|
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: 1297.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGI 80
Cdd:PRK11176 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 81 TSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
Cdd:PRK11176 81 TSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 161 FYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQ 240
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFT 320
Cdd:PRK11176 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 321 ILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI 400
Cdd:PRK11176 321 ILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 401 LMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERG 560
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
570 580
....*....|....*....|..
3B5W_D 561 THNDLLEHRGVYAQLHKMQFGQ 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: 946.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 12 TFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISW 91
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 92 VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIIL 171
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 172 IVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSIS 251
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 252 DPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEG 331
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 332 KRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT 411
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 412 LASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGV 571
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
570
....*....|.
3B5W_D 572 YAQLHKMQFGQ 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: 677.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 8 STWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSY 87
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL 167
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 168 SIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSA 247
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 248 SSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQE 327
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 328 KDE--GKRVIERATGDVEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH 405
Cdd:COG1132 324 IPDppGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 406 DLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
3B5W_D 566 LEHRGVYAQLHKMQFGQ 582
Cdd:COG1132 562 LARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-579 |
5.24e-174 |
|
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: 509.76 E-value: 5.24e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 12 TFRRLWPTIAPFKAGLI-VAGVALILNaasdtfMLSLLKPLL-----DDGFGKTDRSVLVWMPLVVIGLMILRGITSYVS 85
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLqVLLASLLIN------LLALATPLFtqvviDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 86 SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSW 165
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 166 QLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMV 245
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 246 SASSISDPIIQLIASLALAFVLYAASFpSVMD-SLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFTILD 323
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAY-LVIDgQLTLGQL-IAFNILSGrFLAPVAQLIGLLQRFQDAKIALERLDDILD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 324 SEQEKDEGKRVIERAT--GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL 401
Cdd:COG2274 454 LPPEREEGRSKLSLPRlkGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 402 MDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLL 481
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD-PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGT 561
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
570
....*....|....*...
3B5W_D 562 HNDLLEHRGVYAQLHKMQ 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 |
6.97e-148 |
|
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: 425.49 E-value: 6.97e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLH 576
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-580 |
6.02e-141 |
|
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: 420.65 E-value: 6.02e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 14 RRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVS 93
Cdd:TIGR02204 7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIV 173
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 174 LAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDP 253
Cdd:TIGR02204 167 AVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 254 IIQLIASLALAFVLYAASFPSVMDSLTAGTIT-VVFSSMIALMrPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDE-- 330
Cdd:TIGR02204 247 IVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGqFVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKApa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 331 -GKRVIERATGDVEFRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR 408
Cdd:TIGR02204 326 hPKTLPVPLRGEIEFEQVNFAYPARpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 409 EYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|..
3B5W_D 569 RGVYAQLHKMQF 580
Cdd:TIGR02204 565 GGLYARLARLQF 576
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
6-579 |
8.89e-132 |
|
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: 398.04 E-value: 8.89e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 6 DLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDrsVLVWMPlvvIGLMILRGITSYVS 85
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAA--ALLVVP---VGLLLAYGLLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 86 SYCISW---VSGKVVM-TMRR---RLFGHMMGMPVSF-FDKQSTGtlLSRityDSEQvASSSSGALI---------TVVr 148
Cdd:COG5265 92 VLFGELrdaLFARVTQrAVRRlalEVFRHLHALSLRFhLERQTGG--LSR---DIER-GTKGIEFLLrfllfnilpTLL- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 149 EGASIIGlfIMMFYYSWQLS-IILIVLAPIVSIAIRVVSKRFRnISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:COG5265 165 EIALVAG--ILLVKYDWWFAlITLVTVVLYIAFTVVVTEWRTK-FRREMNEADSEANTRAVDSLLNYETVKYFGNEAREA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 228 KRFDKvsNRMRLQGMKMVSASSISD-PIIQ-LIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVN 305
Cdd:COG5265 242 RRYDE--ALARYERAAVKSQTSLALlNFGQaLIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 306 AQFQRGMAACQTLFTILDSEQE-KD-EGKRVIERATGDVEFRNVTFTY-PGRdvPALRNINLKIPAGKTVALVGRSGSGK 382
Cdd:COG5265 320 REIRQALADMERMFDLLDQPPEvADaPDAPPLVVGGGEVRFENVSFGYdPER--PILKGVSFEVPAGKTVAIVGPSGAGK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 383 STIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDF 462
Cdd:COG5265 398 STLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDA-SEEEVEAAARAAQIHDF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 463 INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTI 542
Cdd:COG5265 477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556
|
570 580 590
....*....|....*....|....*....|....*..
3B5W_D 543 EKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:COG5265 557 VDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-570 |
3.01e-129 |
|
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: 389.89 E-value: 3.01e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 14 RRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGF-GKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWV 92
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILI 172
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 173 VLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISD 252
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 253 PIIQLIASLALAFVLYAASFpsvmdSLTAGTITVvFSSMIALM------RPLKSLtnvNAQF---QRGMAACQTLFTILD 323
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGF-----RLLGGSLTL-FAALFVLLlapeffLPLRDL---GSFYharANGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 324 S-EQEKDEGKRVIERATG-DVEFRNVTFTYPGRDvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL 401
Cdd:COG4988 317 ApEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 402 MDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLL 481
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD-ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGT 561
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
3B5W_D 562 HNDLLEHRG 570
Cdd:COG4988 555 HEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
342-579 |
2.49e-125 |
|
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: 368.02 E-value: 2.49e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVA 420
Cdd:cd03249 1 IEFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
95-577 |
5.88e-117 |
|
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: 358.69 E-value: 5.88e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 95 KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQ-------VASSSSGALITvvregasIIGLFIMMFYYSWQL 167
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAldnlylrVLLPLLVALLV-------ILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 168 SIILIVLAPIVSIAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVS 246
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLgRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 247 ASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSE- 325
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPp 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 326 QEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH 405
Cdd:COG4987 318 AVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGV 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 406 DLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
Cdd:COG4987 398 DLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLAR-PDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEEL 556
|
490
....*....|..
3B5W_D 566 LEHRGVYAQLHK 577
Cdd:COG4987 557 LAQNGRYRQLYQ 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
72-575 |
7.36e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 362.89 E-value: 7.36e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSSY----CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVV 147
Cdd:TIGR00958 204 IFFMCLLSIASSVSAGlrggSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 148 REGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 228 KRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 308 FQRGMAACQTLFTILDSE-QEKDEGKRVIERATGDVEFRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTI 385
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 386 ASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTeQYSREQIEEAARMAYAMDFINK 465
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLT-DTPDEEIMAAAKAANAHDFIME 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAalDELQKNRTSLVIAHRLSTIEKA 545
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
490 500 510
....*....|....*....|....*....|
3B5W_D 546 DEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:TIGR00958 681 DQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-579 |
4.11e-113 |
|
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: 336.51 E-value: 4.11e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVA 420
Cdd:cd03253 1 IEFENVTFAYdPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDA-TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
27-316 |
2.01e-107 |
|
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: 324.38 E-value: 2.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
3B5W_D 267 LYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 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 |
3.71e-105 |
|
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: 316.09 E-value: 3.71e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYpGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRG 570
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-580 |
3.86e-98 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 310.35 E-value: 3.86e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 101 RRRL------FGHMMGMPVSFFDKQSTGTLLSRITydseQVASSSSGALITVVREG-ASIIGLFIMM---FYYSWQLSII 170
Cdd:PRK13657 86 RRRLavlteyFERIIQLPLAWHSQRGSGRALHTLL----RGTDALFGLWLEFMREHlATLVALVVLLplaLFMNWRLSLV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 171 LIVLAPIVSIAIRVVSKRfrniSKNMQNTM-GQVTTSAEQMLKGHKEVLI---FGGQEVETKRFDKVSNRMR------LQ 240
Cdd:PRK13657 162 LVVLGIVYTLITTLVMRK----TKDGQAAVeEHYHDLFAHVSDAIGNVSVvqsYNRIEAETQALRDIADNLLaaqmpvLS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTagtiTVVFSSMiaLMRPLKSLTN-VNAQFQRGmAACQTLF 319
Cdd:PRK13657 238 WWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVA----FVGFATL--LIGRLDQVVAfINQVFMAA-PKLEEFF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 320 TILDSEQEKDE--GKRVIERATGDVEFRNVTFTYPGRDvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDE 397
Cdd:PRK13657 311 EVEDAVPDVRDppGAIDLGRVKGAVEFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 398 GEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGEN 477
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDA-TDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIV 557
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
490 500
....*....|....*....|...
