|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-582 |
0e+00 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 1267.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 1 MQNDKDLSTWQTFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGI 80
Cdd:PRK11176 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 81 TSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMM 160
Cdd:PRK11176 81 TSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 161 FYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQ 240
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
Cdd:PRK11176 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 321 ILDSEQEKDEGTRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQI 400
Cdd:PRK11176 321 ILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 401 LLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVM 480
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
570 580
....*....|....*....|..
gi 488987387 561 THHDLLEHKGVYAQLHKMQFGE 582
Cdd:PRK11176 561 THAELLAQNGVYAQLHKMQFGQ 582
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
12-582 |
0e+00 |
|
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: 911.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 12 TFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISW 91
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 92 VSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLIL 171
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 172 IVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSIS 251
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 252 DPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEG 331
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 332 TRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK 411
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 412 LSSLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAI 491
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGV 571
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
570
....*....|.
gi 488987387 572 YAQLHKMQFGE 582
Cdd:TIGR02203 561 YAQLHNMQFRE 571
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
8-582 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 682.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 8 STWQTFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSY 87
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 88 CISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQL 167
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 168 SLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSA 247
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 248 SSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQE 327
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 328 KDE--GTRVIERAKGNLKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH 405
Cdd:COG1132 324 IPDppGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 406 DLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQ 485
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDL 565
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
gi 488987387 566 LEHKGVYAQLHKMQFGE 582
Cdd:COG1132 562 LARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-579 |
3.40e-171 |
|
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: 502.83 E-value: 3.40e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 12 TFRRLWPIIAPFKAGLI-VAAVALVLNagsdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMVLRGITSYIS 85
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLqVLLASLLIN------LLALATPLFtqvviDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 86 SYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSW 165
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 166 QLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMV 245
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 246 SASSISDPIIQLIASLALAFVLYAASFpSVMD-TLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFAILD 323
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAY-LVIDgQLTLGQL-IAFNILSGrFLAPVAQLIGLLQRFQDAKIALERLDDILD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 324 SEQEKDEGTRVIERA--KGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIL 401
Cdd:COG2274 454 LPPEREEGRSKLSLPrlKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 402 LDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVML 481
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD-PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 482 SGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT 561
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
570
....*....|....*...
gi 488987387 562 HHDLLEHKGVYAQLHKMQ 579
Cdd:COG2274 693 HEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-576 |
3.00e-147 |
|
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: 423.57 E-value: 3.00e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLH 576
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-580 |
5.33e-140 |
|
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: 417.95 E-value: 5.33e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 14 RRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVS 93
Cdd:TIGR02204 7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 94 GKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIV 173
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 174 LAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:TIGR02204 167 AVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTIT-VVFSSMIALMrPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDE-- 330
Cdd:TIGR02204 247 IVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGqFVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKApa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 331 -GTRVIERAKGNLKFENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR 408
Cdd:TIGR02204 326 hPKTLPVPLRGEIEFEQVNFAYPARpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 409 EYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQR 488
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|..
gi 488987387 569 KGVYAQLHKMQF 580
Cdd:TIGR02204 565 GGLYARLARLQF 576
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-579 |
1.12e-134 |
|
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: 405.36 E-value: 1.12e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 6 DLSTWQTFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDrsVLLWMPlvvIGLMVLRGITSYIS 85
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAA--ALLVVP---VGLLLAYGLLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 86 SYCISW---VSGKVVM-TMRR---RLFGHMMGMPVAF-FDKQSTGtlLSRI----TYDSEQVASSSSSALITVVREGASI 153
Cdd:COG5265 92 VLFGELrdaLFARVTQrAVRRlalEVFRHLHALSLRFhLERQTGG--LSRDiergTKGIEFLLRFLLFNILPTLLEIALV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 154 IGLFVmmFYYSWQLSLILIV-LAPIVSVAIRVVSKRFRnISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDK 232
Cdd:COG5265 170 AGILL--VKYDWWFALITLVtVVLYIAFTVVVTEWRTK-FRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 233 VSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGM 312
Cdd:COG5265 247 ALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQAL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 313 AACQTLFAILDSEQE-KD-EGTRVIERAKGNLKFENVTFTY-PGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLI 389
Cdd:COG5265 327 ADMERMFDLLDQPPEvADaPDAPPLVVGGGEVRFENVSFGYdPERPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 390 TRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNG 469
Cdd:COG5265 405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR-PDASEEEVEAAARAAQIHDFIESLPDG 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 470 LDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:COG5265 484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
|
570 580 590
....*....|....*....|....*....|
gi 488987387 550 VVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:COG5265 564 VLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-570 |
4.17e-131 |
|
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: 394.90 E-value: 4.17e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 14 RRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGF-GKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWV 92
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 93 SGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILI 172
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 173 VLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISD 252
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 253 PIIQLIASLALAFVLYAASFpsvmdTLTAGTITVvFSSMIALM------RPLKSLtnvNAQF---QRGMAACQTLFAILD 323
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGF-----RLLGGSLTL-FAALFVLLlapeffLPLRDL---GSFYharANGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 324 S-EQEKDEGTRVIERAKGN-LKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIL 401
Cdd:COG4988 317 ApEPAAPAGTAPLPAAGPPsIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 402 LDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVML 481
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR-PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 482 SGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT 561
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
gi 488987387 562 HHDLLEHKG 570
Cdd:COG4988 555 HEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
344-579 |
3.65e-122 |
|
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: 359.93 E-value: 3.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALV 422
Cdd:cd03249 3 FKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPIL 502
Cdd:cd03249 83 SQEPVLFDGTIAENIRYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
95-577 |
1.70e-119 |
|
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: 365.24 E-value: 1.70e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 95 KVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVL 174
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 175 APIVSVAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:COG4987 165 LLLAGLLLPLLAARLgRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSE-QEKDEGT 332
Cdd:COG4987 245 LLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPpAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 333 RVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKL 412
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 413 SSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIA 492
Cdd:COG4987 405 DDLRRRIAVVPQRPHLFDTTLRENLRLAR-PDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALA 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVY 572
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
....*
gi 488987387 573 AQLHK 577
Cdd:COG4987 564 RQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
344-579 |
2.83e-115 |
|
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: 342.29 E-value: 2.83e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTY-PGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALV 422
Cdd:cd03253 3 FENVTFAYdPGRPV--LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPIL 502
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGR-PDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
72-575 |
4.52e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 355.57 E-value: 4.52e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISSY----CISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVV 147
Cdd:TIGR00958 204 IFFMCLLSIASSVSAGlrggSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 148 REGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVET 227
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 228 KRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 308 FQRGMAACQTLFAILDSE-QEKDEGTRVIERAKGNLKFENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTI 385
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 386 ASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEeYSREQIEEAARMAYAMDFINK 465
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIME 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 466 MDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAalDELQKNRTSLVIAHRLSTIEQA 545
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
490 500 510
....*....|....*....|....*....|
gi 488987387 546 DEIVVVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
27-316 |
2.67e-105 |
|
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: 318.60 E-value: 2.67e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488987387 267 LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAE 290
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-570 |
7.30e-104 |
|
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: 312.62 E-value: 7.30e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYpGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGR-PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKG 570
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-580 |
5.33e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 299.57 E-value: 5.33e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 101 RRRL------FGHMMGMPVAFFDKQSTGTLLsritydseQVASSSSSALITV----VREG-ASIIGLFVMM---FYYSWQ 166
Cdd:PRK13657 86 RRRLavlteyFERIIQLPLAWHSQRGSGRAL--------HTLLRGTDALFGLwlefMREHlATLVALVVLLplaLFMNWR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 167 LSLILIVLAPIVSVAIRVVSKRfrniSKNMQNTMGQ----VTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMR---- 238
Cdd:PRK13657 158 LSLVLVVLGIVYTLITTLVMRK----TKDGQAAVEEhyhdLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLaaqm 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 239 --LQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTagtiTVVFSSMiaLMRPLKSLTN-VNAQFQRGmAAC 315
Cdd:PRK13657 234 pvLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVA----FVGFATL--LIGRLDQVVAfINQVFMAA-PKL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 316 QTLFAILDSEQEKDE--GTRVIERAKGNLKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFY 393
Cdd:PRK13657 307 EEFFEVEDAVPDVRDppGAIDLGRVKGAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 394 DVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTI 473
Cdd:PRK13657 386 DPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR-PDATDEEMRAAAERAQAHDFIERKPDGYDTV 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 474 IGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVED 553
Cdd:PRK13657 465 VGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
490 500
....*....|....*....|....*..
gi 488987387 554 GRIVERGTHHDLLEHKGVYAQLHKMQF 580
Cdd:PRK13657 545 GRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
69-581 |
6.76e-94 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 302.43 E-value: 6.76e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGL-MVLRGIT----SYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSAL 143
Cdd:TIGR01846 178 LSVLALaMLAVAIFepalGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 144 ITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQ 223
Cdd:TIGR01846 257 LTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 224 EVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSsMIA--LMRPLKSL 301
Cdd:TIGR01846 337 PQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQL-VAFN-MLAgrVTQPVLRL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 302 TNVNAQFQRGMAACQTLFAILDSEQEKDEGTRV-IERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGS 380
Cdd:TIGR01846 415 AQLWQDFQQTGIALERLGDILNSPTEPRSAGLAaLPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 381 GKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEeYSREQIEEAARMAYAM 460
Cdd:TIGR01846 495 GKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG-APFEHVIHAAKLAGAH 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 461 DFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
Cdd:TIGR01846 574 DFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLS 653
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 488987387 541 TIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQFG 581
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
344-579 |
2.70e-92 |
|
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: 283.22 E-value: 2.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVS 423
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILI 503
Cdd:cd03252 83 QENVLFNRSIRDNIALAD-PGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-555 |
3.05e-92 |
|
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: 280.42 E-value: 3.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488987387 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGR 555
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-575 |
5.81e-91 |
|
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: 294.93 E-value: 5.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 25 AGLIVAAVALVLNAGSDTFM--------LSLLKPLLddgfgktdrsvllwmpLVVIGLMVLRGITSYISSYCISWVSGKV 96
Cdd:TIGR03796 162 AGLLLVLPGLVIPAFSQIFVdeilvqgrQDWLRPLL----------------LGMGLTALLQGVLTWLQLYYLRRLEIKL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 97 VMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDsEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAP 176
Cdd:TIGR03796 226 AVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 177 IVSVAIRVVSKRFRNISKNMQNTMGQVTTSAeqmlkghkevlMFGGQEVETKR--------FDKVSN---KMRLQGMKMV 245
Cdd:TIGR03796 305 INVLALQLVSRRRVDANRRLQQDAGKLTGVA-----------ISGLQSIETLKasglesdfFSRWAGyqaKLLNAQQELG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 246 SASSISDPIIQLIASLALAFVLYAASFpSVMD-TLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDS 324
Cdd:TIGR03796 374 VLTQILGVLPTLLTSLNSALILVVGGL-RVMEgQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 325 EQEKDEG--------TRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD 396
Cdd:TIGR03796 453 PVDPLLEepegsaatSEPPRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 397 EGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIA-YARTeeYSREQIEEAARMAYAMDFINKMDNGLDTIIG 475
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTlWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 476 ENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIEQADEIVVVEDGR 555
Cdd:TIGR03796 611 EGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGK 688
|
570 580
....*....|....*....|
gi 488987387 556 IVERGTHHDLLEHKGVYAQL 575
Cdd:TIGR03796 689 VVQRGTHEELWAVGGAYARL 708
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-579 |
1.39e-87 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 282.37 E-value: 1.39e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 44 MLSLLKPLL----DDGF---GKTDRSVLLWmplvvIGLMVLRGITSYISSYCisW------VSGKVVMTMRRRLFGHMMG 110
Cdd:PRK10789 9 MLQLIPPKVvgiiVDGVteqHMTTGQILMW-----IGTMVLIAVVVYLLRYV--WrvllfgASYQLAVELREDFYRQLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 111 MPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRE---GASIigLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:PRK10789 82 QHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmGCAV--LIVMSTQISWQLTLLALLPMPVMAIMIKRYGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 268 YAASFPSVMDTLTAGTIT---VVFSSMIALMRPLKSLTNVnaqFQRGMAACQTLFAILDSEQEKDEGTRVIERAKGNLKF 344
Cdd:PRK10789 240 GGGSWMVVNGSLTLGQLTsfvMYLGLMIWPMLALAWMFNI---VERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDA-TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-579 |
3.65e-87 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 281.99 E-value: 3.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 1 MQNDKDLstWQTFRRLWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVV--IGLMVLR 78
Cdd:PRK10790 1 MRSFSQL--WPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayVGLQLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 79 GITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFV 158
Cdd:PRK10790 79 AGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 159 MMFYYSWQLSLILIVLAPIVSVaIRVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSN-- 235
Cdd:PRK10790 159 AMFSLDWRMALVAIMIFPAVLV-VMVIYQRYSTpIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRsh 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 236 -KMRLQGMKMvsASSISDPIIQLIASLALAFVLYAASFPSVmdtltaGTITV-VFSSMIA----LMRPLKSLTNVNAQFQ 309
Cdd:PRK10790 238 yMARMQTLRL--DGFLLRPLLSLFSALILCGLLMLFGFSAS------GTIEVgVLYAFISylgrLNEPLIELTTQQSMLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 310 RGMAACQTLFAILDSEQEkDEGTRVIERAKGNLKFENVTFTY-PGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASL 388
Cdd:PRK10790 310 QAVVAGERVFELMDGPRQ-QYGNDDRPLQSGRIDIDNVSFAYrDDNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 389 ITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARteEYSREQIEEAARMAYAMDFINKMDN 468
Cdd:PRK10790 387 LMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR--DISEEQVWQALETVQLAELARSLPD 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 469 GLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEI 548
Cdd:PRK10790 465 GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTI 544
|
570 580 590
....*....|....*....|....*....|.
gi 488987387 549 VVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:PRK10790 545 LVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-551 |
4.52e-86 |
|
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: 277.25 E-value: 4.52e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 24 KAGLIVAAVALVLNAGSDTFMLSLLKPLLDD-GFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRR 102
Cdd:TIGR02857 2 RRALALLALLGVLGALLIIAQAWLLARVVDGlISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 103 RLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRegASIIGLFVM--MFYYSWQLSLILIVLAPIVSV 180
Cdd:TIGR02857 82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVL--AVIVPLAILaaVFPQDWISGLILLLTAPLIPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 181 AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:TIGR02857 160 FMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 261 LALAFVLYAASFpsvmdTLTAGTITVVFSSMIALMRP--LKSLTNVNAQF---QRGMAACQTLFAILDS-EQEKDEGTRV 334
Cdd:TIGR02857 240 LSVALVAVYIGF-----RLLAGDLDLATGLFVLLLAPefYLPLRQLGAQYharADGVAAAEALFAVLDAaPRPLAGKAPV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 335 IERAKGNLKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSS 414
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARA 494
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIRLARPDA-SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARA 472
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVV 551
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-576 |
4.04e-85 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 275.94 E-value: 4.04e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 151 ASIIGLFVMMFYYSW---QLSLILIVLAPIVSVAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVE 226
Cdd:PRK11160 143 AALVVILVLTIGLSFfdlTLALTLGGILLLLLLLLPLLFYRLgKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRY 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 227 TKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMDTLTAGTIT--VVFSSMIALmrplKSLTNV 304
Cdd:PRK11160 223 RQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAG-GVGGNAQPGALIalFVFAALAAF----EALMPV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 305 NAQFQ---RGMAACQTLFAILdsEQEKD---EGTRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRS 378
Cdd:PRK11160 298 AGAFQhlgQVIASARRINEIT--EQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 379 GSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYArTEEYSREQIEEAAR--- 455
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA-APNASDEALIEVLQqvg 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 456 MAYAMDfinkMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
Cdd:PRK11160 455 LEKLLE----DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 488987387 536 AHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLH 576
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
339-556 |
9.23e-81 |
|
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: 253.16 E-value: 9.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 339 KGNLKFENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRD 417
Cdd:cd03248 9 KGIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSC-SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-579 |
1.13e-78 |
|
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: 261.81 E-value: 1.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 4 DKDLSTWQTFRrlwpiiapFKAGLIVAAVALVLNAGSDTFMLSLLKP-----LLDDGFGKTDRSVLLWMPLVVIGLMVLR 78
Cdd:TIGR03797 118 DKALGLRDLLR--------FALRGARRDLLAILAMGLLGTLLGMLVPiatgiLIGTAIPDADRSLLVQIALALLAAAVGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 79 GITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVregASIIGLF- 157
Cdd:TIGR03797 190 AAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAMGISQIRRILSGSTLTTLL---SGIFALLn 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 158 -VMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEvLMFGGQEVE-----TKRFD 231
Cdd:TIGR03797 267 lGLMFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISK-LRVAGAENRafarwAKLFS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 232 KvSNKMRLQGMKMVSASSISDPIIQLIASLALafvLYAASFPSVMDTLTAGTI---TVVFSSMIALMRPL-KSLTNVNA- 306
Cdd:TIGR03797 346 R-QRKLELSAQRIENLLTVFNAVLPVLTSAAL---FAAAISLLGGAGLSLGSFlafNTAFGSFSGAVTQLsNTLISILAv 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 307 --QFQRgmaaCQtlfAILDSEQEKDEGTRVIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKST 384
Cdd:TIGR03797 422 ipLWER----AK---PILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 385 IASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFIN 464
Cdd:TIGR03797 495 LLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA--GGAPLTLDEAWEAARMAGLAEDIR 572
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 465 KMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRtsLVIAHRLSTIEQ 544
Cdd:TIGR03797 573 AMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRN 650
|
570 580 590
....*....|....*....|....*....|....*
gi 488987387 545 ADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHKMQ 579
Cdd:TIGR03797 651 ADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-560 |
3.11e-75 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 238.64 E-value: 3.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAYARTEeYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPL-ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
98-577 |
4.87e-74 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 247.11 E-value: 4.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 98 MTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPI 177
Cdd:TIGR01192 89 ATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGIL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 178 VSVAIRVVSKRFRN----ISKNMQNTMGQVTTSAEQMLKGHKevlmFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:TIGR01192 169 YILIAKLVMQRTKNgqaaVEHHYHNVFKHVSDSISNVSVVHS----YNRIEAETSALKQFTNNLLSAQYPVLDWWALASG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 254 IIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDE--G 331
Cdd:TIGR01192 245 LNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEpaD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 332 TRVIERAKGNLKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK 411
Cdd:TIGR01192 325 APELPNVKGAVEFRHITFEFANSS-QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVT 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 412 LSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAI 491
Cdd:TIGR01192 404 RESLRKSIATVFQDAGLFNRSIRENIRLGR-EGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAI 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGV 571
Cdd:TIGR01192 483 ARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGR 562
|
....*.
gi 488987387 572 YAQLHK 577
Cdd:TIGR01192 563 FYKLLR 568
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-561 |
1.25e-70 |
|
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: 226.61 E-value: 1.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT 561
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
279-568 |
3.62e-68 |
|
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: 230.79 E-value: 3.62e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 279 LTAGTItvvFSSMIALMR---PLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGTRvIERAKGNLKFENVTFTYPGRE 355
Cdd:COG4618 269 ITPGAM---IAASILMGRalaPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMP-LPRPKGRLSVENLTVVPPGSK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 356 VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVAN 435
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 436 NIAyaRTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:COG4618 425 NIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488987387 516 ERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG4618 503 EAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
27-314 |
1.13e-66 |
|
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: 218.57 E-value: 1.13e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488987387 267 LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
79-539 |
2.39e-64 |
|
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: 219.92 E-value: 2.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 79 GITSYISSYCISWVSGKVVMT----MRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASII 154
Cdd:TIGR02868 63 GIGRAVFRYLERLVGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 155 GLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKV 233
Cdd:TIGR02868 143 AAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAaRAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 234 SNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASfPSVMD-TLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGM 312
Cdd:TIGR02868 223 DRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGG-PAVADgRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 313 AACQTLFAILDSEQEKDEGtrVIERAKG------NLKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIA 386
Cdd:TIGR02868 302 AAAERIVEVLDAAGPVAEG--SAPAAGAvglgkpTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 387 SLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFINKM 466
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLAR-PDATDEELWAALERVGLADWLRAL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 467 DNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
69-575 |
2.70e-64 |
|
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: 223.46 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGLM---VLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALIT 145
Cdd:TIGR01193 197 IISIGLIiayIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILS 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 146 VVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEV 225
Cdd:TIGR01193 276 LFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 226 ETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSSMIA-LMRPLKSLTNV 304
Cdd:TIGR01193 356 RYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQL-ITFNALLSyFLTPLENIINL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 305 NAQFQRGMAACQTLFAIL--DSEQEKDEGTRVIERAKGNLKFENVTFTYpGREVAALRNINLDIPEGKTVALVGRSGSGK 382
Cdd:TIGR01193 435 QPKLQAARVANNRLNEVYlvDSEFINKKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 383 STIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDF 462
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 463 INKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQkNRTSLVIAHRLSTI 542
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|...
gi 488987387 543 EQADEIVVVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-565 |
3.22e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 225.68 E-value: 3.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 8 STWQTFRRL----WPIIAPFKAG-------LIVAAVALVLNAGSDTFMLSLLKPLLDD-GFGKTDRSVLLwmPLVVIGLM 75
Cdd:PTZ00265 32 GTFELYKKIktqkIPFFLPFKCLpashrklLGVSFVCATISGGTLPFFVSVFGVIMKNmNLGENVNDIIF--SLVLIGIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 76 VLrgITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIG 155
Cdd:PTZ00265 110 QF--ILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 156 LFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRnISKNM-----QNTMGQVttsaEQMLKGHKEVLMFGGQEVETKRF 230
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-INKKTsllynNNTMSII----EEALVGIRTVVSYCGEKTILKKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 231 DkVSNKmrLQGMKMVSASSISDPIIQLIASLALAFvlYAASF----PSVMDTLT----------AGTITVVFSSMIALMR 296
Cdd:PTZ00265 263 N-LSEK--LYSKYILKANFMESLHIGMINGFILAS--YAFGFwygtRIIISDLSnqqpnndfhgGSVISILLGVLISMFM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 297 PLKSLTNVNaQFQRGMAACQTLFAILDSE---QEKDEGTRVIERAKgnLKFENVTFTYPGR-EVAALRNINLDIPEGKTV 372
Cdd:PTZ00265 338 LTIILPNIT-EYMKSLEATNSLYEIINRKplvENNDDGKKLKDIKK--IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 373 ALVGRSGSGKSTIASLITRFYDVDEGQILL-DGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYA----RTEEYSR 447
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDLEALS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 448 EQIEE------------------------------------AARMAYAM----------------DFINKMDNGLDTIIG 475
Cdd:PTZ00265 495 NYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTikdsevvdvskkvlihDFVSALPDKYETLVG 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 476 ENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIVVVED 553
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
650
....*....|..
