGQKMMPYRDKRAGKISERLAITSEIIENIQ 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 242 VVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVI-------------------------------- 289
Cdd:TIGR01271 272 SVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVflsvvpyalikgiilrrifttisycivlrmtv 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 290 ------AILLWYGgQMVLIDKSLDGAAFIAYMGLAYNILTPAKAISKASYGVKRGNAaaeRVLEILDQENPITSKPDAiv 363
Cdd:TIGR01271 352 trqfpgAIQTWYD-SLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTASWDEGIG---ELFEKIKQNNKARKQPNG-- 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 364 ktsfDDSIEVKNinFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqslr 443
Cdd:TIGR01271 426 ----DDGLFFSN--FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------ 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 gLMGLVTQDSILFNDTIKANISLGkldATDDE-----IIEALKIAnafEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIA 518
Cdd:TIGR01271 488 -RISFSPQTSWIMPGTIKDNIIFG---LSYDEyrytsVIKACQLE---EDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFV-QVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGT 597
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
570
....*....|...
gi 1776288214 598 Y-NKLVTMQSFES 609
Cdd:TIGR01271 641 FsSLLLGLEAFDN 653
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
371-587 |
1.23e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 108.88 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQslRGLMGLVT 450
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-NDTIKANISLG-KLDAT-DDEI----IEALKIANAFEFVNELPLgiytnigdsgnKLSGGQKQRLSIARAVLK 523
Cdd:PRK09452 93 QSYALFpHMTVFENVAFGlRMQKTpAAEItprvMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALEnMMQNR---TSIVIAH-RLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:PRK09452 162 KPKVLLLDESLSALDYKLRKQMQNELK-ALQRKlgiTFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
371-594 |
1.70e-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: 105.11 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQdETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRglMGLVT 450
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-NDTIKANISLG---------KLDATDDEIIEALKIAnafEFVNELPLgiytnigdsgnKLSGGQKQRLSIARA 520
Cdd:cd03299 78 QNYALFpHMTVYKNIAYGlkkrkvdkkEIERKVLEIAEMLGID---HLLNRKPE-----------TLSGGEQQRVAIARA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 521 VLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03299 144 LVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
371-583 |
2.17e-25 |
|
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: 102.51 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqslrglmglvt 450
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 qDSILFNDTIKANislgkldatddeiieALKIANAFEfvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPPIMIL 530
Cdd:cd03216 62 -KEVSFASPRDAR---------------RAGIAMVYQ-------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 531 DEATSAL-DTESEKFVQVaLENMM-QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:cd03216 107 DEPTAALtPAEVERLFKV-IRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
379-587 |
2.63e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 105.54 E-value: 2.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 379 KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLMGLVTQDSI- 454
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 455 LFN--DTIKANIS-----LGKLDATD-----DEIIEALKIANafEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVL 522
Cdd:PRK10419 101 AVNprKTVREIIReplrhLLSLDKAErlaraSEMLRAVDLDD--SVLDKRP-----------PQLSGGQLQRVCLARALA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 523 KNPPIMILDEATSALDTESEKFVqVALENMMQNRTSIV---IAHRLSTIQK-ADLIVVMQKGKIVEQGT 587
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGV-IRLLKKLQQQFGTAclfITHDLRLVERfCQRVMVMDNGQIVETQP 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
371-593 |
2.83e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.05 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL--RGLmGL 448
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERarAGI-GY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLG-------KLDATDDEIIE---ALKianafEFVNELplgiytnigdsGNKLSGGQKQRLSI 517
Cdd:cd03224 80 VPEGRRIFPElTVEENLLLGayarrraKRKARLERVYElfpRLK-----ERRKQL-----------AGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALdteSEKFVQV---ALENMMQNRTSIVI----AHRLSTIqkADLIVVMQKGKIVEQGTHDE 590
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAE 218
|
...
gi 1776288214 591 LIA 593
Cdd:cd03224 219 LLA 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
370-591 |
6.41e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINfKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRglMGL 448
Cdd:PRK10851 2 SIEIANIK-KSFGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLG----------KLDATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSI 517
Cdd:PRK10851 79 VFQHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAH-RLSTIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
76-345 |
7.96e-25 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 104.90 E-value: 7.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 76 YITTTKGTHES-GYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRI 154
Cdd:cd18573 25 VASKESGDIEIfGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 155 SADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIE 234
Cdd:cd18573 105 SSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 235 ETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLiDKSL---DGAAF 311
Cdd:cd18573 185 ERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA-SGELtvgDLTSF 263
|
250 260 270
....*....|....*....|....*....|....*...
gi 1776288214 312 I---AYMGLAYNILTpakaiskASYG-VKRGNAAAERV 345
Cdd:cd18573 264 LmyaVYVGSSVSGLS-------SFYSeLMKGLGASSRL 294
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
340-580 |
1.06e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 108.36 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 340 AAAERVLEILD--QENPITSKPDAIVKTSFDDSIEVKNINFK-YQDETVLKDFSLSIKKGQTVALVGQSGSGKST----I 412
Cdd:COG4178 330 ATVDRLAGFEEalEAADALPEAASRIETSEDGALALEDLTLRtPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 413 ANLmtrfYDVNDGTISidginikdmnLQSLRGLMgLVTQDSILFNDTIKANIS--LGKLDATDDEIIEALKIANAFEFVN 490
Cdd:COG4178 410 AGL----WPYGSGRIA----------RPAGARVL-FLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAE 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 491 ELplgiyTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK 570
Cdd:COG4178 475 RL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549
|
250
....*....|
gi 1776288214 571 ADLIVVMQKG 580
Cdd:COG4178 550 HDRVLELTGD 559
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
371-594 |
1.88e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.88 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQ----DETVLKDFSLSIKKGQTVALVGQSGSGKST---IANLMTRfydVNDGTISIDGINI---KDMNLQ 440
Cdd:PRK11153 2 IELKNISKVFPqggrTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLtalSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQDsilFN----DTIKANISLG-KLDATDDEIIEAlKIANAFEFVNelplgiytnIGDSGNK----LSGGQ 511
Cdd:PRK11153 79 KARRQIGMIFQH---FNllssRTVFDNVALPlELAGTPKAEIKA-RVTELLELVG---------LSDKADRypaqLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 512 KQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMmqNRT---SIV-IAHRLSTI-QKADLIVVMQKGKIVEQG 586
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRElglTIVlITHEMDVVkRICDRVAVIDAGRLVEQG 223
|
....*...
gi 1776288214 587 THDELIAH 594
Cdd:PRK11153 224 TVSEVFSH 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
371-586 |
2.07e-24 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 101.56 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlRGLmGLVT 450
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RDI-AMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF-NDTIKANISLG-KLDATDDEIIEAlKIANAFEFvnelpLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03301 79 QNYALYpHMTVYDNIAFGlKLRKVPKDEIDE-RVREVAEL-----LQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQN--RTSIVIAH-RLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
370-592 |
4.06e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQdSILFNDTIKAN----------ISL-GKLDATDDEIIE-ALKIANAFEFVNELplgiytnIGDsgnkLSGGQKQRLSI 517
Cdd:PRK11231 82 PQ-HHLTPEGITVRelvaygrspwLSLwGRLSAEDNARVNqAMEQTRINHLADRR-------LTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESekfvQVALENMM-----QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEV 225
|
.
gi 1776288214 592 I 592
Cdd:PRK11231 226 M 226
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
371-594 |
4.50e-24 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 101.84 E-value: 4.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET---------VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQS 441
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRGLMGLVTQDSilfNDTIKANISLGK-LDA-----TD-DEIIEALKIANAFEFVNELP--LGIYTNIgdsgnkLSGGQK 512
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGQiLEEplrlnTDlTAEEREERIFATLRLVGLLPehANFYPHM------LSSGQK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTEsekfVQVALENMM---QNRTS---IVIAHRLSTIQK-ADLIVVMQKGKIVEQ 585
Cdd:COG4167 156 QRVALARALILQPKIIIADEALAALDMS----VRSQIINLMlelQEKLGisyIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231
|
....*....
gi 1776288214 586 GTHDELIAH 594
Cdd:COG4167 232 GKTAEVFAN 240
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
371-594 |
4.75e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 4.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI----KDMNLQS 441
Cdd:PRK13634 3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRGLMGLVTQ--DSILFNDTIKANISLGKLD--ATDDeiiEALKIANAFEFVNELPLGIYTNigdSGNKLSGGQKQRLSI 517
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEE---DAKQKAREMIELVGLPEELLAR---SPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEK-----FVQVALEnmmQNRTSIVIAHRLSTI-QKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKemmemFYKLHKE---KGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
...
gi 1776288214 592 IAH 594
Cdd:PRK13634 234 FAD 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
371-594 |
4.98e-24 |
|
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: 101.08 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL-MGLV 449
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISL-----GKLDATDDEIIEALkianafefVNELplGIYTNIGDSGNKLSGGQKQRLSIARAVLK 523
Cdd:cd03218 81 PQEASIFRKlTVEENILAvleirGLSKKEREEKLEEL--------LEEF--HITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLS-TIQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
371-594 |
6.51e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 105.92 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKN--INFKYQDET--VLKDFSLSIKKGQTVALVGQSGSGKS----TIANLMTRFYDVNDGTISIDGINIKDMNLQSL 442
Cdd:COG4172 7 LSVEDlsVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGL----MGLVTQDSI-----LFndTIKANIS--------LGKLDATDdEIIEALK---IANAFEFVNELPlgiytnigd 502
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLH--TIGKQIAevlrlhrgLSGAAARA-RALELLErvgIPDPERRLDAYP--------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 503 sgNKLSGGQKQRLSIARAVLKNPPIMILDEATSALD-TesekfVQ---VALENMMQNRT--SIV-IAHRLSTIQK-ADLI 574
Cdd:COG4172 155 --HQLSGGQRQRVMIAMALANEPDLLIADEPTTALDvT-----VQaqiLDLLKDLQRELgmALLlITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 1776288214 575 VVMQKGKIVEQGTHDELIAH 594
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
87-345 |
7.77e-24 |
|
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: 101.71 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 87 GYVLS---IMVAI-IISIfllknLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQ 162
Cdd:cd18548 36 SYILRtglLMLLLaLLGL-----IAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 163 NSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKV 242
Cdd:cd18548 111 NFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 243 VKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEF-MGITVIAIlLWYGGQMVLIDKSLDGA--AFIAYMGLay 319
Cdd:cd18548 191 IRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLiMNLAIVAI-LWFGGHLINAGSLQVGDlvAFINYLMQ-- 267
|
250 260
....*....|....*....|....*.
gi 1776288214 320 nILTPAKAISKASYGVKRGNAAAERV 345
Cdd:cd18548 268 -ILMSLMMLSMVFVMLPRASASAKRI 292
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
370-593 |
1.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETV-----LKDFSLSIKKGQTVALVGQSGSGKSTianLMTRFYDV---NDGTISIDGINIK----DM 437
Cdd:PRK13641 2 SIKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKST---LMQHFNALlkpSSGTITIAGYHITpetgNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 438 NLQSLRGLMGLVTQ--DSILFNDTIKANISLGKLD--ATDDEIIEAlkianAFEFVNELplGIYTNIGD-SGNKLSGGQK 512
Cdd:PRK13641 79 NLKKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEK-----ALKWLKKV--GLSEDLISkSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTESEK-FVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDE 590
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKE 231
|
...
gi 1776288214 591 LIA 593
Cdd:PRK13641 232 IFS 234
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
371-593 |
1.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIK--DMNLQSLRGLMG 447
Cdd:PRK13639 2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQ--DSILFNDTIKANISLGKL------DATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIAR 519
Cdd:PRK13639 82 IVFQnpDDQLFAPTVEEDVAFGPLnlglskEEVEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
370-593 |
2.50e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 2.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF-------YDvnDGTISIDGINIKDMNLQ 440
Cdd:PRK15134 7 AIENLSVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGlvTQDSILFNDTIkanISLGKLDATDDEIIEALKI-------ANAFEFVNELP-LGIY---TNIGDSGNKLSG 509
Cdd:PRK15134 85 TLRGVRG--NKIAMIFQEPM---VSLNPLHTLEKQLYEVLSLhrgmrreAARGEILNCLDrVGIRqaaKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 510 GQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQN 239
|
....*..
gi 1776288214 587 THDELIA 593
Cdd:PRK15134 240 RAATLFS 246
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
353-597 |
2.98e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 101.84 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 353 NPITSKPDAIVKTSFDDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI 432
Cdd:PRK11607 2 NDAIPRPQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 433 NIKDMnlQSLRGLMGLVTQDSILF-NDTIKANISLG----KL--DATDDEIIEALKIANAFEFVNELPlgiytnigdsgN 505
Cdd:PRK11607 82 DLSHV--PPYQRPINMMFQSYALFpHMTVEQNIAFGlkqdKLpkAEIASRVNEMLGLVHMQEFAKRKP-----------H 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 506 KLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAH-RLSTIQKADLIVVMQKGKI 582
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKF 228
|
250
....*....|....*
gi 1776288214 583 VEQGTHDELIAHNGT 597
Cdd:PRK11607 229 VQIGEPEEIYEHPTT 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
386-593 |
5.05e-23 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 100.96 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIK---KGQTV-ALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD----MNLQSLRGLMGLVTQDSILFN 457
Cdd:TIGR02142 9 LGDFSLDADftlPGQGVtAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 458 D-TIKANISLGKLDATDDEIiealkiANAFEFVNELpLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSA 536
Cdd:TIGR02142 89 HlSVRGNLRYGMKRARPSER------RISFERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 537 LDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
370-587 |
5.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 5.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI----KDMNLQ 440
Cdd:PRK13649 2 GINLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQ--DSILFNDTIKANISLGKLDATDDEiIEALKIANafefvNELPL-GIYTNIGD-SGNKLSGGQKQRLS 516
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAR-----EKLALvGISESLFEkNPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIV-IAHRLSTIQK-ADLIVVMQKGKIVEQGT 587
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
371-586 |
5.92e-23 |
|
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: 96.83 E-value: 5.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF--YDVNDGTISIDGINIKDMNLQSlRGLMGL 448
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEE-RARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VtqdsILFNDTIKanislgkldatddeiIEALKIANAFEFVNElplgiytnigdsgnKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03217 80 F----LAFQYPPE---------------IPGVKNADFLRYVNE--------------GFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMM-QNRTSIVIAH--RLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
368-591 |
7.27e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMg 447
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICM- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 lVTQDSILF-NDTIKANISLG--KLDATDDEII----EALKIAN--AFE--FVNElplgiytnigdsgnkLSGGQKQRLS 516
Cdd:PRK11432 83 -VFQSYALFpHMSLGENVGYGlkMLGVPKEERKqrvkEALELVDlaGFEdrYVDQ---------------ISGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11432 147 LARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
97-315 |
1.49e-22 |
|
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: 98.39 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 97 IISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEP 176
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 177 LTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVF 256
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELY 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 257 QNSTERFFNLSnsignrQNLASPASEFMGITVIAI------LLWYGGQMVlIDKSLDGAAFIAYM 315
Cdd:cd18574 208 EEEVEKAAKLN------EKLGLGIGIFQGLSNLALngivlgVLYYGGSLV-SRGELTAGDLMSFL 265
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
371-591 |
1.94e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.91 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN-----DGTISIDGINIKDMNLQSLRGL 445
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQ-DSILFNDTIKANISLG-KLD-------ATDDEIIEALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQRLS 516
Cdd:PRK14247 84 VQMVFQiPNPIPNLSIFENVALGlKLNrlvkskkELQERVRWALEKAQLWDEVKD-------RLDAPAGKLSGGQQQRLC 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
371-565 |
2.21e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDV-----NDGTISIDGINI--KDMNLQSLR 443
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSILFNDTIKANISLG------KLDAtdDEIIE-ALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQRLS 516
Cdd:PRK14243 91 RRIGMVFQKPNPFPKSIYDNIAYGaringyKGDM--DELVErSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLC 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRL 565
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
371-594 |
2.60e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.48 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN-LQSLR-GLmGL 448
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAaGI-AI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLGKLDAT------DDEIIEALKIANAFEFvnELPLGiyTNIGDsgnkLSGGQKQRLSIARAV 521
Cdd:COG1129 84 IHQELNLVPNlSVAENIFLGREPRRgglidwRAMRRRARELLARLGL--DIDPD--TPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 522 LKNPPIMILDEATSAL-DTESEKFVQVaLENMMQNRTSIV-IAHRLSTIQK-ADLIVVMQKGKIVEQG-----THDELIA 593
Cdd:COG1129 156 SRDARVLILDEPTASLtEREVERLFRI-IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTEDELVR 234
|
.