3B5W_D 558 ERGTHNDLLEHRGVYAQLHKMQF 580
Cdd:PRK13657 549 ESGSFDELVARGGRFAALLRAQG 571
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
62-581 |
7.16e-97 |
|
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: 310.14 E-value: 7.16e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 62 SVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSG 141
Cdd:TIGR01846 176 STLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTG 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 142 ALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFG 221
Cdd:TIGR01846 255 SALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATA 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 222 GQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTItVVFSsMIA--LMRPLK 299
Cdd:TIGR01846 335 TEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQL-VAFN-MLAgrVTQPVL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 300 SLTNVNAQFQRGMAACQTLFTILDSEQE-KDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRS 378
Cdd:TIGR01846 413 RLAQLWQDFQQTGIALERLGDILNSPTEpRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPS 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 379 GSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTeQYSREQIEEAARMAY 458
Cdd:TIGR01846 493 GSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNP-GAPFEHVIHAAKLAG 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
Cdd:TIGR01846 572 AHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHR 651
|
490 500 510 520
....*....|....*....|....*....|....*....|...
3B5W_D 539 LSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQFG 581
Cdd:TIGR01846 652 LSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-575 |
5.83e-96 |
|
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: 308.03 E-value: 5.83e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 25 AGLIVAGVALILNAASDTFM--------LSLLKPLLddgfgktdrsvlvwmpLVVIGLMILRGITSYVSSYCISWVSGKV 96
Cdd:TIGR03796 162 AGLLLVLPGLVIPAFSQIFVdeilvqgrQDWLRPLL----------------LGMGLTALLQGVLTWLQLYYLRRLEIKL 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 97 VMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDsEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAP 176
Cdd:TIGR03796 226 AVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 177 IVSIAIRVVSKRFRNISKNMQNTMGQVTTSAeqmlkghkevlIFGGQEVETKR--------FDKVSN---RMRLQGMKMV 245
Cdd:TIGR03796 305 INVLALQLVSRRRVDANRRLQQDAGKLTGVA-----------ISGLQSIETLKasglesdfFSRWAGyqaKLLNAQQELG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 246 SASSISDPIIQLIASLALAFVLYAASFpSVMD-SLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDS 324
Cdd:TIGR03796 374 VLTQILGVLPTLLTSLNSALILVVGGL-RVMEgQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRN 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 325 EQEKDEGKRVI--------ERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID 396
Cdd:TIGR03796 453 PVDPLLEEPEGsaatseppRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPW 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 397 EGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIA-YARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIG 475
Cdd:TIGR03796 533 SGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTlWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELA 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIEKADEIVVVEDGV 555
Cdd:TIGR03796 611 EGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLERGK 688
|
570 580
....*....|....*....|
3B5W_D 556 IVERGTHNDLLEHRGVYAQL 575
Cdd:TIGR03796 689 VVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-554 |
1.55e-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: 281.19 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVANNIayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
3B5W_D 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDG 554
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-579 |
3.07e-91 |
|
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: 280.53 E-value: 3.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVANNIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03252 81 VLQENVLFNRSIRDNIALAD-PGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
29-551 |
5.84e-89 |
|
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: 284.56 E-value: 5.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 29 VAGVALILNAAsdtfmlsLLKPLLDD-GFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGH 107
Cdd:TIGR02857 14 LGALLIIAQAW-------LLARVVDGlISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 108 MMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegASIIGLFIM--MFYYSWQLSIILIVLAPIVSIAIRVV 185
Cdd:TIGR02857 87 VAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVL--AVIVPLAILaaVFPQDWISGLILLLTAPLIPIFMILI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 186 SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAF 265
Cdd:TIGR02857 165 GWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVAL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 266 VLYAASFpsvmdSLTAGTITVVFSSMIALMRP--LKSLTNVNAQF---QRGMAACQTLFTILDS-EQEKDEGKRVIERAT 339
Cdd:TIGR02857 245 VAVYIGF-----RLLAGDLDLATGLFVLLLAPefYLPLRQLGAQYharADGVAAAEALFAVLDAaPRPLAGKAPVTAAPA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:TIGR02857 320 SSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAENIRLARPDA-SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVV 551
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-579 |
2.31e-88 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 285.07 E-value: 2.31e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 13 FRRLWPTI-------APFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVV--IGLMILRGITSY 83
Cdd:PRK10790 4 FSQLWPTLkrllaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayVGLQLLAAGLHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 84 VSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
Cdd:PRK10790 84 AQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 164 SWQLSIILIVLAPIVSIaIRVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN-----RM 237
Cdd:PRK10790 164 DWRMALVAIMIFPAVLV-VMVIYQRYSTpIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRshymaRM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 238 ---RLQGMKMvsassisDPIIQLIASLALAFVLYAASFPSVmdsltaGTITV-VFSSMIA----LMRPLKSLTNVNAQFQ 309
Cdd:PRK10790 243 qtlRLDGFLL-------RPLLSLFSALILCGLLMLFGFSAS------GTIEVgVLYAFISylgrLNEPLIELTTQQSMLQ 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 310 RGMAACQTLFTILDSEQEkDEGKRVIERATGDVEFRNVTFTYpGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLI 389
Cdd:PRK10790 310 QAVVAGERVFELMDGPRQ-QYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 390 TRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARteQYSREQIEEAARMAYAMDFINKMDNG 469
Cdd:PRK10790 388 MGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR--DISEEQVWQALETVQLAELARSLPDG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIV 549
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTIL 545
|
570 580 590
....*....|....*....|....*....|
3B5W_D 550 VVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-579 |
9.74e-85 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 274.67 E-value: 9.74e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 44 MLSLLKPLLD----DGF---GKTDRSVLVWmplvvIGLMILRGITSYVSSYCisW------VSGKVVMTMRRRLFGHMMG 110
Cdd:PRK10789 9 MLQLIPPKVVgiivDGVteqHMTTGQILMW-----IGTMVLIAVVVYLLRYV--WrvllfgASYQLAVELREDFYRQLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 111 MPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRE---GASIigLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSK 187
Cdd:PRK10789 82 QHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmGCAV--LIVMSTQISWQLTLLALLPMPVMAIMIKRYGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 268 YAASFPSVMDSLTAGTIT---VVFSSMIALMRPLKSLTNVnaqFQRGMAACQTLFTILDSEQEKDEGKRVI--ERATGDV 342
Cdd:PRK10789 240 GGGSWMVVNGSLTLGQLTsfvMYLGLMIWPMLALAWMFNI---VERGSAAYSRIRAMLAEAPVVKDGSEPVpeGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRnvTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:PRK10789 317 NIR--QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
Cdd:PRK10789 395 SQTPFLFSDTVANNIALGRPDA-TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-576 |
5.52e-83 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 270.16 E-value: 5.52e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 151 ASIIGLFIMMFYYSW---QLSIIL--IVLApiVSIAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQE 224
Cdd:PRK11160 143 AALVVILVLTIGLSFfdlTLALTLggILLL--LLLLLPLLFYRLgKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAED 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 225 VETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMDSLTAGTIT--VVFSSMIALmrplKSLT 302
Cdd:PRK11160 221 RYRQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAG-GVGGNAQPGALIalFVFAALAAF----EALM 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 303 NVNAQFQ---RGMAACQTLFTILdsEQEKD---EGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVG 376
Cdd:PRK11160 296 PVAGAFQhlgQVIASARRINEIT--EQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 377 RSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYArTEQYSREQIEEAAR- 455
Cdd:PRK11160 374 RTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA-APNASDEALIEVLQq 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 456 --MAYAMDfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
Cdd:PRK11160 453 vgLEKLLE----DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVL 528
|
410 420 430 440
....*....|....*....|....*....|....*....|...