gi 488987387 554 GrivERGTHHDL 565
Cdd:PTZ00265 655 R---ERGSTVDV 663
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
211-575 |
4.07e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 207.00 E-value: 4.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 211 LKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVlyAASFP-SVMDTLTAGT----IT 285
Cdd:PRK11174 209 LRGLETLRLFNRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALV--AVYFGfSYLGELNFGHygtgVT 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 286 VvFSSMIALM------RPLKSL-TNVNAQFQrGMAACQTLFAILDSE-QEKDEGTRVIERAKGN-LKFEN-VTFTYPGRE 355
Cdd:PRK11174 287 L-FAGFFVLIlapefyQPLRDLgTFYHAKAQ-AVGAAESLVTFLETPlAHPQQGEKELASNDPVtIEAEDlEILSPDGKT 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 356 VAAlrNINLDIPEGKTVALVGRSGSGKSTIASLITRF--YdvdEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTV 433
Cdd:PRK11174 365 LAG--PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTL 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 ANNIAYARtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:PRK11174 440 RDNVLLGN-PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 514 ESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
27-298 |
1.43e-57 |
|
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: 194.01 E-value: 1.43e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRL 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 105 FGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 488987387 265 FVLYAASFPSVMDTLTAGTITVVFSSMIALMRPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-560 |
1.18e-55 |
|
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: 185.59 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKlSSLRDQVAL 421
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfinkmdngldtiigenGVMLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
312-568 |
1.24e-55 |
|
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: 195.89 E-value: 1.24e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 312 MAACQTLFAILDSEQEKDEGTRVIERAKGNLKFENVTFTYPGR---EVAALRNINLDIPEGKTVALVGRSGSGKSTIASL 388
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 389 ITRFYDVDEGQILLDGHDLREYKLSSLRD---QVALVSQN-VHLFN--DTVANNIAYA--RTEEYSREQIEEaaRMAYAM 460
Cdd:COG1123 311 LLGLLRPTSGSILFDGKDLTKLSRRSLRElrrRVQMVFQDpYSSLNprMTVGDIIAEPlrLHGLLSRAERRE--RVAELL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 461 DFInkmdnGLDT-IIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH 537
Cdd:COG1123 389 ERV-----GLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISH 463
|
250 260 270
....*....|....*....|....*....|..
gi 488987387 538 RLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG1123 464 DLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
297-568 |
2.72e-54 |
|
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: 192.95 E-value: 2.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 297 PLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGTRvIERAKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVG 376
Cdd:TIGR01842 273 PIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMP-LPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 377 RSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARM 456
Cdd:TIGR01842 352 PSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG-ENADPEKIIEAAKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 457 AYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVI 535
Cdd:TIGR01842 431 AGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVI 510
|
250 260 270
....*....|....*....|....*....|...
gi 488987387 536 AHRLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:TIGR01842 511 THRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-569 |
4.99e-54 |
|
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: 183.30 E-value: 4.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVH--LFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFInkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRE--RVEEALELV-----GLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEHK 569
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-556 |
1.24e-52 |
|
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: 177.41 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 502 LILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-315 |
3.31e-52 |
|
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: 180.28 E-value: 3.31e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRL 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 105 FGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488987387 265 FVLYAASFPSVMDTLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVL-YAFIQYIQrFFRPIRDLAEKFNILQSAMASA 291
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-555 |
4.87e-52 |
|
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: 177.27 E-value: 4.87e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 343 KFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALV 422
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQN--VHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfinkmdNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03225 81 FQNpdDQFFGPTVEEEVAFGlENLGLPEEEIEERVEEALEL-------VGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI-EQADEIVVVEDGR 555
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDGK 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-578 |
8.81e-52 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 192.17 E-value: 8.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 65 LWMPLVVIGLMvlrgITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFD--KQSTGTLLSRITYDSEqvasssssA 142
Cdd:PTZ00265 870 LYILVIAIAMF----ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH--------L 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 143 LITVVREGASIIGLFVMMFYYSWQLS-----LILIVLAPIVSVAIRVVSKRFR-----NISKNMQNTMGQV--TTSAEQM 210
Cdd:PTZ00265 938 LKTGLVNNIVIFTHFIVLFLVSMVMSfyfcpIVAAVLTGTYFIFMRVFAIRARltankDVEKKEINQPGTVfaYNSDDEI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 211 LK-----------GHKEVLMFGGQEVETKRFDK-VSNKMRLQGMKMVSASSI---SDPIIQLIASLALAFVLYAASFPSV 275
Cdd:PTZ00265 1018 FKdpsfliqeafyNMNTVIIYGLEDYFCNLIEKaIDYSNKGQKRKTLVNSMLwgfSQSAQLFINSFAYWFGSFLIRRGTI 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 276 -MDTLTAGTITVVFSSMIA--LMRPLKSLTNVNAQFQR--GMAACQTLFAILDSEQEKDEGTRVIeraKGNLKFENVTFT 350
Cdd:PTZ00265 1098 lVDDFMKSLFTFLFTGSYAgkLMSLKGDSENAKLSFEKyyPLIIRKSNIDVRDNGGIRIKNKNDI---KGKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 351 YPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDV---------------------------------- 395
Cdd:PTZ00265 1175 YISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 396 --------------------DEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAAR 455
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-EDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 456 MAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSL 533
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 488987387 534 VIAHRLSTIEQADEIVVVED----GRIVE-RGTHHDLLE-HKGVYAQLHKM 578
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
342-556 |
8.37e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 8.37e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:COG4619 1 LELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIAYA---RTEEYSREQIEEA-ARMAYAMDFinkmdngLDTIIGEngvmLSGGQRQRIAIARALLR 497
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKFDRERALELlERLGLPPDI-------LDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
27-314 |
5.31e-50 |
|
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: 174.51 E-value: 5.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDD------GFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTM 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 101 RRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSV 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 181 AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 488987387 261 LALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAG 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-316 |
2.45e-49 |
|
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: 172.62 E-value: 2.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488987387 267 LYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAE 290
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
8.72e-48 |
|
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: 168.84 E-value: 8.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGsdtfmLSLLKP--------------------LLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISS 86
Cdd:cd18564 1 LALALLALLLETA-----LRLLEPwplkvviddvlgdkplpgllGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 87 YCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQ 166
Cdd:cd18564 76 YLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 167 LSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVS 246
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAAR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 247 ASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18564 236 LQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAE 305
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
1.03e-47 |
|
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: 174.32 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD---EGQILLDGHDLREYKLSSLRDQ 418
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQN--VHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfinkmdNGLDTIIGENGVMLSGGQRQRIAIARAL 495
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlENLGLSRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-560 |
2.79e-47 |
|
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: 165.05 E-value: 2.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDV-----DEGQILLDGHDLRE--YKLSS 414
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFINKMDNGLDtiigengvmLSGGQRQR 488
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQA----DEIVVVEDGRIVERG 560
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH---NMQQAarvaDRTAFLLNGRLVEFG 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-555 |
1.55e-46 |
|
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: 162.25 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAA---LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHdlreyklsslrdq 418
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFNDTVANNIAYArtEEYSREQIEEAARmAYAMDF-INKMDNGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG--KPFDEERYEKVIK-ACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 498 NSPILILDEATSALDTESERAI--QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGR 555
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
342-560 |
2.51e-46 |
|
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: 162.68 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLR 416
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNV-----------HLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQ 485
Cdd:cd03257 82 KEIQMVFQDPmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-561 |
3.56e-46 |
|
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: 161.43 E-value: 3.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARmayamdfinkmdngldtiIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT 561
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
359-509 |
4.46e-46 |
|
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: 158.97 E-value: 4.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFND-TVANNI 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 438 AYARTEEYsREQIEEAARMAYAMDFINkMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:pfam00005 81 RLGLLLKG-LSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-558 |
1.13e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 160.59 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKST---IASLITRfydVDEGQILLDGHD---LREYKLS 413
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 414 SLR-DQVALVSQNVHLFND-TVANNIAYARteEYSREQIEEAARMAYAM-------DFINKMdngldtiIGEngvmLSGG 484
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPElTALENVALPL--LLAGVSRKERRERARELlervglgDRLDHR-------PSQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-568 |
7.86e-45 |
|
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: 158.51 E-value: 7.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPG--REVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLR 416
Cdd:cd03258 2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFINKMDNGlDTIIGEngvmLSGGQRQRIAIARA 494
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE--RVLELLELVGLEDKA-DAYPAQ----LSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-577 |
1.41e-44 |
|
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: 170.51 E-value: 1.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 70 VVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRE 149
Cdd:TIGR00957 1010 VYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGS 1089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 150 GASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEvetkR 229
Cdd:TIGR00957 1090 LFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQE----R 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 230 FDKVSNKMRLQGMKMVSASSISDPIIQL-IASLALAFVLYAASFPSV-MDTLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:TIGR00957 1166 FIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 308 FQRGMAACQTLFAILDSEQEKD---EGTRVIER--AKGNLKFENVTFTY-PGREVAaLRNINLDIPEGKTVALVGRSGSG 381
Cdd:TIGR00957 1246 METNIVAVERLKEYSETEKEAPwqiQETAPPSGwpPRGRVEFRNYCLRYrEDLDLV-LRHINVTIHGGEKVGIVGRTGAG 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 382 KSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMD 461
Cdd:TIGR00957 1325 KSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD--PFSQYSDEEVWWALELAHLKT 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 462 FINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
Cdd:TIGR00957 1403 FVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNT 1482
|
490 500 510
....*....|....*....|....*....|....*.
gi 488987387 542 IEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQLHK 577
Cdd:TIGR00957 1483 IMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-567 |
2.82e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.15 E-value: 2.82e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyKLSSLRDQVAL 421
Cdd:COG1131 1 IEVRGLTKRYGDKT--ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAY-ARTeeYSREQIEEAARMAYAMDFINkMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFfARL--YGLPRKEARERIDELLELFG-LTDAADRKVGT----LSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLE 567
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-555 |
3.60e-44 |
|
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: 154.32 E-value: 3.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 343 KFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALV 422
Cdd:cd00267 1 EIENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQnvhlfndtvanniayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRNSPIL 502
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 503 ILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQA-DEIVVVEDGR 555
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
4.59e-44 |
|
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: 158.42 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGsdTFMLS--LLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGH 107
Cdd:cd18576 1 GLILLLLSSA--IGLVFplLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 108 MMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:cd18576 79 LQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:cd18576 159 RIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488987387 268 YAASFPSVMDTLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18576 239 WYGGRLVLAGELTAGDLVafLLYTLFIA--GSIGSLADLYGQLQKALGA 285
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-560 |
4.76e-44 |
|
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: 155.76 E-value: 4.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLreYKLSSLRDQVAL 421
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfiNKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGlKLRGVPKAEIRARVRELLEL---VGLEGLLNRYPHE----LSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-556 |
5.13e-44 |
|
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: 156.11 E-value: 5.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLR 416
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiskLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 -DQVALVSQNVHLFND-TVANNIAYArtEEYSREQIEEAARMAYAMdfINKMdnGLDTIIGENGVMLSGGQRQRIAIARA 494
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELP--LLLAGVPKKERRERAEEL--LERV--GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-568 |
1.30e-43 |
|
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: 155.54 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAYART-EEYSREQIEEAARMAYAMdfinkMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALVPKlLKWPKEKIRERADELLAL-----VGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-568 |
5.27e-43 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.16 E-value: 5.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLR 416
Cdd:COG1135 2 IELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFI---NKMDNGLDTiigengvmLSGGQRQRIAI 491
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEIRK--RVAELLELVglsDKADAYPSQ--------LSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVF 229
|
..
gi 488987387 567 EH 568
Cdd:COG1135 230 AN 231
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
9.95e-43 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 154.98 E-value: 9.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDD----GFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRR 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 103 RLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 183 RVVSKRFRNI-------SKNMQNTMGQVttsaeqmLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPII 255
Cdd:cd18563 161 YFFWKKIRRLfhrqwrrWSRLNSVLNDT-------LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 256 QLIASLALAFVLYAASfPSVM-DTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18563 234 TFLTSLGTLIVWYFGG-RQVLsGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAE 294
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-569 |
1.15e-42 |
|
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: 153.21 E-value: 1.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQ 418
Cdd:COG1127 6 IEVRNLTKSFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNIAYARTE--EYSREQIEEAARMAYAM----DFINKMdngldtiIGEngvmLSGGQRQRIAI 491
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPLREhtDLSEAEIRELVLEKLELvglpGAADKM-------PSE----LSGGMRKRVAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLAS 232
|
.
gi 488987387 569 K 569
Cdd:COG1127 233 D 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-566 |
2.33e-42 |
|
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: 152.51 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:COG1120 2 LEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHL-FNDTVANNIAYAR----------TEEySREQIEEAARMAYAMDFINKMdngLDTiigengvmLSGGQRQRIA 490
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrpSAE-DREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-570 |
4.15e-42 |
|
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: 152.58 E-value: 4.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD-LREYKLSSLRDQVA 420
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQN-----VhlfNDTVANNIAYA------RTEEYsREQIEEAARMAYAMDFINKmdngldtiigeNGVMLSGGQRQRI 489
Cdd:TIGR04520 81 MVFQNpdnqfV---GATVEDDVAFGlenlgvPREEM-RKRVDEALKLVGMEDFRDR-----------EPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT------ 561
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifs 225
|
....*....
gi 488987387 562 HHDLLEHKG 570
Cdd:TIGR04520 226 QVELLKEIG 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-558 |
4.17e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 150.97 E-value: 4.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQ 418
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEAARMAyamdfINKMdnGLDTIIGENGVMLSGGQRQRIAIARALL 496
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlRVTGKSRKEIRRRVREV-----LDLV--GLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADE-IVVVEDGRIVE 558
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-570 |
2.59e-41 |
|
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: 149.62 E-value: 2.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSsLRDQVAL 421
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAY-ARTEEYSREQIEE-AARMAYAMDfinkMDNGLDTIIGEngvmLSGGQRQRIAIARALLRN 498
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYfAELYGLFDEELKKrIEELIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEHKG 570
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
5.45e-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: 148.80 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQN----VHLFNdTVANNIAYARTEEYSREQIEEAARMAYAMdfinkmdnGLDTiigenGVM------LSGGQRQRI 489
Cdd:COG1124 82 QMVFQDpyasLHPRH-TVDRILAEPLRIHGLPDREERIAELLEQV--------GLPP-----SFLdryphqLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
..
gi 488987387 567 EH 568
Cdd:COG1124 228 AG 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
344-568 |
1.37e-40 |
|
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: 147.26 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQVA 420
Cdd:cd03261 3 LRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLFND-TVANNIAYARTE--EYSREQIEEAARMAYAM----DFINKMDngldtiiGEngvmLSGGQRQRIAIAR 493
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPLREhtRLSEEEIREIVLEKLEAvglrGAEDLYP-------AE----LSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
341-568 |
3.42e-40 |
|
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: 148.66 E-value: 3.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKfenVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYD---VDEGQILLDGHDLREYKLSSLRD 417
Cdd:COG0444 6 NLK---VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 ----QVALVSQN-------VHlfndTVanniayarteeysREQIEE----------AARMAYAMDFINKMdnGLDtiiGE 476
Cdd:COG0444 83 irgrEIQMIFQDpmtslnpVM----TV-------------GDQIAEplrihgglskAEARERAIELLERV--GLP---DP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 477 NGVM------LSGGQRQRIAIARALLRNSPILILDEATSALD-TeseraIQAA----LDELQKNR-TSLV-IAHRLSTIE 543
Cdd:COG0444 141 ERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELgLAILfITHDLGVVA 215
|
250 260
....*....|....*....|....*.
gi 488987387 544 Q-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG0444 216 EiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
27-314 |
4.43e-40 |
|
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: 147.58 E-value: 4.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGsdtfmLSLLKPLL-----DDGFGKtdrSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMR 101
Cdd:cd18551 1 LILALLLSLLGTA-----ASLAQPLLvknliDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 102 RRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVA 181
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 182 IRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488987387 262 ALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGA 285
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
342-568 |
8.74e-40 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 148.32 E-value: 8.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDlreykLSSL---RDQ 418
Cdd:COG3842 6 LELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-----VTGLppeKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFINKMdngldtiIGEngvmLSGGQRQRIAIA 492
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRARVAELLELvgleGLADRY-------PHQ----LSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS---TIeqADEIVVVEDGRIVERGTHHDLLE 567
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYE 225
|
.
gi 488987387 568 H 568
Cdd:COG3842 226 R 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-555 |
3.71e-39 |
|
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: 141.56 E-value: 3.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSS--LRDQV 419
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLF-NDTVANNIAYArteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRN 498
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
342-568 |
4.54e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 143.21 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL--REYKLSSLRDQV 419
Cdd:COG1126 2 IEIENLHKSFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFND-TVANNIAYA--RTEEYSREQIEEAARMAYAM----DFINKMDNgldtiigengvMLSGGQRQRIAIA 492
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApiKVKKMSKAEAEERAMELLERvglaDKADAYPA-----------QLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH-----RlstiEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHemgfaR----EVADRVVFMDGGRIVEEGPPEEFF 224
|
..
gi 488987387 567 EH 568
Cdd:COG1126 225 EN 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-559 |
8.72e-39 |
|
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: 141.84 E-value: 8.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlreYKLSSLRDQV 419
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFN-DTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFINKMDNgldtiigengvMLSGGQRQRIAIAR 493
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEELLELvglsGFENAYPH-----------QLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVE--DGRIVER 559
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-313 |
1.08e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 143.78 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLK--GHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488987387 265 FVLYAASFPSVMDTLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTL-VAFTALLGrLYGPLTQLLNIQVDLMTSLA 289
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
102-570 |
1.24e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 152.44 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 102 RRLFGHMMG----MPVAFFDKQSTGTLLSRITYDSEQVAsssssalitvvREGASIIGLFVMMFyysWQL--SLILIVLA 175
Cdd:PLN03232 983 KRLHDAMLNsilrAPMLFFHTNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---WQLlsTFALIGTV 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 176 PIVSV-AIRVVSKRFRNISKNMQNT------MGQVTTSA-----EQMLKGHKEVLMFGGQEvetkRFDKVSNKMRLQGMK 243
Cdd:PLN03232 1049 STISLwAIMPLLILFYAAYLYYQSTsrevrrLDSVTRSPiyaqfGEALNGLSSIRAYKAYD----RMAKINGKSMDNNIR 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 244 MVSASSISDPIIQL-IASLALAFVLYAASFPSVMDTLTAGTitVVFSSMIALMRPLKS-----LTNVNAQFQRGMAACQT 317
Cdd:PLN03232 1125 FTLANTSSNRWLTIrLETLGGVMIWLTATFAVLRNGNAENQ--AGFASTMGLLLSYTLnittlLSGVLRQASKAENSLNS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 318 LFAILDSEQEKDEGTRVIER--------AKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLI 389
Cdd:PLN03232 1203 VERVGNYIDLPSEATAIIENnrpvsgwpSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAL 1282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 390 TRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFINKMDNG 469
Cdd:PLN03232 1283 FRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID--PFSEHNDADLWEALERAHIKDVIDRNPFG 1360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 470 LDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PLN03232 1361 LDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKIL 1440
|
490 500
....*....|....*....|.
gi 488987387 550 VVEDGRIVERGTHHDLLEHKG 570
Cdd:PLN03232 1441 VLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
30-314 |
1.79e-38 |
|
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: 143.08 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 110 GMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF 189
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 488987387 270 ASFPSVMDTLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18557 241 GGYLVLSGQLTVGELTsfILYTIMVA--SSVGGLSSLLADIMKALGA 285
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
341-566 |
2.46e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.05 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPGREVaalrNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQVA 420
Cdd:COG3840 1 MLRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT--ALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLFND-TVANNIAYAR------TEEySREQIEEAARmayamdfinKMdnGLDTIIGENGVMLSGGQRQRIAIAR 493
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLrpglklTAE-QRAQVEQALE---------RV--GLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
27-314 |
4.48e-38 |
|
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: 142.22 E-value: 4.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488987387 267 LYAASFPSVMDTLTAGTItVVFSSMIALM-RPLKSLTNVNAQFQRGMAA 314
Cdd:cd18545 242 YWYGGKLVLGGAITVGVL-VAFIGYVGRFwQPIRNLSNFYNQLQSAMAS 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
340-570 |
6.02e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 150.66 E-value: 6.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD--PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKG 570
Cdd:PLN03130 1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
343-569 |
7.60e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.90 E-value: 7.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 343 KFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALV 422
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNV--HLFNDTVANNIAYA-RTEEYSREQ----IEEAARMAyamdfinKMDNGLDtiigENGVMLSGGQRQRIAIARAL 495
Cdd:PRK13632 89 FQNPdnQFIGATVEDDIAFGlENKKVPPKKmkdiIDDLAKKV-------GMEDYLD----KEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA--HRLSTIEQADEIVVVEDGRIVERGTHHDLLEHK 569
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
345-568 |
8.74e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.98 E-value: 8.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGRevAALRNINLDIPEGKTVALVGRSGSGKST----IASLITrfydVDEGQILLDGHDLrEYKLSSLRDQVA 420
Cdd:COG1118 6 RNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLET----PDSGRIVLNGRDL-FTNLPPRERRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLF-NDTVANNIAYA-RTEEYSREQIeeAARmayAMDFINKMdnGLDTIIG----EngvmLSGGQRQRIAIARA 494
Cdd:COG1118 79 FVFQHYALFpHMTVAENIAFGlRVRPPSKAEI--RAR---VEELLELV--QLEGLADrypsQ----LSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 495 LLRNSPILILDEATSALDT----ESERAIQAALDELQknRTSLVIAH------RLstieqADEIVVVEDGRIVERGTHHD 564
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELG--GTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220
|
....
gi 488987387 565 LLEH 568
Cdd:COG1118 221 VYDR 224
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-575 |
1.09e-37 |
|
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: 140.04 E-value: 1.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAYARTeeYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK--CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHK-GVYAQL 575
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASL 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
345-560 |
1.34e-37 |
|
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: 137.18 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:cd03214 3 ENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLFNdtvanniayarTEEYSREQIEEaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRNSPILIL 504
Cdd:cd03214 81 ALELLG-----------LAHLADRPFNE----------------------------LSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 505 DEATSALDTeserAIQAALDEL------QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:cd03214 122 DEPTSHLDI----AHQIELLELlrrlarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-556 |
2.14e-37 |
|
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: 136.37 E-value: 2.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSsLRDQVAL 421
Cdd:cd03230 1 IEVRNLSKRYGKKT--ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIayarteeysreqieeaarmayamdfinkmdngldtiigengvMLSGGQRQRIAIARALLRNSP 500
Cdd:cd03230 78 LPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-568 |
4.82e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklssLRDQVAL 421
Cdd:COG1121 7 IELENLTVSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND---TVANNIAYARTEE------YSREQIEEAARmayAMDFINkMDNGLDTIIGEngvmLSGGQRQRIAIA 492
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDVVLMGRYGRrglfrrPSRADREAVDE---ALERVG-LEDLADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVErGTHHDLLEH 568
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
343-568 |
8.83e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.94 E-value: 8.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 343 KFENVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRD 417
Cdd:PRK11153 3 ELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQnvHlFN----DTVANNIAYA-RTEEYSREQIEeaARMAYAMDFI---NKMD----NgldtiigengvmLSGGQ 485
Cdd:PRK11153 83 QIGMIFQ--H-FNllssRTVFDNVALPlELAGTPKAEIK--ARVTELLELVglsDKADrypaQ------------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTH 562
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
....*.