gi 1776288214 594 H 594
Cdd:COG1129 235 L 235
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
372-594 |
2.61e-22 |
|
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: 96.20 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL--RGLmGLV 449
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarLGI-GYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISLGKLDATDDEIIEAlkianAFEFVNEL-PLgIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGAYARRDRAEVRA-----DLERVYELfPR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 528 MILDEATSALdteSEKFVQV---ALENMMQNRTSIVI----AHRLSTIqkADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG0410 158 LLLDEPSLGL---APLIVEEifeIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLAD 226
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
72-324 |
4.71e-22 |
|
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: 96.75 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 72 YLSYYITTTKGTHESGYVLSIMVAIIISIFLLKnladYAAMFFITFL--RNGVL--RDMRNAMYKKTLELPLAFYSEKRK 147
Cdd:cd18549 23 LIVRYIIDDLLPSKNLRLILIIGAILLALYILR----TLLNYFVTYWghVMGARieTDMRRDLFEHLQKLSFSFFDNNKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 148 GDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQG 227
Cdd:cd18549 99 GQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 228 TFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNlSNSIGNRQ--NLASPASEFMGITVIAILLwYGGQMVLIDKs 305
Cdd:cd18549 179 EINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLE-SKKKAYKAmaYFFSGMNFFTNLLNLVVLV-AGGYFIIKGE- 255
|
250
....*....|....*....
gi 1776288214 306 LDGAAFIAYMGLAYNILTP 324
Cdd:cd18549 256 ITLGDLVAFLLYVNVFIKP 274
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
371-574 |
4.83e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN-----DGTISIDGINIKDMNLQS--LR 443
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvdLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSILFNDTIKANISLG------KLDATDDEIIE-ALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQRLS 516
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEkSLKGASIWDEVKD-------RLHDSALGLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHrlsTIQKADLI 574
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
370-587 |
6.49e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.61 E-value: 6.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL---RGLM 446
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 glvTQDSIL-FNDTIKANISLGKLD-----ATDDEII-EALKIANAFEFVNELplgiYTnigdsgnKLSGGQKQRLSIAR 519
Cdd:PRK13548 82 ---PQHSSLsFPFTVEEVVAMGRAPhglsrAEDDALVaAALAQVDLAHLAGRD----YP-------QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 520 aVL-------KNPPIMILDEATSALDTesekFVQVALENMMQNRTS------IVIAHRLS-TIQKADLIVVMQKGKIVEQ 585
Cdd:PRK13548 148 -VLaqlwepdGPPRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVAD 222
|
..
gi 1776288214 586 GT 587
Cdd:PRK13548 223 GT 224
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
371-593 |
1.15e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.26 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLkdFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLmglvt 450
Cdd:PRK10771 2 LKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-PSRRPV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 qdSILFND-------TIKANISLG-----KLDATDDEIIEAlkIANAF---EFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:PRK10771 74 --SMLFQEnnlfshlTVAQNIGLGlnpglKLNAAQREKLHA--IARQMgieDLLARLP-----------GQLSGGQRQRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTesekfvqvALENMM----------QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVE 584
Cdd:PRK10771 139 ALARCLVREQPILLLDEPFSALDP--------ALRQEMltlvsqvcqeRQLTLLMVSHSLEDAARiAPRSLVVADGRIAW 210
|
....*....
gi 1776288214 585 QGTHDELIA 593
Cdd:PRK10771 211 DGPTDELLS 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
386-580 |
1.24e-21 |
|
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: 93.55 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKS-----TIANLMTRFYDVNDGTISIDGINIKDMNLQSlRGLMGLVTQDSILFNDTI 460
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSslllaILGEMQTLEGKVHWSNKNESEPSFEATRSRN-RYSVAYAAQKPWLLNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLGKL--DATDDEIIEALKIANAFEFvneLPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALD 538
Cdd:cd03290 96 EENITFGSPfnKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1776288214 539 TE-SEKFVQVALENMMQN--RTSIVIAHRLSTIQKADLIVVMQKG 580
Cdd:cd03290 173 IHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
371-590 |
1.49e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIdGINIKdmnlqslrglMGLVT 450
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILF--NDTIKANISLGkldATDDEIIEALKIANAFEFVNELplgIYTNIGDsgnkLSGGQKQRLSIARAVLKNPPIM 528
Cdd:COG0488 385 QHQEELdpDKTVLDELRDG---APGGTEQEVRGYLGRFLFSGDD---AFKPVGV----LSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 529 ILDEATSALDTES-EkfvqvALENMMQN--RTSIVIAH-R--LSTIqkADLIVVMQKGKIVE-QGTHDE 590
Cdd:COG0488 455 LLDEPTNHLDIETlE-----ALEEALDDfpGTVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
89-355 |
2.04e-21 |
|
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: 95.21 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 89 VLSIMVAIIISIFLLKNLAD-------YAAMFFI--------TFLRNGVL--------RDMRNAMYKKTLELPLAFYSEK 145
Cdd:cd18578 27 VFAILFSKLISVFSLPDDDElrseanfWALMFLVlaivagiaYFLQGYLFgiagerltRRLRKLAFRAILRQDIAWFDDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 146 RK--GDVISRISADVNEVQN---SFLA-ILELIVkeplTIIFTITTMLIISPKLTLFVFIFIPV---SGYIISLIGKQLK 216
Cdd:cd18578 107 ENstGALTSRLSTDASDVRGlvgDRLGlILQAIV----TLVAGLIIAFVYGWKLALVGLATVPLlllAGYLRMRLLSGFE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 217 KQSTKAQQEQGTFLStieETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYG 296
Cdd:cd18578 183 EKNKKAYEESSKIAS---EAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYG 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 297 GQMVLIDKSLDGAAFIAYMGLAYNILTPAKAISKASyGVKRGNAAAERVLEILDQENPI 355
Cdd:cd18578 260 GRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAP-DIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
80-318 |
2.82e-21 |
|
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: 94.62 E-value: 2.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 80 TKGTHESGYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVN 159
Cdd:cd18780 31 GSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 160 EVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGG 239
Cdd:cd18780 111 VLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISN 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 240 LKVVKGYNSENYFNTVFQNSTerffNLSNSIGNRQNLASPAseFMGIT------VIAILLWYGGQMVLIDKSLDGA--AF 311
Cdd:cd18780 191 IRTVRSFAKETKEVSRYSEKI----NESYLLGKKLARASGG--FNGFMgaaaqlAIVLVLWYGGRLVIDGELTTGLltSF 264
|
250
....*....|..
gi 1776288214 312 IAY-----MGLA 318
Cdd:cd18780 265 LLYtltvaMSFA 276
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-586 |
3.01e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.37 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN-----DGTISIDGINI--KDMNLQSL 442
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILF-NDTIKANISLG----KLDATDDEIIE----ALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQ 513
Cdd:PRK14267 84 RREVGMVFQYPNPFpHLTIYDNVAIGvklnGLVKSKKELDErvewALKKAALWDEVKD-------RLNDYPSNLSGGQRQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
371-591 |
3.62e-21 |
|
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: 92.43 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI-KDMnlQSLRGLMGLV 449
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREP--REVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISL-GKL-----DATDDEIIEALKIANAFEFVNELpLGIYtnigdsgnklSGGQKQRLSIARAVL 522
Cdd:cd03265 79 FQDLSVDDElTGWENLYIhARLygvpgAERRERIDELLDFVGLLEAADRL-VKTY----------SGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 523 KNPPIMILDEATSALDTESEKFVQVALENMM--QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
114-315 |
5.75e-21 |
|
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: 93.38 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 114 FITFLRNG--------VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITT 185
Cdd:cd18572 51 LFSGLRGGcfsyagtrLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 186 MLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFN 265
Cdd:cd18572 131 MFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 266 lsnsIGNRQNLAS----PASEFMGITVIAILLWYGGQMVLiDKSLDGAAFIAYM 315
Cdd:cd18572 211 ----LSVRQALAYagyvAVNTLLQNGTQVLVLFYGGHLVL-SGRMSAGQLVTFM 259
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
371-583 |
8.17e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.46 E-value: 8.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETV-----LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL 445
Cdd:COG1101 2 LELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQD---------SILFNDTI------KANISLGKLDATDDEIIEALKianafefvnELPLG----IYTNIGdsgnK 506
Cdd:COG1101 82 IGRVFQDpmmgtapsmTIEENLALayrrgkRRGLRRGLTKKRRELFRELLA---------TLGLGlenrLDTKVG----L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 507 LSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFV-----QVALENmmqNRTSIVIAHRLS-TIQKADLIVVMQKG 580
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVlelteKIVEEN---NLTTLMVTHNMEqALDYGNRLIMMHEG 225
|
...
gi 1776288214 581 KIV 583
Cdd:COG1101 226 RII 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
371-595 |
1.10e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.81 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETV-LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFNDTIKanislGKLDATDDEIIEA----LKIANAFEFVNelplGIYTNIgdsgnKLSGGQKQRLSIARAVLKNP 525
Cdd:PRK10522 403 FTDFHLFDQLLG-----PEGKPANPALVEKwlerLKMAHKLELED----GRISNL-----KLSKGQKKRLALLLALAEER 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 526 PIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQKADLIVVMQKGKIVE-QGTHDELIAHN 595
Cdd:PRK10522 469 DILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASRD 541
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
368-593 |
1.12e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDMNLQSLRG 444
Cdd:PRK13636 3 DYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 LMGLVTQ--DSILFNDTIKANISLGKLDAT--DDEIIEalKIANAFEfvnelplgiYTNIGDSGNK----LSGGQKQRLS 516
Cdd:PRK13636 83 SVGMVFQdpDNQLFSASVYQDVSFGAVNLKlpEDEVRK--RVDNALK---------RTGIEHLKDKpthcLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 517 IARAVLKNPPIMILDEATSALD----TESEKFVQVALENMmqNRTSIVIAHRLSTIQ-KADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
..
gi 1776288214 592 IA 593
Cdd:PRK13636 230 FA 231
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
386-592 |
1.61e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.94 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL----MGLVTQD-SILFNDTI 460
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLGKLDATddeIIEALKIANAFEFVNELPLGIYTNigDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTE 540
Cdd:PRK10070 124 LDNTAFGMELAG---INAEERREKALDALRQVGLENYAH--SYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 541 SEKFVQVALENMM--QNRTSIVIAHRL-STIQKADLIVVMQKGKIVEQGTHDELI 592
Cdd:PRK10070 199 IRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
368-594 |
2.37e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.80 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIK------------ 435
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkva 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 436 DMN-LQSLRGLMGLVTQDSILFND-TIKANI--------SLGKLDATDDEIIEALKIAnafefVNELPLGIYTNigdsgn 505
Cdd:PRK10619 83 DKNqLRLLRTRLTMVFQHFNLWSHmTVLENVmeapiqvlGLSKQEARERAVKYLAKVG-----IDERAQGKYPV------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 506 KLSGGQKQRLSIARAVLKNPPIMILDEATSALDTEsekFVQVALENMMQ----NRTSIVIAHRLSTIQK-ADLIVVMQKG 580
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
250
....*....|....
gi 1776288214 581 KIVEQGTHDELIAH 594
Cdd:PRK10619 229 KIEEEGAPEQLFGN 242
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
370-591 |
2.42e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.87 E-value: 2.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN-----DGTISIDGINI--KDMNLQSL 442
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILFNDTIKANISLG--------KLDAtdDEIIE-ALKIANAFEFVNElplgiytNIGDSGNKLSGGQKQ 513
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI--DDIVEsALKDADLWDEIKH-------KIHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALEN--MMQNRTSIVIAHRLSTIQK-ADLIVVMQK-----GKIVEQ 585
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEF 237
|
....*.
gi 1776288214 586 GTHDEL 591
Cdd:PRK14258 238 GLTKKI 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
386-594 |
2.99e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.95 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLRGLMGLVTQD---------- 452
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 453 --SILfNDTIKANISLGKldATDDEIIEAL--KIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK11308 111 vgQIL-EEPLLINTSLSA--AERREKALAMmaKVGLRPEHYDRYP-----------HMFSGGQRQRIAIARALMLDPDVV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 529 ILDEATSALDTEsekfVQVALENMM-----QNRTSIV-IAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK11308 177 VADEPVSALDVS----VQAQVLNLMmdlqqELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
94-319 |
3.12e-20 |
|
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: 91.40 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 94 VAIIISIFLLKNLADYAAMFFITFL--RNG--VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVnEVQNSFL--A 167
Cdd:cd18546 38 LLLAAAAYLAVVLAGWVAQRAQTRLtgRTGerLLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDI-DALSELLqtG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 ILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVsgyiISLIGKQLKKQSTKAQQEQ----GTFLSTIEETIGGLKVV 243
Cdd:cd18546 117 LVQLVV-SLLTLVGIAVVLLVLDPRLALVALAALPP----LALATRWFRRRSSRAYRRAreriAAVNADLQETLAGIRVV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 244 KGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlidksLDG-------AAFIAYMG 316
Cdd:cd18546 192 QAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRV-----AAGtltvgvlVAFLLYLR 266
|
...
gi 1776288214 317 LAY 319
Cdd:cd18546 267 RFF 269
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
378-586 |
3.31e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.62 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 378 FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTI----SIdginikdmnlqslrglmGLVTQDS 453
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSI-----------------AYVPQQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 454 ILFNDTIKANISLgkLDATDDE-IIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDE 532
Cdd:PTZ00243 731 WIMNATVRGNILF--FDEEDAArLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 533 ATSALDTE-SEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQG 586
Cdd:PTZ00243 809 PLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
384-602 |
3.93e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 89.76 E-value: 3.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI-------------------NIKdmnlqsLRG 444
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelgagfhpeltgreNIY------LNG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 -LMGLVTQDsilfndtIKANIslgkldatdDEIIEalkianaF----EFVNeLPLGIYtnigdsgnklSGGQKQRLSIAR 519
Cdd:COG1134 114 rLLGLSRKE-------IDEKF---------DEIVE-------FaelgDFID-QPVKTY----------SSGMRARLAFAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 520 AVLKNPPIMILDEATSALDTE-SEKFVQvALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAHng 596
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAfQKKCLA-RIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA-- 236
|
....*.
gi 1776288214 597 tYNKLV 602
Cdd:COG1134 237 -YEALL 241
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
371-586 |
4.74e-20 |
|
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: 88.96 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLm 446
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFND-TIKANIS-LGKLdatddeiiEALKIANAFEFVNELP--LGIYTNIGDSGNKLSGGQKQRLSIARAVL 522
Cdd:cd03266 81 GFVSDSTGLYDRlTARENLEyFAGL--------YGLKGDELTARLEELAdrLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 523 KNPPIMILDEATSALD-TESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03266 153 HDPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
371-583 |
5.66e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 5.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQ--DET--VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL- 445
Cdd:PRK10535 5 LELKDIRRSYPsgEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 ---MGLVTQD-SILFNDTIKANISLGKLDATddeIIEALKIANAFEFVNELPLGiyTNIGDSGNKLSGGQKQRLSIARAV 521
Cdd:PRK10535 85 rehFGFIFQRyHLLSHLTAAQNVEVPAVYAG---LERKQRLLRAQELLQRLGLE--DRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 522 LKNPPIMILDEATSALDTESEKFVQVALENMM-QNRTSIVIAHRLSTIQKADLIVVMQKGKIV 583
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
377-591 |
6.17e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 90.30 E-value: 6.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 377 NFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqslrgLMGLVTQDSILF 456
Cdd:cd03291 44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 457 NDTIKANISLGkldATDDE-----IIEALKIAnafEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:cd03291 111 PGTIKENIIFG---VSYDEyryksVVKACQLE---EDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 532 EATSALDTESEKFV-QVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:cd03291 185 SPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
371-586 |
6.44e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.21 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QD-SILFNDTIKANISLGK---------LDATDDEIIE-ALKIANAFEFVNElplgiytnigdSGNKLSGGQKQRLSIAR 519
Cdd:PRK09536 84 QDtSLSFEFDVRQVVEMGRtphrsrfdtWTETDRAAVErAMERTGVAQFADR-----------PVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 520 AVLKNPPIMILDEATSALDTESE-KFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
371-586 |
8.09e-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: 88.11 E-value: 8.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDMN----LQSLRG 444
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpLDIAARNrigyLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 LMGLVT-QDSILFNDTIKAnisLGKLDATD--DEIIEALKIANAFEFVNElplgiytnigdsgnKLSGGQKQRLSIARAV 521
Cdd:cd03269 81 LYPKMKvIDQLVYLAQLKG---LKKEEARRriDEWLERLELSEYANKRVE--------------ELSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 522 LKNPPIMILDEATSALDTES-EKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
373-563 |
8.21e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 373 VKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiNIKdmnlqslrglMGLVTQD 452
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 453 SILFND-TIKANISLG----------------KLDATDDEIIEALKIANAFEFVN--ELP---------LGIYTNIGDSG 504
Cdd:COG0488 70 PPLDDDlTVLDTVLDGdaelraleaeleeleaKLAEPDEDLERLAELQEEFEALGgwEAEaraeeilsgLGFPEEDLDRP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 505 -NKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESekfvqVA-LENMMQNRTS--IVIAH 563
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES-----IEwLEEFLKNYPGtvLVVSH 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-592 |
8.75e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 8.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 342 AERVLEILDQENPITSKPDAIVKTSFDDS---IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTR 418
Cdd:PRK13536 10 APRRLELSPIERKHQGISEAKASIPGSMStvaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 419 FYDVNDGTISIDGINIKDmNLQSLRGLMGLVTQ-DSILFNDTIKAN-ISLGKLDATDDEIIEALkIANAFEFVnELPLGI 496
Cdd:PRK13536 90 MTSPDAGKITVLGVPVPA-RARLARARIGVVPQfDNLDLEFTVRENlLVFGRYFGMSTREIEAV-IPSLLEFA-RLESKA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 497 YTNIGDsgnkLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMM-QNRTSIVIAHRLSTIQK-ADLI 574
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRL 242
|
250 260
....*....|....*....|..