3B5W_D 534 VIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLH 576
Cdd:PRK11160 529 MITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-579 |
7.72e-82 |
|
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: 270.29 E-value: 7.72e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 4 DKDLSTWQTFRrlwptiapFKAGLIVAGVALILNAASDTFMLSLLKP-----LLDDGFGKTDRSVLVWMPLVVIGLMILR 78
Cdd:TIGR03797 118 DKALGLRDLLR--------FALRGARRDLLAILAMGLLGTLLGMLVPiatgiLIGTAIPDADRSLLVQIALALLAAAVGA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 79 GITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSR---ITYDSEQVASSSSGALITvvregaSIIG 155
Cdd:TIGR03797 190 AAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRamgISQIRRILSGSTLTTLLS------GIFA 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 156 LF--IMMFYYSWQLSIILIVLApIVSIAIRVVSKrFRNISKN--MQNTMGQVTTSAEQMLKGHKEVLIFGGQE----VET 227
Cdd:TIGR03797 264 LLnlGLMFYYSWKLALVAVALA-LVAIAVTLVLG-LLQVRKErrLLELSGKISGLTVQLINGISKLRVAGAENrafaRWA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 228 KRFDKvSNRMRLQGMKMVSASSISDPIIQLIASLALafvLYAASFPSVMDSLTAGTI---TVVFSSMIALMRPL-KSLTN 303
Cdd:TIGR03797 342 KLFSR-QRKLELSAQRIENLLTVFNAVLPVLTSAAL---FAAAISLLGGAGLSLGSFlafNTAFGSFSGAVTQLsNTLIS 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 304 VNA---QFQRgmaaCQTlftILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGS 380
Cdd:TIGR03797 418 ILAvipLWER----AKP---ILEALPEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGS 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 381 GKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYAM 460
Cdd:TIGR03797 491 GKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA--GGAPLTLDEAWEAARMAGLA 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRtsLVIAHRLS 540
Cdd:TIGR03797 569 EDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLS 646
|
570 580 590
....*....|....*....|....*....|....*....
3B5W_D 541 TIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHKMQ 579
Cdd:TIGR03797 647 TIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
340-556 |
2.52e-80 |
|
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: 252.01 E-value: 2.52e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQ 418
Cdd:cd03248 10 GIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFNDTVANNIAYARTeQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQ-SCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVI 556
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
98-577 |
2.61e-75 |
|
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: 250.58 E-value: 2.61e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 98 MTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEqvasSSSGALITVVREG-ASIIGLFIMM---FYYSWQLSIILIV 173
Cdd:TIGR01192 89 ATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATE----TLFGLWLEFMRQHlATFVALFLLIptaFAMDWRLSIVLMV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 174 LAPIVSIAIRVVSKRFRN----ISKNMQNTMGQVTTSAEQMLKGHKEVLIfggqEVETKRFDKVSNRMRLQGMKMVSASS 249
Cdd:TIGR01192 165 LGILYILIAKLVMQRTKNgqaaVEHHYHNVFKHVSDSISNVSVVHSYNRI----EAETSALKQFTNNLLSAQYPVLDWWA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 250 ISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKD 329
Cdd:TIGR01192 241 LASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQRE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 330 E--GKRVIERATGDVEFRNVTFTYPGRDvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL 407
Cdd:TIGR01192 321 EpaDAPELPNVKGAVEFRHITFEFANSS-QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 408 REYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGA-TDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:TIGR01192 479 RLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQ 558
|
490
....*....|
3B5W_D 568 HRGVYAQLHK 577
Cdd:TIGR01192 559 KDGRFYKLLR 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-560 |
5.84e-75 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 237.87 E-value: 5.84e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERG 560
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-561 |
1.90e-71 |
|
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: 228.53 E-value: 1.90e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGT 561
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
27-314 |
2.68e-68 |
|
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: 222.81 E-value: 2.68e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
3B5W_D 267 LYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
69-575 |
1.26e-65 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 227.31 E-value: 1.26e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 69 LVVIGLM---ILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALIT 145
Cdd:TIGR01193 197 IISIGLIiayIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILS 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 146 VVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEV 225
Cdd:TIGR01193 276 LFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 226 ETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTItVVFSSMIA-LMRPLKSLTNV 304
Cdd:TIGR01193 356 RYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQL-ITFNALLSyFLTPLENIINL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 305 NAQFQRGMAACQTLFTILDSEQEKDEGKRVIERAT--GDVEFRNVTFTYpGRDVPALRNINLKIPAGKTVALVGRSGSGK 382
Cdd:TIGR01193 435 QPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNlnGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 383 STIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDF 462
Cdd:TIGR01193 514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDD 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 463 INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQkNRTSLVIAHRLSTI 542
Cdd:TIGR01193 594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVA 672
|
490 500 510
....*....|....*....|....*....|...
3B5W_D 543 EKADEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:TIGR01193 673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
279-568 |
3.32e-65 |
|
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: 222.70 E-value: 3.32e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 279 LTAGTItvvFSSMIALMR---PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRvIERATGDVEFRNVTFTYPGRD 355
Cdd:COG4618 269 ITPGAM---IAASILMGRalaPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMP-LPRPKGRLSVENLTVVPPGSK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 356 VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVAN 435
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 436 NIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:COG4618 425 NIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 516 ERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:COG4618 503 EAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
79-539 |
2.94e-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: 219.54 E-value: 2.94e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 79 GITSYVSSYCISWVSGKVVMT----MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASII 154
Cdd:TIGR02868 63 GIGRAVFRYLERLVGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 155 GLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233
Cdd:TIGR02868 143 AAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAaRAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 234 SNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASfPSVMD-SLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGM 312
Cdd:TIGR02868 223 DRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGG-PAVADgRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVR 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 313 AACQTLFTILDSEQEKDEGkrVIERATG------DVEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIA 386
Cdd:TIGR02868 302 AAAERIVEVLDAAGPVAEG--SAPAAGAvglgkpTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGKSTLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 387 SLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARTEQySREQIEEAARMAYAMDFINKM 466
Cdd:TIGR02868 379 ATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA-TDEELWAALERVGLADWLRAL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:TIGR02868 458 PDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-565 |
2.35e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 220.29 E-value: 2.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 8 STWQTFRRL----WPTIAPFKAG-------LIVAGVALILNAASDTFMLSLLKPLLDD-GFGKTDRSVLvwMPLVVIGlm 75
Cdd:PTZ00265 32 GTFELYKKIktqkIPFFLPFKCLpashrklLGVSFVCATISGGTLPFFVSVFGVIMKNmNLGENVNDII--FSLVLIG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 76 ILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIG 155
Cdd:PTZ00265 108 IFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 156 LFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRnISKNM-----QNTMGQVttsaEQMLKGHKEVLIFGGQEVETKRF 230
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-INKKTsllynNNTMSII----EEALVGIRTVVSYCGEKTILKKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 231 DKVSnrmRLQGMKMVSASSISDPIIQLIASLALAFvlYAASF----PSVMDSLT----------AGTITVVFSSMIALMR 296
Cdd:PTZ00265 263 NLSE---KLYSKYILKANFMESLHIGMINGFILAS--YAFGFwygtRIIISDLSnqqpnndfhgGSVISILLGVLISMFM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 297 PLKSLTNVNaQFQRGMAACQTLFTILDSE---QEKDEGKRVieRATGDVEFRNVTFTYPGR-DVPALRNINLKIPAGKTV 372
Cdd:PTZ00265 338 LTIILPNIT-EYMKSLEATNSLYEIINRKplvENNDDGKKL--KDIKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 373 ALVGRSGSGKSTIASLITRFYDIDEGEILM-DGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYA----RTEQYSR 447
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDLEALS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 448 EQIEE------------------------------------AARMAYAM----------------DFINKMDNGLDTVIG 475
Cdd:PTZ00265 495 NYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTikdsevvdvskkvlihDFVSALPDKYETLVG 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEKADEIVVVED 553
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
650
....*....|..