gi 488987387 563 HDLLEH 568
Cdd:PRK11153 226 SEVFSH 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
1.17e-36 |
|
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: 138.00 E-value: 1.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 110 GMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF 189
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 488987387 270 ASFpSVMD-TLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18575 241 GAH-DVLAgRMSAGELSqfVFYAVLAA--GSVGALSEVWGDLQRAAGA 285
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-558 |
1.26e-36 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR--EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklssLRDQV 419
Cdd:COG1116 8 LELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFN-DTVANNIAYA-RTEEYSREQIEEAARmayamDFINKMdnGLDtiigenGVM------LSGGQRQRIAI 491
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERAR-----ELLELV--GLA------GFEdayphqLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH------RLstieqADEIVVVED--GRIVE 558
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
27-314 |
1.77e-36 |
|
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: 137.54 E-value: 1.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGsdtfmLSLLKPLL-----DD-GFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTM 100
Cdd:cd18541 1 YLLGILFLILVDL-----LQLLIPRIigraiDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 101 RRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRegASIIGLFV--MMFYYSWQLSLILIVLAPIV 178
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVD--ALFLGVLVlvMMFTISPKLTLIALLPLPLL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 179 SVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLI 258
Cdd:cd18541 154 ALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLL 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 259 ASLALAFVLYAASFPSVMDTLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAA 314
Cdd:cd18541 234 IGLSFLIVLWYGGRLVIRGTITLGDL-VAFNSYLGMLIwPMMALGWVINLIQRGAAS 289
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-568 |
6.62e-36 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 134.29 E-value: 6.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLreYKLSSLRDQVAL 421
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFInKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlRLKKLPKAEIKE--RVAEALDLV-QLEGYANRKPSQ----LSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-556 |
1.19e-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: 133.04 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL--REYKLSSLRDQV 419
Cdd:cd03262 1 IEIKNLHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLF-NDTVANNIAYA--RTEEYSREQIEEAArmayaMDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALL 496
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApiKVKGMSKAEAEERA-----LELLEKV--GLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRI 556
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
352-568 |
1.24e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.40 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 352 PGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQVALVsqnvhl 428
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMV------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 429 FND---------TVANNIAYARTEeysREQIEEAARMAYAMDFINKMdnGLDT-IIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:COG4608 101 FQDpyaslnprmTVGDIIAEPLRI---HGLASKAERRERVAELLELV--GLRPeHADRYPHEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 499 SPILILDEATSALDTeserAIQAA----LDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG4608 176 PKLIVCDEPVSALDV----SIQAQvlnlLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-561 |
3.21e-35 |
|
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: 132.69 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQ 418
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNIAYARTEE----------YSREQIEEAarmAYAMDfinkmDNGLDTIIGENGVMLSGGQRQ 487
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglFPKEEKQRA---LAALE-----RVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGT 561
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGP 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-557 |
5.44e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 132.10 E-value: 5.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGReVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQ 418
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNI-----AYART-----EEYSREQIEEAARMAYAMDFINKMDNGLDTiigengvmLSGGQRQ 487
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlGRTSTwrsllGLFPPEDRERALEALERVGLADKAYQRADQ--------LSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
27-316 |
6.94e-35 |
|
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: 133.38 E-value: 6.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVReGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGN-LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488987387 267 LYAASFPSVMDTLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18543 240 LALGGWLVANGSLTLGTL-VAFSAYLTMLVwPVRMLGWLLAMAQRARAAAE 289
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
51-313 |
1.50e-34 |
|
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: 132.57 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 51 LLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITY 130
Cdd:cd18549 28 IIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 131 D----SEQVASSSSSALITVVRegasIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTS 206
Cdd:cd18549 108 DlfdiSELAHHGPEDLFISIIT----IIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 207 AEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTItV 286
Cdd:cd18549 184 LEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDL-V 262
|
250 260
....*....|....*....|....*...
gi 488987387 287 VFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18549 263 AFLLYVNvFIKPIRRLVNFTEQYQKGMA 290
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
16-565 |
1.79e-34 |
|
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: 137.24 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 16 LWPIIAPFKAGLIVAAVALVLNAGSDTFMLSLLkpllDDGFGKTDrSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGK 95
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALI----NQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 96 VVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSaLITVVREGASIIGLFVMMFYYSWQLSLILIVLA 175
Cdd:COG4615 79 AVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 176 PIVSVAIRVVSKRFR---NISKNMQNTMGQVTTSaeqMLKGHKEVLMFG--GQEVETKRFDKVSNKMRLQGMKMVSASSI 250
Cdd:COG4615 158 GLGVAGYRLLVRRARrhlRRAREAEDRLFKHFRA---LLEGFKELKLNRrrRRAFFDEDLQPTAERYRDLRIRADTIFAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 251 SDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVfssMIALMRPLKSLTNVNAQFQRGMAACQ---TLFAILDSEQE 327
Cdd:COG4615 235 ANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLV---LLFLRGPLSQLVGALPTLSRANVALRkieELELALAAAEP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 328 KDEGTRVIERAKG--NLKFENVTFTYPGREVA---ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILL 402
Cdd:COG4615 312 AAADAAAPPAPADfqTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 403 DGHDLREYKLSSLRDQVALVSQNVHLFNDTvanniaYARTEEYSREQIEEaarmayamdFINKMDngLDTIIG-ENGVM- 480
Cdd:COG4615 392 DGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPARARE---------LLERLE--LDHKVSvEDGRFs 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 ---LSGGQRQRIAIARALLRNSPILILDEatsaldteseraiQAA--------------LDEL-QKNRTSLVIAHRLSTI 542
Cdd:COG4615 455 ttdLSQGQRKRLALLVALLEDRPILVFDE-------------WAAdqdpefrrvfytelLPELkARGKTVIAISHDDRYF 521
|
570 580
....*....|....*....|...
gi 488987387 543 EQADEIVVVEDGRIVERGTHHDL 565
Cdd:COG4615 522 DLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
359-568 |
2.58e-34 |
|
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: 130.15 E-value: 2.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREykLSSLRDQVALVSQNVHLF-NDTVANNI 437
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN--LPPEKRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 438 AYA-RTEEYSREQIEEAAR-MAYAMdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:cd03299 93 AYGlKKRKVDKKEIERKVLeIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 516 ERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03299 165 KEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-316 |
3.95e-34 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 130.98 E-value: 3.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488987387 267 LYAASFPSVMDTLTAGTITVVFS-SMIALMrPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINyLMQILM-SLMMLSMVFVMLPRASASAK 290
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
19-318 |
4.46e-34 |
|
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: 131.06 E-value: 4.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 19 IIAPFKAGLIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMplvvIGLMVLRGITSYISSYCISWVSGKVVM 98
Cdd:cd18577 5 LLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYF----VYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 99 TMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIV 178
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 179 SVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLI 258
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 259 ASLALAFVLYAASFPSVMDTLTAGTI-TVVFSSMIALMrplkSLTNVNAQ---FQRGMAACQTL 318
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEISPGDVlTVFFAVLIGAF----SLGQIAPNlqaFAKARAAAAKI 300
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-568 |
5.68e-34 |
|
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: 129.00 E-value: 5.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQVAL 421
Cdd:cd03296 3 IEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT--DVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAYARTEEYSREQIEEAARMAYAMDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSP 500
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 501 ILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-568 |
7.34e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 7.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNV--HLFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFINkMDNGLDtiigENGVMLSGGQRQRIAIARALLRN 498
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGlENIGVPREEMVE--RVDQALRQVG-MEDFLN----REPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 499 SPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-557 |
7.99e-34 |
|
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: 128.03 E-value: 7.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 343 KFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlreYKLSSLRDQVALV 422
Cdd:cd03235 1 EVEDLTVSYGGHPV--LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNvHLFN--------DTVANNIaYARTEEYSREQIEEAARMAYAMDFINkMDNGLDTIIGEngvmLSGGQRQRIAIARA 494
Cdd:cd03235 74 PQR-RSIDrdfpisvrDVVLMGL-YGHKGLFRRLSKADKAKVDEALERVG-LSELADRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIV 557
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
19-285 |
1.01e-33 |
|
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: 130.06 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 19 IIAPFKAGLIVAAVALVLNAGSDtfmlsllkplldDGFGKTDRSVLLWMPLVVIGlmvlrGITSYISSYCISWVSGKVVM 98
Cdd:cd18780 13 LALPYFFGQVIDAVTNHSGSGGE------------EALRALNQAVLILLGVVLIG-----SIATFLRSWLFTLAGERVVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 99 TMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIV 178
Cdd:cd18780 76 RLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 179 SVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLI 258
Cdd:cd18780 156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAA 235
|
250 260
....*....|....*....|....*..
gi 488987387 259 ASLALAFVLYAASFPSVMDTLTAGTIT 285
Cdd:cd18780 236 AQLAIVLVLWYGGRLVIDGELTTGLLT 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
1.07e-33 |
|
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: 134.81 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR---------EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDvDEGQILLDGHD---LRE 409
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDldgLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 410 YKLSSLRDQVALVsqnvhlFND---------TVANNIAyartE-------EYSREQIEEaaRMAYAMDfinkmDNGLDTi 473
Cdd:COG4172 355 RALRPLRRRMQVV------FQDpfgslsprmTVGQIIA----EglrvhgpGLSAAERRA--RVAEALE-----EVGLDP- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 474 igenGVM------LSGGQRQRIAIARALLRNSPILILDEATSALDteseRAIQAA----LDELQKNR--TSLVIAHRLST 541
Cdd:COG4172 417 ----AARhrypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAV 488
|
250 260
....*....|....*....|....*...
gi 488987387 542 IEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG4172 489 VRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-565 |
1.57e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.99 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRD---- 417
Cdd:COG1129 5 LEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVHLFND-TVANNIAYARteEYSR-------EQIEEAARmayAMDFINkMDNGLDTIIGEngvmLSGGQRQRI 489
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFLGR--EPRRgglidwrAMRRRARE---LLARLG-LDIDPDTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSAL-DTESER--AIqaaLDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGTHHD 564
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLtEREVERlfRI---IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAE 226
|
.
gi 488987387 565 L 565
Cdd:COG1129 227 L 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
356-568 |
1.66e-33 |
|
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: 128.92 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 356 VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSL----RDQVALVSQNVHLF-N 430
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 431 DTVANNIAYArteeYSREQIEEAARMAYAMDFINKMDNG--LDTIIGEngvmLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:cd03294 117 RTVLENVAFG----LEVQGVPRAEREERAAEALELVGLEgwEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 509 SALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-567 |
2.12e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 128.76 E-value: 2.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFY---DVDEGQILLDGHDLREYKLSSLRDQ 418
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNV--HLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAmdfinkmDNGLDTIIGENGVMLSGGQRQRIAIARAL 495
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEMIKIVRDVLA-------DVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-568 |
4.09e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.56 E-value: 4.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNV--HLFNDTVANNIAYArTEEYS---REQIEEAARMAYAMDFINKMDNGLDTiigengvmLSGGQRQRIAIARALL 496
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFG-LENHAvpyDEMHRRVSEALKQVDMLERADYEPNA--------LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
342-568 |
2.87e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 127.50 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKlsslRDq 418
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPKD----RN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNV----HLfndTVANNIAYA-RTEEYSREQIE----EAARMAyamdfinKMDNGLDTIIGEngvmLSGGQRQRI 489
Cdd:COG3839 77 IAMVFQSYalypHM---TVYENIAFPlKLRKVPKAEIDrrvrEAAELL-------GLEDLLDRKPKQ----LSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAhrlsTIEQ------ADEIVVVEDGRIVERGTH 562
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV----THDQveamtlADRIAVMNDGRIQQVGTP 218
|
....*.
gi 488987387 563 HDLLEH 568
Cdd:COG3839 219 EELYDR 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
361-560 |
3.63e-32 |
|
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: 123.17 E-value: 3.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 361 NINLDIPEGkTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK----LSSLRDQVALVSQNVHLF-NDTVAN 435
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRkkinLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 436 NIAYARTEEYSREQIEEAARMAYAMdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488987387 516 ERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-557 |
5.94e-32 |
|
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: 121.00 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRDQ--- 418
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDArra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 -VALVSQnvhlfndtvanniayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLR 497
Cdd:cd03216 76 gIAMVYQ--------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 498 NSPILILDEATSAL-DTESERAIqAALDELQKN-RTSLVIAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-560 |
8.45e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 123.61 E-value: 8.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDL--REYKLSS 414
Cdd:COG1117 12 IEVRNLNVYYGDKQ--ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDfinKMDNGLDtiigENGVMLSGGQRQR 488
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESLRKAALWD---EVKDRLK----KSALGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLStieQA----DEIVVVEDGRIVERG 560
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQ---QAarvsDYTAFFYLGELVEFG 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-560 |
9.06e-32 |
|
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: 122.36 E-value: 9.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSlRDqVAL 421
Cdd:cd03301 1 VELENVTKRFGNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfinkmdNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDERVREVAEL-------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH-RLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
30-314 |
1.33e-31 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 123.81 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 110 GMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF 189
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488987387 270 ASFPSVMDTLTAGT-ITVVFSSMIaLMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18572 241 GGHLVLSGRMSAGQlVTFMLYQQQ-LGEAFQSLGDVFSSLMQAVGA 285
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
333-575 |
2.22e-31 |
|
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: 130.45 E-value: 2.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 333 RVIERAKGN-LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlreyk 411
Cdd:TIGR00957 627 RTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 412 lsslrdQVALVSQNVHLFNDTVANNIAYAR--TEEYSREQIEEAARMAYamdfINKMDNGLDTIIGENGVMLSGGQRQRI 489
Cdd:TIGR00957 700 ------SVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRV 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:TIGR00957 770 SLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELL 849
|
....*....
gi 488987387 567 EHKGVYAQL 575
Cdd:TIGR00957 850 QRDGAFAEF 858
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-315 |
3.50e-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: 123.03 E-value: 3.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKT-DRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLF 105
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 106 GHMMGMPVAFFDKQSTGTLLSRITYDS---EQVASSSSSALITVVregASIIGLFVMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVanvERLIADGIPQGITNV---LTLVGVAIILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 183 RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488987387 263 LAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-561 |
4.41e-31 |
|
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: 120.30 E-value: 4.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReYKLSSLRDQVAL 421
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIA-YARTEEYSREQI-EEAARMAYAMDFINKMdnglDTIIGEngvmLSGGQRQRIAIARALLRN 498
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLKGLPKSEIkEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGT 561
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-550 |
5.25e-31 |
|
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: 119.89 E-value: 5.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKST----IASLITrfydVDEGQILLDGHDLREyKLSSLRD 417
Cdd:COG4133 3 LEAENLSCRRGERLL--FSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVHLFND-TVANNIAYART---EEYSREQIEEA-ARMayamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIA 492
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWAAlygLRADREAIDEAlEAV------------GLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADEIVV 550
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
27-314 |
8.89e-31 |
|
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: 121.83 E-value: 8.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVvs 186
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 187 krFRNISKN----MQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18546 159 --FRRRSSRayrrARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488987387 263 LAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
342-561 |
8.98e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 121.69 E-value: 8.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTY-PGR--EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL--REYKLSSLR 416
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFInkmdnGLD--TIIGENGVMLSGGQRQRIAI 491
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpINLGLSEEEIEN--RVKRAMNIV-----GLDyeDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGT 561
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-556 |
1.50e-30 |
|
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: 118.66 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQ 418
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFInkmdnGLDTIIGENGVMLSGGQRQRIAIARALL 496
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFAlEVTGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhrlstiEQADEIV--------VVEDGRI 556
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAKELVdttrhrviALERGKL 214
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
69-567 |
3.05e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 126.82 E-value: 3.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGLMVLRGITSYISSYCISWVSGKV-VMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVV 147
Cdd:PTZ00243 1001 LYVYLGIVLLGTFSVPLRFFLSYEAMRRgSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLL 1080
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 148 REGASIIGLFVMMFYYSwqlSLILIVLAPIVSVAIRVV---SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQE 224
Cdd:PTZ00243 1081 QCLFSICSSILVTSASQ---PFVLVALVPCGYLYYRLMqfyNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAH 1157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 225 V----ETKRFDKVSNKMRLQ-------GMKMVSASSISDPIIQLI---------ASLALAFVlyaaSFPSVMDTLTAGT- 283
Cdd:PTZ00243 1158 LvmqeALRRLDVVYSCSYLEnvanrwlGVRVEFLSNIVVTVIALIgvigtmlraTSQEIGLV----SLSLTMAMQTTATl 1233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 284 ------ITVVFSSMIALMRPLKSLTNVN-----------AQFQR--GMAACQTlfaildseqekdeGTRVIERAK----- 339
Cdd:PTZ00243 1234 nwlvrqVATVEADMNSVERLLYYTDEVPhedmpeldeevDALERrtGMAADVT-------------GTVVIEPASptsaa 1300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 ------GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLS 413
Cdd:PTZ00243 1301 phpvqaGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 414 SLRDQVALVSQNVHLFNDTVANNIayARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIAR 493
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDGTVRQNV--DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMAR 1458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 494 ALL-RNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PTZ00243 1459 ALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
342-567 |
3.20e-30 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.98 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQVAL 421
Cdd:PRK09452 15 VELRGISKSFDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIE----EAARMAYAMDFINKmdngldtiigeNGVMLSGGQRQRIAIARAL 495
Cdd:PRK09452 91 VFQSYALFpHMTVFENVAFGlRMQKTPAAEITprvmEALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLstiEQA----DEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQ---EEAltmsDRIVVMRDGRIEQDGTPREIYE 234
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
3.75e-30 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 119.89 E-value: 3.75e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAI---- 182
Cdd:cd18540 84 HLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSiyfq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 183 RVVSKRFRNISKnmQNTmgQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18540 164 KKILKAYRKVRK--INS--RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488987387 263 LAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-566 |
3.79e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.15 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgrEVAALRnINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQVAL 421
Cdd:PRK10771 2 LKLTDITWLY---HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT--TTPPSRRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAYA-----RTEEYSREQIEEAARMAYAMDFINKMDngldtiiGEngvmLSGGQRQRIAIARAL 495
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-316 |
6.19e-30 |
|
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: 119.54 E-value: 6.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 64 LLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSAL 143
Cdd:cd18573 40 LKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 144 ITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQ 223
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 224 EVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTIT-------VVFSSMIalmr 296
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTsflmyavYVGSSVS---- 275
|
250 260
....*....|....*....|
gi 488987387 297 plkSLTNVNAQFQRGMAACQ 316
Cdd:cd18573 276 ---GLSSFYSELMKGLGASS 292
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
345-557 |
1.60e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 115.43 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYpGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLreyKLSSLRDQVALVSQ 424
Cdd:cd03226 3 ENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NV--HLFNDTVANNIAY-ARTEEYSREQIEEAARmayamdfinKMDngLDTIIGENGVMLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03226 79 DVdyQLFTDSVREELLLgLKELDAGNEQAETVLK---------DLD--LYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 502 LILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIVVVEDGRIV 557
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
342-560 |
1.60e-28 |
|
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: 113.06 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTvALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKlSSLRDQVAL 421
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAY-ARTEEYSREQIEeaARMAYAMDFINkMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYiAWLKGIPSKEVK--ARVDEVLELVN-LGDRAKKKIGS----LSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-560 |
1.96e-28 |
|
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: 112.59 E-value: 1.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 364 LDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSslRDQVALVSQNVHLFND-TVANNIAYART 442
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 443 -----EEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESER 517
Cdd:cd03298 97 pglklTAEDRQAIEVALARV-----------GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488987387 518 AIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03298 166 EMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
358-567 |
3.35e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 112.53 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSS---LRDQVALVSQNVHLFND-TV 433
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPherARAGIGYVPEGRRIFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 ANNI---AYARTEEYSREQIEEaarmAYAMdFINkmdngLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:cd03224 93 EENLllgAYARRRAKRKARLER----VYEL-FPR-----LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 511 LDTESERAIQAALDELQKNRTSLVIahrlstIEQ--------ADEIVVVEDGRIVERGTHHDLLE 567
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEGVTILL------VEQnarfaleiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-566 |
3.75e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 113.93 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREY-KLSSLRDQVA 420
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFsKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQN--VHLFNDTVANNIAYArTEEYSREQIEEAARMAYAMDFInkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFG-PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-566 |
8.20e-28 |
|
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: 112.10 E-value: 8.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQ-ILLDGHDLREYKLSSLRDQVA 420
Cdd:COG1119 4 LELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLF---NDTVANNI---AYA---RTEEYSREQIEEAARMAYAMDFINKMDNGLDTiigengvmLSGGQRQRIAI 491
Cdd:COG1119 82 LVSPALQLRfprDETVLDVVlsgFFDsigLYREPTDEQRERARELLELLGLAHLADRPFGT--------LSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQA-DEIVVVEDGRIVERGTHHDLL 566
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
344-568 |
1.08e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 111.72 E-value: 1.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLS--SLRDQVAL 421
Cdd:PRK09493 4 FKNVSKHFGPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDerLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVA-NNIAYA--RTEEYSREQIEEAARmayamDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:PRK09493 82 VFQQFYLFPHLTAlENVMFGplRVRGASKEEAEKQAR-----ELLAKV--GLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-561 |
1.28e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.52 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 352 PGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREY---KLSSLRDQVALVSQNVH- 427
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQNPYg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 428 ----------LFNDTVANNIAYARTEEysREQIeeAARMAYAmdfinkmdnGLDTiigENGV----MLSGGQRQRIAIAR 493
Cdd:PRK11308 104 slnprkkvgqILEEPLLINTSLSAAER--REKA--LAMMAKV---------GLRP---EHYDryphMFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 494 ALLRNSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGT 561
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDV----SVQAQvlnlMMDLQQElGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
2.47e-27 |
|
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: 115.94 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFEN--VTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKS----TIASLITRFYDVDEGQILLDGHDL---REYKL 412
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 413 SSLR-DQVALVSQ------N-VHlfndTVANNI--------------AYARTEEYSRE-QIEEAARMAYAMDFinkmdng 469
Cdd:COG4172 87 RRIRgNRIAMIFQepmtslNpLH----TIGKQIaevlrlhrglsgaaARARALELLERvGIPDPERRLDAYPH------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 470 ldtiigengvMLSGGQRQRIAIARALLrNSP-ILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEQ-A 545
Cdd:COG4172 156 ----------QLSGGQRQRVMIAMALA-NEPdLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLlITHDLGVVRRfA 224
|
250 260
....*....|....*....|...
gi 488987387 546 DEIVVVEDGRIVERGTHHDLLEH 568
Cdd:COG4172 225 DRVAVMRQGEIVEQGPTAELFAA 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
168-575 |
2.91e-27 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 117.77 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 168 SLILIVLAPIVSVAIRvvskRFRNISKN-MQNTMGQVTTSAEqmlkghkevLMFGGQEVETKRFDKvSNKMRLQGMKMVS 246
Cdd:PLN03232 447 SLILFLLIPLQTLIVR----KMRKLTKEgLQWTDKRVGIINE---------ILASMDTVKCYAWEK-SFESRIQGIRNEE 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 247 ASSISDPiiQLIASLAlAFVLyaASFPSVMDTLTAGTITVV---------FSSM--IALMR-PLKSLTNVNAQFQRGMAA 314
Cdd:PLN03232 513 LSWFRKA--QLLSAFN-SFIL--NSIPVVVTLVSFGVFVLLggdltparaFTSLslFAVLRsPLNMLPNLLSQVVNANVS 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 315 CQTLFAILDSEQEKDEGTRVIERAKGNLKFENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGK-STIASLITRF 392
Cdd:PLN03232 588 LQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGEL 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 393 YDVDEGQILLdghdlreyklsslRDQVALVSQNVHLFNDTVANNIAYARTEEYSR--EQIEEAArMAYAMDFINKMDNgl 470
Cdd:PLN03232 668 SHAETSSVVI-------------RGSVAYVPQVSWIFNATVRENILFGSDFESERywRAIDVTA-LQHDLDLLPGRDL-- 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 471 dTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PLN03232 732 -TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
410 420
....*....|....*....|....*.