gi 1776288214 575 VVMQKG-KIVEQGTH---DELI 592
Cdd:PRK13536 243 CVLEAGrKIAEGRPHaliDEHI 264
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
371-594 |
1.27e-19 |
|
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: 88.26 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLMGLV- 449
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP-PHEIARLGIGr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 T-QDSILFND-TIKANISLG-------------------KLDATDDEIIEALKIAnafEFVNELPlgiytnigdsGNkLS 508
Cdd:cd03219 80 TfQIPRLFPElTVLENVMVAaqartgsglllararreerEARERAEELLERVGLA---DLADRPA----------GE-LS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 509 GGQKQRLSIARAVLKNPPIMILDEATSAL-DTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225
|
....*...
gi 1776288214 587 THDELIAH 594
Cdd:cd03219 226 TPDEVRNN 233
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
370-591 |
1.30e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.78 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL------R 443
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GL---MGLVTQdsILFndtikanisLGKL-DATDDEIIEALKianafEFVNELplgiytNIGDSGNK----LSGGQKQRL 515
Cdd:COG4152 81 GLypkMKVGEQ--LVY---------LARLkGLSKAEAKRRAD-----EWLERL------GLGDRANKkveeLSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTES-EKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
366-601 |
1.79e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 89.30 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 366 SFDDSIEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDG-TISID---GINIKD 436
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 437 MN-LQSLRGLMGLVTQ--DSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFVnELPlgiYTNIGDSGNKLSGGQKQ 513
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLP---EDYVKRSPFELSGGQKR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEK-FVQVALE-NMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDE 590
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237
|
250
....*....|.
gi 1776288214 591 LIAHNGTYNKL 601
Cdd:PRK13645 238 IFSNQELLTKI 248
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
371-584 |
1.84e-19 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 87.87 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN---LQSLR 443
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedaRARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 G-LMGLVTQDSILFnDTIKA--NISL-----GKLDATD--DEIIEALKIAnafEFVNELPlgiytnigdsgNKLSGGQKQ 513
Cdd:COG4181 89 ArHVGFVFQSFQLL-PTLTAleNVMLplelaGRRDARAraRALLERVGLG---HRLDHYP-----------AQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQKADLIVVMQKGKIVE 584
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
384-591 |
2.03e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 92.03 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTrFYDVNDGTISID-GINIKDMNLQSLRGLMGLVTQDSILFND---- 458
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGVKGSGSvLLNGMPIDAKEMRAISAYVQQDDLFIPTltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 459 ---TIKANISLGKLDATD------DEIIEALKIANAFEfvnelplgiyTNIGDSGNK--LSGGQKQRLSIARAVLKNPPI 527
Cdd:TIGR00955 118 ehlMFQAHLRMPRRVTKKekrervDEVLQALGLRKCAN----------TRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNRTSIVIA-HRLST--IQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
371-587 |
3.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI----KDMNLQS 441
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRGLMGLVTQ--DSILFNDTIKANISLGK----LDATDDEIIEALK---IANAFEFVNELPLgiytnigdsgnKLSGGQK 512
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPqnfgIPKEKAEKIAAEKlemVGLADEFWEKSPF-----------ELSGGQM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 513 QRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQN-RTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGT 587
Cdd:PRK13643 151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
371-608 |
4.28e-19 |
|
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: 90.63 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLM--TRFYDVNDGTI----------------SIDGI 432
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 433 NIKDMNlqslrGLMGLVTQDSILFNDTIKANI------------SLGKLDATDDEIIEALK---------IANAFEFVNE 491
Cdd:TIGR03269 81 PCPVCG-----GTLEPEEVDFWNLSDKLRRRIrkriaimlqrtfALYGDDTVLDNVLEALEeigyegkeaVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 492 LPLGiyTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQ 569
Cdd:TIGR03269 156 VQLS--HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIE 233
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1776288214 570 K-ADLIVVMQKGKIVEQGTHDELIAhngtynklVTMQSFE 608
Cdd:TIGR03269 234 DlSDKAIWLENGEIKEEGTPDEVVA--------VFMEGVS 265
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
384-595 |
6.07e-19 |
|
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: 86.63 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLMGLV-T-QDSILFND-TI 460
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIArTfQNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLG---------------------KLDATDDEIIEALKIANAFEFVNELPlgiytnigdsGNkLSGGQKQRLSIAR 519
Cdd:COG0411 97 LENVLVAaharlgrgllaallrlprarrEEREARERAEELLERVGLADRADEPA----------GN-LSYGQQRRLEIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 520 AVLKNPPIMILDEATSAL-DTESEKFVQVALE-NMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDElIAHN 595
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE-VRAD 243
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
70-345 |
7.23e-19 |
|
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: 87.53 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 70 QDYLSYYITTTKGTHESGYVLSIMVAIIISIFLLKnladYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGD 149
Cdd:cd18577 30 TDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLS----YIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 150 VISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTF 229
Cdd:cd18577 106 LTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 230 LSTIEETIGGLKVVKGYNSENYFNTVFQNSTERffnlSNSIGNRQNLASPASE----FMGITVIAILLWYGGQMVlIDKS 305
Cdd:cd18577 186 GSIAEEALSSIRTVKAFGGEEKEIKRYSKALEK----ARKAGIKKGLVSGLGLgllfFIIFAMYALAFWYGSRLV-RDGE 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1776288214 306 LDG----AAFIAYMGLAY---NILTPAKAISKASygvkrgnAAAERV 345
Cdd:cd18577 261 ISPgdvlTVFFAVLIGAFslgQIAPNLQAFAKAR-------AAAAKI 300
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
366-591 |
7.55e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 366 SFDDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI------NIKDMNL 439
Cdd:PRK14246 6 SAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 440 QSLRGLMGLVTQDSILF-NDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNKLSGGQKQRLSIA 518
Cdd:PRK14246 86 IKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
377-586 |
1.13e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 85.28 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 377 NFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmNLQSLRGLMG-----LVTQ 451
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLGGgfnpeLTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 DSILFNDTIKaNISLGKLDATDDEIIEALKIANAFefvnELPLGIYtnigdsgnklSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:cd03220 103 ENIYLNGRLL-GLSRKEIDEKIDEIIEFSELGDFI----DLPVKTY----------SSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 532 EATSALDTESEKFVQVALENMMQNRTSIVIA-HRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
371-591 |
1.39e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQ-DETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLV 449
Cdd:PRK13652 4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQ--DSILFNDTIKANISLGKLDATDDEIIEALKIANAFEFvnelpLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK13652 84 FQnpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHM-----LGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 528 MILDEATSALDTESEKFVqVALENMMQNR---TSIVIAHRLSTI-QKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKEL-IDFLNDLPETygmTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
372-591 |
2.65e-18 |
|
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: 84.11 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL--RGlMGLV 449
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERarAG-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISLGkLDAT-------DDEIIE---ALKianafEFVNELplgiytnigdsGNKLSGGQKQRLSIA 518
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTG-LAALprrsrkiPDEIYElfpVLK-----EMLGRR-----------GGDLSGGQQQQLAIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 519 RAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
371-581 |
2.77e-18 |
|
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: 81.73 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTIsidginikdmnlqslrglmglvt 450
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 qdsilfndTIKANISLGKLDatddeiiealkianafefvnelplgiytnigdsgnKLSGGQKQRLSIARAVLKNPPIMIL 530
Cdd:cd03221 58 --------TWGSTVKIGYFE-----------------------------------QLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 531 DEATSALDTESekfvQVALENMMQN--RTSIVIAHRLSTIQK-ADLIVVMQKGK 581
Cdd:cd03221 95 DEPTNHLDLES----IEALEEALKEypGTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
369-591 |
3.01e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 88.37 E-value: 3.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFKYQDET----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN------ 438
Cdd:PRK10261 11 DVLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 439 -------LQSLRGL-MGLVTQDSIL-------FNDTIKANISLGKLDATDDEIIEA------LKIANAFEFVNELPlgiy 497
Cdd:PRK10261 91 seqsaaqMRHVRGAdMAMIFQEPMTslnpvftVGEQIAESIRLHQGASREEAMVEAkrmldqVRIPEAQTILSRYP---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 498 tnigdsgNKLSGGQKQRLSIARAVLKNPPIMILDEATSALD-TESEKFVQvaLENMMQNRTS---IVIAHRLSTIQK-AD 572
Cdd:PRK10261 167 -------HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvTIQAQILQ--LIKVLQKEMSmgvIFITHDMGVVAEiAD 237
|
250
....*....|....*....
gi 1776288214 573 LIVVMQKGKIVEQGTHDEL 591
Cdd:PRK10261 238 RVLVMYQGEAVETGSVEQI 256
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
371-589 |
4.35e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.39 E-value: 4.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKD----MNLqslrG 444
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaIAL----G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 LmGLVTQDSILFND-TIKANISLG---------KLDATDDEIIEalkIANAFEFvnELPLGIYtnIGDsgnkLSGGQKQR 514
Cdd:COG3845 82 I-GMVHQHFMLVPNlTVAENIVLGleptkggrlDRKAARARIRE---LSERYGL--DVDPDAK--VED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 515 LSIARAVLKNPPIMILDEATSAL-DTESEKFVQVaLENMMQNRTSIV-IAHRLSTIQK-ADLIVVMQKGKIVeqGTHD 589
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELFEI-LRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
373-582 |
6.16e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.96 E-value: 6.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 373 VKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTIsIDGinikDMNLQSLRGLMGLVTQD 452
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 453 SILFN-DTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGiytnigdsgnkLSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:PRK11247 90 ARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-----------LSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 532 EATSALDTESEKFVQVALENMMQNR--TSIVIAHRLS-TIQKADLIVVMQKGKI 582
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
371-532 |
1.03e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.77 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD--MNLQSLRGlMGL 448
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKRARLG-IGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANI----SLGKLDATD-DEIIEALkianafefVNELplGIyTNIGDS-GNKLSGGQKQRLSIARAV 521
Cdd:COG1137 83 LPQEASIFRKlTVEDNIlavlELRKLSKKErEERLEEL--------LEEF--GI-THLRKSkAYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 1776288214 522 LKNPPIMILDE 532
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
371-587 |
2.11e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 82.00 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF--YDVNDGTISIDGINIKDMN--LQSLRGLM 446
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpeERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 ----------GLVTQD--SILFNDTIKANiSLGKLDAtddeiIEALKIANA-FEFVNELPLGIYTNIGDSgnkLSGGQKQ 513
Cdd:CHL00131 88 lafqypieipGVSNADflRLAYNSKRKFQ-GLPELDP-----LEFLEIINEkLKLVGMDPSFLSRNVNEG---FSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIV-IAH--RLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
88-345 |
2.13e-17 |
|
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: 83.24 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSIMVAIIISIFL-LKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFL 166
Cdd:cd18554 42 YKLFTIIGIMFFIFLiLRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 167 AILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGY 246
Cdd:cd18554 122 TGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSF 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 247 NSENYFNTVFQNSTERFFNLSNSIGNRQnlASPASEFMGITVIAILLWYG-GQMVLIDKSLDGAAFIAYMGLAYNILTPA 325
Cdd:cd18554 202 ALEKHEQKQFDKRNGHFLTRALKHTRWN--AKTFSAVNTITDLAPLLVIGfAAYLVIEGNLTVGTLVAFVGYMERMYSPL 279
|
250 260
....*....|....*....|
gi 1776288214 326 KAISKASYGVKRGNAAAERV 345
Cdd:cd18554 280 RRLVNSFTTLTQSFASMDRV 299
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
94-345 |
2.30e-17 |
|
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: 83.38 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 94 VAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVqNSFL-----AI 168
Cdd:cd18565 57 GGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQL-ERFLddganSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 169 LELIVkeplTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNS 248
Cdd:cd18565 136 IRVVV----TVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 249 ENYFNTVFQNSTERFFNlSNSIGNRQNLA-SPASEFMGITVIAILLWYGGQMVLID-----KSLDGAAFIAYMGLAYNIL 322
Cdd:cd18565 212 EDFERERVADASEEYRD-ANWRAIRLRAAfFPVIRLVAGAGFVATFVVGGYWVLDGpplftGTLTVGTLVTFLFYTQRLL 290
|
250 260
....*....|....*....|...
gi 1776288214 323 TPAKAISKASYGVKRGNAAAERV 345
Cdd:cd18565 291 WPLTRLGDLIDQYQRAMASAKRV 313
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
384-594 |
2.40e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.53 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDvNDGTISIDGINIKDMNLQSL---RGLMGLVTQDSilfndti 460
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP------- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 kaNISLG-KLDATddEII-EALKI-----------ANAFEFVNELPLGIYTNIGDSGnKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK15134 372 --NSSLNpRLNVL--QIIeEGLRVhqptlsaaqreQQVIAVMEEVGLDPETRHRYPA-EFSGGQRQRIAIARALILKPSL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 528 MILDEATSALDteseKFVQ---VALENMMQNR---TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK15134 447 IILDEPTSSLD----KTVQaqiLALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAA 516
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
84-330 |
2.85e-17 |
|
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: 82.61 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 84 HESGYVLSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISAdvNEVQN 163
Cdd:cd18568 35 HKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRFQE--NQKIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 164 SFLA--ILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLK 241
Cdd:cd18568 113 RFLTrsALTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 242 VVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNI 321
Cdd:cd18568 192 TIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLV-ISGQLTIGQLVAFNMLFGSV 270
|
....*....
gi 1776288214 322 LTPAKAISK 330
Cdd:cd18568 271 INPLLALVG 279
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
387-594 |
2.86e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.22 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 387 KDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRglmgLVTQD-SILFNDTIKaniS 465
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR----AVRSDiQMIFQDPLA---S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 466 LGKLDATDDEIIEALKI-------ANAFEFVNE--LPLGIYTN-IGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATS 535
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTyhpklsrQEVKDRVKAmmLKVGLLPNlINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 536 ALDTEsekfVQVALENMMQNRTS------IVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK15079 191 ALDVS----IQAQVVNLLQQLQRemglslIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
364-592 |
3.26e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.76 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 364 KTSFDDSIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL- 442
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILFNDTIKANIS---------LGKLDATDDEiiealKIANAFEFVNELPLGiyTNIGDSgnkLSGGQKQ 513
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAigrypwhgaLGRFGAADRE-----KVEEAISLVGLKPLA--HRLVDS---LSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 514 RLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAhRLSTIQKA----DLIVVMQKGKIVEQGTHD 589
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPA 233
|
...
gi 1776288214 590 ELI 592
Cdd:PRK10575 234 ELM 236
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
385-586 |
8.55e-17 |
|
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: 79.62 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 385 VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVND---GTISIDGiniKDMNLQSLRGLMGLVTQDSILFND--- 458
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 459 ----TIKANISLGKLdaTDDEIIEALKianafEFVNELPLGIyTNIGDSGNK-LSGGQKQRLSIARAVLKNPPIMILDEA 533
Cdd:cd03234 99 retlTYTAILRLPRK--SSDAIRKKRV-----EDVLLRDLAL-TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 534 TSALDTESE-KFVQVALENMMQNRTSIVIAH--RLSTIQKADLIVVMQKGKIVEQG 586
Cdd:cd03234 171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
370-540 |
1.17e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.06 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN---DGTISIDGINIKDMNLQsLRGLm 446
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-QRRI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILF-NDTIKANISLGkLDAT------DDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIAR 519
Cdd:COG4136 79 GILFQDDLLFpHLSVGENLAFA-LPPTigraqrRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLR 146
|
170 180
....*....|....*....|.
gi 1776288214 520 AVLKNPPIMILDEATSALDTE 540
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAA 167
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
371-593 |
1.50e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.83 E-value: 1.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNIN---------FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDMNL 439
Cdd:PRK15112 5 LEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhpLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 440 QSLRGLMglVTQD-----------SILFNDTIKANISLGKlDATDDEIIEALKIanafefVNELP--LGIYTNIgdsgnk 506
Cdd:PRK15112 85 RSQRIRM--IFQDpstslnprqriSQILDFPLRLNTDLEP-EQREKQIIETLRQ------VGLLPdhASYYPHM------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 507 LSGGQKQRLSIARAVLKNPPIMILDEATSALD-TESEKFVQVALEnmMQNRTSI----VIAHRLSTIQKADLIVVMQKGK 581
Cdd:PRK15112 150 LAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLE--LQEKQGIsyiyVTQHLGMMKHISDQVLVMHQGE 227
|
250
....*....|..
gi 1776288214 582 IVEQGTHDELIA 593
Cdd:PRK15112 228 VVERGSTADVLA 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
386-580 |
1.74e-16 |
|
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: 79.05 E-value: 1.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLrglmgLVTQD-SILFNDTIKANI 464
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNySLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 465 SLGKldatdDEIIEALKIANAFEFVNE-LPLgiyTNIGDSGNK----LSGGQKQRLSIARAVLKNPPIMILDEATSALDT 539
Cdd:TIGR01184 76 ALAV-----DRVLPDLSKSERRAIVEEhIAL---VGLTEAADKrpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776288214 540 ESEKFVQVALENMMQNR--TSIVIAHRL-STIQKADLIVVMQKG 580
Cdd:TIGR01184 148 LTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
376-594 |
1.95e-16 |
|
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: 81.30 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 376 INFKYQdetvLKDFSLSIK-----KGQTvALVGQSGSGKSTIANLM---TRfydVNDGTISIDGiNI-----KDMNLQSL 442
Cdd:COG4148 5 VDFRLR----RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAIaglER---PDSGRIRLGG-EVlqdsaRGIFLPPH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 443 RGLMGLVTQDSILFND-TIKANISLG------KLDATD-DEIIEALKIAnafEFVNELPlgiytnigdsgNKLSGGQKQR 514
Cdd:COG4148 76 RRRIGYVFQEARLFPHlSVRGNLLYGrkraprAERRISfDEVVELLGIG---HLLDRRP-----------ATLSGGERQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESEKFVQVALENmMQNRTSIVI---AHRLSTIQK-ADLIVVMQKGKIVEQGTHDE 590
Cdd:COG4148 142 VAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER-LRDELDIPIlyvSHSLDEVARlADHVVLLEQGRVVASGPLAE 220
|
....