3B5W_D 554 GvivERGTHNDL 565
Cdd:PTZ00265 655 R---ERGSTVDV 663
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-575 |
2.42e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 213.17 E-value: 2.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 151 ASIIGLFIMM--FYYSWQLSIILIVLAPIVSIAIRVV------SKRfrnisKNMQnTMGQVttSAEQM--LKGHKEVLIF 220
Cdd:PRK11174 147 AVLVPLLILIavFPINWAAGLILLGTAPLIPLFMALVgmgaadANR-----RNFL-ALARL--SGHFLdrLRGLETLRLF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 221 GGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVlyAASFP-SVMDSLTAGT----ITVvFSSMIALM 295
Cdd:PRK11174 219 NRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASISIALV--AVYFGfSYLGELNFGHygtgVTL-FAGFFVLI 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 296 ------RPLKSL-TNVNAQFQrGMAACQTLFTILDSEQE--KDEGKRVIERATGDVEFRNVTFTYPGrDVPALRNINLKI 366
Cdd:PRK11174 296 lapefyQPLRDLgTFYHAKAQ-AVGAAESLVTFLETPLAhpQQGEKELASNDPVTIEAEDLEILSPD-GKTLAGPLNFTL 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 367 PAGKTVALVGRSGSGKSTIASLITRF--YdidEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQ 444
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN-PD 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 445 YSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD 524
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 525 ELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
27-298 |
2.32e-60 |
|
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: 201.33 E-value: 2.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGF--GKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRL 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 105 FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRV 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
3B5W_D 265 FVLYAASFPSVMDSLTAGTITVVFSSMIALMRPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-578 |
3.79e-57 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 207.96 E-value: 3.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 65 VWMPLVVIGLMILRGITSYVSSYciswVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDseqVASSSSGA 142
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNV----IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRD---VHLLKTGL 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 143 LITVVregasIIGLFIMMFYYSWQLS-----IILIVLAPIVSIAIRVVSKRFR-----NISKNMQNTMGQV--TTSAEQM 210
Cdd:PTZ00265 943 VNNIV-----IFTHFIVLFLVSMVMSfyfcpIVAAVLTGTYFIFMRVFAIRARltankDVEKKEINQPGTVfaYNSDDEI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 211 LK-----------GHKEVLIFGGQEVETKRFDK-VSNRMRLQGMKMVSASSI---SDPIIQLIASLALAFVLYAASFPSV 275
Cdd:PTZ00265 1018 FKdpsfliqeafyNMNTVIIYGLEDYFCNLIEKaIDYSNKGQKRKTLVNSMLwgfSQSAQLFINSFAYWFGSFLIRRGTI 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 276 -MDSLTAGTITVVFSSMIA--LMRPLKSLTNVNAQFQR--GMAACQTLFTILDSEQEKDEGKRVIEratGDVEFRNVTFT 350
Cdd:PTZ00265 1098 lVDDFMKSLFTFLFTGSYAgkLMSLKGDSENAKLSFEKyyPLIIRKSNIDVRDNGGIRIKNKNDIK---GKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 351 YPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDI---------------------------------- 395
Cdd:PTZ00265 1175 YISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 396 --------------------DEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQYSREQIEEAAR 455
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-EDATREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 456 MAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSL 533
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 534 VIAHRLSTIEKADEIVVVED----GVIVE-RGTHNDLLE-HRGVYAQLHKM 578
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-560 |
3.39e-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: 184.44 E-value: 3.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTlASLRNQVAL 421
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVANNIayarteqysreqieeaarmayamdfinkmdngldtvigenGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERG 560
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-568 |
4.63e-55 |
|
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: 195.26 E-value: 4.63e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 20 IAPFKAGLIVAGVAL----ILNAASDTFMLSLLKPLLDDGFGKTdrsvLVWMPLVVIGLMILRGITSYVSSYCISWVSGK 95
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSfvinILMLAPPLYMLQVYDRVLTSGSVPT----LLMLTVLALGLYLFLGLLDALRSFVLVRIGEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 96 VVMTMRRRLFGHMMGMPVSFFDKQSTGTLlsritYDSEQVAS-SSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVL 174
Cdd:TIGR01842 77 LDGALNQPIFAASFSATLRRGSGDGLQAL-----RDLDQLRQfLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 175 APIVSIAIrvVSKRF--RNISKNMQNTMgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMK------MVS 246
Cdd:TIGR01842 152 VVLVGLAL--LNNRAtkKPLKEATEASI-RANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAasdragMLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 247 ASSISDPIIQLIASLALAFVLyaasfpSVMDSLTAGTItvVFSSMIA--LMRPLKSLTNVNAQFQRGMAACQTLFTILDS 324
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLGAYL------AIDGEITPGMM--IAGSILVgrALAPIDGAIGGWKQFSGARQAYKRLNELLAN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 325 EQEKDEGKRvIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDG 404
Cdd:TIGR01842 301 YPSRDPAMP-LPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 405 HDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYARtEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG-ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEKADEIVVVEDGVIVERGTHN 563
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERD 538
|
....*
3B5W_D 564 DLLEH 568
Cdd:TIGR01842 539 EVLAK 543
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-554 |
4.95e-54 |
|
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: 182.67 E-value: 4.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQN--VHLFNDTVANNIAYA-RTEQYSREQIEEaaRMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:cd03225 81 FQNpdDQFFGPTVEEEVAFGlENLGLPEEEIEE--RVEEALELVG-LEGLRDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI-EKADEIVVVEDG 554
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-569 |
1.96e-53 |
|
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: 181.38 E-value: 1.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVH--LFNDTVANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRE--RVEEALELV-----GLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEHR 569
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-315 |
1.97e-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: 181.05 E-value: 1.97e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGF--GKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRL 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 105 FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRV 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 265 FVLYAASFPSVMDSLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVL-YAFIQYIQrFFRPIRDLAEKFNILQSAMASA 291
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
4.80e-52 |
|
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: 186.26 E-value: 4.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR---DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT---LASL 415
Cdd:COG1123 261 LEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQVALVSQN-VHLFN--DTVANNIAYA--RTEQYSREQIEEaaRMAYAMDFInkmdnGLDT-VIGENGVLLSGGQRQRI 489
Cdd:COG1123 341 RRRVQMVFQDpYSSLNprMTVGDIIAEPlrLHGLLSRAERRE--RVAELLERV-----GLPPdLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
..
3B5W_D 567 EH 568
Cdd:COG1123 494 AN 495
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
27-314 |
1.42e-51 |
|
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: 178.75 E-value: 1.42e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDD------GFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTM 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 101 RRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSI 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 181 AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 261 LALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAG 294
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
70-577 |
1.65e-51 |
|
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: 191.31 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 70 VVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRE 149
Cdd:TIGR00957 1010 VYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGS 1089
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 150 GASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEvetkR 229
Cdd:TIGR00957 1090 LFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQE----R 1165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 230 FDKVSNRMRLQGMKMVSASSISDPIIQL-IASLALAFVLYAASFPSV-MDSLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:TIGR00957 1166 FIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSE 1245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 308 FQRGMAACQTLFTIldSEQEKDEGKRVIERA-------TGDVEFRNVTFTY-PGRDVpALRNINLKIPAGKTVALVGRSG 379
Cdd:TIGR00957 1246 METNIVAVERLKEY--SETEKEAPWQIQETAppsgwppRGRVEFRNYCLRYrEDLDL-VLRHINVTIHGGEKVGIVGRTG 1322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 380 SGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYA 459
Cdd:TIGR00957 1323 AGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD--PFSQYSDEEVWWALELAHL 1400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 460 MDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:TIGR00957 1401 KTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRL 1480
|
490 500 510
....*....|....*....|....*....|....*...