gi 488987387 550 VVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:PLN03232 811 LVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
361-568 |
3.36e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 112.89 E-value: 3.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 361 NINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklSSL--RDqVALVSQNVHLF-NDTVANNI 437
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIqqRD-ICMVFQSYALFpHMSLGENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 438 AYA-RTEEYSREQIEEAARMAYAM-DFINKMDNGLDTIigengvmlSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:PRK11432 100 GYGlKMLGVPKEERKQRVKEALELvDLAGFEDRYVDQI--------SGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 516 ERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK11432 172 RRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
317-554 |
4.20e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 115.67 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 317 TLFAILDSEQEKDEGTRVIERAKGN-LKFENVTFTYP-GREVaaLRNINLDIPEGKTVALVGRSGSGKST----IASLit 390
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGaLALEDLTLRTPdGRPL--LEDLSLSLKPGERLLITGPSGSGKSTllraIAGL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 391 rfYDVDEGQILLDGHDlreyklsslrdQVALVSQNVHLFNDTVANNIAY-ARTEEYSREQIEEAARMAYAMDFINKMDNG 469
Cdd:COG4178 413 --WPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 470 LDTiigenGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:COG4178 480 ADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
....*
gi 488987387 550 VVEDG 554
Cdd:COG4178 555 ELTGD 559
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
342-556 |
6.48e-27 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 108.41 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgrEVAALRnINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDlrEYKLSSLRDQVAL 421
Cdd:TIGR01277 1 LALDKVRYEY---EHLPME-FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAYA-----RTEEYSREQIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAIARAL 495
Cdd:TIGR01277 75 LFQENNLFAHlTVRQNIGLGlhpglKLNAEQQEKVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRI 556
Cdd:TIGR01277 144 VRPNPILLLDEPFSALDPLLREEMLALVKQLcsERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-576 |
7.04e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.64 E-value: 7.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPG---REVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDG----HDLREYKLSS 414
Cdd:PRK13646 3 IRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQ--NVHLFNDTVANNIAYArtEEYSREQIEEAArmAYAMDFInkMDNGLD-TIIGENGVMLSGGQRQRIAI 491
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFG--PKNFKMNLDEVK--NYAHRLL--MDLGFSrDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
....*...
gi 488987387 569 KGVYAQLH 576
Cdd:PRK13646 237 KKKLADWH 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-558 |
8.25e-27 |
|
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: 108.68 E-value: 8.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGRE--VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR---EYKLSSLR 416
Cdd:COG4181 9 IELRGLTKTVGTGAgeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 -DQVALVSQNVHLF-NDTVANNIAYARTEEYSREQIEEAARMAYAMdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARA 494
Cdd:COG4181 89 aRHVGFVFQSFQLLpTLTALENVMLPLELAGRRDARARARALLERV--------GLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIA-HRLSTIEQADEIVVVEDGRIVE 558
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
349-554 |
1.08e-26 |
|
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: 108.19 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 349 FTYpGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIL----LDGHDLREYKLSSLRDQVALVSQ 424
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLFNDTVANNIAYARTEEYSR-EQIEEAARMAYAMDFinkMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILI 503
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRyKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488987387 504 LDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEQADEIVVVEDG 554
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-560 |
1.10e-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: 107.69 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQV-A 420
Cdd:cd03268 1 LKTNDLTKTYGKKRV--LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSqnVHLFND---TVANNIAYARTEEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:cd03268 77 LIE--APGFYPnltARENLRLLARLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-557 |
1.14e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.41 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFT-YPG--REVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSL 415
Cdd:COG1101 2 LELKNLSKTfNPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 rdqVALVSQNVHL---FNDTVANN--IAYARTEEYSREQIEEAARMAYAMDFINKMDNGL----DTIIGengvMLSGGQR 486
Cdd:COG1101 82 ---IGRVFQDPMMgtaPSMTIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLstiEQA----DEIVVVEDGRIV 557
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
345-566 |
1.21e-26 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 109.02 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:COG4604 5 KNVSKRYGGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHlFND--TVANNIAYAR--------TEEySREQIEEAarMAYaMDFINKMDNGLDTiigengvmLSGGQRQRIAIARA 494
Cdd:COG4604 83 ENH-INSrlTVRELVAFGRfpyskgrlTAE-DREIIDEA--IAY-LDLEDLADRYLDE--------LSGGQRQRAFIAMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAAL----DELqkNRTSLVIAHrlsTIEQA----DEIVVVEDGRIVERGTHHDLL 566
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLrrlaDEL--GKTVVIVLH---DINFAscyaDHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
14-325 |
1.32e-26 |
|
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: 110.23 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 14 RRLWPIIApfkAGLIVAAVALVLNAGSdTFMLS-LLKPLLDDGFGKTDRSVLLWMpLVVIGLMVLRGITSYISSYCISWV 92
Cdd:cd18578 5 KPEWPLLL---LGLIGAIIAGAVFPVF-AILFSkLISVFSLPDDDELRSEANFWA-LMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 93 SGKVVMTMRRRLFGHMMGMPVAFFDKQ--STGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLI 170
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPenSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 171 LIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSI 250
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 251 SDPIIQLIASLALAFVLYA---------ASFPSVMDTLTAgtitVVFSSMIALMrplksLTNVNAQFQRGMAACQTLFAI 321
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYggrlvangeYTFEQFFIVFMA----LIFGAQSAGQ-----AFSFAPDIAKAKAAAARIFRL 310
|
....
gi 488987387 322 LDSE 325
Cdd:cd18578 311 LDRK 314
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-557 |
2.81e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRDQVAL 421
Cdd:COG3845 6 LELRGITKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 ----VSQNVHLFND-TVANNIAYARTEEYS--------REQIEEAARmAYAMDfINkmdngLDTIIGEngvmLSGGQRQR 488
Cdd:COG3845 81 gigmVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkaaRARIRELSE-RYGLD-VD-----PDAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 489 IAIARALLRNSPILILDEATSAL-DTESERAIqAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
342-561 |
3.48e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 107.14 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRdq 418
Cdd:cd03219 1 LEVRGLTKRFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNI---AYARTEE------YSREQIEEAARMAYAMDFInKMDNGLDTIIGEngvmLSGGQRQR 488
Cdd:cd03219 77 IGRTFQIPRLFPElTVLENVmvaAQARTGSglllarARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 489 IAIARALLRNSPILILDEATSAL-DTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGT 561
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
342-566 |
3.88e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK11231 3 LRTENLTVGYGTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQnVHLFND--TVANNIAYARTEEYS---REQIEEAARMAYAMDfinkmDNGLDTIIGENGVMLSGGQRQRIAIARALL 496
Cdd:PRK11231 81 LPQ-HHLTPEgiTVRELVAYGRSPWLSlwgRLSAEDNARVNQAME-----QTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLStieQA----DEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTPEEVM 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
355-575 |
4.29e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 114.06 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLItrfydVDEGQILLDGHDLreyklssLRDQVALVSQNVHLFNDTVA 434
Cdd:PLN03130 629 ERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-----LGELPPRSDASVV-------IRGTVAYVPQVSWIFNATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 435 NNIAYArtEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTE 514
Cdd:PLN03130 697 DNILFG--SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAH 774
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 515 SERAI--QAALDELQkNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:PLN03130 775 VGRQVfdKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
359-565 |
9.74e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 108.63 E-value: 9.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRDQVALVSQNVHLFND-TVANNI 437
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRKVGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 438 AYARTEEYSREQIEEAARMAYAMDFINKMDngLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESER 517
Cdd:PRK10851 96 AFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488987387 518 AIQAALDELQKNR--TSLVIAH-RLSTIEQADEIVVVEDGRIVERGTHHDL 565
Cdd:PRK10851 174 ELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
344-568 |
3.71e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGR---EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREY----KLSSLR 416
Cdd:PRK13649 5 LQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMDFINkmdnglDTIIGENGVMLSGGQRQRIAIAR 493
Cdd:PRK13649 85 KKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL--STIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
342-561 |
4.19e-25 |
|
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: 104.74 E-value: 4.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRdq 418
Cdd:COG0411 5 LEVRGLTKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHRIARLG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNI--------------AYARTEEYSREQIEEAARMAYAMDFInkmdnGLDTIIGENGVMLSG 483
Cdd:COG0411 81 IARTFQNPRLFPElTVLENVlvaaharlgrgllaALLRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
.
gi 488987387 561 T 561
Cdd:COG0411 236 T 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-571 |
4.88e-25 |
|
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: 103.91 E-value: 4.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPgrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSS---LRDQ 418
Cdd:COG0410 4 LEVENLHAGYG--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPhriARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNI---AYARTeeySREQIEEAARMAYAM-----DFINKMdngldtiigenGVMLSGGQRQRI 489
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYARR---DRAEVRADLERVYELfprlkERRRQR-----------AGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALdteserA------IQAALDELQKNRTSLVIahrlstIEQ--------ADEIVVVEDGR 555
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL------ApliveeIFEIIRRLNREGVTILL------VEQnarfaleiADRAYVLERGR 213
|
250
....*....|....*.
gi 488987387 556 IVERGTHHDLLEHKGV 571
Cdd:COG0410 214 IVLEGTAAELLADPEV 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
342-569 |
7.79e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 7.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR---EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL----REYKLSS 414
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTE-EYSREQIEEAARMAYAMdfinkmdNGLD-TIIGENGVMLSGGQRQRIA 490
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEEDAKQKAREMIEL-------VGLPeELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
..
gi 488987387 568 HK 569
Cdd:PRK13634 236 DP 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
342-559 |
8.38e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR--EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSSLRdqv 419
Cdd:COG4525 4 LTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFN-DTVANNIAYARteeysREQ-IEEAARMAYAMDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGL-----RLRgVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQA----DEIVVVED--GRIVER 559
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-575 |
9.58e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 103.22 E-value: 9.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRF--YDVDEGQILLDGHDLREykLSSlrDQV 419
Cdd:COG0396 1 LEIKNLHVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILE--LSP--DER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 A-----LVSQN--------VHLFNDTVANNIayaRTEEYSREQI-----EEAARMAYAMDFINKmdnGLDtiigengVML 481
Cdd:COG0396 75 AragifLAFQYpveipgvsVSNFLRTALNAR---RGEELSAREFlkllkEKMKELGLDEDFLDR---YVN-------EGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 482 SGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAH--RLSTIEQADEIVVVEDGRIVE 558
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVK 221
|
250
....*....|....*....
gi 488987387 559 RGTHH--DLLEHKGvYAQL 575
Cdd:COG0396 222 SGGKElaLELEEEG-YDWL 239
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
341-562 |
1.10e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH------DLREYKLSS 414
Cdd:COG4161 2 SIQLKNINCFYGSHQ--ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLF-NDTVANNIAYA--RTEEYSREQ-IEEAARMAYAMDFINKMDngldtiigENGVMLSGGQRQRIA 490
Cdd:COG4161 80 LRQKVGMVFQQYNLWpHLTVMENLIEApcKVLGLSKEQaREKAMKLLARLRLTDKAD--------RFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTH 562
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-573 |
1.35e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 104.55 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIAS-----LITRFYDVDEGQILLDGHDLREYKLSS-----------LRDQ 418
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQ--NVHLFNDTVANNIAYARTEeYSREQIEEAARMAYamdFINKMdnGLD-TIIGENGVMLSGGQRQRIAIARAL 495
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFGPVA-LGVKKSEAKKLAKF---YLNKM--GLDdSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 496 LRNSPILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGTHHDLLEHKGVYA 573
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-566 |
1.81e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDLREYKLSSLRDQVALVSQ----- 424
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 -NVHLFnDTVANNIAYARTEEySREQIEEAARMAY-AMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPIL 502
Cdd:PRK14247 95 pNLSIF-ENVALGLKLNRLVK-SKKELQERVRWALeKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStieqaDEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVF 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
342-555 |
1.87e-24 |
|
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: 101.74 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENV--TFTY---PGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDgHDLREYKLSSL- 415
Cdd:COG4778 5 LEVENLskTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 -RDQVAL-------VSQNVH--------------LFNDTVANNIAYARTEEY-SREQIEEAARMAYAMDFinkmdngldt 472
Cdd:COG4778 84 pREILALrrrtigyVSQFLRviprvsaldvvaepLLERGVDREEARARARELlARLNLPERLWDLPPATF---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 473 iigengvmlSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVV 550
Cdd:COG4778 154 ---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVD 224
|
....*
gi 488987387 551 VEDGR 555
Cdd:COG4778 225 VTPFS 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
357-565 |
1.88e-24 |
|
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: 102.96 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 357 AALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSS---LRDQVALVSQN-VHLFN-- 430
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 431 DTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 511 LDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVE-RGTHHDL 565
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEeCDVAQLL 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
374-568 |
2.04e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 104.11 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 374 LVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREykLSSLRDQVALVSQNVHLF-NDTVANNIAYA-RTEEYSREQIe 451
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 452 eAARMAYAMDFINKMDNGLDTIIgengvMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR- 530
Cdd:TIGR01187 78 -KPRVLEALRLVQLEEFADRKPH-----QLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488987387 531 -TSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:TIGR01187 152 iTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-565 |
2.76e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 106.53 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRDQ--- 418
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAAlaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 -VALVSQNVHLFND-TVANNIAYARTEEySREQIEEAARMAYAMDFINKMDNGLD--TIIGEngvmLSGGQRQRIAIARA 494
Cdd:PRK11288 80 gVAIIYQELHLVPEmTVAENLYLGQLPH-KGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 495 LLRNSPILILDEATSALdteSERAIQ---AALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVErgTHHDL 565
Cdd:PRK11288 155 LARNARVIAFDEPTSSL---SAREIEqlfRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
342-561 |
3.11e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.17 E-value: 3.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpGREVAaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDV-----DEGQILLDGHDLREYKL--SS 414
Cdd:PRK14243 11 LRTENLNVYY-GSFLA-VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVdpVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAY-ARTEEYS---REQIEEAARMAYAMDFINKMdngldtiIGENGVMLSGGQRQRIA 490
Cdd:PRK14243 89 VRRRIGMVFQKPNPFPKSIYDNIAYgARINGYKgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGT 561
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
342-560 |
3.97e-24 |
|
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: 99.93 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAA----LRNINLDIPEGKTVALVGRSGSGKSTIASLIT--RFYDVDEGQILLDGHDLreyKLSSL 415
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 RDQVALVSQNVHLF-NDTVanniayarteeysREqieeaarmayAMDFINKMDNgldtiigengvmLSGGQRQRIAIARA 494
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTV-------------RE----------TLMFAAKLRG------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIVVVEDGRIVERG 560
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
358-563 |
4.28e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 4.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH--DLR----EYKLSSLRDQVALVSQNVHLF-N 430
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRELRRNVGMVFQQYNLWpH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 431 DTVANNIAYA--RTEEYSREQIeeaarMAYAMDFINKMDngLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:PRK11124 97 LTVQQNLIEApcRVLGLSKDQA-----LARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 509 SALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHH 563
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
345-560 |
7.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYP-GREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVS 423
Cdd:PRK13647 8 EDLHFRYKdGTK--ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QNV--HLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFINKMDNgldtiigengvMLSGGQRQRIAIARALL 496
Cdd:PRK13647 86 QDPddQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEALKAvrmwDFRDKPPY-----------HLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-556 |
8.14e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 100.91 E-value: 8.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQiLLDGhdlrEYKLSSLRDQVAL 421
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFN-DTVANNIAYARTEEYsREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSP 500
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQW-RDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRI 556
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
346-556 |
8.49e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.35 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTY-PGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:PRK13650 9 NLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NV--HLFNDTVANNIAYARTE-----EYSREQIEEAARMAYAMDFINKmdngldtiigeNGVMLSGGQRQRIAIARALLR 497
Cdd:PRK13650 89 NPdnQFVGATVEDDVAFGLENkgiphEEMKERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 498 NSPILILDEATSALDTESE----RAIQAALDELQknRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRleliKTIKGIRDDYQ--MTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-561 |
8.79e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 8.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReYKLSSL---RDQ 418
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNV--HLFNDTVANNIAYAR-----TEEYSREQIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAI 491
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIE-QADEIVVVEDGRIVERGT 561
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-567 |
1.00e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.40 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDghdlreyklsslrDQVALVSQNVHLFNDTVANNIA 438
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 YARTEEYSReqIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTE-SER 517
Cdd:PTZ00243 743 FFDEEDAAR--LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488987387 518 AIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
342-549 |
1.33e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK10247 8 LQLQNVGYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIAYArteeYS-REQIEEAARMAYAMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSP 500
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFP----WQiRNQQPDPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488987387 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
362-566 |
1.40e-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: 102.50 E-value: 1.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 362 INLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK----LSSLRDQVALVSQNVHLFND-TVANN 436
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 437 IAYARTE---EYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:TIGR02142 96 LRYGMKRarpSERRISFERVIELL-----------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-566 |
1.67e-23 |
|
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: 102.10 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 361 NINLDIPEGKTVALVGRSGSGKST----IASLITrfydVDEGQILLDGHDL----REYKLSSLRDQVALVSQNVHLFND- 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTllraIAGLER----PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 432 TVANNIAYAR---TEEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:COG4148 93 SVRGNLLYGRkraPRAERRISFDEVVELL-----------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 509 SALDTESERAIqaaLDELQKNRTSLVI-----AHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:COG4148 162 AALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-567 |
2.62e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 99.48 E-value: 2.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:PRK10575 15 RNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLFND-TVANNIAYARTEEY---------SREQIEEAARMAYAMDFINKMdngLDTiigengvmLSGGQRQRIAIARA 494
Cdd:PRK10575 93 QLPAAEGmTVRELVAIGRYPWHgalgrfgaaDREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhRLSTIEQA----DEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-569 |
2.98e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTY-PGR--EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR----EYKLSS 414
Cdd:PRK13641 3 IKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQ--NVHLFNDTVANNIAYAR-----TEEYSREQieeaarmayAMDFINKMdnGLDT-IIGENGVMLSGGQR 486
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPknfgfSEDEAKEK---------ALKWLKKV--GLSEdLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGTHHD 564
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*
gi 488987387 565 LLEHK 569
Cdd:PRK13641 232 IFSDK 236
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
342-568 |
3.04e-23 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.53 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR-------EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLrEYKLSS 414
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQ-VALVSQNVhlfNDTVANNIAYAR------------TEEYSREQIEEAARMA-----YAMDFINkmdngldtiige 476
Cdd:COG4167 84 YRCKhIRMIFQDP---NTSLNPRLNIGQileeplrlntdlTAEEREERIFATLRLVgllpeHANFYPH------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 477 ngvMLSGGQRQRIAIARALLRNSPILILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:COG4167 149 ---MLSSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqIINLMLELQEKLgiSYIYVSQHLGIVKHiSDKVLVMH 224
|
250
....*....|....*.
gi 488987387 553 DGRIVERGTHHDLLEH 568
Cdd:COG4167 225 QGEVVEYGKTAEVFAN 240
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
359-558 |
4.09e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLS---SLRDQVALVsqnvhlFNDTVAN 435
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMV------FQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 436 NIAYARTEEYSRE------QIEEAARMAYAMDFINKMDngLD-TIIGENGVMLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:PRK10419 102 VNPRKTVREIIREplrhllSLDKAERLARASEMLRAVD--LDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488987387 509 SALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIVVVEDGRIVE 558
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-560 |
4.77e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.91 E-value: 4.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAalRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK10253 8 LRGEQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIA---YARTEEYSREQIEEAARMAYAMdfinkMDNGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:PRK10253 86 LAQNATTPGDiTVQELVArgrYPHQPLFTRWRKEDEEAVTKAM-----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
345-561 |
5.14e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.69 E-value: 5.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQ 424
Cdd:PRK13548 6 RNLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHL-FNDTVANNIA---YARTEEYSREQIEEAARMAYAmdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNS- 499
Cdd:PRK13548 84 HSSLsFPFTVEEVVAmgrAPHGLSRAEDDALVAAALAQV---------DLAHLAGRDYPQLSGGEQQRVQLARVLAQLWe 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 500 -----PILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLS-TIEQADEIVVVEDGRIVERGT 561
Cdd:PRK13548 155 pdgppRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
342-548 |
5.65e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDLREYKLSS-- 414
Cdd:PRK14239 6 LQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIYSPRTDTvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFINkmDNGLDTIIGengvmLSGGQRQR 488
Cdd:PRK14239 84 LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWDEVK--DRLHDSALG-----LSGGQQQR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQADEI 548
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
341-568 |
5.85e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 100.17 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRD--- 417
Cdd:PRK15079 19 DIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 ------QVALVSQNVHLfndTVANNIAYA-RT--EEYSREQIEEAARmayAMdfinKMDNGL-DTIIGENGVMLSGGQRQ 487
Cdd:PRK15079 99 diqmifQDPLASLNPRM---TIGEIIAEPlRTyhPKLSRQEVKDRVK---AM----MLKVGLlPNLINRYPHEFSGGQCQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 488 RIAIARALLRNSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK15079 169 RIGIARALILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREmGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELG 244
|
....*...
gi 488987387 561 THHDLLEH 568
Cdd:PRK15079 245 TYDEVYHN 252
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-560 |
8.21e-23 |
|
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: 97.05 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 348 TFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRdQVALVSQNVH 427
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 428 LFND-TVANNIAY-------ARTEEYSReqIEEAARMAYAMDFINKMDNGLDTiigengvmlsgGQRQRIAIARALLRNS 499
Cdd:cd03266 89 LYDRlTARENLEYfaglyglKGDELTAR--LEELADRLGMEELLDRRVGGFST-----------GMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
50-314 |
9.24e-23 |
|
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: 99.18 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 50 PLLDDGFGKTDRSVLLWM-PLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRI 128
Cdd:cd18565 38 PLVPASLGPADPRGQLWLlGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 129 TYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAE 208
Cdd:cd18565 118 NNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 209 QMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASF------PSVMDTLTAG 282
Cdd:cd18565 198 NNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYwvldgpPLFTGTLTVG 277
|
250 260 270
....*....|....*....|....*....|...
gi 488987387 283 TItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18565 278 TL-VTFLFYTQrLLWPLTRLGDLIDQYQRAMAS 309
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-549 |
1.41e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.38 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 351 YPGRevAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDlreyklsslrdQVALVSQNVHL-- 428
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 429 -FNDTVANNIA---YARTEEYSREQIEEAARMAYAMDFInkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILIL 504
Cdd:NF040873 69 sLPLTVRDLVAmgrWARRGLWRRLTRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488987387 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
345-568 |
1.68e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 96.74 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQI-----LLDG-HDLREYK--LSSLR 416
Cdd:PRK11264 7 KNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKglIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNVHLF-NDTVANNIAYART--EEYSREQIEEAARMAYAMDFINKMDNGLDTiigengvMLSGGQRQRIAIAR 493
Cdd:PRK11264 85 QHVGFVFQNFNLFpHRTVLENIIEGPVivKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
67-316 |
1.80e-22 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 97.87 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 67 MPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITV 146
Cdd:cd18554 48 IGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 147 VREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVE 226
Cdd:cd18554 128 WLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 227 TKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNA 306
Cdd:cd18554 208 QKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFT 287
|
250
....*....|
gi 488987387 307 QFQRGMAACQ 316
Cdd:cd18554 288 TLTQSFASMD 297
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-515 |
2.07e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhDLReyklsslrdqVALVS 423
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QNVHLFND-TVANNIAYARTEEYS-REQIEEA-ARMAYAMDFINKMDNGLDTIIGENG---------VM----------- 480
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAELRAlEAELEELeAKLAEPDEDLERLAELQEEFEALGGweaearaeeILsglgfpeedld 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488987387 481 -----LSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:COG0488 148 rpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-568 |
2.20e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 2.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLdGHDLReyklsslrdqVAL 421
Cdd:COG0488 316 LELEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF--NDTVANNIAyarteEYSREQIEEAARmAY--AMDFINKMdngLDTIIGEngvmLSGGQRQRIAIARALLR 497
Cdd:COG0488 383 FDQHQEELdpDKTVLDELR-----DGAPGGTEQEVR-GYlgRFLFSGDD---AFKPVGV----LSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEIVVVEDGRIVER-GTHHDLLEH 568
Cdd:COG0488 450 PPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-560 |
2.52e-22 |
|
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: 94.90 E-value: 2.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRF--YDVDEGQILLDGHDLREyklsslrdqv 419
Cdd:cd03217 1 LEIKDLHVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITD---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 alvsqnvhlfndtvanniayARTEEYSRE------QIEEAARMAYAMDFINKMDNGldtiigengvmLSGGQRQRIAIAR 493
Cdd:cd03217 69 --------------------LPPEERARLgiflafQYPPEIPGVKNADFLRYVNEG-----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-574 |
4.11e-22 |
|
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: 96.46 E-value: 4.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVdEGQILLDGHDLREYKLSSLRDQV 419
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD--PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKGVYAQ 574
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-579 |
4.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTY----PGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK-LSSLR 416
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNVHlfNDTVA----NNIAYArTEEYSREQIEEAARMAYAMDFINKMDngldtIIGENGVMLSGGQRQRIAIA 492
Cdd:PRK13633 85 NKAGMVFQNPD--NQIVAtiveEDVAFG-PENLGIPPEEIRERVDESLKKVGMYE-----YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRIVERGThhdlleHKG 570
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT------PKE 230
|
....*....