gi 1776288214 591 LIAH 594
Cdd:COG4148 221 VLSR 224
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
378-593 |
2.03e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.67 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 378 FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNLqSLRGLMGLVTQDSILFN 457
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG---KPLDY-SKRGLLALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 458 D--------TIKANI--SLGKLDATDDEII----EALKIANAFEFVNElPLGIytnigdsgnkLSGGQKQRLSIARAVLK 523
Cdd:PRK13638 85 DpeqqifytDIDSDIafSLRNLGVPEAEITrrvdEALTLVDAQHFRHQ-PIQC----------LSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 524 NPPIMILDEATSALDTESE-KFVQVALENMMQNRTSIVIAHRLSTI-QKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRtQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
385-580 |
2.19e-16 |
|
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: 78.63 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 385 VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISID----GINI-----KDMnLQSLRGLMGLVTQdsil 455
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLaqaspREI-LALRRRTIGYVSQ---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 456 FNDTI----------KANISLGkldaTDDEiiEALKIA-NAFEFVNeLPLGIYTNigdSGNKLSGGQKQRLSIARAVLKN 524
Cdd:COG4778 101 FLRVIprvsaldvvaEPLLERG----VDRE--EARARArELLARLN-LPERLWDL---PPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 525 PPIMILDEATSALDTESEKFVQVALENMMQNRTSIV-IAHRLSTIQK-ADLIVVMQKG 580
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
370-591 |
2.70e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.84 E-value: 2.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLmGLV 449
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-PAERGV-GMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILF-NDTIKANISLG-KLDATDDEIIEAlKIANAFEFvneLPLGiytNIGDSGNK-LSGGQKQRLSIARAVLKNPP 526
Cdd:PRK11000 81 FQSYALYpHLSVAENMSFGlKLAGAKKEEINQ-RVNQVAEV---LQLA---HLLDRKPKaLSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 527 IMILDEATSALDTesekfvqvALENMMQ----------NRTSIVIAH-RLSTIQKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11000 154 VFLLDEPLSNLDA--------ALRVQMRieisrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
371-604 |
2.71e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.90 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN--DGTISIDG-----INIKDmnlqSLR 443
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGeelqaSNIRD----TER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQDSILFND-TIKANISLGKlDATDDEIIEALKI-ANAFEFVNELPLGI--YTNIGDsgnkLSGGQKQRLSIAR 519
Cdd:PRK13549 82 AGIAIIHQELALVKElSVLENIFLGN-EITPGGIMDYDAMyLRAQKLLAQLKLDInpATPVGN----LGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 520 AVLKNPPIMILDEATSALdTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVeqGTHDeliAHNG 596
Cdd:PRK13549 157 ALNKQARLLILDEPTASL-TESETAVLLDIIRDLKAHgiACIYISHKLNEVKAiSDTICVIRDGRHI--GTRP---AAGM 230
|
....*...
gi 1776288214 597 TYNKLVTM 604
Cdd:PRK13549 231 TEDDIITM 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
390-586 |
2.84e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.21 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 390 SLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI---KDMNLQSLRGLMGLVTQDSIlfndtikanISL 466
Cdd:PRK10261 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDPY---------ASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 467 GKLDATDDEIIEALKI-------------ANAFEFVNELPLGIYTnigdSGNKLSGGQKQRLSIARAVLKNPPIMILDEA 533
Cdd:PRK10261 415 DPRQTVGDSIMEPLRVhgllpgkaaaarvAWLLERVGLLPEHAWR----YPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 534 TSALDTEsekfVQVALENMM---QNRTSIV---IAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK10261 491 VSALDVS----IRGQIINLLldlQRDFGIAylfISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
369-593 |
2.86e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.97 E-value: 2.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFkYQDETVLKDFSLSIKKGQTVALVGQSGSGKS-TIANLM------TRfydVNDGTISIDGINIKdmnLQS 441
Cdd:PRK10418 3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpagVR---QTAGRVLLDGKPVA---PCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRG-LMGLVTQD-SILFN----------DTIKAnisLGKL--DATDDEIIEALKIANAFEFVNELPLgiytnigdsgnKL 507
Cdd:PRK10418 76 LRGrKIATIMQNpRSAFNplhtmhtharETCLA---LGKPadDATLTAALEAVGLENAARVLKLYPF-----------EM 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 508 SGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTS--IVIAHRLSTIQK-ADLIVVMQKGKIVE 584
Cdd:PRK10418 142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVE 221
|
....*....
gi 1776288214 585 QGTHDELIA 593
Cdd:PRK10418 222 QGDVETLFN 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
372-582 |
3.47e-16 |
|
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: 76.70 E-value: 3.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQdetvLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL-MGLVT 450
Cdd:cd03215 6 EVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QD----SILFNDTIKANISLGKLdatddeiiealkianafefvnelplgiytnigdsgnkLSGGQKQRLSIARAVLKNPP 526
Cdd:cd03215 82 EDrkreGLVLDLSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPR 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQNRTSIVIahrLST-----IQKADLIVVMQKGKI 582
Cdd:cd03215 125 VLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
371-538 |
3.85e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 78.75 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKY----QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlQSLRGL- 445
Cdd:COG4525 4 LTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG--------VPVTGPg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 --MGLVTQDSILFN-DTIKANISLG-KLDATDDeiIEALKIANAFefvneLPLgiyTNIGDSGNK----LSGGQKQRLSI 517
Cdd:COG4525 76 adRGVVFQKDALLPwLNVLDNVAFGlRLRGVPK--AERRARAEEL-----LAL---VGLADFARRriwqLSGGMRQRVGI 145
|
170 180
....*....|....*....|.
gi 1776288214 518 ARAVLKNPPIMILDEATSALD 538
Cdd:COG4525 146 ARALAADPRFLLMDEPFGALD 166
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
371-538 |
6.42e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.82 E-value: 6.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlrglmGLVT 450
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFN-DTIKANISLG-KLDATDdeiiEALKIANAFEFVNELPLgiytniGDSGNK----LSGGQKQRLSIARAVLKN 524
Cdd:PRK11248 77 QNEGLLPwRNVQDNVAFGlQLAGVE----KMQRLEIAHQMLKKVGL------EGAEKRyiwqLSGGQRQRVGIARALAAN 146
|
170
....*....|....
gi 1776288214 525 PPIMILDEATSALD 538
Cdd:PRK11248 147 PQLLLLDEPFGALD 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
371-578 |
8.05e-16 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 77.06 E-value: 8.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFNDTIKANISLG---KLDATDDEIIealkIANAFEFvnELPLGIYT-NIgdsgNKLSGGQKQRLSIARAVLKNPP 526
Cdd:PRK10247 88 QTPTLFGDTVYDNLIFPwqiRNQQPDPAIF----LDDLERF--ALPDTILTkNI----AELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQNRTSIVI--AHRLSTIQKADLIVVMQ 578
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQ 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
374-593 |
8.48e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 8.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 374 KNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISID--GINIKDMNLQSLRGLMGLVTQ 451
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 DSILFNDTIKANIsLGKLDATDDEIIEALKiANAFEFVNELPLgiyTNIGDS-GNKLSGGQKQRLSIARAVLKNPPIMIL 530
Cdd:PRK10895 87 ASIFRRLSVYDNL-MAVLQIRDDLSAEQRE-DRANELMEEFHI---EHLRDSmGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 531 DEATSALDTESEKFVQVALENMMQNRTSIVIA-HRL-STIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
374-592 |
1.32e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 374 KNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDS 453
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 454 ILFND-TIKANISLGKL----------DATDDEIIEALKIAnafefvnelplGIYTNIGDSGNKLSGGQKQRLSIARAVL 522
Cdd:PRK10253 91 TTPGDiTVQELVARGRYphqplftrwrKEDEEAVTKAMQAT-----------GITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 523 KNPPIMILDEATSALDTESE-KFVQVALE-NMMQNRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDELI 592
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQiDLLELLSElNREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
390-591 |
1.39e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 78.24 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 390 SLSIKKGQTVALVGQSGSGKS----TIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGlvTQDSILFNDTIKaniS 465
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVG--AEVAMIFQDPMT---S 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 466 LGKLDATDDEIIEALKI----------ANAFEFVNE--LP-----LGIYTnigdsgNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVhqggnkktrrQRAIDLLNQvgIPdpasrLDVYP------HQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 529 ILDEATSALD-TESEKFVQVALE-NMMQNRTSIVIAHRLSTI-QKADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11022 176 IADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
90-314 |
1.43e-15 |
|
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: 77.50 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYsEKRK-GDVISRISAdVNEVQNSFL-A 167
Cdd:cd18567 41 LTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF-EKRHlGDIVSRFGS-LDEIQQTLTtG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 ILELIVkEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQS----TKAQQEQGTFLstieETIGGLKVV 243
Cdd:cd18567 119 FVEALL-DGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRATeeqiVASAKEQSHFL----ETIRGIQTI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 244 KGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEF-MGITVIAIlLWYGGQMVlidksLDGA-------AFIAY 314
Cdd:cd18567 194 KLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLlFGLENILV-IYLGALLV-----LDGEftvgmlfAFLAY 266
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
371-594 |
1.79e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 77.54 E-value: 1.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlRGLMGLVT 450
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFND-TIKANISL-GKLDATDDEIIEALkIANAFEFVnELPLGIYTNIGDsgnkLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK13537 87 QFDNLDPDfTVRENLLVfGRYFGLSAAAARAL-VPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNRTSIVI-------AHRLstiqkADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPHALIES 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
375-593 |
2.00e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 77.06 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 375 NINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDV-----NDGTISIDGINIKDM-NLQSLRGLMGL 448
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFNDTIKANISLGkldatddeiIEALKIANAFEF-------VNELPL--GIYTNIGDSGNKLSGGQKQRLSIAR 519
Cdd:PRK14271 106 LFQRPNPFPMSIMDNVLAG---------VRAHKLVPRKEFrgvaqarLTEVGLwdAVKDRLSDSPFRLSGGQQQLLCLAR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 520 AVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
371-593 |
2.24e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 2.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNlQSLRGLMG--L 448
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILF-NDTIKANISLGKLDATDDEIIEALKIANafefvnelpLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK15439 91 VPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAA---------LGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 528 MILDEATSALD-TESEK-FVQValeNMMQNR-TSIV-IAHRLSTI-QKADLIVVMQKGKIVEQG-----THDELIA 593
Cdd:PRK15439 162 LILDEPTASLTpAETERlFSRI---RELLAQgVGIVfISHKLPEIrQLADRISVMRDGTIALSGktadlSTDDIIQ 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
373-589 |
3.36e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.73 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 373 VKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG-----INIKDMNLQSLRGLM- 446
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 ---GLVTQ---DSILFNDTIKANIS----------LGKLDATDDEIIEALKIANAfefvnelplgiytNIGDSGNKLSGG 510
Cdd:PRK11701 89 tewGFVHQhprDGLRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDAA-------------RIDDLPTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 511 QKQRLSIARAVLKNPPIMILDEATSALDTEsekfVQVALENMMQNRTS------IVIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLLVMKQGRVV 231
|
....*.
gi 1776288214 584 EQGTHD 589
Cdd:PRK11701 232 ESGLTD 237
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
15-345 |
5.51e-15 |
|
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: 75.98 E-value: 5.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 15 KKYAFLNIFFNVLYALFStlsfvALIPMLqvlfdkNKQITEKPVYHGILkiqdygqDYLSYYITTTkgthesgyvLSIMV 94
Cdd:cd18540 1 KKLLILLIILMLLVALLD-----AVFPLL------TKYAIDHFITPGTL-------DGLTGFILLY---------LGLIL 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 95 AIIISIFLLKNLADYaamffitfLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVK 174
Cdd:cd18540 54 IQALSVFLFIRLAGK--------IEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 175 EPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNT 254
Cdd:cd18540 126 GITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 255 VFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLIDKSLDG--AAFIAYmglAYNILTPAKAISKAS 332
Cdd:cd18540 206 EFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGtlVAFISY---ATQFFEPIQQLARVL 282
|
330
....*....|...
gi 1776288214 333 YGVKRGNAAAERV 345
Cdd:cd18540 283 AELQSAQASAERV 295
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
379-586 |
9.83e-15 |
|
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: 73.91 E-value: 9.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 379 KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI---NIKDMNLQSLRGLMGLVTQ---- 451
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwKRRKKFLRRIGVVFGQKTQlwwd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 ----DSILFNDTIkANISLGKLDATDDEIIEALKIAnafEFVNElPLgiytnigdsgNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03267 110 lpviDSFYLLAAI-YDLPPARFKKRLDELSELLDLE---ELLDT-PV----------RQLSLGQRMRAEIAAALLHEPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:cd03267 175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
369-586 |
1.31e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.53 E-value: 1.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFKYQD-ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKdmnlQSLR-GLM 446
Cdd:PRK15056 5 AGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQkNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDS-------ILFNDTIKANIS-----LGKLDATDDEIIEAlkianAFEFVNELPLGiYTNIGDsgnkLSGGQKQR 514
Cdd:PRK15056 81 AYVPQSEevdwsfpVLVEDVVMMGRYghmgwLRRAKKRDRQIVTA-----ALARVDMVEFR-HRQIGE----LSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESE-KFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQG 586
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
371-591 |
2.14e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 74.35 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDET-----VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDM-------- 437
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 438 ----------------NLQSLRGLMGLVTQ--DSILFNDTIKANISLGKLD-ATDDEiiEALKIANAFEFVNELPLGIyt 498
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSmGVSKE--EAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 499 nIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRL-STIQKADLIVV 576
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIF 237
|
250
....*....|....*.