3B5W_D 540 STIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQLHK 577
Cdd:TIGR00957 1481 NTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
343-556 |
6.32e-50 |
|
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: 170.09 E-value: 6.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNDTVANNIayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd03246 82 PQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 503 ILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEKADEIVVVEDGVI 556
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
343-556 |
1.12e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.77 E-value: 1.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:COG4619 2 ELEGLSFRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNDTVANNIAYA---RTEQYSREQIEEA-ARMAYAMDFinkmdngLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPfqlRERKFDRERALELlERLGLPPDI-------LDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 499 SPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-316 |
6.40e-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: 171.46 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
3B5W_D 267 LYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAE 290
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
1.64e-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: 173.55 E-value: 1.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID---EGEILMDGHDLREYTLASLRNQ 418
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQN--VHLFNDTVANNIAYA-RTEQYSREQIEEAARMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlENLGLSRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 496 LRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTI-EKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-561 |
2.00e-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: 162.20 E-value: 2.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 338 ATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRN 417
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARmayamdfinkmdngldtvIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGT 561
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-554 |
3.03e-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: 161.48 E-value: 3.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRD---VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITrfydideGEI-LMDGHdlreytlASLRN 417
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL-------GELeKLSGS-------VSVPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFNDTVANNIAYArtEQYSREQIEEAARmAYAMDF-INKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03250 67 SIAYVSQEPWIQNGTIRENILFG--KPFDEERYEKVIK-ACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 497 RDSPILILDEATSALDTESERAI--QAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDG 554
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-560 |
4.90e-46 |
|
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: 161.58 E-value: 4.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGEILMDGHDLRE--YTLAS 414
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQNVHLFNDTVANNIAYA------RTEQYSREQIEEAARMAYAMDFINKMDNGLDtvigengvlLSGGQRQR 488
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
7.25e-46 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 163.84 E-value: 7.25e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAAsdtfmLSLLKP--------------------LLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSS 86
Cdd:cd18564 1 LALALLALLLETA-----LRLLEPwplkvviddvlgdkplpgllGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 87 YCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQ 166
Cdd:cd18564 76 YLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 167 LSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVS 246
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAAR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 247 ASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18564 236 LQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAE 305
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-558 |
4.41e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 159.05 E-value: 4.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--GRDVPALRNINLKIPAGKTVALVGRSGSGKST---IASLITRFydiDEGEILMDGHD---LREYTLA 413
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDRP---TSGEVLIDGQDissLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQ-VALVSQNVHLFND-TVANNIAYARTeqYSREQIEEAARMAYAM-------DFINKMdngldtvIGEngvlLSGG 484
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVALPLL--LAGVSRKERRERARELlervglgDRLDHR-------PSQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEIVVVEDGVIVE 558
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
6.86e-45 |
|
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: 160.73 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 30 AGVALILNAAsdTFMLS--LLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGH 107
Cdd:cd18576 1 GLILLLLSSA--IGLVFplLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 108 MMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSK 187
Cdd:cd18576 79 LQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:cd18576 159 RIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3B5W_D 268 YAASFPSVMDSLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18576 239 WYGGRLVLAGELTAGDLVafLLYTLFIA--GSIGSLADLYGQLQKALGA 285
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
359-509 |
7.52e-45 |
|
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: 155.88 E-value: 7.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFND-TVANNI 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 438 AYARTEQYsREQIEEAARMAYAMDFINkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:pfam00005 81 RLGLLLKG-LSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
342-560 |
7.78e-45 |
|
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: 158.44 E-value: 7.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRD--VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLR 416
Cdd:cd03257 2 LEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQNVHL-FND--TVanniayarteqysREQIEEAARMAYAMD----FINKMDNGLDTVIGENGVL------LSG 483
Cdd:cd03257 82 KEIQMVFQDPMSsLNPrmTI-------------GEQIAEPLRIHGKLSkkeaRKEAVLLLLVGVGLPEEVLnrypheLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-568 |
1.77e-44 |
|
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: 157.74 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPG--RDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRN-- 417
Cdd:cd03258 2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 -QVALVSQNVHLFND-TVANNIAYA-RTEQYSREQIEEaaRMAYAMDFINKMDNGlDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:cd03258 82 rRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE--RVLELLELVGLEDKA-DAYPAQ----LSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-567 |
2.23e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 2.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAsLRNQVAL 421
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAY-ARTeqYSREQIEEAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFfARL--YGLPRKEARERIDELLELFG-LTDAADRKVGT----LSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEK-ADEIVVVEDGVIVERGTHNDLLE 567
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-554 |
1.18e-43 |
|
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: 152.78 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQnvhlfndtvanniayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 503 ILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKA-DEIVVVEDG 554
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-568 |
1.43e-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: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLF-NDTVANNIAYART-EQYSREQIEEAARMAYAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALVPKlLKWPKEKIRERADELLAL-----VGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-567 |
9.98e-43 |
|
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: 9.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:COG1127 6 IEVRNLTKSFGDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYARTE--QYSREQIEEAARMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRIAI 491
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPLREhtDLSEAEIRELVLEKLELvglpGAADKM-------PSE----LSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLE 567
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-560 |
1.65e-42 |
|
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: 151.52 E-value: 1.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLreYTLASLRNQVAL 421
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLF-NDTVANNIAYARTEQY-SREQIEEAARMAYAMdfiNKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGLKLRGvPKAEIRARVRELLEL---VGLEGLLNRYPHE----LSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEIVVVEDGVIVERG 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 |
1.85e-42 |
|
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: 151.87 E-value: 1.85e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRD--VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT---LASLR 416
Cdd:cd03255 1 IELKNLSKTYGGGGekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 N-QVALVSQNVHLFND-TVANNIAYArtEQYSREQIEEAARMAYAMdfINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03255 81 RrHIGFVFQSFNLLPDlTALENVELP--LLLAGVPKKERRERAEEL--LERV--GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEIVVVEDGVI 556
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
4.99e-42 |
|
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: 151.49 E-value: 4.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQN----VHLFNdTVANNIAYARTEQYSREQIEEAARMAYAMdfinkmdnGLDTvigenGVL------LSGGQRQRI 489
Cdd:COG1124 82 QMVFQDpyasLHPRH-TVDRILAEPLRIHGLPDREERIAELLEQV--------GLPP-----SFLdryphqLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLL 227
|
..
3B5W_D 567 EH 568
Cdd:COG1124 228 AG 229
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
343-570 |
1.22e-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: 150.39 E-value: 1.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAsLRNQVALV 422
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLF-NDTVANNIAY-ARTEQYSREQIEE-AARMAYAMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:COG4555 80 PDERGLYdRLTVRENIRYfAELYGLFDEELKKrIEELIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEHRG 570
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-568 |
1.94e-41 |
|
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: 150.66 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD-LREYTLASLRNQVA 420
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQN-----VhlfNDTVANNIAYA-------RTEQysREQIEEAARMAYAMDFINKmdngldtvigeNGVLLSGGQRQR 488
Cdd:TIGR04520 81 MVFQNpdnqfV---GATVEDDVAFGlenlgvpREEM--RKRVDEALKLVGMEDFRDR-----------EPHLLSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLL 566
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIF 224
|
..
3B5W_D 567 EH 568
Cdd:TIGR04520 225 SQ 226
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
1.97e-41 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 151.51 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDD----GFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRR 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAI 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 183 RVVSKRFRNI-------SKNMQNTMGQVttsaeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPII 255
Cdd:cd18563 161 YFFWKKIRRLfhrqwrrWSRLNSVLNDT-------LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 256 QLIASLALAFVLYAASfPSVM-DSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18563 234 TFLTSLGTLIVWYFGG-RQVLsGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAE 294
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
27-314 |
4.15e-41 |
|
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: 150.28 E-value: 4.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAAsdtfmLSLLKPLL-----DDGFGKtdrSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMR 101
Cdd:cd18551 1 LILALLLSLLGTA-----ASLAQPLLvknliDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 102 RRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIA 181
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 182 IRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
3B5W_D 262 ALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGA 285
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-568 |
1.15e-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: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:cd03261 1 IELRGLTKSFGGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYARTE--QYSREQIEEAARMAYAM----DFINKMDngldtviGEngvlLSGGQRQRIAI 491
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPLREhtRLSEEEIREIVLEKLEAvglrGAEDLYP-------AE----LSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
32-314 |
1.58e-40 |
|
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: 148.86 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 32 VALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRN 191
Cdd:cd18557 83 EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 192 ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAAS 271
Cdd:cd18557 163 LSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
3B5W_D 272 FPSVMDSLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18557 243 YLVLSGQLTVGELTsfILYTIMVA--SSVGGLSSLLADIMKALGA 285
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-313 |
3.08e-40 |
|
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: 148.01 E-value: 3.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLK--GHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
3B5W_D 265 FVLYAASFPSVMDSLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTL-VAFTALLGrLYGPLTQLLNIQVDLMTSLA 289
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-561 |
3.69e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 3.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLR 416
Cdd:COG1135 2 IELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQNVHLFND-TVANNIAYA-RTEQYSREQIEEaarmayamdfinKMDNGLDTVigenGvL----------LSGG 484
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEIRK------------RVAELLELV----G-LsdkadaypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEK-ADEIVVVEDGVIVER 559
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
..
3B5W_D 560 GT 561
Cdd:COG1135 223 GP 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-558 |
4.56e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.20 E-value: 4.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYA-RTEQYSREQIEEAARMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRIAIA 492
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlRVTGKSRKEIRRRVREVLDLvglsDKAKAL-------PHE----LSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEKADE-IVVVEDGVIVE 558
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-566 |
8.51e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.57 E-value: 8.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:COG1120 2 LEAENLSVGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHL-FNDTVANNIAYART------EQYS---REQIEEAARMAYAMDFINKMdngLDTvigengvlLSGGQRQRIAI 491
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRYphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-554 |
1.96e-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: 142.33 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAS--LRNQV 419
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLF-NDTVANNIAYArteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRD 498
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEK-ADEIVVVEDG 554
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
342-568 |
3.56e-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: 143.60 E-value: 3.56e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL--REYTLASLRNQV 419
Cdd:COG1126 2 IEIENLHKSF-G-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNIAYA--RTEQYSREQIEEAArMAYamdfinkmdngLDTVigenGVL---------LSGGQRQ 487
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApiKVKKMSKAEAEERA-MEL-----------LERV----GLAdkadaypaqLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH-----RlstiEKADEIVVVEDGVIVERGT 561
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHemgfaR----EVADRVVFMDGGRIVEEGP 219
|
....*..