gi 488987387 571 VYAQLHKMQ 579
Cdd:PRK13633 231 IFKEVEMMK 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
342-566 |
5.87e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.93 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR-EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVA 420
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNV--HLFNDTVANNIAYArTEEYSREQIEEAARMAYAMDFINKMDngldtIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-571 |
7.61e-22 |
|
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: 94.53 E-value: 7.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSS-LRDQVA 420
Cdd:cd03218 1 LRAENLSKRYGKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLFND-TVANNI-AYARTEEYSREQIEEaaRMAYAMDfinkmDNGLDTIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:cd03218 79 YLPQEASIFRKlTVEENIlAVLEIRGLSKKEREE--KLEELLE-----EFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIVVVEDGRIVERGTHHDLLEHKGV 571
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
263-574 |
1.00e-21 |
|
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: 100.37 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 263 LAFVLY--AASFPSVMDT-LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGTR------ 333
Cdd:TIGR01271 1117 IIFVFFfiAVTFIAIGTNqDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGgggkyq 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 334 -----VIER--------AKGNLKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVdEGQI 400
Cdd:TIGR01271 1197 lstvlVIENphaqkcwpSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEI 1275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 401 LLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNI-AYARteeYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGV 479
Cdd:TIGR01271 1276 QIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQ---WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGY 1352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 480 MLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVER 559
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQY 1432
|
330
....*....|....*
gi 488987387 560 GTHHDLLEHKGVYAQ 574
Cdd:TIGR01271 1433 DSIQKLLNETSLFKQ 1447
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-560 |
1.44e-21 |
|
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: 93.11 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklsSLRDQVAL 421
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIAY-ARTEEYSREQIEEAARmayamDFINKMD--NGLDTIIGEngvmLSGGQRQRIAIARALLR 497
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlAQLKGLKKEEARRRID-----EWLERLElsEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
342-568 |
1.93e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGRevAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREykLSSLRDQVAL 421
Cdd:PRK11607 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLF-NDTVANNIAY-------ARTEEYSReqIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAIAR 493
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFglkqdklPKAEIASR--VNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 494 ALLRNSPILILDEATSALDTE-SERAIQAALDELQK-NRTSLVIAH-RLSTIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-568 |
2.05e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRD----QVALVSQNVHLF-NDT 432
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 433 VANNIAYArteeYSREQIEEAARMAYAMDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALD 512
Cdd:PRK10070 123 VLDNTAFG----MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 513 TESERAIQAALDELQ--KNRTSLVIAHRL-STIEQADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-557 |
3.32e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.87 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGRE--VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSL---- 415
Cdd:PRK10535 5 LELKDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 RDQVALVSQNVHLFND-TVANNI----AYArteeysreQIEEAARMAYAMDFINKMdnGLDTIIGENGVMLSGGQRQRIA 490
Cdd:PRK10535 85 REHFGFIFQRYHLLSHlTAAQNVevpaVYA--------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIV 557
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
342-514 |
3.60e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD---EGQILLDGHDLREykLSSLRDQ 418
Cdd:COG4136 2 LSLENLTITLGGRPL--LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLF-NDTVANNIAYARTEEYSREQIEEAARMAYAmdfinkmDNGLDTIIGENGVMLSGGQRQRIAIARALLR 497
Cdd:COG4136 78 IGILFQDDLLFpHLSVGENLAFALPPTIGRAQRRARVEQALE-------EAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170
....*....|....*..
gi 488987387 498 NSPILILDEATSALDTE 514
Cdd:COG4136 151 EPRALLLDEPFSKLDAA 167
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
51-314 |
3.79e-21 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 94.05 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 51 LLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITy 130
Cdd:cd18570 28 LIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 131 DSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQM 210
Cdd:cd18570 107 DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 211 LKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVM-DTLTAGTItVVFS 289
Cdd:cd18570 187 LKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSY-LVIkGQLSLGQL-IAFN 264
|
250 260
....*....|....*....|....*.
gi 488987387 290 SMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18570 265 ALLGyFLGPIENLINLQPKIQEAKVA 290
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-566 |
3.89e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 95.68 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHL-FNDTV 433
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 ANNIAYARTEEYSR-EQIEEAARMAY--AMDfinkmDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:PRK09536 95 RQVVEMGRTPHRSRfDTWTETDRAAVerAME-----RTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 511 LDTESE-RAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
340-561 |
4.58e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 340 GNLKFENVTFTYPGR---EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH----DLREYK- 411
Cdd:PRK13645 5 KDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKKIKe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 412 LSSLRDQVALVSQ--NVHLFNDTVANNIAY------ARTEEYSREQIEEAARMAYAMDFINKmdngldtiigeNGVMLSG 483
Cdd:PRK13645 85 VKRLRKEIGLVFQfpEYQLFQETIEKDIAFgpvnlgENKQEAYKKVPELLKLVQLPEDYVKR-----------SPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVLRiADEVIVMHEGKVISIG 233
|
.
gi 488987387 561 T 561
Cdd:PRK13645 234 S 234
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
357-566 |
4.92e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 357 AALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH------DLREYKLSSLRDQVALVSQNVHLF- 429
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 NDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIiGENGVMLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 510 ALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
342-569 |
5.96e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 91.82 E-value: 5.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSS---LRDQ 418
Cdd:TIGR03410 1 LEVSNLNVYYGQSHI--LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT--KLPPherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLFND-TVANNI--AYARTEEYSREQIEEAarmaYAMDFInkmdngLDTIIGENGVMLSGGQRQRIAIARAL 495
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLltGLAALPRRSRKIPDEI----YELFPV------LKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLLEHK 569
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-555 |
1.03e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.38 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD--EGQILLDGHDLreyKLSSLRDQ- 418
Cdd:PRK13549 6 LEMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL---QASNIRDTe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 ---VALVSQNVHLFND-TVANNIayarteeYSREQIEEAARMAYAMDFIN--------KMDNGLDTIIGEngvmLSGGQR 486
Cdd:PRK13549 81 ragIAIIHQELALVKElSVLENI-------FLGNEITPGGIMDYDAMYLRaqkllaqlKLDINPATPVGN----LGLGQQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 487 QRIAIARALLRNSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:PRK13549 150 QLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-563 |
1.55e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 90.32 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTY-PGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRD 417
Cdd:PRK10908 2 IRFEHVSKAYlGGRQ--ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVHLFND-TVANN------IAYARTEEYSReqieeaaRMAYAMDFINKMDNGLDTIIgengvMLSGGQRQRIA 490
Cdd:PRK10908 80 QIGMIFQDHHLLMDrTVYDNvaipliIAGASGDDIRR-------RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTIEQAD-EIVVVEDGRIVerGTHH 563
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH--GGVG 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-561 |
2.07e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPGReVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKlSSLRDqVA 420
Cdd:PRK11650 3 GLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-PADRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLF-NDTVANNIAY----ARTEEYSREQ-IEEAARMAYAMDFinkmdngLDTIIGEngvmLSGGQRQRIAIARA 494
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMAYglkiRGMPKAEIEErVAEAARILELEPL-------LDRKPRE----LSGGQRQRVAMGRA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIVVVEDGRIVERGT 561
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
345-565 |
3.60e-20 |
|
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: 89.35 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD-LREYKlsSLRDQVALVS 423
Cdd:cd03265 4 ENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVREPR--EVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QNVHLFNDTVA--NNIAYARTEEYSREQIEEaaRMAYAMDFINKMDNGlDTIIGEngvmLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03265 80 QDLSVDDELTGweNLYIHARLYGVPGAERRE--RIDELLDFVGLLEAA-DRLVKT----YSGGMRRRLEIARSLVHRPEV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 502 LILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDL 565
Cdd:cd03265 153 LFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
359-565 |
3.61e-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: 91.07 E-value: 3.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlreyklsslrdQVALVSQNVHLFNDTVANNIA 438
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 YART-EEYSREQIEEAARMAYAMDFINKMDNgldTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESER 517
Cdd:cd03291 120 FGVSyDEYRYKSVVKACQLEEDITKFPEKDN---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488987387 518 AI-QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDL 565
Cdd:cd03291 197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-561 |
6.99e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.17 E-value: 6.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLRE------------ 409
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 410 ---YKLSSLRDQvalvsqnvhlfndtvannIAY-ARTEEYSREQIEEAAR--------MAYAMDFINKmdngldtiigen 477
Cdd:COG4152 80 rglYPKMKVGEQ------------------LVYlARLKGLSKAEAKRRADewlerlglGDRANKKVEE------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 478 gvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSlVI--AHRLSTIEQ-ADEIVVVEDG 554
Cdd:COG4152 130 ---LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKG 205
|
....*..
gi 488987387 555 RIVERGT 561
Cdd:COG4152 206 RKVLSGS 212
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-576 |
8.27e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.86 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNV--HLFNDTVANNIAYART-----EEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARA 494
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPInlgldEETVAHRVSSALHML-----------GLEELRDRVPHHLSGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTI-EQADEIVVVEDGRIVERGTHHDLLEHKGV 571
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
....*
gi 488987387 572 YAQLH 576
Cdd:PRK13652 232 LARVH 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-567 |
8.69e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 8.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 354 REVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH---DLREYKLSSLRDQVALVSQNVHLFN 430
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 431 D---TVANNIAYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILILDEA 507
Cdd:PRK10261 415 DprqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 508 TSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
314-560 |
9.64e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 314 ACQTLFA---------ILDSEQEkDEGTRVIERAKGNLKFENVTFTYPGR---------EVAALRNINLDIPEGKTVALV 375
Cdd:PRK15134 240 RAATLFSapthpytqkLLNSEPS-GDPVPLPEPASPLLDVEQLQVAFPIRkgilkrtvdHNVVVKNISFTLRPGETLGLV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 376 GRSGSGKSTIASLITRFYDvDEGQILLDG---HDLREYKLSSLRDQVALVSQ------NVHLfndTVANNIA-------- 438
Cdd:PRK15134 319 GESGSGKSTTGLALLRLIN-SQGEIWFDGqplHNLNRRQLLPVRHRIQVVFQdpnsslNPRL---NVLQIIEeglrvhqp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 ---YARTEEYSREQIEE-----AARMAYAMDFinkmdngldtiigengvmlSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:PRK15134 395 tlsAAQREQQVIAVMEEvgldpETRHRYPAEF-------------------SGGQRQRIAIARALILKPSLIILDEPTSS 455
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488987387 511 LDTESERAIQAALDELQ-KNRTS-LVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK15134 456 LDKTVQAQILALLKSLQqKHQLAyLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-560 |
9.76e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 9.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPgrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSslRDQVA 420
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLF-NDTVANNIAY-------ARTEEYSR-EQIEEAARMAYAMDFINKmdngldtiigengvMLSGGQRQRIAI 491
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFglklagaKKEEINQRvNQVAEVLQLAHLLDRKPK--------------ALSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-555 |
1.10e-19 |
|
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: 85.58 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLdGHDLReyklsslrdqVAL 421
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQnvhlfndtvanniayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03221 68 FEQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 502 LILDEATSALDTESERAIQAALDELQknRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-568 |
1.67e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--------------------GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIL 401
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 402 LDGhdlreyKLSSLrdqVAL---------VSQNVHLfndtvanniaYARTEEYSREQIEEaaRMAYAMDF--INKMdngL 470
Cdd:COG1134 85 VNG------RVSAL---LELgagfhpeltGRENIYL----------NGRLLGLSRKEIDE--KFDEIVEFaeLGDF---I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 471 DTIIGengvMLSGGQRQRIAIARALLRNSPILILDEATSALDTE-SERAiQAALDELQKNRTSLVIA-HRLSTIEQ-ADE 547
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKC-LARIRELRESGRTVIFVsHSMGAVRRlCDR 215
|
250 260
....*....|....*....|.
gi 488987387 548 IVVVEDGRIVERGTHHDLLEH 568
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
27-289 |
1.89e-19 |
|
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: 89.06 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNagsdtfMLSLLKPL-----LDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMR 101
Cdd:cd18567 5 LQILLLSLALE------LFALASPLylqlvIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 102 RRLFGHMMGMPVAFFDKQSTGTLLSRItyDS-EQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLIlIVLAPIVSV 180
Cdd:cd18567 79 SNLFRHLLRLPLSYFEKRHLGDIVSRF--GSlDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALI-VLAAVALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 181 AIRVVS-KRFRNIsknmqnTMGQVTTSAEQ------MLKGHKEVLMFGGQEVETKRF-----DKVSNKMRLQGMKMVSAS 248
Cdd:cd18567 156 LLRLALyPPLRRA------TEEQIVASAKEqshfleTIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQILFSA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 488987387 249 sisdpIIQLIASLALAFVLYAASFpSVMD-TLTAGTITVVFS 289
Cdd:cd18567 230 -----ANGLLFGLENILVIYLGAL-LVLDgEFTVGMLFAFLA 265
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-561 |
2.40e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 87.74 E-value: 2.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSslRDQVALVSQNVHLFND-TV 433
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQIA--RMGVVRTFQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 ANNIAYA--------------RTEEYSREQIEEAARMAYAMDFInkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGT 561
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGT 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-567 |
3.22e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 88.25 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTY-PGREVA--ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQI----LLDGHDLREYKLSS 414
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFAsrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMDFINKmdngldTIIGENGVMLSGGQRQRIAI 491
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpQNFGIPKEKAEKIAAEKLEMVGLAD------EFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
359-565 |
3.39e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 92.28 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlreyklsslrdQVALVSQNVHLFNDTVANNIA 438
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 YART-EEYSREQIEEAARMAYAMDFINKMDNgldTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESER 517
Cdd:TIGR01271 509 FGLSyDEYRYTSVIKACQLEEDIALFPEKDK---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488987387 518 AI-QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGTHHDL 565
Cdd:TIGR01271 586 EIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
342-565 |
7.73e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 86.29 E-value: 7.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaalRNINLDIPEGKTVALVGRSGSGKS-TIASLI------TRfydVDEGQILLDGhdlREYKLSS 414
Cdd:PRK10418 5 IELRNIALQAAQPLV---HGVSLTLQRGRVLALVGGSGSGKSlTCAAALgilpagVR---QTAGRVLLDG---KPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQ-VALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFInkmdnGLD---TIIGENGVMLSGGQRQRIA 490
Cdd:PRK10418 76 LRGRkIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALEAV-----GLEnaaRVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDL 565
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-561 |
9.05e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 9.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDL--REYKLSS 414
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFI-NKmdngldtiIGENGVMLSGGQRQ 487
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLWDEIkHK--------IHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALD--ELQKNRTSLVIAHRLSTIEQADEIVVV------EDGRIVER 559
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEF 237
|
..
gi 488987387 560 GT 561
Cdd:PRK14258 238 GL 239
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
346-568 |
1.31e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.09 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLI-------------TRFydvdEGQILLDghdLREYKL 412
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALmgllaangriggsATF----NGREILN---LPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 413 SSLR-DQVALVsqnvhlFNDTVANNIAYARTEE-----------YSR-EQIEEAARMAYAMdfinKMDNGLDTIigengV 479
Cdd:PRK09473 92 NKLRaEQISMI------FQDPMTSLNPYMRVGEqlmevlmlhkgMSKaEAFEESVRMLDAV----KMPEARKRM-----K 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 480 M----LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:PRK09473 157 MypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMY 236
|
250
....*....|....*.
gi 488987387 553 DGRIVERGTHHDLLEH 568
Cdd:PRK09473 237 AGRTMEYGNARDVFYQ 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-558 |
1.71e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.69 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD--EGQILLDGhDLREYKlsSLRD-- 417
Cdd:NF040905 2 LEMRGITKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG-EVCRFK--DIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 ---------QVALVSQnvhLfndTVANNIaYARTEEYSREQIEEAARMAYAMDFINKMdnGL----DTIIGENGVmlsgG 484
Cdd:NF040905 77 algiviihqELALIPY---L---SIAENI-FLGNERAKRGVIDWNETNRRARELLAKV--GLdespDTLVTDIGV----G 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVE 558
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-566 |
1.85e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.61 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 347 VTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDL---REYKLSSLR-D 417
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLlhaSEQTLRGVRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVAL------VSQN-VHLFNDTVANNIAY--------ARTEEYS---REQIEEAA-RMAyamDFINKmdngldtiigeng 478
Cdd:PRK15134 93 KIAMifqepmVSLNpLHTLEKQLYEVLSLhrgmrreaARGEILNcldRVGIRQAAkRLT---DYPHQ------------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 479 vmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:PRK15134 157 --LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGR 234
|
250
....*....|.
gi 488987387 556 IVERGTHHDLL 566
Cdd:PRK15134 235 CVEQNRAATLF 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-560 |
2.11e-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: 84.12 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP--------------------GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIL 401
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 402 LDGhdlreyKLSSLRD-QVAL-----VSQNVHLfndtvaNNIAYARTEEYSREQIEEAARMAYAMDFInkmdnglDTIIG 475
Cdd:cd03220 81 VRG------RVSSLLGlGGGFnpeltGRENIYL------NGRLLGLSRKEIDEKIDEIIEFSELGDFI-------DLPVK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 476 EngvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVED 553
Cdd:cd03220 142 T----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEK 217
|
....*..
gi 488987387 554 GRIVERG 560
Cdd:cd03220 218 GKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-561 |
3.91e-18 |
|
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: 87.55 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLI--TRFYDVDEGQIL------------------ 401
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 402 ---------------LDGHDLREYKLSSLRDQVALVSQNVHLF--NDTVANNIAYARTE-EYSREqieEAARMAYAMDFI 463
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEiGYEGK---EAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 464 NKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST 541
Cdd:TIGR03269 156 VQLSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|.
gi 488987387 542 IEQ-ADEIVVVEDGRIVERGT 561
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGT 252
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-292 |
5.24e-18 |
|
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: 85.02 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 71 VIGLMVLrgITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREG 150
Cdd:cd18558 67 IIGAIVL--ITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 151 ASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRF 230
Cdd:cd18558 145 ATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRY 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 231 DKVSNKMRLQGMKMVSASSISDPIIQLI--ASLALAFvLYAASFPSVMDTLTAGTITVVFSSMI 292
Cdd:cd18558 225 AQNLEIAKRNGIKKAITFNISMGAAFLLiyASYALAF-WYGTYLVTQQEYSIGEVLTVFFSVLI 287
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-556 |
6.53e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 6.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReyKLSS-----LRDQ-VALVSQNVHLFND- 431
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMS--KLSSaakaeLRNQkLGFIYQFHHLLPDf 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 432 TVANNIAYAR-TEEYSREQIEEAAR-MAYAMdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLrNSPILIL-DEAT 508
Cdd:PRK11629 103 TALENVAMPLlIGKKKPAEINSRALeMLAAV--------GLEHRANHRPSELSGGERQRVAIARALV-NNPRLVLaDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488987387 509 SALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-557 |
1.05e-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: 82.32 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVT--FTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDE---GQILLDGHDLREYKLssl 415
Cdd:cd03234 3 VLPWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 RDQVALVSQ-NVHLFNDTVANNIAYA---RTEEYSREQIEEAarmayaMDFINKMDNGLDTIIGENGVM-LSGGQRQRIA 490
Cdd:cd03234 80 QKCVAYVRQdDILLPGLTVRETLTYTailRLPRKSSDAIRKK------RVEDVLLRDLALTRIGGNLVKgISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIVVVEDGRIV 557
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
359-566 |
1.91e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR-------------EYKLSSLRDQVALVSQN 425
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 426 VHLFND-TVANNIAYARTEEYSREQIEEAARmayAMDFINKMdnGLD-TIIGENGVMLSGGQRQRIAIARALLRNSPILI 503
Cdd:PRK10619 101 FNLWSHmTVLENVMEAPIQVLGLSKQEARER---AVKYLAKV--GIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 504 LDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
357-556 |
2.08e-17 |
|
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: 80.17 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 357 AALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRDQVALvsqnvhlfndtvanN 436
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRA--------------G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 437 IAYArTEEYSREQIeeaarmayamdfinkmdnGLDTIIGEN---GVMLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:cd03215 77 IAYV-PEDRKREGL------------------VLDLSVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488987387 514 ESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:cd03215 138 GAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
322-570 |
2.77e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 83.34 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 322 LDSEQEKDEGTRVIERAKGNL-----KFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD 396
Cdd:PRK13536 17 SPIERKHQGISEAKASIPGSMstvaiDLAGVSKSYGDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 397 EGQILLDGHDLREyKLSSLRDQVALVSQNVHLFND-TVANN-IAYARTEEYSREQIEEAarMAYAMDFInKMDNGLDTII 474
Cdd:PRK13536 95 AGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEAV--IPSLLEFA-RLESKADARV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 475 GEngvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:PRK13536 171 SD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLE 246
|
250
....*....|....*....