gi 1776288214 577 MQKGKIVEQG-THDEL 591
Cdd:PRK13651 238 FKDGKIIKDGdTYDIL 253
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
371-594 |
3.83e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 73.99 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKN--INFKYQDE--TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN---DGTISIDG---INIKDMNLQ 440
Cdd:PRK09473 13 LDVKDlrVTFSTPDGdvTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGreiLNLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGlmglvTQDSILFND-----------------TIKANISLGKLDATDDEI--IEALKIANAFEFVNELPlgiytnig 501
Cdd:PRK09473 93 KLRA-----EQISMIFQDpmtslnpymrvgeqlmeVLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYP-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 502 dsgNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTEsekfVQVALENMMQ------NRTSIVIAHRLSTIQK-ADLI 574
Cdd:PRK09473 160 ---HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVT----VQAQIMTLLNelkrefNTAIIMITHDLGVVAGiCDKV 232
|
250 260
....*....|....*....|
gi 1776288214 575 VVMQKGKIVEQGTHDELIAH 594
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQ 252
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
379-594 |
4.61e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.30 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 379 KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIAN-LMTRFYDVN-DGTISIDGINIKDMNLQSlrglMGLVTQDSILF 456
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANNRKPTKQILKR----TGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 457 -NDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTN--IGDSGNK-LSGGQKQRLSIARAVLKNPPIMILDE 532
Cdd:PLN03211 153 pHLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 533 ATSALDTESEKFVQVALENMMQNRTSIVIA-HRLST--IQKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
371-587 |
7.01e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTI----ANLMT------RFYDVNDGTISIDGINIKDmnLQ 440
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITgdksagSHIELLGRTVQREGRLARD--IR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 441 SLRGLMGLVTQDSILFND-TIKANISLGKLDAT--------------DDEIIEALKIANAFEFVNElplgiytnigdSGN 505
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAHQ-----------RVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 506 KLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLS-TIQKADLIVVMQKGKI 582
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
....*
gi 1776288214 583 VEQGT 587
Cdd:PRK09984 232 FYDGS 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
390-591 |
1.43e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 390 SLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlQSLRGL-------MGLVT--QDSILFNDT- 459
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG--------QHIEGLpghqiarMGVVRtfQHVRLFREMt 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 ------------IKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIYTNiGDSGNkLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK11300 97 vienllvaqhqqLKTGLFSGLLKTPAFRRAESEALDRAATWLERVGLLEHAN-RQAGN-LAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 528 MILDEATSALD-TESEKFVQVALENMMQNRTSI-VIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11300 175 LMLDEPAAGLNpKETKELDELIAELRNEHNVTVlLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
375-587 |
1.51e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 375 NINFKYQD----ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL----M 446
Cdd:PRK11629 10 NLCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILFND-TIKANISLGKLdatddeiIEALKIANAFEFVNEL--PLGIYTNIGDSGNKLSGGQKQRLSIARAVLK 523
Cdd:PRK11629 90 GFIYQFHHLLPDfTALENVAMPLL-------IGKKKPAEINSRALEMlaAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 524 NPPIMILDEATSALD--TESEKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQGT 587
Cdd:PRK11629 163 NPRLVLADEPTGNLDarNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
376-586 |
1.71e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 376 INFKYQdetvLKDFSLSIK-----KGQTvALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDM----NLQSLRGLM 446
Cdd:PRK11144 4 LNFKQQ----LGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekgiCLPPEKRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 GLVTQDSILF-NDTIKANISLG---KLDATDDEIIEALKIANafeFVNELPLGiytnigdsgnkLSGGQKQRLSIARAVL 522
Cdd:PRK11144 79 GYVFQDARLFpHYKVRGNLRYGmakSMVAQFDKIVALLGIEP---LLDRYPGS-----------LSGGEKQRVAIGRALL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 523 KNPPIMILDEATSALDTESEKFVQVALENMMQN-RTSIV-IAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK11144 145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILyVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
380-577 |
1.78e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 69.18 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 380 YQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqslRGLMGLVTQDSIL---F 456
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 457 NDTIKANISLG---------KLDATD----DEIIEALKIAnAFEfvnELPLGiytnigdsgnKLSGGQKQRLSIARAVLK 523
Cdd:NF040873 71 PLTVRDLVAMGrwarrglwrRLTRDDraavDDALERVGLA-DLA---GRQLG----------ELSGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 524 NPPIMILDEATSALDTESEKFVQVAL-ENMMQNRTSIVIAHRLSTIQKADLIVVM 577
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
389-594 |
1.99e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.86 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 389 FSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNdGTISIDGINIKDMNLQSL-----RGLMGlvtQD-SILFNDtika 462
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-WHVTADRFRWNGIDLLKLsprerRKIIG---REiAMIFQE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 463 niSLGKLDAT---DDEIIEAL---------------KIANAFEFVNElpLGI--YTNIGDS-GNKLSGGQKQRLSIARAV 521
Cdd:COG4170 98 --PSSCLDPSakiGDQLIEAIpswtfkgkwwqrfkwRKKRAIELLHR--VGIkdHKDIMNSyPHELTEGECQKVMIAMAI 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 522 LKNPPIMILDEATSALDTESEkfVQV--ALENMMQNR-TSIV-IAHRLSTI-QKADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQ--AQIfrLLARLNQLQgTSILlISHDLESIsQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
386-593 |
2.15e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNLQSLRGLMG----LVTQDSILFND-TI 460
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAALAagvaIIYQELHLVPEmTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLGKLDATDDEIIEALKIANAFEFVNELPLGIytnigDSGNK---LSGGQKQRLSIARAVLKNPPIMILDEATSAL 537
Cdd:PRK11288 97 AENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDI-----DPDTPlkyLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 538 DT-ESEKFVQVALENMMQNRTSIVIAHRLSTI-QKADLIVVMQKGKIVE------QGTHDELIA 593
Cdd:PRK11288 172 SArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQ 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
371-586 |
2.27e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGI--NIKDMNLQSLRGLmGL 448
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKLAAQLGI-GI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILFND-TIKANISLGKL---DATDDEIIEALKIANAFEFVnELPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKN 524
Cdd:PRK09700 85 IYQELSVIDElTVLENLYIGRHltkKVCGVNIIDWREMRVRAAMM-LLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 525 PPIMILDEATSALDTESEKFVQVALENMMQNRTSIV-IAHRLSTIQK-ADLIVVMQKGKIVEQG 586
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
382-562 |
2.56e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 382 DETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGlvTQDSILFNDTIK 461
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 462 ANISL--GKLDATDDEIIEALkianafEFVNelpLGIYTNIgdSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDT 539
Cdd:PRK13539 92 ENLEFwaAFLGGEELDIAAAL------EAVG---LAPLAHL--PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....*.
gi 1776288214 540 ESEKfvqvALENMMQ---NRTSIVIA 562
Cdd:PRK13539 161 AAVA----LFAELIRahlAQGGIVIA 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
381-564 |
3.31e-13 |
|
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: 67.95 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 381 QDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqsLRGLMgLVTQdsilfndti 460
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE----------GEDLL-FLPQ--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLGKLDatddeiiEALkianafefvnelplgIYTnigdSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTE 540
Cdd:cd03223 72 RPYLPLGTLR-------EQL---------------IYP----WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180
....*....|....*....|....*.
gi 1776288214 541 SEKfvqvALENMMQNR--TSIVIAHR 564
Cdd:cd03223 126 SED----RLYQLLKELgiTVISVGHR 147
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
384-585 |
3.67e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL----MGLVTQdSILFNDT 459
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhVGFVFQ-SFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 IKA--NISLGKL------DATDDEIIEALKIANAFEFVNELPlgiytnigdsgNKLSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:PRK10584 103 LNAleNVELPALlrgessRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 532 EATSALDTES-EKFVQVALE-NMMQNRTSIVIAHRLSTIQKADLIVVMQKGKIVEQ 585
Cdd:PRK10584 172 EPTGNLDRQTgDKIADLLFSlNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
371-604 |
6.17e-13 |
|
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: 71.39 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN--DGTISIDGINIKDMNLQSL-RGLMG 447
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFND-TIKANISLG-KLDATDDEIIEALKIANAFEFVNELPLGIYTNIGDSGNkLSGGQKQRLSIARAVLKNP 525
Cdd:TIGR02633 82 IIHQELTLVPElSVAENIFLGnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGD-YGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 526 PIMILDEATSALdTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVeqGTHDeliAHNGTYNKLV 602
Cdd:TIGR02633 161 RLLILDEPSSSL-TEKETEILLDIIRDLKAHgvACVYISHKLNEVKAvCDTICVIRDGQHV--ATKD---MSTMSEDDII 234
|
..
gi 1776288214 603 TM 604
Cdd:TIGR02633 235 TM 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
383-584 |
6.93e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.06 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 383 ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYdvnDGTISIDGINIKDMNLQSLRGLMglvtqDSILFNDTIKA 462
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL---KGTPVAGCVDVPDNQFGREASLI-----DAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 463 NIslgkldatddEIIEALKIANAFEFVNelplgiytnigdSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESE 542
Cdd:COG2401 115 AV----------ELLNAVGLSDAVLWLR------------RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1776288214 543 KFVQVALENMMQNR--TSIVIAHR---LSTIQkADLIVVMQKGKIVE 584
Cdd:COG2401 173 KRVARNLQKLARRAgiTLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
298-587 |
7.07e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 71.97 E-value: 7.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 298 QMVLIDKSLDG--AAFI--AYMGlAYNILTPAKAISKASYGVKrGNAAAERVLEILDQENPITSK------PDAIVKTSF 367
Cdd:TIGR01257 841 KMMLLDAALYGllAWYLdqVFPG-DYGTPLPWYFLLQESYWLG-GEGCSTREERALEKTEPLTEEmedpehPEGINDSFF 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIE-------VKNIN--FKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIkDMN 438
Cdd:TIGR01257 919 ERELPglvpgvcVKNLVkiFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETN 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 439 LQSLRGLMGLVTQDSILFNDTIKANISL--GKLDATDDEiiEA-LKIANAFEfvnelPLGIYTNIGDSGNKLSGGQKQRL 515
Cdd:TIGR01257 998 LDAVRQSLGMCPQHNILFHHLTVAEHILfyAQLKGRSWE--EAqLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKL 1070
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLStiqKADL----IVVMQKGKIVEQGT 587
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
371-579 |
7.27e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 7.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDginikdmnlQSLRglMGLVT 450
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN---------GKLR--IGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QdSILFNDTIKANIS---LGKLDATDDEIIEALKIANAFEFVNElPLgiytnigdsgNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK09544 74 Q-KLYLDTTLPLTVNrflRLRPGTKKEDILPALKRVQAGHLIDA-PM----------QKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 528 MILDEATSALDTESekfvQVALENMM-QNRTS-----IVIAHrlstiqkaDLIVVMQK 579
Cdd:PRK09544 142 LVLDEPTQGVDVNG----QVALYDLIdQLRREldcavLMVSH--------DLHLVMAK 187
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
372-534 |
7.33e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 7.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINfkyqDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDmNLQSLRGLMGLV 449
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRS-PRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQD----SILFNDTIKANISLGKLD--------------ATDDEIIEALKIAnafefvnelPLGIYTNIGDsgnkLSGGQ 511
Cdd:COG1129 333 PEDrkgeGLVLDLSIRENITLASLDrlsrgglldrrrerALAEEYIKRLRIK---------TPSPEQPVGN----LSGGN 399
|
170 180
....*....|....*....|...
gi 1776288214 512 KQRLSIARAVLKNPPIMILDEAT 534
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
371-542 |
1.05e-12 |
|
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: 67.13 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFNDTIKANISLGKLDATDDEIIEALKIAN--AFEfvnELPLgiytnigdsgNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEEALARVGlnGFE---DRPV----------AQLSAGQQRRVALARLLLSGRPLW 147
|
170
....*....|....
gi 1776288214 529 ILDEATSALDTESE 542
Cdd:cd03231 148 ILDEPTTALDKAGV 161
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
370-591 |
2.11e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 68.72 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNINFKYQDET-VLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTrfydVNDGTISIDGINIKDMNlQSLRG 444
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGLER----ITSGEIWIGGRVVNELE-PADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 L-MglVTQDSILF-NDTIKANISLG-KLDATDDEIIEAlKIANAF------EFVNELPlgiytnigdsgNKLSGGQKQRL 515
Cdd:PRK11650 78 IaM--VFQNYALYpHMSVRENMAYGlKIRGMPKAEIEE-RVAEAArilelePLLDRKP-----------RELSGGQRQRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTeseKF-VQVALE-NMMQNR---TSIVIAH-RLSTIQKADLIVVMQKGKIvEQ-GTH 588
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLDA---KLrVQMRLEiQRLHRRlktTSLYVTHdQVEAMTLADRVVVMNGGVA-EQiGTP 219
|
...
gi 1776288214 589 DEL 591
Cdd:PRK11650 220 VEV 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
371-599 |
2.67e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.83 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKD-MNLQSLRGLMGLV 449
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQDSILFND-TIKANISLGKLDATDDEIIEalKIANAFEFVNELplgiYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK11614 86 PEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELFPRL----HERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 529 ILDEATSALdteSEKFVQVALENMMQNRTS-----IVIAHRLSTIQKADLIVVMQKGKIVEQGTHDELIAHNGTYN 599
Cdd:PRK11614 160 LLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRS 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
371-588 |
3.36e-12 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 66.74 E-value: 3.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTI-ANLMTRF-YDVNDGTISIDGINIKDMNLQSLRG---L 445
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSPEDRAGegiF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MG-------------LVTQDSILFNDTIKANISLGKLDATD--DEIIEALKianafefvneLPLGIYT---NIGdsgnkL 507
Cdd:PRK09580 82 MAfqypveipgvsnqFFLQTALNAVRSYRGQEPLDRFDFQDlmEEKIALLK----------MPEDLLTrsvNVG-----F 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 508 SGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQ-NRTSIVIAH--RLSTIQKADLIVVMQKGKIVE 584
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226
|
....
gi 1776288214 585 QGTH 588
Cdd:PRK09580 227 SGDF 230
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
131-301 |
4.64e-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: 67.14 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 131 YKKTLELPLAFYSEKRKGDVISRisadVNEVQN--SFL--AILELIVKEPLTIIFtITTMLIISPKLTLFVFIFIPVSGY 206
Cdd:cd18588 82 FRHLLRLPLSYFESRQVGDTVAR----VRELESirQFLtgSALTLVLDLVFSVVF-LAVMFYYSPTLTLIVLASLPLYAL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 207 IISLIGKQLKKQSTKAQQ---EQGTFLStieETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEF 283
Cdd:cd18588 157 LSLLVTPILRRRLEEKFQrgaENQSFLV---ETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQL 233
|
170
....*....|....*...
gi 1776288214 284 MGITVIAILLWYGGQMVL 301
Cdd:cd18588 234 IQKLTTLAILWFGAYLVM 251
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
111-314 |
1.13e-11 |
|
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: 65.80 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 111 AMFFITFLRNGVlrDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIIS 190
Cdd:cd18784 58 GLFTLAMARLNI--RIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 191 PKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSnsi 270
Cdd:cd18784 136 WQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLK--- 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776288214 271 gNRQNLA----SPASEFMGITVIAILLWYGGQMVLIDKsLDGAAFIAY 314
Cdd:cd18784 213 -IKEALAyggyVWSNELTELALTVSTLYYGGHLVITGQ-ISGGNLISF 258
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
90-324 |
1.14e-11 |
|
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: 65.69 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISadvnEVQNsflaIL 169
Cdd:cd18782 41 LYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS----ELDT----IR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTI-------IFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKV 242
Cdd:cd18782 113 GFLTGTALTTlldvlfsVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 243 VKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLiDKSLDGAAFIAYMGLAYNIL 322
Cdd:cd18782 193 VKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVL-RGELTLGQLIAFRILSGYVT 271
|
..
gi 1776288214 323 TP 324
Cdd:cd18782 272 GP 273
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
386-564 |
1.38e-11 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 64.51 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINI---KDMNLQSLRGLMGLVTQDS-ILFNDTIK 461
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 462 ANISLGKL--DATDDEIIEalKIANAFEFVnelplGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDT 539
Cdd:PRK10908 98 DNVAIPLIiaGASGDDIRR--RVSAALDKV-----GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190
....*....|....*....|....*....|...
gi 1776288214 540 E--------SEKFVQVALENMMQNRTSIVIAHR 564
Cdd:PRK10908 171 AlsegilrlFEEFNRVGVTVLMATHDIGLISRR 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
371-596 |
1.45e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.22 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTIS-IDGINI------------KDM 437
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwSENANIgyyaqdhaydfeNDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 438 NL--------------QSLRGLmglvtqdsilfndtikanisLGKLDATDDEIIEALKIanafefvnelplgiytnigds 503
Cdd:PRK15064 400 TLfdwmsqwrqegddeQAVRGT--------------------LGRLLFSQDDIKKSVKV--------------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 504 gnkLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMmqNRTSIVIAH-R--LSTIqkADLIVVMQKG 580
Cdd:PRK15064 439 ---LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY--EGTLIFVSHdRefVSSL--ATRIIEITPD 511
|
250
....*....|....*..
gi 1776288214 581 KIVE-QGTHDELIAHNG 596
Cdd:PRK15064 512 GVVDfSGTYEEYLRSQG 528
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
386-589 |
1.70e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVN--DGTISIDG--INIKDMNLQSLRGL------MGLVTQDSIl 455
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevCRFKDIRDSEALGIviihqeLALIPYLSI- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 456 fndtiKANISLGK---------LDATDDEIIEALKIANafefVNELPLGIYTNIGDsgnklsgGQKQRLSIARAVLKNPP 526
Cdd:NF040905 96 -----AENIFLGNerakrgvidWNETNRRARELLAKVG----LDESPDTLVTDIGV-------GKQQLVEIAKALSKDVK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 527 IMILDEATSAL-DTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEqgTHD 589
Cdd:NF040905 160 LLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE--TLD 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
386-592 |
2.61e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGiniKDMNL----QSLRGLMGLVTQD-SILFNDTI 460
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFngpkSSQEAGIGIIHQElNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISLG-------------KLDATDDEIIEALKIA-NAFEFVNELPLgiytnigdsgnklsgGQKQRLSIARAVLKNPP 526
Cdd:PRK10762 97 AENIFLGrefvnrfgridwkKMYAEADKLLARLNLRfSSDKLVGELSI---------------GEQQMVEIAKVLSFESK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 527 IMILDEATSAL-DTESEKFVQVALENMMQNRTSIVIAHRLSTI-QKADLIVVMQKGKI-----VEQGTHDELI 592
Cdd:PRK10762 162 VIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFiaereVADLTEDSLI 234
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
90-329 |
3.31e-11 |
|
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: 64.45 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 90 LSIMVAIIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRIsadvnevqNSFLAIL 169
Cdd:cd18555 41 LNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRA--------NSNVYIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 170 ELIVKEPLTIIFTITT-------MLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKV 242
Cdd:cd18555 113 QILSNQVISLIIDLLLlviyliyMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIET 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 243 VKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAYMGLAYNIL 322
Cdd:cd18555 193 IKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLV-INGELTLGELIAFSSLAGSFL 271
|
....*..