3B5W_D 562 HNDLLEH 568
Cdd:COG1126 220 PEEFFEN 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-568 |
8.06e-39 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 146.01 E-value: 8.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 338 ATGDVEFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLrEYTLASLRN 417
Cdd:COG3842 2 AMPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 qVALVSQNVHLF-NDTVANNIAYA-RTEQYSREQIEEAARMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRIAI 491
Cdd:COG3842 79 -VGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRARVAELLELvgleGLADRY-------PHQ----LSGGQQQRVAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS---TIekADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIY 224
|
..
3B5W_D 567 EH 568
Cdd:COG3842 225 ER 226
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-550 |
1.08e-38 |
|
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: 141.46 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRD--VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlasLRNQV 419
Cdd:cd03293 1 LEVRNVSKTYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFN-DTVANNIAYA-RTEQYSREQIEEAARMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRIAIAR 493
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEELLELvglsGFENAY-------PHQ----LSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 494 ALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEIVV 550
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVV 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-556 |
1.29e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlasLRNQVAL 421
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND---TVANNIAYARTEQ------YSREQIEEAARmayAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDVVLMGRYGRrglfrrPSRADREAVDE---ALERVG-LEDLADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 493 RALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
27-314 |
1.46e-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: 143.38 E-value: 1.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
3B5W_D 267 LYAASFPSVMDSLTAGTItVVFSSMIALM-RPLKSLTNVNAQFQRGMAA 314
Cdd:cd18545 242 YWYGGKLVLGGAITVGVL-VAFIGYVGRFwQPIRNLSNFYNQLQSAMAS 289
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-575 |
3.05e-38 |
|
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: 141.58 E-value: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK--CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHR-GVYAQL 575
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASL 252
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
1.34e-37 |
|
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: 141.73 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRN--VTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYD---IDEGEILMDGHDLREYTLASLR 416
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 ----NQVALVSQN-------VHlfndTVanniayarteqysREQIEE----------AARMAYAMDFINKMdnGLDtviG 475
Cdd:COG0444 82 kirgREIQMIFQDpmtslnpVM----TV-------------GDQIAEplrihgglskAEARERAIELLERV--GLP---D 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 476 ENGVL------LSGGQRQRIAIARALLRDSPILILDEATSALD-TeseraIQAA----LDELQKNR-TSLV-IAHRLSTI 542
Cdd:COG0444 140 PERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELgLAILfITHDLGVV 214
|
250 260
....*....|....*....|....*..
3B5W_D 543 EK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:COG0444 215 AEiADRVAVMYAGRIVEEGPVEELFEN 241
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
27-314 |
2.18e-37 |
|
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: 140.24 E-value: 2.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAAsdtfmLSLLKPLL-----DD-GFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTM 100
Cdd:cd18541 1 YLLGILFLILVDL-----LQLLIPRIigraiDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 101 RRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSI 180
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 181 AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 261 LALAFVLYAASFPSVMDSLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAA 314
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDL-VAFNSYLGMLIwPMMALGWVINLIQRGAAS 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-570 |
2.47e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 148.73 E-value: 2.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 338 ATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRN 417
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLD--PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRG 570
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-556 |
2.55e-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: 135.99 E-value: 2.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTlASLRNQVAL 421
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIayarteqysreqieeaarmayamdfinkmdngldtvigengvLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03230 78 LPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
340-570 |
3.23e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 148.20 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQV 419
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PLN03232 1313 SIIPQSPVLFSGTVRFNID--PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRG 570
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
343-569 |
5.83e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 137.19 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvpALRnINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAslRNQVALV 422
Cdd:COG3840 3 RLDDLTYRYGDF---PLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFND-TVANNIAYAR-------TEQysREQIEEAARmayamdfinKMdnGLDtvigenGVL------LSGGQRQR 488
Cdd:COG3840 77 FQENNLFPHlTVAQNIGLGLrpglkltAEQ--RAQVEQALE---------RV--GLA------GLLdrlpgqLSGGQRQR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:COG3840 138 VALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
....
3B5W_D 566 LEHR 569
Cdd:COG3840 218 LDGE 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
342-567 |
1.10e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNV--HLFNDTVANNIAYA-RTEQYSREQ----IEEAARMAyamdfinKMDNGLDtvigENGVLLSGGQRQRIAIARA 494
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGlENKKVPPKKmkdiIDDLAKKV-------GMEDYLD----KEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA--HRLSTIEKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
343-560 |
1.61e-36 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 134.10 E-value: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:cd03214 1 EVENLSVGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNdtvanniayarTEQYSREQIEEaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd03214 79 PQALELLG-----------LAHLADRPFNE----------------------------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 503 ILDEATSALDTeserAIQAALDEL------QKNRTSLVIAHRLS-TIEKADEIVVVEDGVIVERG 560
Cdd:cd03214 120 LLDEPTSHLDI----AHQIELLELlrrlarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-557 |
2.00e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 136.34 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:COG3638 3 LELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNI-----AYARTEQ-----YSREQIEEAARMayamdfinkmdngLDTVigenGVL------- 480
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlGRTSTWRsllglFPPEDRERALEA-------------LERV----GLAdkayqra 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 --LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVEDGV 555
Cdd:COG3638 145 dqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
3B5W_D 556 IV 557
Cdd:COG3638 225 VV 226
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
51-313 |
2.16e-36 |
|
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: 137.58 E-value: 2.16e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 51 LLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITY 130
Cdd:cd18549 28 IIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 131 DSEQVASSSSGA----LITVVRegasIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTS 206
Cdd:cd18549 108 DLFDISELAHHGpedlFISIIT----IIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 207 AEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTItV 286
Cdd:cd18549 184 LEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDL-V 262
|
250 260
....*....|....*....|....*...
3B5W_D 287 VFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18549 263 AFLLYVNvFIKPIRRLVNFTEQYQKGMA 290
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-550 |
2.81e-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: 135.99 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR--DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlasLRNQV 419
Cdd:COG1116 8 LELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFN-DTVANNIAYA-RTEQYSREQIEEAARmayamDFINKMdnGLDtvigenGVL------LSGGQRQRIAI 491
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERAR-----ELLELV--GLA------GFEdayphqLSGGMRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH------RLstiekADEIVV 550
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVV 211
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
4.72e-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: 136.46 E-value: 4.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 30 AGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 110 GMPVSFFDKQSTGTLLSRITYDSEQ----VASSSSGALitvvREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVV 185
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLiqtvVGSSLSIAL----RNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 186 SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAF 265
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 266 VLYAASFpSVMD-SLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18575 237 VLWLGAH-DVLAgRMSAGELSqfVFYAVLAA--GSVGALSEVWGDLQRAAGA 285
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-556 |
1.17e-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: 1.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL--REYTLASLRNQV 419
Cdd:cd03262 1 IEIKNLHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLF-NDTVANNIAYA--RTEQYSREQIEEAArmayaMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApiKVKGMSKAEAEERA-----LELLEKV--GLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-506 |
2.12e-35 |
|
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: 139.93 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 13 FRRLWptiAPFKAGLIVAGVALILNAASDTFMLSLLkpllDDGFGKTDrSVLVWMPLVVIGLMILRGITSYVSSYCISWV 92
Cdd:COG4615 4 LRLLL---RESRWLLLLALLLGLLSGLANAGLIALI----NQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVaSSSSGALITVVREGASIIGLFIMMFYYSWQLSIILI 172
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 173 VLAPIVSIAIRVVSKRFR---NISKNMQNTMGQVTTSaeqMLKGHKEVLIFG--GQEVETKRFDKVSNRMRLQGMKMVSA 247
Cdd:COG4615 155 VLLGLGVAGYRLLVRRARrhlRRAREAEDRLFKHFRA---LLEGFKELKLNRrrRRAFFDEDLQPTAERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 248 SSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVF----SSMIALMRPLKSLTNVNAQFQRgMAACQTLFTILD 323
Cdd:COG4615 232 FALANNWGNLLFFALIGLILFLLPALGWADPAVLSGFVLVLlflrGPLSQLVGALPTLSRANVALRK-IEELELALAAAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 324 SEQEKDEGKRVIeRATGDVEFRNVTFTYPGRDVP---ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI 400
Cdd:COG4615 311 PAAADAAAPPAP-ADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 401 LMDGHDLREYTLASLRNQVALVSQNVHLFNDTvanniayarteqYSREQIEEAARmayAMDFINKMDngLDTVIG-ENGV 479
Cdd:COG4615 390 LLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------------LGLDGEADPAR---ARELLERLE--LDHKVSvEDGR 452
|
490 500 510
....*....|....*....|....*....|.