gi 488987387 553 DGRIVERGTHHDLL-EHKG 570
Cdd:PRK13536 247 AGRKIAEGRPHALIdEHIG 265
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-538 |
3.79e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.12 E-value: 3.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQI-LLDGHDL-----REY-KLSS 414
Cdd:cd03223 1 IELENLSLATPDGRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLlflpqRPYlPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVhlfndtvanniayarteeysreqieeaarmayamdfinkmdngldtiigengvmLSGGQRQRIAIARA 494
Cdd:cd03223 80 LREQLIYPWDDV------------------------------------------------------LSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELqknRTSLV-IAHR 538
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHR 147
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
342-559 |
3.95e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.28 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGRevAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHdlreyKLSSLRDQVAL 421
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFN-DTVANNIAYA-RTEEYSREQIEEAARMAYAMdfinkmdNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAFGlQLAGVEKMQRLEIAHQMLKK-------VGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 500 PILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQ----ADEIVVVE--DGRIVER 559
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH---DIEEavfmATELVLLSpgPGRVVER 212
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-571 |
4.30e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 81.82 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP-GREvaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH--DLREYKLSSLRDQ 418
Cdd:PRK13636 6 LKVEELNYNYSdGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNV--HLFNDTVANNIAY-ARTEEYSREQIEEAARMAYAMDFINKMDNgldtiigENGVMLSGGQRQRIAIARAL 495
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFgAVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIE-QADEIVVVEDGRIVERGTHHDLLEHKGV 571
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
345-568 |
4.38e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD-----EGQILLDGHDLREYKLSSL--RD 417
Cdd:PRK14267 8 VNLRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVHLF-NDTVANNIA-------YARTEEYSREQIEEAARMAYAMDfinKMDNGLDTIIGEngvmLSGGQRQRI 489
Cdd:PRK14267 86 EVGMVFQYPNPFpHLTIYDNVAigvklngLVKSKKELDERVEWALKKAALWD---EVKDRLNDYPSN----LSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEH 568
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
326-560 |
5.17e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.45 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 326 QEKDEGtrVIERAKGNLKFENvtftypgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGH 405
Cdd:cd03267 13 YSKEPG--LIGSLKSLFKRKY-------REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 406 DLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINkMDNGLDTIIGEngvmLSGGQ 485
Cdd:cd03267 84 VPWKRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVRQ----LSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-565 |
7.81e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHdlREYKLSSLRDQ--- 418
Cdd:PRK15439 12 LCARSISKQYSGVEV--LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 VALVSQNVHLF-NDTVANNIAY--ARTEEYSREQIEEAARMAYAMDfinkmdngLDTIIGengvMLSGGQRQRIAIARAL 495
Cdd:PRK15439 88 IYLVPQEPLLFpNLSVKENILFglPKRQASMQKMKQLLAALGCQLD--------LDSSAG----SLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDL 565
Cdd:PRK15439 156 MRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
358-561 |
8.82e-17 |
|
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: 84.68 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLrEYKLSSLRDQVALVSQNVHLFND-TVANN 436
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 437 IA-YARTEEYSRE--QIEEAARMAyamdfinkmDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:TIGR01257 1024 ILfYAQLKGRSWEeaQLEMEAMLE---------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488987387 514 ESERAIQAALDELQKNRTSLVIAHRLSTIE-QADEIVVVEDGRIVERGT 561
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
359-557 |
8.91e-17 |
|
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: 79.82 E-value: 8.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLrdqvaLVSQNVHLFN-DTVANNI 437
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 438 AYA-------RTEEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:TIGR01184 76 ALAvdrvlpdLSKSERRAIVEEHIALV-----------GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488987387 511 LDTESERAIQAALDEL-QKNR-TSLVIAHRLstieqaDEIVVVEDgRIV 557
Cdd:TIGR01184 145 LDALTRGNLQEELMQIwEEHRvTVLMVTHDV------DEALLLSD-RVV 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-559 |
9.08e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.13 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRD-QVA 420
Cdd:PRK10762 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSsQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVS---QNVHLF-NDTVANNIAYAR--TEEYSR----EQIEEAARMAYAMdfinKMDNGLDTIIGEngvmLSGGQRQRIA 490
Cdd:PRK10762 80 GIGiihQELNLIpQLTIAENIFLGRefVNRFGRidwkKMYAEADKLLARL----NLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 491 IARALLRNSPILILDEATSAL-DTESErAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIVVVEDGR-IVER 559
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGQfIAER 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
342-558 |
1.06e-16 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.10 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVAL 421
Cdd:PRK10522 323 LELRNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNDTVANNIAYARTEEYsrEQIEEAARMAYAMDFinkMDNGLDTIigengvMLSGGQRQRIAIARALLRNSPI 501
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANPALV--EKWLERLKMAHKLEL---EDGRISNL------KLSKGQKKRLALLLALAEERDI 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 502 LILDEATSALDTESERAI-QAALDELQ-KNRTSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
353-560 |
1.81e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 83.23 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 353 GREVAALRNINLDIPEGKTVALVGRSGSGKST----IASLITRFYDVDEGQILLDGHDLREYKlSSLRDQVALVSQN-VH 427
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIK-KHYRGDVVYNAETdVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 428 LFNDTVANNIAYA--------RTEEYSREqiEEAARMA-YAMDfINKMDNGLDTIIGENGVM-LSGGQRQRIAIARALLR 497
Cdd:TIGR00956 150 FPHLTVGETLDFAarcktpqnRPDGVSRE--EYAKHIAdVYMA-TYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 498 NSPILILDEATSALDT----ESERAIQAALDELqkNRTSLVIAHRLS--TIEQADEIVVVEDGRIVERG 560
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSatalEFIRALKTSANIL--DTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-569 |
2.25e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 2.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyKLSSLRDQVAL 421
Cdd:PRK13537 8 IDFRNVEKRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNI-AYARTEEYSREQIEeaARMAYAMDFInKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:PRK13537 85 VPQFDNLDPDfTVRENLlVFGRYFGLSAAAAR--ALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEHK 569
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-571 |
2.72e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.38 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPgrEVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSS-LRDQVA 420
Cdd:PRK11614 6 LSFDKVSAHYG--KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLFND-TVANNIA----YARTEEYSReqieeaaRMAYAMDFINKMdngLDTIIGENGVMlSGGQRQRIAIARAL 495
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAmggfFAERDQFQE-------RIKWVYELFPRL---HERRIQRAGTM-SGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 496 LRNSPILILDEATSALdteSERAIQAALDELQKNRTS-----LVIAHRLSTIEQADEIVVVEDGRIVERGTHHDLLEHKG 570
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 488987387 571 V 571
Cdd:PRK11614 230 V 230
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-557 |
3.33e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.41 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD--EGQILLDGHDLreyKLSSLRDQ- 418
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPL---KASNIRDTe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 ---VALVSQNVHLFND-TVANNIAYARteeysrEQIEEAARMAYAMdFINKMDN-----GLDTIIGENGVM-LSGGQRQR 488
Cdd:TIGR02633 77 ragIVIIHQELTLVPElSVAENIFLGN------EITLPGGRMAYNA-MYLRAKNllrelQLDADNVTRPVGdYGGGQQQL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 489 IAIARALLRNSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
358-563 |
3.36e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 78.90 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVD---EGQILLDGHDL-REYKLS----SLRDQVALVSQNVHLF 429
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGRTVqREGRLArdirKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 ND-TVANNI--------AYART--EEYSREQIEEAARMAYAMDFINKMDNGLDTiigengvmLSGGQRQRIAIARALLRN 498
Cdd:PRK09984 99 NRlSVLENVligalgstPFWRTcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHH 563
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQ 238
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
66-309 |
3.80e-16 |
|
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: 79.06 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 66 WMPLVVIGL---MVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYdSEQVASSSSSA 142
Cdd:cd18569 40 WLRPLLLGMaltALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQS-NDRVANLLSGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 143 LITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQ---VTTSAEQMLkghkEVLM 219
Cdd:cd18569 119 LATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKltgTTMSGLQMI----ETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 220 FGGQEVETkrFDKVSN---KMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMD-TLTAGTItVVFSS-MIAL 294
Cdd:cd18569 195 ASGAESDF--FSRWAGyqaKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGL-LVMDgALTIGML-VAFQSlMASF 270
|
250
....*....|....*
gi 488987387 295 MRPLKSLTNVNAQFQ 309
Cdd:cd18569 271 LAPVNSLVGLGGTLQ 285
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-567 |
3.91e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 79.36 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGR---EVAALRNINLDIPEGKTVALVGRSGSGKSTI-----ASLI------------------TRFYDV 395
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFiehlnALLLpdtgtiewifkdeknkkkTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 396 DEGQILLDGHDLREYK-LSSLRDQVALVSQ--NVHLFNDTVANNIAY-ARTEEYSREQIEEAARmayamDFINKMdnGLD 471
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFgPVSMGVSKEEAKKRAA-----KYIELV--GLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 472 -TIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL-STIEQADEI 548
Cdd:PRK13651 156 eSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*....
gi 488987387 549 VVVEDGRIVERGTHHDLLE 567
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILS 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-561 |
4.57e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL--REYKLSSLRDQVALVS 423
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QNVH------LFND---------TVANNIAYA-RTEE-YSREQ-IEEAARMayaMDFINKMDNglDTIIGENGVMLSGGQ 485
Cdd:PRK10261 99 RHVRgadmamIFQEpmtslnpvfTVGEQIAESiRLHQgASREEaMVEAKRM---LDQVRIPEA--QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV--IAHRLSTI-EQADEIVVVEDGRIVERGT 561
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVaEIADRVLVMYQGEAVETGS 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-566 |
4.83e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 4.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDV-----DEGQILLDGHDLREYK-LSSLRDQV 419
Cdd:PRK14271 26 NLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRdVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIaYARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIIGENGVMLSGGQRQRIAIARALLRNS 499
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNV-LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
358-573 |
4.86e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhdlREYKLSSLRDQ----VALVSQNVH---LF- 429
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDAiragIAYVPEDRKgegLVl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 NDTVANNIAYARTEEYSREQ-IEEAARMAYAMDFINKMD---NGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILILD 505
Cdd:COG1129 344 DLSIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 506 EATSALDTESERAIQAALDELQKNRTSLVIAhrlST-----IEQADEIVVVEDGRIVERGTHHDLLEHKGVYA 573
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIVGELDREEATEEAIMAA 489
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
30-314 |
6.75e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 78.48 E-value: 6.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18561 1 SVLLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 110 GMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF 189
Cdd:cd18561 81 KLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18561 161 KDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 488987387 270 ASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18561 241 GALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
356-582 |
1.14e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 77.14 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 356 VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLrEYKLSSLRdqvalvSQNVHL-FNDtva 434
Cdd:PRK15112 26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYR------SQRIRMiFQD--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 435 nniayARTEEYSREQIEEAarmayaMDFINKMDNGLDTIIGENGV-------------------MLSGGQRQRIAIARAL 495
Cdd:PRK15112 96 -----PSTSLNPRQRISQI------LDFPLRLNTDLEPEQREKQIietlrqvgllpdhasyyphMLAPGQKQRLGLARAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEhkgvy 572
Cdd:PRK15112 165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA----- 239
|
250
....*....|....*..
gi 488987387 573 AQLHKM-------QFGE 582
Cdd:PRK15112 240 SPLHELtkrliagHFGE 256
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
30-232 |
1.34e-15 |
|
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: 77.35 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 30 AAVALVLNAGSDTFMLSLLKPLLDD-----GFGKTDRSVLLwMPLVVIGLMVLRGITSYISSYCISwvsgKVVMTMRRRL 104
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGiviekSQDKFSRAIII-MGLLAIASSVAAGIRGGLFTLAMA----RLNIRIRNLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 105 FGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:cd18784 76 FRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488987387 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFDK 232
Cdd:cd18784 156 YGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSE 203
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
27-309 |
1.43e-15 |
|
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: 77.55 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAgsdtfmLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMR 101
Cdd:cd18555 5 ISILLLSLLLQL------LTLLIPILtqyviDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 102 RRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLApIVSVA 181
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 182 IRVVSKRfRNISKNMQNTMGQVTTSAEQ--MLKGHKEVLMFGgqeVETKRFDKVSNKMrlqgMKMVSA-------SSISD 252
Cdd:cd18555 157 LLLLTRK-KIKKLNQEEIVAQTKVQSYLteTLYGIETIKSLG---SEKNIYKKWENLF----KKQLKAfkkkerlSNILN 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 253 PIIQLIASLALAFVLYAASFPSVMDTLTAGTItVVFSSM-IALMRPLKSLTNVNAQFQ 309
Cdd:cd18555 229 SISSSIQFIAPLLILWIGAYLVINGELTLGEL-IAFSSLaGSFLTPIVSLINSYNQFI 285
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-560 |
1.65e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR--EYKLSSlRDQV 419
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAA-QLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFND-TVANNIAYAR--TEEYSREQIEEAARM---AYAMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIAR 493
Cdd:PRK09700 83 GIIYQELSVIDElTVLENLYIGRhlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
342-582 |
3.64e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.32 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKL-SSLRDQVA 420
Cdd:PRK10895 4 LTAKNLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVHLFND-TVANNIAYART--EEYSREQIEEAARMAYAMDFINKMDNGLdtiigenGVMLSGGQRQRIAIARALLR 497
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRL-STIEQADEIVVVEDGRIVERGTHHDLLEHKgvyaQL 575
Cdd:PRK10895 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE----HV 230
|
....*..
gi 488987387 576 HKMQFGE 582
Cdd:PRK10895 231 KRVYLGE 237
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
359-567 |
4.41e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 4.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKST----IASLITRFYDVDeGQILLDGH--DLREYKLSSlrdqvALVSQNVHLFNDT 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnaLAFRSPKGVKGS-GSVLLNGMpiDAKEMRAIS-----AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 433 VANNIAYARTEEYSREQIEEAARMAYAMDFINKMdnGL----DTIIGENGVM--LSGGQRQRIAIARALLRNSPILILDE 506
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 507 ATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-536 |
4.98e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 4.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 353 GREVAALR-------NINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDlreYKLSSLRDQVALVS-Q 424
Cdd:PRK13539 5 GEDLACVRggrvlfsGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLGhR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLFNDTVANNIAY-ARTEEYSREQIEEAArmaYAMdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILI 503
Cdd:PRK13539 82 NAMKPALTVAENLEFwAAFLGGEELDIAAAL---EAV--------GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190
....*....|....*....|....*....|...
gi 488987387 504 LDEATSALDTESERAIqAALDELQKNRTSLVIA 536
Cdd:PRK13539 151 LDEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
342-571 |
5.67e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLreyklSSL------ 415
Cdd:COG1137 4 LEAENLVKSYGKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-----THLpmhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 416 RDQVALVSQNVHLFND-TVANNI-AYARTEEYSREQIEEaaRMAYAMDfinkmDNGLDTIIGENGVMLSGGQRQRIAIAR 493
Cdd:COG1137 77 RLGIGYLPQEASIFRKlTVEDNIlAVLELRKLSKKEREE--RLEELLE-----EFGITHLRKSKAYSLSGGERRRVEIAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 494 ALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HR----LSTIEQAdeiVVVEDGRIVERGTHHDLLEH 568
Cdd:COG1137 150 ALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITdHNvretLGICDRA---YIISEGKVLAEGTPEEILNN 226
|
...
gi 488987387 569 KGV 571
Cdd:COG1137 227 PLV 229
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
60-309 |
5.78e-15 |
|
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: 75.67 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 60 DRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRItYDSEQVASSS 139
Cdd:cd18568 37 NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 140 SSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLM 219
Cdd:cd18568 116 TRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 220 FGgqeVETKRFDKVSNKM------RLQGMKMVSASSIsdpIIQLIASLALAFVL-YAASFpsVMD-TLTAGTItVVFSSM 291
Cdd:cd18568 196 LA---AERPIRWRWENKFakalntRFRGQKLSIVLQL---ISSLINHLGTIAVLwYGAYL--VISgQLTIGQL-VAFNML 266
|
250
....*....|....*....
gi 488987387 292 IA-LMRPLKSLTNVNAQFQ 309
Cdd:cd18568 267 FGsVINPLLALVGLWDELQ 285
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-557 |
8.91e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.99 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTyPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL--------REYKLS 413
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 414 SL---RDQVALVSqnvhlfNDTVANNIA--YARTEEYSR-EQIEEAARMAYAMDFINKMD---NGLDTIIGengvMLSGG 484
Cdd:COG3845 337 YIpedRLGRGLVP------DMSVAENLIlgRYRRPPFSRgGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EQADEIVVVEDGRIV 557
Cdd:COG3845 407 NQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAvLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-567 |
3.03e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.61 E-value: 3.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 324 SEQEKDegtRVIERAKGNLKFENVTFTYPGRE---VAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQI 400
Cdd:TIGR03269 265 SEVEKE---CEVEVGEPIIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 401 -------LLDGHDLREYKLSSLRDQVALVSQNVHLF-NDTVANNIayarTEEYSREQIEEAARM--AYAMDFINKMDNGL 470
Cdd:TIGR03269 342 nvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMkaVITLKMVGFDEEKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 471 DTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERA----IQAALDELqkNRTSLVIAHRLSTI-EQA 545
Cdd:TIGR03269 418 EEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEM--EQTFIIVSHDMDFVlDVC 495
|
250 260
....*....|....*....|..
gi 488987387 546 DEIVVVEDGRIVERGTHHDLLE 567
Cdd:TIGR03269 496 DRAALMRDGKIVKIGDPEEIVE 517
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
345-560 |
3.89e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREvAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLrdqVALVSQ 424
Cdd:PRK15056 10 NDVTVTWRNGH-TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVH-------LFNDTVA----NNIAYAR-TEEYSREQIEEAARMAYAMDFINKMdngldtiIGEngvmLSGGQRQRIAIA 492
Cdd:PRK15056 86 SEEvdwsfpvLVEDVVMmgryGHMGWLRrAKKRDRQIVTAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 493 RALLRNSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
347-565 |
6.68e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.85 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 347 VTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKS----TIASLITRFYDVDEGQILLDGHDLREYKLSSLRDqvaLV 422
Cdd:PRK11022 11 VHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRN---LV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVHL-FNDTVAN-NIAYarTEEYsreQIEEA----------ARMAYAMDFINKMdnGLDTIIGENGV---MLSGGQRQ 487
Cdd:PRK11022 88 GAEVAMiFQDPMTSlNPCY--TVGF---QIMEAikvhqggnkkTRRQRAIDLLNQV--GIPDPASRLDVyphQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGTHHD 564
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 488987387 565 L 565
Cdd:PRK11022 241 I 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-576 |
6.80e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 354 REVAALRNINLDIPEGKTVALVGRSGSGKST----IASLITRfydvDEGQILLDGHD--LREYKLssLRdQVALV----S 423
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVpfKRRKEF--AR-RIGVVfgqrS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QnvhLFND-TVANNIAYAR------TEEYsREQIEEAARMAYAMDFINKMdngldtiigengV-MLSGGQRQRIAIARAL 495
Cdd:COG4586 106 Q---LWWDlPAIDSFRLLKaiyripDAEY-KKRLDELVELLDLGELLDTP------------VrQLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDLLEHKGVY 572
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
....
gi 488987387 573 AQLH 576
Cdd:COG4586 250 KTIV 253
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-560 |
1.62e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.21 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 361 NINLDIP-EGKTvALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDL----REYKLSSLRDQVALVSQNVHLF-NDTVA 434
Cdd:PRK11144 16 TVNLTLPaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 435 NNIAYArteeysreqieeaarMAyamdfiNKMDNGLDTIIGENGV---------MLSGGQRQRIAIARALLRNSPILILD 505
Cdd:PRK11144 95 GNLRYG---------------MA------KSMVAQFDKIVALLGIeplldrypgSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 506 EATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAReiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
359-557 |
1.82e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.60 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKST----IASLITRFYDVdEGQILLDGHDLREYKlSSLRDQVALVSQN-VHLFNDTV 433
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFA-EKYPGEIIYVSEEdVHFPTLTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 anniayarteeysREQIEEAARMayamdfinkmdNGLDTIIGengvmLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:cd03233 101 -------------RETLDFALRC-----------KGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 514 ESeraiqaALDELQKNRTslvIAH--RLSTI-----------EQADEIVVVEDGRIV 557
Cdd:cd03233 152 ST------ALEILKCIRT---MADvlKTTTFvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
345-557 |
2.04e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGreVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLrEYKLS--SLRDQVALV 422
Cdd:PRK10982 2 SNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkeALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVHLFND-TVANNIAYARteeYSREQIeeaarmayamdFI--NKMDNGLDTIIGENGV---------MLSGGQRQRIA 490
Cdd:PRK10982 79 HQELNLVLQrSVMDNMWLGR---YPTKGM-----------FVdqDKMYRDTKAIFDELDIdidprakvaTLSVSQMQMIE 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:PRK10982 145 IAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWI 213
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
349-560 |
2.99e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 349 FTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK--LSSLRDQVALVSQN- 425
Cdd:PRK13638 9 FRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgLLALRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 426 -VHLFNDTVANNIAYA------RTEEYSReQIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAIARALLRN 498
Cdd:PRK13638 87 eQQIFYTDIDSDIAFSlrnlgvPEAEITR-RVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERG 560
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
342-570 |
3.02e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRF--YDVDEGQILLDGHDLREyKLSSLRDQV 419
Cdd:CHL00131 8 LEIKNLHASVNENEI--LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD-LEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 420 ALVSQNVHLFNDTVANNIAYARTeEYSREQIEEAARMAYAMDFINKMDNGLDtIIGENGVML--------SGGQRQRIAI 491
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRL-AYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAH--RLSTIEQADEIVVVEDGRIVERG--THHDLL 566
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGdaELAKEL 242
|
....
gi 488987387 567 EHKG 570
Cdd:CHL00131 243 EKKG 246
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
72-238 |
3.32e-13 |
|
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: 70.44 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISSYC----ISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVV 147
Cdd:cd18590 39 IGLMCLFSLGSSLSAGLrgglFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 148 REGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVET 227
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEA 198
|
170
....*....|.
gi 488987387 228 KRFDKVSNKMR 238
Cdd:cd18590 199 CRYSEALERTY 209
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
346-565 |
3.42e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.18 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPGREVAAlrNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD---LREYKLSSLRDQVALV 422
Cdd:PRK11831 12 GVSFTRGNRCIFD--NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVHLFND-TVANNIAYARTEEysrEQIEEAARMAYAMDFINKMdnGLDtiiGENGVM---LSGGQRQRIAIARALLRN 498
Cdd:PRK11831 90 FQSGALFTDmNVFDNVAYPLREH---TQLPAPLLHSTVMMKLEAV--GLR---GAAKLMpseLSGGMARRAALARAIALE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEQADEIVVVEDGRIVERGTHHDL 565
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
369-566 |
7.41e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 68.42 E-value: 7.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 369 GKTVALVGRSGSGKST----IASLITrfydvDEGQILLDGHDLREYKLSSLRDQVALVSQNVH-LFNDTV----ANNIAY 439
Cdd:PRK03695 22 GEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVfqylTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 440 ARTEEYSREQIEEAARMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAIARALLRNSP-------ILILDEATSALD 512
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 513 TeserAIQAALDEL-----QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK03695 166 V----AQQAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
72-279 |
8.28e-13 |
|
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: 69.04 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISS------YCISwvSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALIT 145
Cdd:cd18589 39 ITVMSLLTIASAVSEfvcdliYNIT--MSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 146 VVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEV 225
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 226 ETKRF-DKVSNKMRLQGMKMVS------ASSISDPII---------QLIASLAL------AFVLYAASFPSVMDTL 279
Cdd:cd18589 197 EAQRYrQRLQKTYRLNKKEAAAyavsmwTSSFSGLALkvgilyyggQLVTAGTVssgdlvTFVLYELQFTSAVEVL 272
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
354-566 |
8.55e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.70 E-value: 8.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 354 REVAALRNINLDIPEGKTVALVGRSGSGKSTI---------ASLITRFYDVdEGQILLDGHDLREY---KLSSLRDQVAL 421
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARV-TGDVTLNGEPLAAIdapRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFNdtvANNIA------YAR----TEEYSREQIEEAARMAyamdfinkmdnGLDTIIGENGVMLSGGQRQRIAI 491
Cdd:PRK13547 91 AAQPAFAFS---AREIVllgrypHARragaLTHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 492 ARALLRNSP---------ILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVER 559
Cdd:PRK13547 157 ARVLAQLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAH 236
|
....*..
gi 488987387 560 GTHHDLL 566
Cdd:PRK13547 237 GAPADVL 243
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
72-314 |
3.17e-12 |
|
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: 67.57 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGA 151
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 152 SIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFD 231
Cdd:cd18574 129 QTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 232 KVSNKMRlqgmKMVSASSISDPIIQLIASLALA----FVLYAASFPSVMDTLTAGTITvvfSSMIALMRPLKSLTNVNA- 306
Cdd:cd18574 209 EEVEKAA----KLNEKLGLGIGIFQGLSNLALNgivlGVLYYGGSLVSRGELTAGDLM---SFLVATQTIQRSLAQLSVl 281
|
250
....*....|
gi 488987387 307 --QFQRGMAA 314
Cdd:cd18574 282 fgQYVKGKSA 291
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
369-559 |
4.15e-12 |
|
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: 64.32 E-value: 4.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 369 GKTVALVGRSGSGKSTIASLITRFYDVDEGQ-ILLDGHDLREYKLSSLRDqvalvsqnvhlfndtvanniayarteeysr 447
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 448 eqieeaarmayamdfinkmdngldTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALD--- 524
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 488987387 525 ---ELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVER 559
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
342-525 |
4.67e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 65.07 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKlSSLRDQVAL 421
Cdd:TIGR01189 1 LAARNLACSRGERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNVHLFND-TVANNIA-YARTEEYSREQIEEA-ARMayamdfinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRN 498
Cdd:TIGR01189 78 LGHLPGLKPElSALENLHfWAAIHGGAQRTIEDAlAAV------------GLTGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180
....*....|....*....|....*..
gi 488987387 499 SPILILDEATSALDTESERAIQAALDE 525
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
341-568 |
4.83e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 67.24 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTftyPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYD----VDEGQILLDGHDLreYKLSSlR 416
Cdd:COG4170 8 NLTIEIDT---PQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDL--LKLSP-R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQNVHL-FNDTvannIAYARTEEYSREQIEEA---------------ARMAYAMDFINKMDngldtIIGENGVM 480
Cdd:COG4170 82 ERRKIIGREIAMiFQEP----SSCLDPSAKIGDQLIEAipswtfkgkwwqrfkWRKKRAIELLHRVG-----IKDHKDIM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 ------LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:COG4170 153 nsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQwADTITVL 232
|
250
....*....|....*..