gi 1776288214 323 TPAKAIS 329
Cdd:cd18555 272 TPIVSLI 278
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
389-590 |
4.76e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 389 FSLSIKKGQTVALVGQSGSGKST----IANLMTrfydvNDGTISIDGINIKDMNLQSL---RGLmgLVTQDSILFNDTI- 460
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELarhRAY--LSQQQTPPFAMPVf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 -------KANISLGKLDATDDEIIEALKIANafefvnelplgiytNIGDSGNKLSGGQKQRLSIARAVLK-----NP--P 526
Cdd:PRK03695 88 qyltlhqPDKTRTEAVASALNEVAEALGLDD--------------KLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 527 IMILDEATSALDTESekfvQVALENMM-----QNRTSIVIAHRLS-TIQKADLIVVMQKGKIVEQGTHDE 590
Cdd:PRK03695 154 LLLLDEPMNSLDVAQ----QAALDRLLselcqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
371-591 |
7.67e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 63.25 E-value: 7.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSL---RGLMG 447
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQDSILFND-TIKANISLGKLDATD--DEII--------EALKIANAfefVNELPlgiytnigdsgNKLSGGQKQRLS 516
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHTQlpAPLLhstvmmklEAVGLRGA---AKLMP-----------SELSGGMARRAA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 517 IARAVLKNPPIMILDEATSALDTESEK-FVQVALE-NMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDEL 591
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGvLVKLISElNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
371-572 |
9.82e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.50 E-value: 9.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVT 450
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QDSILFNDTIKAN------ISLGKLDAtdDEIIEALKIANAFEFvnelPLGIytnigdsgnkLSGGQKQRLSIARAVLKN 524
Cdd:PRK13540 82 RSGINPYLTLRENclydihFSPGAVGI--TELCRLFSLEHLIDY----PCGL----------LSSGQKRQVALLRLWMSK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 525 PPIMILDEATSALDtesEKFVQVALENMMQNRTS----IVIAHRLSTIQKAD 572
Cdd:PRK13540 146 AKLWLLDEPLVALD---ELSLLTIITKIQEHRAKggavLLTSHQDLPLNKAD 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
368-593 |
1.92e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQ--DETVLK---DFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISID-GINIKDMNLQS 441
Cdd:TIGR03269 277 EPIIKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 --LRG----LMGLVTQDSILF-NDTIKANIS----------LGKLDAtddeiIEALKIAN-----AFEFVNELPlgiytn 499
Cdd:TIGR03269 357 pdGRGrakrYIGILHQEYDLYpHRTVLDNLTeaiglelpdeLARMKA-----VITLKMVGfdeekAEEILDKYP------ 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 500 igdsgNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEkfVQVAlENMMQNR-----TSIVIAHRLSTIQK-ADL 573
Cdd:TIGR03269 426 -----DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITK--VDVT-HSILKAReemeqTFIIVSHDMDFVLDvCDR 497
|
250 260
....*....|....*....|
gi 1776288214 574 IVVMQKGKIVEQGTHDELIA 593
Cdd:TIGR03269 498 AALMRDGKIVKIGDPEEIVE 517
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
371-593 |
3.75e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 61.74 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKN--INFKYQDETV--LKDFSLSIKKGQTVALVGQSGSGKSTIANlmtrfydvndgtiSIDGINiKDmNLQslrglm 446
Cdd:PRK15093 4 LDIRNltIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAK-------------AICGVT-KD-NWR------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 glVTQDSILFNDT-------------IKANISL------GKLDATDD---EIIEAL---------------KIANAFEFV 489
Cdd:PRK15093 63 --VTADRMRFDDIdllrlsprerrklVGHNVSMifqepqSCLDPSERvgrQLMQNIpgwtykgrwwqrfgwRKRRAIELL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 490 NELPLGIYTNIGDS-GNKLSGGQKQRLSIARAVLKNPPIMILDEATSALD--TESEKFVQVALENMMQNRTSIVIAHRLS 566
Cdd:PRK15093 141 HRVGIKDHKDAMRSfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEptTQAQIFRLLTRLNQNNNTTILLISHDLQ 220
|
250 260
....*....|....*....|....*...
gi 1776288214 567 TIQK-ADLIVVMQKGKIVEQGTHDELIA 593
Cdd:PRK15093 221 MLSQwADKINVLYCGQTVETAPSKELVT 248
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
88-324 |
1.04e-09 |
|
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: 59.90 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSI-MVAIIISIFLLKNLADYaamfFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRIsADVNEVQN--- 163
Cdd:cd18566 42 QVLVIgVVIAILLESLLRLLRSY----ILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERL-NSLEQIREflt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 164 --SFLAILELivkePLTIIFtITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLK 241
Cdd:cd18566 117 gqALLALLDL----PFVLIF-LGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIH 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 242 VVKGYNSENyfntvfqNSTERFFNLSNS-------IGNRQNLASPASEFMGITVIAILLWYGGQMVlIDKSLDGAAFIAY 314
Cdd:cd18566 192 TIKAMAMEP-------QMLRRYERLQANaayagfkVAKINAVAQTLGQLFSQVSMVAVVAFGALLV-INGDLTVGALIAC 263
|
250
....*....|
gi 1776288214 315 MGLAYNILTP 324
Cdd:cd18566 264 TMLSGRVLQP 273
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
368-591 |
1.07e-09 |
|
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: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 368 DDSIEVKNINFKYQDETVLK---DFSLSIKKGQTVALVGQSGSGKS-TIANLMTRFYDVNDGTISIDG--INIKDMnLQS 441
Cdd:TIGR02633 255 DVILEARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGkpVDIRNP-AQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 442 LRGLMGLVTQD----SILFNDTIKANISLGKLD-----------ATDDEIIEALKIANAFEFVNELPLGiytnigdsgnK 506
Cdd:TIGR02633 334 IRAGIAMVPEDrkrhGIVPILGVGKNITLSVLKsfcfkmridaaAELQIIGSAIQRLKVKTASPFLPIG----------R 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 507 LSGGQKQRLSIARAVLKNPPIMILDEATSALDTESeKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA-KYEIYKLINQLAQEgvAIIVVSSELAEVLGlSDRVLVIGEGKLK 482
|
....*...
gi 1776288214 584 EQGTHDEL 591
Cdd:TIGR02633 483 GDFVNHAL 490
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
374-586 |
1.33e-09 |
|
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: 58.04 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 374 KNINFKYQDE----TVLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTRFYDVNdGTISIDGINIKDMNLQSlrgl 445
Cdd:cd03233 7 RNISFTTGKGrskiPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKY---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 mglvtQDSILFNdtikanislgkldATDDEIIEALKIANAFEFVNELplgiytNIGDSGNKLSGGQKQRLSIARAVLKNP 525
Cdd:cd03233 82 -----PGEIIYV-------------SEEDVHFPTLTVRETLDFALRC------KGNEFVRGISGGERKRVSIAEALVSRA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 526 PIMILDEATSALDTESE-KFVQVaLENM--MQNRTSIVIAHRLS--TIQKADLIVVMQKGKIVEQG 586
Cdd:cd03233 138 SVLCWDNSTRGLDSSTAlEILKC-IRTMadVLKTTTFVSLYQASdeIYDLFDKVLVLYEGRQIYYG 202
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
372-600 |
1.41e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.67 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQD---ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISI----------DGINIKDMN 438
Cdd:PRK13545 23 KLKDLFFRSKDgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgsaaliaisSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 439 LQS--LRGLMGLVTQDSIlfndtikanislgkldatdDEII-EALKIANAFEFVNElPLGIYtnigdsgnklSGGQKQRL 515
Cdd:PRK13545 103 IENieLKGLMMGLTKEKI-------------------KEIIpEIIEFADIGKFIYQ-PVKTY----------SSGMKSRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDtesEKFVQVALENM----MQNRTSIVIAHRLSTIQ----KAdliVVMQKGKIVEQGT 587
Cdd:PRK13545 153 GFAISVHINPDILVIDEALSVGD---QTFTKKCLDKMnefkEQGKTIFFISHSLSQVKsfctKA---LWLHYGQVKEYGD 226
|
250
....*....|...
gi 1776288214 588 HDELIAHNGTYNK 600
Cdd:PRK13545 227 IKEVVDHYDEFLK 239
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
374-580 |
1.76e-09 |
|
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: 57.64 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 374 KNINF----KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYD--VNDGTISIDGINIKdmnlQSLRGLMG 447
Cdd:cd03232 7 KNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLD----KNFQRSTG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 448 LVTQdsilfNDTIKANISlgkldatddeIIEALKIANAFEfvnelplgiytnigdsgnKLSGGQKQRLSIARAVLKNPPI 527
Cdd:cd03232 83 YVEQ-----QDVHSPNLT----------VREALRFSALLR------------------GLSVEQRKRLTIGVELAAKPSI 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 528 MILDEATSALDTESEKFVQVALENM-MQNRTSIVIAHRLS--TIQKADLIVVMQKG 580
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
372-583 |
1.93e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.43 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFK-YQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGL----- 445
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 ------MGLVTQDSILFN------DTIKAN----ISLGKLDATDDEIIEALKIANAfefvnelplGIYTNIGdsgnKLSG 509
Cdd:COG3845 339 pedrlgRGLVPDMSVAENlilgryRRPPFSrggfLDRKAIRAFAEELIEEFDVRTP---------GPDTPAR----SLSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 510 GQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSI-VIAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
384-591 |
2.41e-09 |
|
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: 57.37 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLM------GLVTQDSILFN 457
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILylghlpGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 458 DTIKANIslgkLDATDDEIIEALKIANAFEFVNeLPLgiytnigdsgNKLSGGQKQRLSIARAVLKNPPIMILDEATSAL 537
Cdd:TIGR01189 94 LHFWAAI----HGGAQRTIEDALAAVGLTGFED-LPA----------AQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1776288214 538 DTES-EKFvqvalenmmqnrTSIVIAHrlstiqkadlivvMQKGKIVEQGTHDEL 591
Cdd:TIGR01189 159 DKAGvALL------------AGLLRAH-------------LARGGIVLLTTHQDL 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
372-540 |
3.27e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMtrfydvndgtisidginIKDMNLQSLRGLMGlvTQ 451
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLM-----------------LGQLQADSGRIHCG--TK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 DSILFND----------TIKANISLGKLDAT----DDEIIEALKianAFEFVnelPLGIYTNIgdsgNKLSGGQKQRLSI 517
Cdd:PRK11147 382 LEVAYFDqhraeldpekTVMDNLAEGKQEVMvngrPRHVLGYLQ---DFLFH---PKRAMTPV----KALSGGERNRLLL 451
|
170 180
....*....|....*....|...
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTE 540
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVE 474
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
383-566 |
4.34e-09 |
|
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: 59.38 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 383 ETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDginiKDMNLQSL--RGLMGLVT-QDSILFNDT 459
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFYVpqRPYMTLGTlRDQIIYPDS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 IKANISLGKLDATDDEIIEALKIANAFEfvnelPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDT 539
Cdd:TIGR00954 541 SEDMKRRGLSDKDLEQILDNVQLTHILE-----REGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
|
170 180
....*....|....*....|....*..
gi 1776288214 540 ESEKFVQVALENMmqNRTSIVIAHRLS 566
Cdd:TIGR00954 616 DVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
379-602 |
4.47e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 379 KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDmNLQSLRGLMGLV----TQ--- 451
Cdd:COG4586 31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVfgqrSQlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 -----DSILFNDTIKaNISLGKLDATDDEIIEALKIAnafEFVNElPLgiytnigdsgNKLSGGQKQRLSIARAVLKNPP 526
Cdd:COG4586 110 dlpaiDSFRLLKAIY-RIPDAEYKKRLDELVELLDLG---ELLDT-PV----------RQLSLGQRMRCELAAALLHRPK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 527 IMILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAHNGTYNKLV 602
Cdd:COG4586 175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIV 253
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
386-586 |
5.77e-09 |
|
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: 55.79 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIanlmtrfydVNDGtisidginIKDMNLQSLRGLMGLVTQDSILFNDTIKANIS 465
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL---------VNEG--------LYASGKARLISFLPKFSRNKLIFIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 466 LGkldatddeiiealkianafefvnelpLGiYTNIGDSGNKLSGGQKQRLSIARAVLKNPP--IMILDEATSALDTES-E 542
Cdd:cd03238 74 VG--------------------------LG-YLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1776288214 543 KFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVM------QKGKIVEQG 586
Cdd:cd03238 127 QLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
386-587 |
6.15e-09 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.24 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIAN------LMTRFYdvndgtisidGINIKDMNLQSLRGLMGL-----VTQDSI 454
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLH----------LKKEQPGNHDRIEGLEHIdkvivIDQSPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 455 --------------------LFNDTIKA---------------NISlgklDATDDEIIEAL-------KIANAFEFVNEL 492
Cdd:cd03271 81 grtprsnpatytgvfdeireLFCEVCKGkrynretlevrykgkSIA----DVLDMTVEEALeffenipKIARKLQTLCDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 493 PLGiYTNIGDSGNKLSGGQKQRLSIARAVLK---NPPIMILDEATSALDTES-EKFVQVALENMMQNRTSIVIAHRLSTI 568
Cdd:cd03271 157 GLG-YIKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDvKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
250 260
....*....|....*....|....*
gi 1776288214 569 QKADLIVVM------QKGKIVEQGT 587
Cdd:cd03271 236 KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
87-314 |
6.89e-09 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 57.48 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 87 GYVLSIMVAIIISIFLLKNLADyaAMFFITFLRngVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFL 166
Cdd:cd18589 36 TAAITVMSLLTIASAVSEFVCD--LIYNITMSR--IHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 167 AILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPV-------SGYIISLIGKQLKKQSTKAQQeqgtflsTIEETIGG 239
Cdd:cd18589 112 ENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLlllvpkfVGKFQQSLAVQVQKSLARANQ-------VAVETFSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 240 LKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVLIDK--SLDGAAFIAY 314
Cdd:cd18589 185 MKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTvsSGDLVTFVLY 261
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
70-252 |
1.24e-08 |
|
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: 56.73 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 70 QDYLSYYITTTKGTHESGYVLSI-MVAIIISIFLLKNLADYAAMFFITFLRNGVlrdmRNAMYKKTLELPLAFYSEKRKG 148
Cdd:cd18579 21 GLLISYLSSYPDEPLSEGYLLALaLFLVSLLQSLLLHQYFFLSFRLGMRVRSAL----SSLIYRKALRLSSSARQETSTG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 149 DVISRISADVNEVQNSFLAILELIVkEPLTIIFtITTMLIISPKLT-----LFVFIFIPVSGYIISLIGKQLKKQSTKAQ 223
Cdd:cd18579 97 EIVNLMSVDVQRIEDFFLFLHYLWS-APLQIIV-ALYLLYRLLGWAalaglGVLLLLIPLQAFLAKLISKLRKKLMKATD 174
|
170 180
....*....|....*....|....*....
gi 1776288214 224 QEqgtfLSTIEETIGGLKVVKGYNSENYF 252
Cdd:cd18579 175 ER----VKLTNEILSGIKVIKLYAWEKPF 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
395-574 |
1.36e-08 |
|
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: 53.92 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 395 KGQTVALVGQSGSGKSTIANLMTRFYDVNDGT-ISIDGINIKDMNLQSLRGLMglvtqdsilfndtikanislgkldatd 473
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 474 deiiealkianafefvnelplgiytnIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMM 553
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170 180
....*....|....*....|....*...
gi 1776288214 554 -------QNRTSIVIAHRLSTIQKADLI 574
Cdd:smart00382 108 llllkseKNLTVILTTNDEKDLGPALLR 135
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
371-567 |
1.98e-08 |
|
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: 57.25 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIdGINIKdmnlqslrglMGLVT 450
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 Q--DSILFNDTIKANISlGKLDATD--DEIIEALKIANAFEFVNelplgiytniGDSGNK---LSGGQKQRLSIARAVLK 523
Cdd:TIGR03719 392 QsrDALDPNKTVWEEIS-GGLDIIKlgKREIPSRAYVGRFNFKG----------SDQQKKvgqLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 524 NPPIMILDEATSALDTESEKfvqvALENMMQN--RTSIVIAH------RLST 567
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLR----ALEEALLNfaGCAVVISHdrwfldRIAT 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
385-562 |
2.25e-08 |
|
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: 56.87 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 385 VLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRF-YDVNDGTISIDGINI------------KD------MNLQSLRGL 445
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDFNGEARPQPGIKVgylpqepqldptKTvrenveEGVAEIKDA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 MGLVTQDSILFNDTIKANISLGKLDATDDEIIEAlkiANAFEFVNEL----------PlgiytniGDSG-NKLSGGQKQR 514
Cdd:TIGR03719 100 LDRFNEISAKYAEPDADFDKLAAEQAELQEIIDA---ADAWDLDSQLeiamdalrcpP-------WDADvTKLSGGERRR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESekfvqVA-LENMMQNRTSIVIA 562
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAES-----VAwLERHLQEYPGTVVA 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
374-590 |
2.31e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 374 KNINFKYQDE-TVLKDFSLSIKKGQTVALVGQSGSGKST----IANLMTRFYDVNDGTISIDGINIKDMNLQsLRGLMGL 448
Cdd:TIGR00956 64 KLKKFRDTKTfDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSILF-NDTIKANISLGKLDATDDEIIEALKIANAFEFVNELPLGIY-------TNIGDSGNK-LSGGQKQRLSIAR 519
Cdd:TIGR00956 143 NAETDVHFpHLTVGETLDFAARCKTPQNRPDGVSREEYAKHIADVYMATYglshtrnTKVGNDFVRgVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 520 AVLKNPPIMILDEATSALDTESekfvqvALENMMQNRTSIVIAHRLSTI------QKA----DLIVVMQKGKIVEQGTHD 589
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPAD 296
|
.