3B5W_D 480 L----LSGGQRQRIAIARALLRDSPILILDE 506
Cdd:COG4615 453 FsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
342-568 |
2.58e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.04 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKST----IASLITrfydIDEGEILMDGHDLreYT-LASLR 416
Cdd:COG1118 3 IEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLET----PDSGRIVLNGRDL--FTnLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQNVHLF-NDTVANNIAYA-RTEQYSREQIeeAARmayAMDFINKMdnGLDTvigengvL-------LSGGQRQ 487
Cdd:COG1118 75 RRVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEI--RAR---VEELLELV--QLEG-------LadrypsqLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 488 RIAIARALLRDSPILILDEATSALDT----ESERAIQAALDELQknRTSLVIAH------RLstiekADEIVVVEDGVIV 557
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELG--GTTVFVTHdqeealEL-----ADRVVVMNQGRIE 213
|
250
....*....|.
3B5W_D 558 ERGTHNDLLEH 568
Cdd:COG1118 214 QVGTPDEVYDR 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-556 |
3.90e-35 |
|
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: 131.50 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlasLRNQVALV 422
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHL---FNDTVANNIAYART------EQYSREQIEEAARmayAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIAR 493
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLYghkglfRRLSKADKAKVDE---ALERVG-LSELADRQIGE----LSGGQQQRVLLAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 494 ALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:cd03235 146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-567 |
3.93e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 133.77 E-value: 3.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFY---DIDEGEILMDGHDLREYTLASLRNQ 418
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNV--HLFNDTVANNIAYA-RTEQYSREQIEEAARMAYAmdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEMIKIVRDVLA-------DVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
343-569 |
5.03e-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: 132.31 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT---LASLRNQV 419
Cdd:cd03256 2 EVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNIAYARTEQ----------YSREQIEEAarmAYAMDfinkmDNGLDTVIGENGVLLSGGQRQR 488
Cdd:cd03256 81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglFPKEEKQRA---LAALE-----RVGLLDKAYQRADQLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAEL 232
|
....
3B5W_D 566 LEHR 569
Cdd:cd03256 233 TDEV 236
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
27-316 |
1.58e-34 |
|
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: 132.22 E-value: 1.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVReGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGN-LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 267 LYAASFPSVMDSLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18543 240 LALGGWLVANGSLTLGTL-VAFSAYLTMLVwPVRMLGWLLAMAQRARAAAE 289
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-568 |
2.37e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNV--HLFNDTVANNIAYA-RTEQYSREQIEEaaRMAYAMDFINkMDNGLDtvigENGVLLSGGQRQRIAIARALLRD 498
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGlENIGVPREEMVE--RVDQALRQVG-MEDFLN----REPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 499 SPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
342-561 |
2.94e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 133.00 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLR 416
Cdd:PRK11153 2 IELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQnvHlFN----DTVANNIAYA-RTEQYSREQIEeaARMAYAMDFI---NKMD----NgldtvigengvlLSGG 484
Cdd:PRK11153 82 RQIGMIFQ--H-FNllssRTVFDNVALPlELAGTPKAEIK--ARVTELLELVglsDKADrypaQ------------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGT 561
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
28-318 |
4.68e-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: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 28 IVAGVALILNA-----ASDTFMLSLLKPLLDDGFGKTDRSVLVWMplvvIGLMILRGITSYVSSYCISWVSGKVVMTMRR 102
Cdd:cd18577 9 IAAGAALPLMTivfgdLFDAFTDFGSGESSPDEFLDDVNKYALYF----VYLGIGSFVLSYIQTACWTITGERQARRIRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAI 182
Cdd:cd18577 85 RYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 183 RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18577 165 GIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAM 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 263 LAFVLYAASFPSVMDSLTAGTI-TVVFSSMIALMrplkSLTNVNAQ---FQRGMAACQTL 318
Cdd:cd18577 245 YALAFWYGSRLVRDGEISPGDVlTVFFAVLIGAF----SLGQIAPNlqaFAKARAAAAKI 300
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-568 |
1.05e-33 |
|
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: 128.23 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAslRNQVAL 421
Cdd:cd03296 3 IEVRNVSKRFG--DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAYARTEQYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 501 ILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-316 |
1.25e-33 |
|
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: 129.83 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVS 186
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 267 LYAASFPSVMDSLTAGTITVVFS-SMIALMrPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINyLMQILM-SLMMLSMVFVMLPRASASAK 290
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-568 |
1.42e-33 |
|
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: 127.74 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQVAL 421
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAYA-RTEQYSREQIEEaaRMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlRLKKLPKAEIKE--RVAEALDLV-QLEGYANRKPSQ----LSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-569 |
1.73e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.61 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLAS----LRN 417
Cdd:COG1129 5 LEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSprdaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFND-TVANNIAYARtEQYS------REQIEEAARmayAMDFINkMDNGLDTVIGEngvlLSGGQRQRIA 490
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFLGR-EPRRgglidwRAMRRRARE---LLARLG-LDIDPDTPVGD----LSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 491 IARALLRDSPILILDEATSAL-DTESER--AIqaaLDELQKNRTSLV-IAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:COG1129 151 IARALSRDARVLILDEPTASLtEREVERlfRI---IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
....
3B5W_D 566 LEHR 569
Cdd:COG1129 228 TEDE 231
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
342-568 |
1.84e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 130.24 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR---------DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LRE 409
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 410 YTLASLRNQVALVsqnvhlFND---------TVANNIAYARTEQysrEQIEEAARMAYAMDFINKMdnGLDT-VIGENGV 479
Cdd:COG4608 88 RELRPLRRRMQMV------FQDpyaslnprmTVGDIIAEPLRIH---GLASKAERRERVAELLELV--GLRPeHADRYPH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQK--NRTSLVIAHRLSTIEK-ADEIVVVE 552
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIQAQvlnlLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMY 232
|
250
....*....|....*.
3B5W_D 553 DGVIVERGTHNDLLEH 568
Cdd:COG4608 233 LGKIVEIAPRDELYAR 248
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
356-568 |
4.30e-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: 127.76 E-value: 4.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 356 VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRN----QVALVSQNVHLF-N 430
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVANNIAYARTEQysreQIEEAARMAYAMDFINKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:cd03294 117 RTVLENVAFGLEVQ----GVPRAEREERAAEALELVGLEgwEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 509 SALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
1.04e-32 |
|
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: 132.12 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR---------DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFydID-EGEILMDGHDLREYT 411
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL--IPsEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 412 ---LASLRNQVALVsqnvhlFND---------TVANNIAyartE-------QYSREQIEEaaRMAYAMDfinkmDNGLDT 472
Cdd:COG4172 354 rraLRPLRRRMQVV------FQDpfgslsprmTVGQIIA----EglrvhgpGLSAAERRA--RVAEALE-----EVGLDP 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 473 VIG-----EngvlLSGGQRQRIAIARALLRDSPILILDEATSALDteseRAIQAA----LDELQKNR--TSLVIAHRLST 541
Cdd:COG4172 417 AARhryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAV 488
|
250 260
....*....|....*....|....*...