gi 488987387 552 EDGRIVERGTHHDLLEH 568
Cdd:COG4170 233 YCGQTVESGPTEQILKS 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
363-551 |
6.06e-12 |
|
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: 68.27 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 363 NLDIP-EGKTVALVGRSGSGKSTIAS-----LITRFYDVDEG----QIL--LDGHDLREYkLSSLRDQ---VALVSQNVH 427
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrFRGTELQDY-FKKLANGeikVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 428 L----FNDTVanniayarteeysREQIEEAARMAYAMDFINK--MDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPI 501
Cdd:COG1245 171 LipkvFKGTV-------------RELLEKVDERGKLDELAEKlgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 502 LILDEATSALD----TESERAIQaalDELQKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:COG1245 234 YFFDEPSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
1.03e-11 |
|
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: 65.33 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTI------ASLITRFYdvdEGQILLDGHDlREYKLSSLrDQVALVSQNvhLFNDT 432
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlyPALARRLH---LKKEQPGNHD-RIEGLEHI-DKVIVIDQS--PIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 433 VANNIA-YA--------------RTEEYSRE-----------------QIEEAA-------RMAYAMDFInkMDNGLDTI 473
Cdd:cd03271 84 PRSNPAtYTgvfdeirelfcevcKGKRYNREtlevrykgksiadvldmTVEEALeffenipKIARKLQTL--CDVGLGYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 474 -IGENGVMLSGGQRQRIAIARALLRNSP---ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEI 548
Cdd:cd03271 162 kLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWI 241
|
.
gi 488987387 549 V 549
Cdd:cd03271 242 I 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
355-575 |
2.13e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.28 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVA 434
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 435 NNIAYARtEEYSREQIEEA-ARMAYamdfinkmdNGLDTIIGENgvmLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:cd03231 92 ENLRFWH-ADHSDEQVEEAlARVGL---------NGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 514 ESERAIqaaldelqknrTSLVIAHrlstieqadeivvVEDGRIVERGTHHDLLEHKGVYAQL 575
Cdd:cd03231 159 AGVARF-----------AEAMAGH-------------CARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-546 |
2.30e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyKLSSLRDQVALVSQN 425
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 426 VHLF-NDTVANNIAYARTEEYSREQIEEAARmayamdfINKMDNGLDTIIGengvMLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK13540 83 SGINpYLTLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488987387 505 DEATSALDtesERAIQAALDELQKNRTS----LVIAHRLSTIEQAD 546
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQEHRAKggavLLTSHQDLPLNKAD 194
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-554 |
2.57e-11 |
|
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: 63.97 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 365 DIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLrEYKLSSLR-DQVALVSQNVHLFNDTVANNiAYARTE 443
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGTVRDLLSSITKDFYTH-PYFKTE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 444 EYSREQIEEAarmayamdfinkMDNGLDTiigengvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESE----RAI 519
Cdd:cd03237 99 IAKPLQIEQI------------LDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVI 158
|
170 180 190
....*....|....*....|....*....|....*
gi 488987387 520 QAALDELQKnrTSLVIAHRLSTIEQADEIVVVEDG 554
Cdd:cd03237 159 RRFAENNEK--TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-551 |
3.72e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 363 NLDIP-EGKTVALVGRSGSGKSTIAS-----LITRFYDVDEG----QIL--LDGHDLREY--KLSSLRDQVALVSQNVHL 428
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEpswdEVLkrFRGTELQNYfkKLYNGEIKVVHKPQYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 429 ----FNDTVANNIayarteeysrEQIEEAARMAYAMDFINkMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK13409 172 ipkvFKGKVRELL----------KKVDERGKLDEVVERLG-LENILDRDISE----LSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488987387 505 DEATSALD----TESERAIQaaldELQKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:PRK13409 237 DEPTSYLDirqrLNVARLIR----ELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
355-558 |
5.66e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR---EYKLSSLRDQ-VALVSQNVHLFN 430
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 431 DTVA-NNI---AYAR--TEEYSREQieeaarmayAMDFINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK10584 102 TLNAlENVelpALLRgeSSRQSRNG---------AKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 505 DEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
342-560 |
1.04e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGRevAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDlreyklSSLRDQVAL 421
Cdd:PRK11701 7 LSVRGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD------GQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 V-SQNVHLFndtvanniayaRTE-EYSREQIEEAARMA------------------Y------AMDFINKMDNGLDTiIG 475
Cdd:PRK11701 79 SeAERRRLL-----------RTEwGFVHQHPRDGLRMQvsaggnigerlmavgarhYgdiratAGDWLERVEIDAAR-ID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 476 ENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLSTIEQ-ADEI 548
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRL 222
|
250
....*....|..
gi 488987387 549 VVVEDGRIVERG 560
Cdd:PRK11701 223 LVMKQGRVVESG 234
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-190 |
1.39e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 62.53 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRItYDSEQVASSSSSALITVVR 148
Cdd:cd18783 46 IGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 488987387 149 EGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFR 190
Cdd:cd18783 125 DATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFR 166
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
342-566 |
1.80e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 62.51 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVT--FTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLIT--------------RFYDVDegqiLLdgh 405
Cdd:PRK15093 4 LDIRNLTieFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDID----LL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 406 dlreyKLSSlRDQVALVSQNVHL-FNDTVAnniAYARTEEYSREQIEEAARMAY--------------AMDFINKMdnGL 470
Cdd:PRK15093 77 -----RLSP-RERRKLVGHNVSMiFQEPQS---CLDPSERVGRQLMQNIPGWTYkgrwwqrfgwrkrrAIELLHRV--GI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 471 ---DTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ- 544
Cdd:PRK15093 146 kdhKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQw 225
|
250 260
....*....|....*....|..
gi 488987387 545 ADEIVVVEDGRIVERGTHHDLL 566
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELV 247
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
342-562 |
1.86e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTI-ASLITRF-YDVDEGQILLDGHDLREYK-------- 411
Cdd:PRK09580 2 LSIKDLHVSVEDKAI--LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSpedrageg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 412 -LSSLRDQVALVSQNVHLFNDTVANNIayartEEYsREQiEEAARMAYAmDFINK----MDNGLDTIIGENGVMLSGGQR 486
Cdd:PRK09580 80 iFMAFQYPVEIPGVSNQFFLQTALNAV-----RSY-RGQ-EPLDRFDFQ-DLMEEkialLKMPEDLLTRSVNVGFSGGEK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA---HRLSTIEQADEIVVVEDGRIVERGTH 562
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
350-549 |
5.76e-10 |
|
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: 58.49 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 350 TYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLItrFYDVDEGQILLDGHDLREYKLSSLrDQVALVsqnvhlf 429
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKARLISFLPKFSRNKLIFI-DQLQFL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 ndtVANNIAYARteeysreqieeaarmayamdfinkmdngldtiIGENGVMLSGGQRQRIAIARALLRNSP--ILILDEA 507
Cdd:cd03238 72 ---IDVGLGYLT--------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488987387 508 TSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWII 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
360-565 |
1.09e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 360 RNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklssLRDQVAlvsQNV----HL--FND-- 431
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYH---QDLlylgHQpgIKTel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 432 TVANNIA-YAR-TEEYSREQIEEA-ARMayamdfinkmdnGLDtiigenGVM------LSGGQRQRIAIARALLRNSPIL 502
Cdd:PRK13538 90 TALENLRfYQRlHGPGDDEALWEAlAQV------------GLA------GFEdvpvrqLSAGQQRRVALARLWLTRAPLW 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 503 ILDEATSALDTeseraiqAALDELqknrTSLVIAHrlstieqadeivvVEDGRIVERGTHHDL 565
Cdd:PRK13538 152 ILDEPFTAIDK-------QGVARL----EALLAQH-------------AEQGGMVILTTHQDL 190
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
359-560 |
1.53e-09 |
|
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: 58.42 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIAslitrfYDV--DEGQilldghdlREYkLSSL------------RDQVALV-- 422
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA------FDTiyAEGQ--------RRY-VESLsayarqflgqmdKPDVDSIeg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 -SQNVHLFNDTVANNiayARTEEYSREQIEEAARMAYAMDFINK-----MDNGLDTIIGENGVM-LSGGQRQRIAIARAL 495
Cdd:cd03270 76 lSPAIAIDQKTTSRN---PRSTVGTVTEIYDYLRLLFARVGIRErlgflVDVGLGYLTLSRSAPtLSGGEAQRIRLATQI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 496 LRN--SPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEIVVV------EDGRIVERG 560
Cdd:cd03270 153 GSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
345-570 |
1.72e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYpgREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREyklSSLRDQV----A 420
Cdd:NF033858 5 EGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcpriA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQ----NvhLFND-TVANNIAY-ARTEEYSREqiEEAARMAYAMDfinkmDNGLDTIIGENGVMLSGGQRQRIAIARA 494
Cdd:NF033858 80 YMPQglgkN--LYPTlSVFENLDFfGRLFGQDAA--ERRRRIDELLR-----ATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIahrLST--IEQA---DEIVVVEDGRIVERGTHHDLLEH 568
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMsVL---VATayMEEAerfDWLVAMDAGRVLATGTPAELLAR 227
|
..
gi 488987387 569 KG 570
Cdd:NF033858 228 TG 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-551 |
2.15e-09 |
|
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: 58.53 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 364 LDIP-EGKTVALVGRSGSGKSTIASLIT--------RFYDVDEGQILLD---GHDLREYKLSSLRDQVALV--SQNVHLF 429
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIvkPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 NDTVANNIAYARTEEYSREQIEEAARmayAMDFINKMDNGLDTiigengvmLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:cd03236 100 PKAVKGKVGELLKKKDERGKLDELVD---QLELRHVLDRNIDQ--------LSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488987387 510 ALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:cd03236 169 YLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-554 |
2.22e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 323 DSEQEKDEgtrviERAKGNLKFE--NVTFTYP--GREVAALRNINLDIPEGKTVALVGRSGSGKSTI----ASLITRFYd 394
Cdd:TIGR00956 744 DVNDEKDM-----EKESGEDIFHwrNLTYEVKikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLlnvlAERVTTGV- 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 395 VDEGQILLDGHDLReyklSSLRDQVALVSQN-VHLFNDTVanniayarteeysREQIEEAARM--------AYAMDFINK 465
Cdd:TIGR00956 818 ITGGDRLVNGRPLD----SSFQRSIGYVQQQdLHLPTSTV-------------RESLRFSAYLrqpksvskSEKMEYVEE 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 466 ------MDNGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILI-LDEATSALDTESERAIQAALDELQKN-RTSLVIAH 537
Cdd:TIGR00956 881 viklleMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIH 960
|
250
....*....|....*....
gi 488987387 538 RLSTI--EQADEIVVVEDG 554
Cdd:TIGR00956 961 QPSAIlfEEFDRLLLLQKG 979
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
335-556 |
2.51e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 335 IERAKGNLKFENVTFTYPGrevaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLreyklSS 414
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-----VT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQNVHLFND----------TVANNIAYARTEEYSRE--QIEEAARMAYAMDFInKMDN----GLDTIIGeng 478
Cdd:PRK10762 319 RSPQDGLANGIVYISEDrkrdglvlgmSVKENMSLTALRYFSRAggSLKHADEQQAVSDFI-RLFNiktpSMEQAIG--- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 479 vMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:PRK10762 395 -LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
359-538 |
2.90e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYKLSSLRDQVALVSQnvhlFNDTVAnnia 438
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----FKDAVE---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 yarteeysreqIEEAARMAYAMDFINKMDNgldtiigengvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESERA 518
Cdd:COG2401 118 -----------LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|..
gi 488987387 519 IQAALDEL-QKNRTSLVIA-HR 538
Cdd:COG2401 175 VARNLQKLaRRAGITLVVAtHH 196
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
27-197 |
3.82e-09 |
|
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: 58.28 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNAGSDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLApivsVAIRVVS 186
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL----VVYYLLQ 156
|
170
....*....|.
gi 488987387 187 KRFRNISKNMQ 197
Cdd:cd18580 157 RYYLRTSRQLR 167
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
359-557 |
3.90e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGhDLREYKLSslRDQVALVSQNVHlfnDTVANNIA 438
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQ--QDPPRNVEGTVY---DFVAEGIE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 439 --------YART-----EEYSREQIEEAARMAYAMDFIN--KMDN---------GL--DTIIGEngvmLSGGQRQRIAIA 492
Cdd:PRK11147 93 eqaeylkrYHDIshlveTDPSEKNLNELAKLQEQLDHHNlwQLENrinevlaqlGLdpDAALSS----LSGGWLRKAALG 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 493 RALLRNSPILILDEATSALDTEserAIQaALDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIE---TIE-WLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
27-191 |
4.51e-09 |
|
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: 57.99 E-value: 4.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 27 LIVAAVALVLNagsdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMR 101
Cdd:cd18782 5 IEVLALSFVVQ------LLGLANPLLfqviiDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 102 RRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVA 181
Cdd:cd18782 79 GTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLL 157
|
170
....*....|
gi 488987387 182 IRVVSKRFRN 191
Cdd:cd18782 158 TFLFGPILRR 167
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
65-318 |
6.43e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 57.23 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 65 LWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRL----FGHMMGMPVAFFDKQSTGTLLS---RITYDSEQVAS 137
Cdd:cd18560 34 LESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELslktFAHLHSLSLDWHLSKKTGEVVRimdRGTESANTLLS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 138 SSSSALITVVREGASIIGLFvmMFYYSWQLSLILIV---LAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAeqmLKGH 214
Cdd:cd18560 114 YLVFYLVPTLLELIVVSVVF--AFHFGAWLALIVFLsvlLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDS---LLNF 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 215 KEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIAL 294
Cdd:cd18560 189 ETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQL 268
|
250 260
....*....|....*....|....
gi 488987387 295 MRPLKSLTNVNAQFQRGMAACQTL 318
Cdd:cd18560 269 FQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
330-540 |
6.53e-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: 58.61 E-value: 6.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 330 EGTRVIERAKGNLKFENVTFTYPGREVAaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHD--- 406
Cdd:TIGR00954 440 PGRGIVEYQDNGIKFENIPLVTPNGDVL-IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklf 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 407 ---LREY-KLSSLRDQValvsqnvhLFNDTVanniayartEEYSREQIEEAarmayamDFINKMDN-GLDTIIGENGV-- 479
Cdd:TIGR00954 519 yvpQRPYmTLGTLRDQI--------IYPDSS---------EDMKRRGLSDK-------DLEQILDNvQLTHILEREGGws 574
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 480 -------MLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDElqKNRTSLVIAHRLS 540
Cdd:TIGR00954 575 avqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-554 |
1.12e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.33 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAA--LRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYD--VDEGQILLDGHDLREyklsSLRD 417
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqlLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQN-VHLFNDTVanniayarteeysREQIEEAARMayamdfinkmdNGldtiigengvmLSGGQRQRIAIARALL 496
Cdd:cd03232 80 STGYVEQQdVHSPNLTV-------------REALRFSALL-----------RG-----------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS--TIEQADEIVVVEDG 554
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-552 |
1.12e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 366 IPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDghdLR-EYKLSSLR-DQVALVSQNvhLFNDTVANNIAYARTE 443
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKpDYDGTVEDL--LRSITDDLGSSYYKSE 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 444 EYSREQIEEAarmayamdfinkMDNGLDTiigengvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESE----RAI 519
Cdd:PRK13409 437 IIKPLQLERL------------LDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAI 496
|
170 180 190
....*....|....*....|....*....|....
gi 488987387 520 QAALDElqKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:PRK13409 497 RRIAEE--REATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
28-309 |
1.82e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.05 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 28 IVAAVALVLNagsdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRR 102
Cdd:cd18566 6 QVLLASLFIN------ILALATPLFilqvyDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 103 RLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18566 80 AAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 183 RVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLMfGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18566 159 ILLGPILRRaLKERSRADERRQNFLIETLTGIHTIKAM-AMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488987387 262 A-LAFVLYAASFpsVMD-TLTAGTItvVFSSMIA--LMRPLKSLTNVNAQFQ 309
Cdd:cd18566 238 SmVAVVAFGALL--VINgDLTVGAL--IACTMLSgrVLQPLQRAFGLWTRFQ 285
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-564 |
1.90e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 369 GKTVALVGRSGSGKSTIASLIT-RFYDVD-EGQILLDGHDLREYKLSslrdQVALVSQNVHLF-NDTVANNIAYAR---- 441
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpHLTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 442 TEEYSREQIEEAARMAYAMDFINKMDNgldTIIGENGVM-LSGGQRQRIAIARALLRNSPILILDEATSALD-TESERAI 519
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLV 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488987387 520 QAALDELQKNRTSLVIAHRLST--IEQADEIVVVEDGRIVERGTHHD 564
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
72-177 |
2.02e-08 |
|
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: 55.97 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGA 151
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTLVLDLV 127
|
90 100
....*....|....*....|....*.
gi 488987387 152 SIIGLFVMMFYYSWQLSLILIVLAPI 177
Cdd:cd18588 128 FSVVFLAVMFYYSPTLTLIVLASLPL 153
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
479-552 |
2.72e-08 |
|
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: 53.73 E-value: 2.72e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 479 VMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-515 |
2.72e-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: 56.48 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 352 PGREVaaLRNINLDIPEGKTVALVGRSGSGKSTI----ASLITRF-------------YDVDEGQiLLDGHDLREYKLSS 414
Cdd:TIGR03719 16 PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKDFngearpqpgikvgYLPQEPQ-LDPTKTVRENVEEG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 415 LRDQVALVSQnvhlFNDTVAnniAYARTEEYSREQIEEAARMAYAMDFIN--KMDNGL------------DTIIGEngvm 480
Cdd:TIGR03719 93 VAEIKDALDR----FNEISA---KYAEPDADFDKLAAEQAELQEIIDAADawDLDSQLeiamdalrcppwDADVTK---- 161
|
170 180 190
....*....|....*....|....*....|....*
gi 488987387 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
345-539 |
3.37e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 345 ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILldghdlREYKLsslrdQVALVSQ 424
Cdd:PRK09544 8 ENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKL-----RIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 425 NVHLfNDTVANNIA-YARTEEYSREQ-IEEAARMAYAMDFINK-MDNgldtiigengvmLSGGQRQRIAIARALLRNSPI 501
Cdd:PRK09544 75 KLYL-DTTLPLTVNrFLRLRPGTKKEdILPALKRVQAGHLIDApMQK------------LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488987387 502 LILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL 539
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
365-552 |
4.27e-08 |
|
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: 55.95 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 365 DIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDghdLR-EYKLSSLRDQvalvsqnvhlFNDTVANNIAYARTE 443
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKiSYKPQYISPD----------YDGTVEEFLRSANTD 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 444 EY--SREQIEEAARMAyamdfINK-MDNGLDTiigengvmLSGGQRQRIAIARALLRNSPILILDEATSALDTESE---- 516
Cdd:COG1245 429 DFgsSYYKTEIIKPLG-----LEKlLDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlava 495
|
170 180 190
....*....|....*....|....*....|....*..
gi 488987387 517 RAIQAALDElqKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:COG1245 496 KAIRRFAEN--RGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-549 |
4.70e-08 |
|
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: 52.75 E-value: 4.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 353 GREVAALRNINLDIPEGKTVALVGRSGSGKSTIA---SLITrfydvdegqiLLDGHDLREYKLSSLRDQVALVSqnvhlf 429
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdaiGLAL----------GGAQSATRRRSGVKAGCIVAAVS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 ndtvanniayarteeysreqieeaarmayaMDFINkmdngldTIIGengvmLSGGQRQRIAIARAL----LRNSPILILD 505
Cdd:cd03227 69 ------------------------------AELIF-------TRLQ-----LSGGEKELSALALILalasLKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488987387 506 EATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
346-515 |
4.89e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 4.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPG-REVaaLRNINLDIPEGKTVALVGRSGSGKSTI----ASLITRFydvdEGQILL----------------DG 404
Cdd:PRK11819 11 RVSKVVPPkKQI--LKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKEF----EGEARPapgikvgylpqepqldPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 405 HDLREYKLSSLRDQVALVSQnvhlFNDTVAnniAYARTEEYSREQIEEAARMAYAMDFIN--KMDNGL------------ 470
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDR----FNEIYA---AYAEPDADFDALAAEQGELQEIIDAADawDLDSQLeiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488987387 471 DTIIGEngvmLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
331-541 |
4.91e-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: 55.71 E-value: 4.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 331 GTRVIErakgnlkFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLdGHDLrey 410
Cdd:TIGR03719 319 GDKVIE-------AENLTKAFGDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 411 klsslrdQVALVSQnvhlFNDTVANNiayaRT--EEYS--REQIE----EAARMAYAMDFINKmdnGLD--TIIGEngvm 480
Cdd:TIGR03719 386 -------KLAYVDQ----SRDALDPN----KTvwEEISggLDIIKlgkrEIPSRAYVGRFNFK---GSDqqKKVGQ---- 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488987387 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST 541
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
363-575 |
5.94e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 363 NLDIPEGKTVALVGRSGSGKSTIASLItrfydvdEGQ-ILLDGH---DLREYKLSSLRDQVALVSQ-----NVHLF---- 429
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGElPLLSGErqsQFSHITRLSFEQLQKLVSDewqrnNTDMLspge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 430 NDTvanniayART-EEYSREQIEEAAR-MAYAMDFinkmdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEA 507
Cdd:PRK10938 96 DDT-------GRTtAEIIQDEVKDPARcEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 508 TSALDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIVVVEDGRIVERGTHHDLLEhKGVYAQL 575
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ-QALVAQL 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-556 |
6.57e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.44 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 360 RNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK-----------LSSLRDQ---------- 418
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlarglvyLPEDRQSsglyldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 ---VALVSQNVHLFNDTVANNiayARTEEYSR------EQIEEAARMayamdfinkmdngldtiigengvmLSGGQRQRI 489
Cdd:PRK15439 360 wnvCALTHNRRGFWIKPAREN---AVLERYRRalnikfNHAEQAART------------------------LSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
153-294 |
7.26e-08 |
|
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: 54.02 E-value: 7.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 153 IIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQEVETKRFD 231
Cdd:cd18585 123 ILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLgKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLE 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 232 KVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASfpsvmDTLTAGTITVVFSSMIAL 294
Cdd:cd18585 203 QLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGA-----PLVQNGALDGALLAMLVF 260
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-564 |
9.88e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 9.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVAaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILldghdlreyklSSLRDQVAL 421
Cdd:PLN03073 509 ISFSDASFGYPGGPLL-FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQNvHLFN-DTVANNIAYarteeysreqieeaarMAYAmdFINKMDNGLDTIIGENGV----------MLSGGQRQRIA 490
Cdd:PLN03073 577 FSQH-HVDGlDLSSNPLLY----------------MMRC--FPGVPEQKLRAHLGSFGVtgnlalqpmyTLSGGQKSRVA 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIE-QADEIVVVEDGRIVE-RGTHHD 564
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISgSVDELWVVSEGKVTPfHGTFHD 711
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
466-549 |
1.02e-07 |
|
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: 55.02 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 466 MDNGLDTI-IGENGVMLSGGQRQRIAIARALLRNS---PILILDEATSALDTESeraIQAALDELQ----KNRTSLVIAH 537
Cdd:TIGR00630 814 CDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDD---IKKLLEVLQrlvdKGNTVVVIEH 890
|
90
....*....|..