gi 1776288214 590 E 590
Cdd:TIGR00956 297 K 297
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
391-605 |
2.43e-08 |
|
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: 57.33 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 391 LSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKdMNLQSLRGLMGLVTQ-DSILFNDTIKANISL-GK 468
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAIDDLLTGREHLYLyAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 469 LDATDDEIIEalKIANAFefVNELPLGIYTNigDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFV-QV 547
Cdd:TIGR01257 2039 LRGVPAEEIE--KVANWS--IQSLGLSLYAD--RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNT 2112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 548 ALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAHNGTyNKLVTMQ 605
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGD-GYIVTMK 2170
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
386-592 |
2.56e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.95 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIAN------LMTRFY--DVNDG-TISIDG-------INIKdmnlQSLRG----- 444
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNgaKTVPGrYTSIEGlehldkvIHID----QSPIGrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 445 ----LMGLVTQDSILFNDTIKA------------NISLGKLDA-TDDEII------------------------EALKIA 483
Cdd:TIGR00630 700 npatYTGVFDEIRELFAETPEAkvrgytpgrfsfNVKGGRCEAcQGDGVIkiemhflpdvyvpcevckgkrynrETLEVK 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 484 ---------------NAFEFVNELP-------------LGiYTNIGDSGNKLSGGQKQRLSIARAVLK---NPPIMILDE 532
Cdd:TIGR00630 780 ykgkniadvldmtveEAYEFFEAVPsisrklqtlcdvgLG-YIRLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDE 858
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1776288214 533 ATSALDTES-EKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVM------QKGKIVEQGTHDELI 592
Cdd:TIGR00630 859 PTTGLHFDDiKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEVA 925
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
126-300 |
2.69e-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: 55.42 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 126 MRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLA----ILELIVKEPLTIIFtittMLIISPKLTLFVFIFI 201
Cdd:cd18590 71 LRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALnanvLLRSLVKTLGMLGF----MLSLSWQLTLLTLIEM 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 202 PVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPAS 281
Cdd:cd18590 147 PLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVR 226
|
170
....*....|....*....
gi 1776288214 282 EFMGITVIAILLWYGGQMV 300
Cdd:cd18590 227 RVLQLGVQVLMLYCGRQLI 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
386-563 |
3.02e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.11 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSL-----SIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGinikdmnlqslrglmglvtqDSILFN-DT 459
Cdd:cd03237 10 LGEFTLeveggSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL--------------------DTVSYKpQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 IKANISlGKLDATDDEIIEALKIANAFEfvNEL--PLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSAL 537
Cdd:cd03237 70 IKADYE-GTVRDLLSSITKDFYTHPYFK--TEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180
....*....|....*....|....*...
gi 1776288214 538 DTESEKFVQVALENMMQN--RTSIVIAH 563
Cdd:cd03237 147 DVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
372-538 |
3.43e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.34 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINF---KYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIAnlMTRF---YDVN-DGTISIDGiniKDMNLQSLR- 443
Cdd:NF040905 259 EVKNWTVyhpLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELA--MSVFgrsYGRNiSGTVFKDG---KEVDVSTVSd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 ----GLMgLVTQDS-----ILfNDTIKANISLGKLDATD-----DEIIEaLKIANafEFVNELPL---GIYTNIGdsgnK 506
Cdd:NF040905 334 aidaGLA-YVTEDRkgyglNL-IDDIKRNITLANLGKVSrrgviDENEE-IKVAE--EYRKKMNIktpSVFQKVG----N 404
|
170 180 190
....*....|....*....|....*....|..
gi 1776288214 507 LSGGQKQRLSIARAVLKNPPIMILDEATSALD 538
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
96-263 |
4.90e-08 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits 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. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 54.86 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 96 IIISIFLLKNLADYAAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILeLIVKE 175
Cdd:cd18553 59 ILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQSFL-FILSE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 176 PLTIIFTITTMLIISPKLTLFVFIFIPVSGYIIS-LIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYNSENYFNT 254
Cdd:cd18553 138 IFVILFIYSLLLYVNWKITLVLTLFLGLNVFFITkIVSKKIKKQGKKREESQKKFYKILSETFGNFKIIKLKSNEKEILK 217
|
....*....
gi 1776288214 255 VFQNSTERF 263
Cdd:cd18553 218 NFSQASLKF 226
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
88-318 |
8.96e-08 |
|
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: 54.06 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSIMVAIIISifllknladYAAMFfiTFLRNGVLR------DMRNAMY--KKTLELPLAFYsEKRKGDVISRISADVN 159
Cdd:cd18783 42 YVLTIGVVIALL---------FEGIL--GYLRRYLLLvattriDARLALRtfDRLLSLPIDFF-ERTPAGVLTKHMQQIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 160 EVQNS-----FLAILELIvkeplTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIE 234
Cdd:cd18783 110 RIRQFltgqlFGTLLDAT-----SLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 235 ETIGGLKVVKGYNSE-----NYFNTVFQNSTERF--FNLSNSIgnrQNLASPASEFMGITVIaillWYGGQMVLiDKSLD 307
Cdd:cd18783 185 ETVHGIRTVKSLALEprqrrEWDERVARAIRARFavGRLSNWP---QTLTGPLEKLMTVGVI----WVGAYLVF-AGSLT 256
|
250
....*....|.
gi 1776288214 308 GAAFIAYMGLA 318
Cdd:cd18783 257 VGALIAFNMLA 267
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
380-583 |
1.08e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 380 YQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDginiKDMNLQSL-----RGLMGLVtqdsi 454
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLqqdppRNVEGTV----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 455 lFN----------DTIKANISLGKLDATD---------DEIIEALKIANAFEFVNElplgIYTNIGDSG-------NKLS 508
Cdd:PRK11147 84 -YDfvaegieeqaEYLKRYHDISHLVETDpseknlnelAKLQEQLDHHNLWQLENR----INEVLAQLGldpdaalSSLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 509 GGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFvqvaLENMMQN-RTSIV-IAHRLSTIQK-ADLIVVMQKGKIV 583
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEW----LEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-318 |
2.39e-07 |
|
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: 52.48 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 122 VLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFI 201
Cdd:cd18585 66 LLSNLRVWFYRKLEPLAPARLQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSPALALILLAGL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 202 PVSGYIISLIGKQLKKQSTKAQQEQGTFLST-IEETIGGLKVVKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPA 280
Cdd:cd18585 146 LLAGVVIPLLFYRLGKKIGQQLVQLRAELRTeLVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQAL 225
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1776288214 281 SEFM-GITVIAIlLWYGGQMVlIDKSLDGA--AFIAYMGLA 318
Cdd:cd18585 226 MILLsGLTVWLV-LWLGAPLV-QNGALDGAllAMLVFAVLA 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
372-603 |
3.54e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKYQDETVLK---DFSLSIKKGQTVALVGQSGSGKStiaNLMTRFYDV----NDGTISIDGINIKDMN-LQSLR 443
Cdd:PRK13549 261 EVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRT---ELVQCLFGAypgrWEGEIFIDGKPVKIRNpQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 444 GLMGLVTQD----SILFNDTIKANISLGKLD--ATDDEIIEALKIANAFEFVNELPLGIYT---NIGdsgnKLSGGQKQR 514
Cdd:PRK13549 338 QGIAMVPEDrkrdGIVPVMGVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQK 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 515 LSIARAVLKNPPIMILDEATSALDTESeKFVQVALENMM--QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIveQGthdEL 591
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGA-KYEIYKLINQLvqQGVAIIVISSELPEVLGlSDRVLVMHEGKL--KG---DL 487
|
250
....*....|..
gi 1776288214 592 IAHNGTYNKLVT 603
Cdd:PRK13549 488 INHNLTQEQVME 499
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
385-580 |
3.56e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 53.70 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 385 VLKDFSLSIKKGQTVALVGQSGSGKSTIANLM----TRFYDvnDGTISIDGINIKDMNLQSLRGLM--------GLVTQD 452
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKKQETFARISGYCeqndihspQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 453 SILFNDTIKANISLGKLDATD--DEIIEALKIANAFEFVNELPlgiytniGDSGnkLSGGQKQRLSIARAVLKNPPIMIL 530
Cdd:PLN03140 973 SLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 531 DEATSALDTESEKFVQVALENMMQN-RTSIVIAHRLS--TIQKADLIVVMQKG 580
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTgRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
386-594 |
4.33e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG-INIKDMNlqslRGLMGLVTQ-DSILFNdTIKAN 463
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAIS----AGLSGQLTGiENIEFK-MLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 464 ISLGKLDATDDEIIEalkianafefVNELPLGIYTNIgdsgNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDtesEK 543
Cdd:PRK13546 115 FKRKEIKAMTPKIIE----------FSELGEFIYQPV----KKYSSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 544 FVQVALENMM----QNRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGTHDELIAH 594
Cdd:PRK13546 178 FAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
372-584 |
5.72e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 372 EVKNINFKyqDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN-LQSLRGLMGLVT 450
Cdd:PRK09700 267 EVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 QD----------SILFNDTIKANISLGKLDAT---DDEIIEALKIANAFEFVNELPLGIYTNIgdsgNKLSGGQKQRLSI 517
Cdd:PRK09700 345 ESrrdngffpnfSIAQNMAISRSLKDGGYKGAmglFHEVDEQRTAENQRELLALKCHSVNQNI----TELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 518 ARAVLKNPPIMILDEATSALDTESEKFVQVALENMM-QNRTSIVIAHRLSTIQKA-DLIVVMQKGKIVE 584
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
371-582 |
6.05e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDEtvLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMN-LQSLRGLMGLV 449
Cdd:PRK10982 251 LEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 450 TQD----------SILFNDTIkANI-----SLGKLDATDDE-----IIEALKIANAfefvnelplGIYTNIGdsgnKLSG 509
Cdd:PRK10982 329 TEErrstgiyaylDIGFNSLI-SNIrnyknKVGLLDNSRMKsdtqwVIDSMRVKTP---------GHRTQIG----SLSG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 510 GQKQRLSIARAVLKNPPIMILDEATSALDTESeKF--VQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVMQKGKI 582
Cdd:PRK10982 395 GNQQKVIIGRWLLTQPEILMLDEPTRGIDVGA-KFeiYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
384-587 |
7.87e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 384 TVLKDFSLSIKKGQTVALVGQSGSGKSTI---------ANLMTRFYDVNdGTISIDG---INIKDMNLQSLRGLMGLVTQ 451
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARVT-GDVTLNGeplAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 452 DSILFndTIKANISLGK---------LDATDDEII-EALKIANAFEFVnelplgiytniGDSGNKLSGGQKQRLSIARAV 521
Cdd:PRK13547 94 PAFAF--SAREIVLLGRypharragaLTHRDGEIAwQALALAGATALV-----------GRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 522 LK---------NPPIMILDEATSALDTESEKFVQVALENMMQ--NRTSIVIAHRLSTIQK-ADLIVVMQKGKIVEQGT 587
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGA 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
371-568 |
8.12e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMT----RFYDvNDGTI------SIDGI-NIK---- 435
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYS-NDLTLfgrrrgSGETIwDIKkhig 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 436 ----DMNLQ-----SLRglmglvtqDSIL--FNDTIkanislGKLDATDDE----IIEALKIanafefvnelpLGIYTNI 500
Cdd:PRK10938 340 yvssSLHLDyrvstSVR--------NVILsgFFDSI------GIYQAVSDRqqklAQQWLDI-----------LGIDKRT 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 501 GDSG-NKLSGGQkQRLS-IARAVLKNPPIMILDEATSALDTESEKFVQVALENMM-QNRTSIV------------IAHRL 565
Cdd:PRK10938 395 ADAPfHSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRL 473
|
...
gi 1776288214 566 STI 568
Cdd:PRK10938 474 EFV 476
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
369-575 |
9.99e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 369 DSIEVKNINFKYQDETVlkDFslsiKKGQTVaLVGQSGSGKSTIanlmtrfydvndgtisIDGINIkdmnlqSLRGLM-- 446
Cdd:cd03240 2 DKLSIRNIRSFHERSEI--EF----FSPLTL-IVGQNGAGKTTI----------------IEALKY------ALTGELpp 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 447 ---GLVTQDSILFNDTIKANISLGKLDATDDEIIEALKIaNAFEFVnelplgIYTNIGDSgNK--------LSGGQKQ-- 513
Cdd:cd03240 53 nskGGAHDPKLIREGEVRAQVKLAFENANGKKYTITRSL-AILENV------IFCHQGES-NWplldmrgrCSGGEKVla 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 514 ----RLSIARAVLKNPPIMILDEATSALDTESekfVQVALENMMQNRTS------IVIAHRLSTIQKADLIV 575
Cdd:cd03240 125 sliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEERKSqknfqlIVITHDEELVDAADHIY 193
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
387-582 |
1.10e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 387 KDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlRGLMGLV-----TQDSILFNDT-- 459
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLDApl 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 -------IKANISLGKLDATDDEIIEALKIAnafefvnelpLGI-YTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILD 531
Cdd:PRK15439 359 awnvcalTHNRRGFWIKPARENAVLERYRRA----------LNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 532 EATSALDTESEKFVQVALENMM-QNRTSIVIAHRLSTI-QKADLIVVMQKGKI 582
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAaQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
389-577 |
1.33e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 389 FSLSI-KKGQTVALVGQSGSGKSTIAN-----LMTRFYDVNDGTiSIDGInikdmnlqsLRGLMGLVTQD--SILFNDTI 460
Cdd:PRK13409 91 YGLPIpKEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEP-SWDEV---------LKRFRGTELQNyfKKLYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KANISL-----------GK----LDATD-----DEIIEALKIANAFEfvNELplgiytnigdsgNKLSGGQKQRLSIARA 520
Cdd:PRK13409 161 KVVHKPqyvdlipkvfkGKvrelLKKVDergklDEVVERLGLENILD--RDI------------SELSGGELQRVAIAAA 226
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1776288214 521 VLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVM 577
Cdd:PRK13409 227 LLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
386-574 |
1.35e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLS-----IKKGQTVALVGQSGSGKSTIANLmtrfydvndgtisidginikdmnlqslrgLMGLVTQDSILFNDTI 460
Cdd:PRK13409 350 LGDFSLEveggeIYEGEVIGIVGPNGIGKTTFAKL-----------------------------LAGVLKPDEGEVDPEL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 461 KanIS------LGKLDATDDEIIEalKIANAFE---FVNEL--PLGIyTNIGDSG-NKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK13409 401 K--ISykpqyiKPDYDGTVEDLLR--SITDDLGssyYKSEIikPLQL-ERLLDKNvKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1776288214 529 ILDEATSALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIqkaDLI 574
Cdd:PRK13409 476 LLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
386-593 |
2.04e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDMNlQSLRGLMGLVTQD-SILFNDTIKA 462
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSK-EALENGISMVHQElNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 463 NISLGKLdATDDEIIEALKIANAFEFVNElPLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALdteSE 542
Cdd:PRK10982 93 NMWLGRY-PTKGMFVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 543 KFVQ---VALENMMQNRTSIV-IAHRLSTI-QKADLIVVMQKGKIV-----EQGTHDELIA 593
Cdd:PRK10982 168 KEVNhlfTIIRKLKERGCGIVyISHKMEEIfQLCDEITILRDGQWIatqplAGLTMDKIIA 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
328-546 |
2.74e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 328 ISKASYGVKRGNAAAERV--LEILDQENPITSKPDaiVKTSF---DDS-----IEVKNINFKYQDETVL-KDFSLSIKKG 396
Cdd:PLN03073 458 IDKFRYNAKRASLVQSRIkaLDRLGHVDAVVNDPD--YKFEFptpDDRpgppiISFSDASFGYPGGPLLfKNLNFGIDLD 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 397 QTVALVGQSGSGKSTIANLMTRFYDVNDGTIsidginikdmnLQSLRGLMGLVTQDSIlfndtikanislgklDATDDEI 476
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------FRSAKVRMAVFSQHHV---------------DGLDLSS 589
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 477 IEALKIANAFEFVNELPLGIYT-NIGDSGN-------KLSGGQKQRLSIARAVLKNPPIMILDEATSALDTES-EKFVQ 546
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAHLgSFGVTGNlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
501-591 |
2.79e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 49.73 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 501 GDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQNRTSIVIAHRL--STIQKADLIVVMQ 578
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVID 218
|
90
....*....|...
gi 1776288214 579 KGKIVEQGTHDEL 591
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
386-574 |
3.82e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.78 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLS-----IKKGQTVALVGQSGSGKSTIANLMTrfydvndGTISIDGINIkDMNL------QSLRGLMGLvTQDSI 454
Cdd:COG1245 351 YGGFSLEveggeIREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEV-DEDLkisykpQYISPDYDG-TVEEF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 455 LFNdTIKANISLGKLDAtddEIIEALKIANAFEfvnelplgiyTNIGDsgnkLSGGQKQRLSIARAVLKNPPIMILDEAT 534
Cdd:COG1245 422 LRS-ANTDDFGSSYYKT---EIIKPLGLEKLLD----------KNVKD----LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1776288214 535 SALDTESEKFVQVALENMMQNR--TSIVIAHRLSTIqkaDLI 574
Cdd:COG1245 484 AHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYI 522
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
394-577 |
4.95e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 4.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 394 KKGQTVALVGQSGSGKSTIAN-----LMTRFYDVNDGTiSIDGInikdmnLQSLRGlMGLVTQDSILFNDTIKA-----N 463
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEP-SWDEV------LKRFRG-TELQDYFKKLANGEIKVahkpqY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 464 ISL------GK----LDATD-----DEIIEALKIANAFEfvnelplgiyTNIGDsgnkLSGGQKQRLSIARAVLKNPPIM 528
Cdd:COG1245 169 VDLipkvfkGTvrelLEKVDergklDELAEKLGLENILD----------RDISE----LSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1776288214 529 ILDEATSALD-TESEKFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVM 577
Cdd:COG1245 235 FFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
386-575 |
5.27e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIAN-----LMTRFYD--------VNDGTIS-IDGINiKDMNLQSLRGL------ 445
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFIEqgfcsnlsIQWGAISrLVHIT-RDLPGRSQRSIpltyik 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 446 -----------------MGLvTQDSILFNDTIKANIS---LGKLDATDD----------------EIIEAL----KIAN- 484
Cdd:PRK00635 690 afddlrelfaeqprskrLGL-TKSHFSFNTPLGACAEcqgLGSITTTDNrtsipcpsclgkrflpQVLEVRykgkNIADi 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 485 ----AFE---FVNELP-----------LGI-YTNIGDSGNKLSGGQKQRLSIARAVL---KNPPIMILDEATSALDTES- 541
Cdd:PRK00635 769 lemtAYEaekFFLDEPsihekihalcsLGLdYLPLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDi 848
|
250 260 270
....*....|....*....|....*....|....