gi 488987387 538 RLSTIEQADEIV 549
Cdd:TIGR00630 891 NLDVIKTADYII 902
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-575 |
1.06e-07 |
|
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: 54.45 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP-GREVAALRNINLDIPEGKTVALVGRSGSGKS-TIASLITRFYDVDEGQILLDGH--DLREyKLSSLRD 417
Cdd:TIGR02633 258 LEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKpvDIRN-PAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 418 QVALVSQNVH----LFNDTVANNIAYARTEEYS-REQIEEAARMAYAMDFINKMD---NGLDTIIGEngvmLSGGQRQRI 489
Cdd:TIGR02633 337 GIAMVPEDRKrhgiVPILGVGKNITLSVLKSFCfKMRIDAAAELQIIGSAIQRLKvktASPFLPIGR----LSGGNQQKA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EQADEIVVVEDGRIVERGTHHDLLE 567
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQ 492
|
....*...
gi 488987387 568 HKGVYAQL 575
Cdd:TIGR02633 493 EQVLAAAL 500
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
66-213 |
3.78e-07 |
|
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: 52.16 E-value: 3.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 66 WMPLVVIGLMVL---RGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSeQVASSSSSA 142
Cdd:cd18779 40 LLGVLGLGLAALvltQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNA-TIRELLTSQ 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 143 LITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKG 213
Cdd:cd18779 119 TLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSG 189
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
321-543 |
5.39e-07 |
|
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: 53.09 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 321 ILDSEQE-KDEGTRVIerAKGN----LKFENVTFTYPGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDV 395
Cdd:TIGR01257 1914 IFDEDDDvAEERQRII--SGGNktdiLRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTV 1991
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 396 DEGQILLDGHDLreykLSSLRDqvalVSQNV-----------------HLFndtvanniAYARTEEYSREQIEEAARMAy 458
Cdd:TIGR01257 1992 TSGDATVAGKSI----LTNISD----VHQNMgycpqfdaiddlltgreHLY--------LYARLRGVPAEEIEKVANWS- 2054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 459 amdfINKMdnGLDTIIGENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAH 537
Cdd:TIGR01257 2055 ----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSH 2128
|
....*.
gi 488987387 538 RLSTIE 543
Cdd:TIGR01257 2129 SMEECE 2134
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
344-564 |
9.40e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 51.71 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 344 FE--NVTftypGREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLR-EYKLSSLRDQVA 420
Cdd:PRK09700 266 FEvrNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAVKKGMA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 421 LVSQNVH---LF-NDTVANNIAYART-------------EEYSREQIEEAARmayamDFINKMDNGLDTIIGEngvmLSG 483
Cdd:PRK09700 342 YITESRRdngFFpNFSIAQNMAISRSlkdggykgamglfHEVDEQRTAENQR-----ELLALKCHSVNQNITE----LSG 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGT 561
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQILT 492
|
...
gi 488987387 562 HHD 564
Cdd:PRK09700 493 NRD 495
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
342-543 |
1.59e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.04 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYP------------------GREVAALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLD 403
Cdd:PRK13545 5 VKFEHVTKKYKmynkpfdklkdlffrskdGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 404 GHDLREYKLSSLRDQVALVsQNVHLfndtvaNNIAYARTEEYSREQIEEAARMAYAMDFINKMDNgldtiigengvMLSG 483
Cdd:PRK13545 85 GSAALIAISSGLNGQLTGI-ENIEL------KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVK-----------TYSS 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIE 543
Cdd:PRK13545 147 GMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVK 207
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
28-178 |
3.13e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 49.33 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 28 IVAAVALVLNAGsdtfmlsLLKPLLDDGFGKTDRSVLLWMPLVV-IGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18584 6 LLAALLIIAQAW-------LLARIIAGVFLEGAGLAALLPLLLLlLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 107 HMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRegASII--GLFVMMFYYSWQLSLILIVLAPIV 178
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVL--AAIVplLILVAVFPLDWVSALILLVTAPLI 150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
470-552 |
5.01e-06 |
|
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: 47.60 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 470 LDTIIGENGVMLSGGQRQ------RIAIARALLRNSPILILDEATSALDTES-ERAIQAALDEL--QKNRTSLVIAHRLS 540
Cdd:cd03240 105 SNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERksQKNFQLIVITHDEE 184
|
90
....*....|..
gi 488987387 541 TIEQADEIVVVE 552
Cdd:cd03240 185 LVDAADHIYRVE 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-556 |
5.22e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVT---FTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKS-TIASLITRFYDVDEGQILLDGHDLR-EYKLSSLR 416
Cdd:PRK13549 260 LEVRNLTawdPVNPHIKR--VDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKiRNPQQAIA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 417 DQVALVSQN------VHLFNdtVANNIAYARTEEYS-REQIEEAARMAYAMDFINKMD---NGLDTIIGEngvmLSGGQR 486
Cdd:PRK13549 338 QGIAMVPEDrkrdgiVPVMG--VGKNITLAALDRFTgGSRIDDAAELKTILESIQRLKvktASPELAIAR----LSGGNQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EQADEIVVVEDGRI 556
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIiVISSELPEVlGLSDRVLVMHEGKL 483
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
331-525 |
6.74e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 331 GTRVIErakgnlkFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLdGHDLrey 410
Cdd:PRK11819 321 GDKVIE-------AENLSKSFGDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV--- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 411 klsslrdQVALVSQNvhlfNDTVANNiayaRT--EEYS--REQI-----EEAARmAYAMDFINKmdnGLDT--IIGengv 479
Cdd:PRK11819 388 -------KLAYVDQS----RDALDPN----KTvwEEISggLDIIkvgnrEIPSR-AYVGRFNFK---GGDQqkKVG---- 444
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488987387 480 MLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDE 525
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
329-537 |
8.05e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.79 E-value: 8.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 329 DEGTRvieraKGNLKF--ENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITrfydvdeGQILLDGHD 406
Cdd:PRK11147 310 EEASR-----SGKIVFemENVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGR 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 407 LR-EYKLsslrdQVALVSQNVHLFN--DTVANNIAYARTEeysreqIEEAAR----MAYAMDFINKMDNGLDTIIGengv 479
Cdd:PRK11147 376 IHcGTKL-----EVAYFDQHRAELDpeKTVMDNLAEGKQE------VMVNGRprhvLGYLQDFLFHPKRAMTPVKA---- 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 480 mLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
Cdd:PRK11147 441 -LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
466-572 |
8.40e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 466 MDNGLDTI-IGENGVMLSGGQRQRIAIARALLRNS---PILILDEATSALDTESeraIQAALDELQK-----NrTSLVIA 536
Cdd:PRK00349 815 VDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFED---IRKLLEVLHRlvdkgN-TVVVIE 890
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 488987387 537 HRLSTIEQADEIVvveD---------GRIVERGTHHDLLEHKGVY 572
Cdd:PRK00349 891 HNLDVIKTADWII---DlgpeggdggGEIVATGTPEEVAKVEASY 932
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
369-554 |
8.46e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 369 GKTVALVGRSGSGKSTIASLI----TRFYDvdEGQILLDGHDLRE---YKLSSLRDQVALVSQNVhlfndTVANNIAYAR 441
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKKQetfARISGYCEQNDIHSPQV-----TVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 442 ----TEEYSREQieeaarmayAMDFINK------MDNGLDTIIGENGVM-LSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:PLN03140 979 flrlPKEVSKEE---------KMMFVDEvmelveLDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488987387 511 LDTESE----RAIQAALDelqKNRTSLVIAHRLS--TIEQADEIVVVEDG 554
Cdd:PLN03140 1050 LDARAAaivmRTVRNTVD---TGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
480-549 |
1.68e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 1.68e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488987387 480 MLSGGQRQRIAIA--RALLRN--SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKYkpAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
32-187 |
2.27e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain] Cd Length: 290 Bit Score: 46.38 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 32 VALVLNAGSDTFMLSLLKPLLddgFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18781 7 ISLLANIAFVFSIANLLQKLL---EGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488987387 112 PVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:cd18781 84 GPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQK 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-571 |
2.61e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 342 LKFENVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQIlldghdlreyKLSSlRDQVAL 421
Cdd:PRK15064 320 LEVENLTKGFDNGPL--FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSE-NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 422 VSQ-NVHLF-ND-TVANNIAYARTEEYSrEQIEEAA--RMAYAMDFINKMDNgldtiigengvMLSGGQRQRIAIARALL 496
Cdd:PRK15064 387 YAQdHAYDFeNDlTLFDWMSQWRQEGDD-EQAVRGTlgRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488987387 497 RNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEIVVVEDGRIVE-RGTHHDLLEHKGV 571
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEEYLRSQGI 529
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
26-188 |
3.29e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 46.08 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 26 GLIVAAVALVlnagsdtfMLSLLKPLLddgFGKTDRSVLLW-MPLVVIGLMVLRGITSYISSYCISWVSGKvvMTMRRRL 104
Cdd:cd18562 3 GLALANVALA--------GVQFAEPVL---FGRVVDALSSGgDAFPLLALWAALGLFSILAGVLVALLADR--LAHRRRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 105 ------FGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSsssaLITVVREG-ASIIGLFVMM---FYYSWQLSLILIVL 174
Cdd:cd18562 70 avmasyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGL----WLGFFREHlAALVSLIVLLpvaLWMNWRLALLLVVL 145
|
170
....*....|....
gi 488987387 175 APIVSVAIRVVSKR 188
Cdd:cd18562 146 AAVYAALNRLVMRR 159
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-537 |
3.87e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 341 NLKFENVTFTYPGREVAALRNINLDIpeGKTVALVGRSGSGKSTIASLITrFYDVD-----------EGQILLDGHDLRE 409
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAF--GRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkncqilhvEQEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 410 YKLSSLRDQVALVSQNVHLF-------------------NDTVANNIAYARTEE-YSR-EQIE------EAARMAYAMDF 462
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVaqqrelefetetgkgkganKDGVDKDAVSQRLEEiYKRlELIDaytaeaRAASILAGLSF 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 463 INKMDNgldtiigENGVMLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
Cdd:PLN03073 334 TPEMQV-------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
32-200 |
3.93e-05 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 45.90 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 32 VALVLNAGSdtfMLSLLKPLL-----DDGFGKTDRSVLLwmpLVVIGLMVL---RGITSYISSYCISWVSGKVVMTMRRR 103
Cdd:cd18571 7 LLLGLLLGS---LLQLIFPFLtqsivDKGINNKDLNFIY---LILIAQLVLflgSTSIEFIRSWILLHISSRINISIISD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 104 LFGHMMGMPVAFFDKQSTGTLLSRItYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLApIVSVA-- 181
Cdd:cd18571 81 FLIKLMRLPISFFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGS-VLYILwi 158
|
170 180
....*....|....*....|....*.
gi 488987387 182 -----IRVV--SKRFRNISKNMQNTM 200
Cdd:cd18571 159 llflkKRKKldYKRFDLSSENQSKLI 184
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
26-194 |
4.20e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.63 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 26 GLIVAAVAL---VLNAGSDTFMLSLLKPLLDDGFGKTDRSVL--------------LWM-PLVVIGLMVLRGITSYISSY 87
Cdd:cd18599 1 GYVVFLFVLllfILSVGSTVFSDWWLSYWLKQGSGNTTNNVDnstvdsgnisdnpdLNFyQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 88 CISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIG-LFVMMFYYSW- 165
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFsLIIIAIVFPWf 160
|
170 180 190
....*....|....*....|....*....|....
gi 488987387 166 -----QLSLILIVLAPIVSVAIRVVsKRFRNISK 194
Cdd:cd18599 161 lialiPLAIIFVFLSKIFRRAIREL-KRLENISR 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-557 |
5.07e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 350 TYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIA-SLITRFYDVD-EGQILLDGhdlREYKLSSLRDQV----ALVS 423
Cdd:NF040905 269 LHPERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDG---KEVDVSTVSDAIdaglAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 424 QN-----VHLfNDTVANNIAYARTEEYSREQ-IEEAARMAYAMDFINKMD---NGLDTIIGEngvmLSGGQRQRIAIARA 494
Cdd:NF040905 344 EDrkgygLNL-IDDIKRNITLANLGKVSRRGvIDENEEIKVAEEYRKKMNiktPSVFQKVGN----LSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 495 LLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGRIV 557
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
362-569 |
5.59e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 362 INLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLReykLSSLRD-------------------QVALV 422
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDairagimlcpedrkaegiiPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 423 SQNVhlfndtvanNIAYARTEEYSREQIEEAARMAYAMDFINKMD---NGLDTIIGEngvmLSGGQRQRIAIARALLRNS 499
Cdd:PRK11288 349 ADNI---------NISARRHHLRAGCLINNRWEAENADRFIRSLNiktPSREQLIMN----LSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGRIVERGTHHDLLEHK 569
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQATERQ 487
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
326-512 |
7.32e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 326 QEKDEGTRVIErAKG-NLKFENvtFTypgrevaALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILL-- 402
Cdd:NF033858 258 PADDDDEPAIE-ARGlTMRFGD--FT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfg 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 403 ---DGHDLreyklsSLRDQVALVSQNVHLFND-TVANNIA-YARTEEYSREQIeeAARMAYAMD-FinkmdnGLDTIIGE 476
Cdd:NF033858 328 qpvDAGDI------ATRRRVGYMSQAFSLYGElTVRQNLElHARLFHLPAAEI--AARVAEMLErF------DLADVADA 393
|
170 180 190
....*....|....*....|....*....|....*.
gi 488987387 477 NGVMLSGGQRQRIAIARALLRNSPILILDEATSALD 512
Cdd:NF033858 394 LPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
69-301 |
1.00e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 44.41 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGLMVLRGITSYISSYCISWVSGKVVMTMR----------------RRLFGHMMGMPVAFFDKQSTGTLLSRITYDS 132
Cdd:cd18582 26 LSAPASALLAVPLLLLLAYGLARILSSLFNELRdalfarvsqravrrlaLRVFRHLHSLSLRFHLSRKTGALSRAIERGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 133 EQVASSSSSALITVVREGASIIGLFVMMFY-YSWQLSLILIV-LAPIVSVAIRVVSKRfRNISKNMQNTMGQVTTSAEQM 210
Cdd:cd18582 106 RGIEFLLRFLLFNILPTILELLLVCGILWYlYGWSYALITLVtVALYVAFTIKVTEWR-TKFRREMNEADNEANAKAVDS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 211 LKGHKEVLMFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSS 290
Cdd:cd18582 185 LLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTY 264
|
250
....*....|.
gi 488987387 291 MIALMRPLKSL 301
Cdd:cd18582 265 LLQLYQPLNFL 275
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-567 |
1.61e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTI----ASLITRFYDVdEGQILLDGHDLREYklsSLRDQVALVSQN-VHLFNDTV 433
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTLllalAGKLDPSLKV-SGEITYNGYRLNEF---VPRKTSAYISQNdVHVGVMTV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 434 ANNIAY-ARTEE--YSREQIEEAARM-----------------AYAM---------DFINK---MDNGLDTIIGENGVM- 480
Cdd:PLN03140 257 KETLDFsARCQGvgTRYDLLSELARRekdagifpeaevdlfmkATAMegvksslitDYTLKilgLDICKDTIVGDEMIRg 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS----TIEQADEIVVVEDGRI 556
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQI 416
|
250
....*....|.
gi 488987387 557 VERGTHHDLLE 567
Cdd:PLN03140 417 VYQGPRDHILE 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
355-565 |
1.64e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 355 EVAALRNINLDIPEGKTVALVGRSGSGKSTiASLITRFYDVDEGQilldghdlREYKLSSLrdqvalvSQNVHLFNDTVA 434
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR--------RPWRF*TW-------CANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 435 NN--IAYARTEEYS-REQIEEAARM---------AYAMDFINKMDngLDTIIGENGVMLSGGQRQRIAIARALLRNSPIL 502
Cdd:NF000106 89 *HrpVR*GRRESFSgRENLYMIGR*ldlsrkdarARADELLERFS--LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488987387 503 ILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGTHHDL 565
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
480-546 |
1.94e-04 |
|
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: 42.84 E-value: 1.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488987387 480 MLSGGQRQRIAIAR--ALLR--NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQAD 546
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvrPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
358-558 |
2.02e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 358 ALRNINLDIPEGKTVALVGRSGSGKSTIASLITRFYDVDEGQILLDGHDLREYK-LSSLRDQVALVSQ---------NVH 427
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEerrstgiyaYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 428 L-FNDTVANNIAY-ARTEEYSREQIEEAARmaYAMDFINKMDNGLDTIIGEngvmLSGGQRQRIAIARALLRNSPILILD 505
Cdd:PRK10982 343 IgFNSLISNIRNYkNKVGLLDNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488987387 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGR---IVE 558
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMpELLGITDRILVMSNGLvagIVD 474
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
69-236 |
2.43e-04 |
|
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: 43.30 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 69 LVVIGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSaLITVVR 148
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQS-FLFILS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 149 EGASIIGLFVMMFYYSWQLSLIL-IVLAPIVSVAIRVVSKRFRN---ISKNMQNTMGQVTTSAeqmLKGHKEVLMFGGQE 224
Cdd:cd18553 137 EIFVILFIYSLLLYVNWKITLVLtLFLGLNVFFITKIVSKKIKKqgkKREESQKKFYKILSET---FGNFKIIKLKSNEK 213
|
170
....*....|..
gi 488987387 225 VETKRFDKVSNK 236
Cdd:cd18553 214 EILKNFSQASLK 225
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-386 |
2.61e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 2.61e-04
10 20
....*....|....*....|....*...
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIA 386
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSLA 43
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-386 |
2.93e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 2.93e-04
10 20
....*....|....*....|....*...
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIA 386
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
72-178 |
3.41e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 42.85 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 72 IGLMVLRGITSYISSYCISWVSGKVVMTMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGA 151
Cdd:cd18606 42 AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLS 121
|
90 100
....*....|....*....|....*..
gi 488987387 152 SIIGLFVMMFYYswqLSLILIVLAPIV 178
Cdd:cd18606 122 SIIGTFILIIIY---LPWFAIALPPLL 145
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
359-386 |
4.44e-04 |
|
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: 43.46 E-value: 4.44e-04
10 20
....*....|....*....|....*...
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKSTIA 386
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-384 |
4.58e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 4.58e-04
10 20
....*....|....*....|....*.
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKST 384
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKST 650
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
346-546 |
6.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 346 NVTFTYPGREVaaLRNINLDIPEGKTVALVGRSGSGKSTIASLIT----RFYDVD---------EGQILLDghdlreykl 412
Cdd:PRK10938 265 NGVVSYNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYSNDltlfgrrrgSGETIWD--------- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 413 ssLRDQVALVSQNVHL---FNDTVANNIAYARTEEYSREQIEEAARMAYAMDFINKMdnGLDTIIGENGVM-LSGGQrQR 488
Cdd:PRK10938 334 --IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWGQ-QR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488987387 489 IA-IARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLV------------IAHRLSTIEQAD 546
Cdd:PRK10938 409 LAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
54-193 |
1.31e-03 |
|
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: 40.98 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 54 DGFGKTDRSVLLWMPLVVIGLMVLRGITSYISSYCISWVsgkvvmtMRRRLFGHMMGMPVAFFDKQSTGTLLSRITYDSE 133
Cdd:cd18605 38 NDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARR-------LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVY 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 134 QVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIvsvaIRVVSKRFRNIS 193
Cdd:cd18605 111 TIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFI----YYRIQRYYRATS 166
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
364-537 |
1.58e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 364 LDIPEGkTVALVGRSGSGKSTIASLIT-------RFYDVDEGQILLDG-----------HDLREYKLSslRDQ------- 418
Cdd:COG0419 19 IDFDDG-LNLIVGPNGAGKSTILEAIRyalygkaRSRSKLRSDLINVGseeasvelefeHGGKRYRIE--RRQgefaefl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 419 -------VALVSQnvhLFNDTVANNIA--YARTEEYSREQIEEAARMAYAMDFINKMDNGLDTIigengVMLSGGQRQRI 489
Cdd:COG0419 96 eakpserKEALKR---LLGLEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488987387 490 AIARALLrnspiLILDeaTSALDTESERAIQAALDELQknrtslVIAH 537
Cdd:COG0419 168 ALADLLS-----LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| PRK05537 |
PRK05537 |
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase; |
331-414 |
1.81e-03 |
|
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
Pssm-ID: 180124 [Multi-domain] Cd Length: 568 Bit Score: 41.20 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 331 GTRVIERAKGNLKFENvTFTYPgrEVAA-LRNinlDIP----EGKTVALVGRSGSGKSTIA-SLITRFYDVDEGQI-LLD 403
Cdd:PRK05537 355 GTELRRRLREGLEIPE-WFSFP--EVVAeLRR---TYPprhkQGFTVFFTGLSGAGKSTIAkALMVKLMEMRGRPVtLLD 428
|
90
....*....|.
gi 488987387 404 GHDLREYkLSS 414
Cdd:PRK05537 429 GDVVRKH-LSS 438
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
481-549 |
2.11e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488987387 481 LSGGQRQRIAIARALLRNSP---ILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
475-552 |
3.49e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 475 GENGVMLSGGQRQRIAIARAL----LRNSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTIEQADEIV 549
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQfIVITLKKEMFENADKLI 168
|
...
gi 488987387 550 VVE 552
Cdd:cd03239 169 GVL 171
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-384 |
4.23e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.23e-03
10 20
....*....|....*....|....*.
gi 488987387 359 LRNINLDIPEGKTVALVGRSGSGKST 384
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKST 646
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
481-557 |
4.75e-03 |
|
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: 40.04 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 LSGGQRQRIAIARA----LLRNSPILILDEATSALD-TESERAIQaALDELQKNRTSLVIAHRLSTIEQADEIVVV---E 552
Cdd:TIGR02168 1090 LSGGEKALTALALLfaifKVKPAPFCILDEVDAPLDdANVERFAN-LLKEFSKNTQFIVITHNKGTMEVADQLYGVtmqE 1168
|
....*..
gi 488987387 553 DG--RIV 557
Cdd:TIGR02168 1169 KGvsKIV 1175
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
481-569 |
5.39e-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: 39.61 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 481 LSGGQRQRIAIARALlrNSP----ILILDEATSAL---DTesERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVV--- 550
Cdd:TIGR00630 489 LSGGEAQRIRLATQI--GSGltgvLYVLDEPSIGLhqrDN--RRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDigp 564
|
90 100
....*....|....*....|..
gi 488987387 551 ---VEDGRIVERGTHHDLLEHK 569
Cdd:TIGR00630 565 gagEHGGEVVASGTPEEILANP 586
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
373-537 |
7.33e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.02 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 373 ALVGRSGSGKSTIASLITrfydvdegqILLDGHDLREYKLSSLRDQVALVSQNVHLFNDTVANNIAYarteeysreQIEE 452
Cdd:cd03279 32 LICGPTGAGKSTILDAIT---------YALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQLGGKKY---------RVER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 453 AARMAYAmDFINKM---DNGLDTIIGENGVMLSGGQRQRIAIARAL-----LRNSP-----ILILDEATSALDTESERAI 519
Cdd:cd03279 94 SRGLDYD-QFTRIVllpQGEFDRFLARPVSTLSGGETFLASLSLALalsevLQNRGgarleALFIDEGFGTLDPEALEAV 172
|
170
....*....|....*....
gi 488987387 520 QAALDELQ-KNRTSLVIAH 537
Cdd:cd03279 173 ATALELIRtENRMVGVISH 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
466-572 |
7.50e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 7.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488987387 466 MDNGLDTI-IGENGVMLSGGQRQRIAIARALLRNSP---ILILDEATSAL---DteseraIQAALDELQK-----NrTSL 533
Cdd:COG0178 811 QDVGLGYIkLGQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhD------IRKLLEVLHRlvdkgN-TVV 883
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488987387 534 VIAHRLSTIEQADEIVvveD---------GRIVERGTHHDLLEHKGVY 572
Cdd:COG0178 884 VIEHNLDVIKTADWII---DlgpeggdggGEIVAEGTPEEVAKVKASY 928
|
|
| |