gi 1776288214 542 EKFVQVALENMMQNRTSIVIAHRLSTIQKADLIV 575
Cdd:PRK00635 849 KALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
133-325 |
6.54e-06 |
|
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350013 [Multi-domain] Cd Length: 294 Bit Score: 48.24 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 133 KTLELPLAFYSEKRKGDVISRISADvNEVQNSFLAILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIG 212
Cdd:cd18569 84 HVLRLPVEFFSQRYAGDIASRVQSN-DRVANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 213 KQLKKQSTKAQQEQGTFLSTieeTIGGLKV---VKGYNSENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVI 289
Cdd:cd18569 163 RKRVDLNRRLLQDSGKLTGT---TMSGLQMietLKASGAESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTN 239
|
170 180 190
....*....|....*....|....*....|....*.
gi 1776288214 290 AILLWYGGQMVlIDKSLDGAAFIAYMGLAYNILTPA 325
Cdd:cd18569 240 AAILGLGGLLV-MDGALTIGMLVAFQSLMASFLAPV 274
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
370-578 |
9.67e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 370 SIEVKNinFK-YQDETVLKdfslsIKKGQTvALVGQSGSGKSTIanlmtrfydvndgtisIDGINIKdMNLQSLRGLMGL 448
Cdd:cd03278 3 KLELKG--FKsFADKTTIP-----FPPGLT-AIVGPNGSGKSNI----------------IDAIRWV-LGEQSAKSLRGE 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 VTQDSIlFNDTIK------ANISLgKLDATDDE--IIEALKIanafefvnelplgiyTNIGDSGNK-------LSGGQKQ 513
Cdd:cd03278 58 KMSDVI-FAGSETrkpanfAEVTL-TFDNSDGRysIISQGDV---------------SEIIEAPGKkvqrlslLSGGEKA 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1776288214 514 RLSIAR--AVLK-NP-PIMILDEATSALDTE-SEKFVQVaLENMMQNRTSIVIAHRLSTIQKADLI--VVMQ 578
Cdd:cd03278 121 LTALALlfAIFRvRPsPFCVLDEVDAALDDAnVERFARL-LKEFSKETQFIVITHRKGTMEAADRLygVTMQ 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
382-562 |
1.04e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 382 DETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDG-TISIDGINIkdmnlqslrglmGLVTQDSILFND-T 459
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIKV------------GYLPQEPQLDPEkT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 460 IKANISLG------KLD---------ATDD--------------EIIEAlkiANAFEFVNEL----------Plgiytni 500
Cdd:PRK11819 87 VRENVEEGvaevkaALDrfneiyaayAEPDadfdalaaeqgelqEIIDA---ADAWDLDSQLeiamdalrcpP------- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 501 GDSG-NKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESekfvqVA-LENMMQNRTSIVIA 562
Cdd:PRK11819 157 WDAKvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES-----VAwLEQFLHDYPGTVVA 215
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
371-563 |
1.28e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIdGINIKdmnlqslrglMGLVT 450
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 451 Q--DSILFNDTIKANISLGkldatdDEIIealKIAN----------AFEFvnelplgiytNIGDSGNK---LSGGQKQRL 515
Cdd:PRK11819 394 QsrDALDPNKTVWEEISGG------LDII---KVGNreipsrayvgRFNF----------KGGDQQKKvgvLSGGERNRL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTESEKfvqvALENMMQN--RTSIVIAH 563
Cdd:PRK11819 455 HLAKTLKQGGNVLLLDEPTNDLDVETLR----ALEEALLEfpGCAVVISH 500
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
382-601 |
2.56e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 45.57 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 382 DETVL-KDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGLVTQDSI------ 454
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIktelta 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 455 ----LFNDTIKAnislgklDATDDEIIEALKIAN--AFEfvnELPLGiytnigdsgnKLSGGQKQRLSIARAVLKNPPIM 528
Cdd:PRK13538 92 lenlRFYQRLHG-------PGDDEALWEALAQVGlaGFE---DVPVR----------QLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 529 ILDEATSALDTESekfvqVA-LENMMQnrtsiviAHrlstiqkadlivvMQKGKIVEQGTHDELIAHNGTYNKL 601
Cdd:PRK13538 152 ILDEPFTAIDKQG-----VArLEALLA-------QH-------------AEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
371-597 |
4.88e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDG--INIKDMNLQSLRGLMgl 448
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIATRRRVGYM-- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 449 vTQDSILFND-TIKANISL-GKL-DATDDEI---IEALkiANAFEFV-------NELPLGIytnigdsgnklsggqKQRL 515
Cdd:NF033858 345 -SQAFSLYGElTVRQNLELhARLfHLPAAEIaarVAEM--LERFDLAdvadalpDSLPLGI---------------RQRL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 516 SIARAVLKNPPIMILDEATSALDTES-EKFVQVALENMMQNRTSIVIA-HRLSTIQKADLIVVMQKGKIVEQGTHDELIA 593
Cdd:NF033858 407 SLAVAVIHKPELLILDEPTSGVDPVArDMFWRLLIELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVA 486
|
....
gi 1776288214 594 HNGT 597
Cdd:NF033858 487 ARGA 490
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
386-593 |
5.17e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 5.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 386 LKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSlrGLM-GLV------TQDSILFND 458
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD--GLAnGIVyisedrKRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 459 TIKANISL----------GKLDAtDDEIIEALKIANAFEfvnelplgIYT-NIGDSGNKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK10762 346 SVKENMSLtalryfsragGSLKH-ADEQQAVSDFIRLFN--------IKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 528 MILDEATSALDTESEKFVQVALENMMQNRTSIVIahrLST-----IQKADLIVVMQKGKI-----VEQGTHDELIA 593
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL---VSSempevLGMSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
72-318 |
6.14e-05 |
|
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: 45.19 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 72 YLSYYIT--TTKGTHESGYVLSIMVAIIISIFLLKNLAdyAAMFFITFLRNGVLRdMRNAMYKKTLELPLAFYSEKRKGD 149
Cdd:cd18580 21 WLDWWSSdwSSSPNSSSGYYLGVYAALLVLASVLLVLL--RWLLFVLAGLRASRR-LHDKLLRSVLRAPMSFFDTTPSGR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 150 VISRISADVN----EVQNSFLAILELIvkepLTIIFTITTMLIISPkltlFVFIFIPVSGYIISLIGK-------QLKKQ 218
Cdd:cd18580 98 ILNRFSKDIGlideELPLALLDFLQSL----FSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRyylrtsrQLRRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 219 STKAQqeqGTFLSTIEETIGGLKVVKGYNSENYF---NTVFQNSTERFFNLSNSI----GNRQNLASpasefMGITVIAI 291
Cdd:cd18580 170 ESESR---SPLYSHFSETLSGLSTIRAFGWQERFieeNLRLLDASQRAFYLLLAVqrwlGLRLDLLG-----ALLALVVA 241
|
250 260
....*....|....*....|....*..
gi 1776288214 292 LLwyggqMVLIDKSLDGaafiAYMGLA 318
Cdd:cd18580 242 LL-----AVLLRSSISA----GLVGLA 259
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
376-540 |
8.90e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.07 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 376 INFKYQDETVLKDFSLSIKKGQTVALVGQSGSGKSTIANLMTRFYDVNDGTISIDGINIKDMNLQSLRGLMGlvtqdsil 455
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLG-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 456 fndtikaniSLGKLDAtDDEIIEALKIANAFE--FVNELPLGIYTNIGDSG------NKLSGGQKQRLSIARAVLKNPPI 527
Cdd:PRK13543 89 ---------HLPGLKA-DLSTLENLHFLCGLHgrRAKQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAPL 158
|
170
....*....|...
gi 1776288214 528 MILDEATSALDTE 540
Cdd:PRK13543 159 WLLDEPYANLDLE 171
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
371-586 |
1.06e-04 |
|
ATP-binding cassette domain I 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: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 371 IEVKNINfkyqdETVLKDFSLSIKKGQTVALVGQSGSGKSTIA-------------------------NLMTRFYDVNDG 425
Cdd:cd03270 1 IIVRGAR-----EHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarqflgQMDKPDVDSIEG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 426 ---TISIDGINIKdmnlQSLRGLMGLVTQ--DS--ILFndtikANISlgkldatddeiiealkIANAFEFVNELPLGiYT 498
Cdd:cd03270 76 lspAIAIDQKTTS----RNPRSTVGTVTEiyDYlrLLF-----ARVG----------------IRERLGFLVDVGLG-YL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 499 NIGDSGNKLSGGQKQRLSIARAVLKN--PPIMILDEATSALDTESEKFVQVALENMM-QNRTSIVIAHRLSTIQKADLIV 575
Cdd:cd03270 130 TLSRSAPTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
|
250
....*....|....*..
gi 1776288214 576 VM------QKGKIVEQG 586
Cdd:cd03270 210 DIgpgagvHGGEIVAQG 226
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
393-414 |
1.18e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 44.54 E-value: 1.18e-04
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
507-583 |
1.38e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 507 LSGGQKQRLSIAR--AVLK-NP-PIMILDEATSALD-TESEKFVQvaLENMMQNRTS-IVIAHRLSTIQKADLI--VVMQ 578
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFKvKPaPFCILDEVDAPLDdANVERFAN--LLKEFSKNTQfIVITHNKGTMEVADQLygVTMQ 1167
|
....*...
gi 1776288214 579 -KG--KIV 583
Cdd:TIGR02168 1168 eKGvsKIV 1175
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
72-263 |
1.52e-04 |
|
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: 44.06 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 72 YLSYYITTTKG-----THESGYVLSIMVAIIISIFLLKNLAdYAAMFFITFLRNGvlRDMRNAMYKKTLELPLAFYSEKR 146
Cdd:cd18605 21 WLSYWVSHSNNsffnfINDSFNFFLTVYGFLAGLNSLFTLL-RAFLFAYGGLRAA--RRLHNKLLSSILFAKMSFFDKTP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 147 KGDVISRISADVNEVQNSFLAILELIVKEPLTIIFTITTMLIISPkltLFVFIFIPVSgYIISLIGKQ-------LKKQS 219
Cdd:cd18605 98 VGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLP---WLLLLLLPLA-FIYYRIQRYyratsreLKRLN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1776288214 220 TKAqqeQGTFLSTIEETIGGLKVVKGYNSENYFNTVFQNSTERF 263
Cdd:cd18605 174 SVN---LSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENN 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
506-578 |
1.61e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 42.94 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1776288214 506 KLSGGQKQRLSIARAVLKNPPIMILDEATSALDTESEKFVQVALENMMQN--RTSIVIAHRLSTIQK-ADLIVVMQ 578
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-579 |
4.72e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.19 E-value: 4.72e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1776288214 506 KLSGGQKQRLSIARAV----LKNPPIMILDEATSALDTES-EKFVQVALENMMQNRTSIVIAHRLSTIQKADLIVVMQK 579
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
394-577 |
4.77e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.35 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 394 KKGQTVALVGQSGSGKST----IANLMTRFYDVNDGTISIDGInikdmnLQSLRG--LMGLVTQdsiLFNDTIKANISLG 467
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTalkiLAGKLKPNLGKFDDPPDWDEI------LDEFRGseLQNYFTK---LLEGDVKVIVKPQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 468 KLD----ATDDEIIEALKIANAFEFVNEL--PLGIYTNIGDSGNKLSGGQKQRLSIARAVLKNPPIMILDEATSALDTES 541
Cdd:cd03236 95 YVDlipkAVKGKVGELLKKKDERGKLDELvdQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1776288214 542 E-KFVQVALENMMQNRTSIVIAHRLSTIQK-ADLIVVM 577
Cdd:cd03236 175 RlNAARLIRELAEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
395-414 |
5.82e-04 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 42.41 E-value: 5.82e-04
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
395-414 |
8.93e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 8.93e-04
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
426-595 |
1.05e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 426 TISIDGINIKDMNLQSLRGLMglvtqdsILFNDTikanislgKLDATDDEIIE-ALK-IANAFEFVNELPLGiYTNIGDS 503
Cdd:TIGR00630 422 AVTVGGKSIADVSELSIREAH-------EFFNQL--------TLTPEEKKIAEeVLKeIRERLGFLIDVGLD-YLSLSRA 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 504 GNKLSGGQKQRLSIAR-------AVLknppiMILDEATSAL---DTesEKFVQVALENMMQNRTSIVIAHRLSTIQKADL 573
Cdd:TIGR00630 486 AGTLSGGEAQRIRLATqigsgltGVL-----YVLDEPSIGLhqrDN--RRLINTLKRLRDLGNTLIVVEHDEDTIRAADY 558
|
170 180
....*....|....*....|....*...
gi 1776288214 574 IVVM------QKGKIVEQGTHDELIAHN 595
Cdd:TIGR00630 559 VIDIgpgageHGGEVVASGTPEEILANP 586
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
469-598 |
1.97e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.21 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 469 LDATddeIIEAL-------KIANAFEFVNELPLGiYTNIGDSGNKLSGGQKQRLSIARAVLKNP---PIMILDEATSALD 538
Cdd:PRK00349 790 LDMT---VEEALeffeaipKIARKLQTLVDVGLG-YIKLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLH 865
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1776288214 539 TES-EKFVQVaLenmmqNR------TSIVIAHRLSTIQKADLIVVM------QKGKIVEQGTHDELIAHNGTY 598
Cdd:PRK00349 866 FEDiRKLLEV-L-----HRlvdkgnTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
87-252 |
3.24e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 39.74 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 87 GYVLSIMVAIIISIFLLkNLADYAAMFFITFLRnGVLRDmrnAMYKKTLELplafySEKRK-----GDVISRISADVNEV 161
Cdd:cd18597 44 GYAIGLFLLQLLSSLLL-NHFFYRSMLTGAQVR-AALTK---AIYRKSLRL-----SGKSRhefpnGKITNLMSTDLSRI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 162 QNSFLAILELIVkEPLTIIFTITtMLIIS------PKLTLFVfIFIPVSGYIISLIGKQLKKQSTKAQQEqgtfLSTIEE 235
Cdd:cd18597 114 DFALGFFHFLWT-APIQIIIAIA-LLIVNlgpsalVGIGVLI-LSIPLQGFLMKKLFKLRKKANKITDKR----VKLTQE 186
|
170
....*....|....*..
gi 1776288214 236 TIGGLKVVKGYNSENYF 252
Cdd:cd18597 187 ILQGIRVIKFYAWEDAF 203
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
88-301 |
4.17e-03 |
|
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: 39.57 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSIMVAIIISIFLlknladyaAMFFITFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRISADVNEVQNSFLA 167
Cdd:cd18558 64 YYLIIGAIVLITAYI--------QGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 168 ILELIVKEPLTIIFTITTMLIISPKLTLFVFIFIPVSGYIISLIGKQLKKQSTKAQQEQGTFLSTIEETIGGLKVVKGYN 247
Cdd:cd18558 136 KIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFG 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1776288214 248 SENYFNTVFQNSTERFFNLSNSIGNRQNLASPASEFMGITVIAILLWYGGQMVL 301
Cdd:cd18558 216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVT 269
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
88-324 |
7.63e-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: 38.68 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 88 YVLSIMVAIIISIFLLKNLADYAAMffiTFLRNGVLRDMRNAMYKKTLELPLAFYSEKRKGDVISRIS--ADVNEVQNSf 165
Cdd:cd18779 42 GVLGLGLAALVLTQLLAGLLRSHLL---LRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSsnATIRELLTS- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 166 lAILELIVKEPLTIIFTItTMLIISPKLTLFVFIFIPVS-GYIISLIGKQ--LKKQSTKAQQEQGTFLStieETIGGLKV 242
Cdd:cd18779 118 -QTLSALLDGTLVLGYLA-LLFAQSPLLGLVVLGLAALQvALLLATRRRVreLMARELAAQAEAQSYLV---EALSGIET 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1776288214 243 VKGYNSENYfntVFQNSTERFFNLSNSIGNRQNLASPASEFMGI---TVIAILLWYGGQMVLiDKSLDGAAFIAYMGLAY 319
Cdd:cd18779 193 LKASGAEDR---ALDRWSNLFVDQLNASLRRGRLDALVDALLATlrlAAPLVLLWVGAWQVL-DGQLSLGTMLALNALAG 268
|
....*
gi 1776288214 320 NILTP 324
Cdd:cd18779 269 AFLAP 273
|
|
| |