3B5W_D 542 IEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:COG4172 489 VRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-544 |
1.98e-32 |
|
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: 124.06 E-value: 1.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFAlEVTGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-----------HRLSTIEK 544
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVAthakelvdttrHRVIALER 211
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
30-314 |
3.17e-32 |
|
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: 125.73 E-value: 3.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 30 AGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 110 GMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRF 189
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
3B5W_D 270 ASFPSVMDSLTAGT-ITVVFSSMIaLMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18572 241 GGHLVLSGRMSAGQlVTFMLYQQQ-LGEAFQSLGDVFSSLMQAVGA 285
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-560 |
4.99e-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: 122.75 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLrEYTLASLRNqVAL 421
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLF-NDTVANNIAYA-RTEQYSREQIEEAARMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDERVREVAEL-------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH-RLSTIEKADEIVVVEDGVIVERG 560
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
340-568 |
6.07e-32 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL-----REytlas 414
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 lRNqVALVSQNV----HLfndTVANNIAYA-------RTEQysREQIEEAARMAyamdfinKMDNGLDTVIGEngvlLSG 483
Cdd:COG3839 75 -RN-IAMVFQSYalypHM---TVYENIAFPlklrkvpKAEI--DRRVREAAELL-------GLEDLLDRKPKQ----LSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS---TIekADEIVVVEDGVIVE 558
Cdd:COG3839 137 GQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQ 214
|
250
....*....|
3B5W_D 559 RGTHNDLLEH 568
Cdd:COG3839 215 VGTPEELYDR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
359-568 |
7.65e-32 |
|
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: 123.21 E-value: 7.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReyTLASLRNQVALVSQNVHLF-NDTVANNI 437
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 438 AYA-RTEQYSREQIEEAAR-MAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03299 93 AYGlKKRKVDKKEIERKVLeIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 516 ERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:cd03299 165 KEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-557 |
9.29e-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: 120.61 E-value: 9.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLAS----LRN 417
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASprdaRRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQnvhlfndtvanniayarteqysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLR 497
Cdd:cd03216 76 GIAMVYQ--------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 498 DSPILILDEATSAL-DTESERAIqAALDELQKN-RTSLVIAHRLSTI-EKADEIVVVEDGVIV 557
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRAQgVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
53-285 |
1.35e-31 |
|
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: 124.28 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 53 DDGFGKTDRSVLVWMPLVVIGlmilrGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDS 132
Cdd:cd18780 35 EEALRALNQAVLILLGVVLIG-----SIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 133 EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLK 212
Cdd:cd18780 110 QVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESIS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 213 GHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTIT 285
Cdd:cd18780 190 NIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLT 262
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-315 |
1.87e-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: 123.80 E-value: 1.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKT-DRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLF 105
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 106 GHMMGMPVSFFDKQSTGTLLSRITYDSEQV----ASSSSGALITVVRegasIIGLFIMMFYYSWQLSIILIVLAPIVSIA 181
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVerliADGIPQGITNVLT----LVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 182 IRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 262 ALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18778 237 GTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-568 |
4.84e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 121.78 E-value: 4.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNV--HLFNDTVANNIAYArTEQYS---REQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALL 496
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFG-LENHAvpyDEMHRRVSEALKQVDMLERADYEPNA--------LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-560 |
5.03e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 121.30 E-value: 5.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYD-ID----EGEILMDGHDL--REYTLAS 414
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPgarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQNVHLFNDTVANNIAYA------RTEQYSREQIEEAARMAyamdfinkmdnGL-DTV---IGENGVLLSGG 484
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESLRKA-----------ALwDEVkdrLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStiekaDEIVVVEDGVIVE 558
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVE 233
|
..
3B5W_D 559 RG 560
Cdd:COG1117 234 FG 235
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
5.06e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 122.59 E-value: 5.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAI---- 182
Cdd:cd18540 84 HLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSiyfq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 183 RVVSKRFRNISKnmQNTmgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18540 164 KKILKAYRKVRK--INS--RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 263 LAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-316 |
6.23e-31 |
|
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: 122.24 E-value: 6.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 64 LVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGAL 143
Cdd:cd18573 40 LKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 144 ITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQ 223
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 224 EVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTIT-------VVFSSMIalmr 296
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTsflmyavYVGSSVS---- 275
|
250 260
....*....|....*....|
3B5W_D 297 plkSLTNVNAQFQRGMAACQ 316
Cdd:cd18573 276 ---GLSSFYSELMKGLGASS 292
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-575 |
8.53e-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: 128.52 E-value: 8.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 274 SVMDSLTAgtitVVFSSMIALMR-PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEG--KRVIERATGD-VEFRNVTF 349
Cdd:TIGR00957 569 NILDAEKA----FVSLALFNILRfPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSieRRTIKPGEGNsITVHNATF 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 350 TYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlreytlaslrnQVALVSQNVHLF 429
Cdd:TIGR00957 645 TWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQ 711
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 430 NDTVANNIAYAR--TEQYSREQIEEAARMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:TIGR00957 712 NDSLRENILFGKalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 508 TSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-569 |
1.05e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 128.36 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 10 WQTFRRLWPtiapFKAGLIVAGVALILNAASDTFMLS---LLKPLLDDGFGKTDRSVLvwmpLVVIGLMILRGITS---Y 83
Cdd:PTZ00243 948 WSTYVAYLR----FCGGLHAAGFVLATFAVTELVTVSsgvWLSMWSTRSFKLSAATYL----YVYLGIVLLGTFSVplrF 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 84 VSSYCISWVSGKvvmTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
Cdd:PTZ00243 1020 FLSYEAMRRGSR---NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSAS 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 164 SwqlSIILIVLAPIVSIAIRVV---SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEV----ETKRFDKVSNR 236
Cdd:PTZ00243 1097 Q---PFVLVALVPCGYLYYRLMqfyNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLvmqeALRRLDVVYSC 1173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 237 MRLQ-------GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITV------------VFSSMIALMRP 297
Cdd:PTZ00243 1174 SYLEnvanrwlGVRVEFLSNIVVTVIALIGVIGTMLRATSQEIGLVSLSLTMAMQTTatlnwlvrqvatVEADMNSVERL 1253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 298 LKSLTNVN-----------AQFQR--GMAACQTlftildseqekdeGKRVIERAT-----------GDVEFRNVTFTYpg 353
Cdd:PTZ00243 1254 LYYTDEVPhedmpeldeevDALERrtGMAADVT-------------GTVVIEPASptsaaphpvqaGSLVFEGVQMRY-- 1318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 354 RD-VP-ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFND 431
Cdd:PTZ00243 1319 REgLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG 1398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 TVANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL-RDSPILILDEATSA 510
Cdd:PTZ00243 1399 TVRQNVD--PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATAN 1476
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHR 569
Cdd:PTZ00243 1477 IDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-561 |
2.29e-30 |
|
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: 118.38 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReYTLASLRNQVAL 421
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIA-YARTEQYSREQI-EEAARMAYAMDFINKMdnglDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLKGLPKSEIkEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-568 |
4.45e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 118.27 E-value: 4.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR--EYTLASLRNQV 419
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNIAYA--RTEQYSREQIEEAARmayamDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENVMFGplRVRGASKEEAEKQAR-----ELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-550 |
1.73e-29 |
|
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: 115.65 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKST----IASLITrfydIDEGEILMDGHDLREyTLASLRN 417
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFND-TVANNIAYART---EQYSREQIEEA-ARMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWAAlygLRADREAIDEAlEAV------------GLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEKADEIVV 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 |
2.55e-29 |
|
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: 117.59 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVvs 186
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 187 krFRNISKN----MQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18546 159 --FRRRSSRayrrARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 263 LAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
361-560 |
1.51e-28 |
|
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: 113.16 E-value: 1.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 361 NINLKIPAGkTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLRE----YTLASLRNQVALVSQNVHLF-NDTVAN 435
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 436 NIAYARTEQYSREQIEEAARMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
3B5W_D 516 ERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-566 |
2.52e-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: 113.64 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEG---EILmdGHDLREYTLASLRNQ 418
Cdd:COG1119 4 LELRNVTVRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLF---NDTVANNI---AYA---RTEQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRI 489
Cdd:COG1119 80 IGLVSPALQLRfprDETVLDVVlsgFFDsigLYREPTDEQRERARELLELLGLAHLADRPFGT--------LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIpPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
332-567 |
2.66e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.59 E-value: 2.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 332 KRVIERATGD--VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLRE 409
Cdd:PRK09452 3 KLNKQPSSLSplVELRGISKSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 410 ytLASLRNQVALVSQNVHLF-NDTVANNIAYA-RTEQYSREQIE----EAARMAYAMDFINKmdngldtvigeNGVLLSG 483
Cdd:PRK09452 81 --VPAENRHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAEITprvmEALRMVQLEEFAQR-----------KPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEIVVVEDGVIVERG 560
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227
|
....*..
3B5W_D 561 THNDLLE 567
Cdd:PRK09452 228 TPREIYE 234
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
363-556 |
3.39e-28 |
|
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: 112.26 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 363 NLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDlrEYTLASLRNQVALVSQNVHLFND-TVANNIAYA- 440
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 441 ----RTEQYSREQIEEAARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:TIGR01277 96 hpglKLNAEQQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
3B5W_D 517 RAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEIVVVEDGVI 556
Cdd:TIGR01277 165 EEMLALVKQLcsERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
120-575 |
4.04e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 120.08 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 120 STGTLLSRITYDS---EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRvvskRFRNISKN- 195
Cdd:PLN03232 396 ASGKVTNMITTDAnalQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVR----KMRKLTKEg 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 196 MQNTMGQVTTSAEqMLKGHKEVLIFGGQEvetkrfdkvSNRMRLQGMKMVSASSISDPiiQLIASLAlAFVLyaASFPSV 275
Cdd:PLN03232 472 LQWTDKRVGIINE-ILASMDTVKCYAWEK---------SFESRIQGIRNEELSWFRKA--QLLSAFN-SFIL--NSIPVV 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 276 MDSLTAGTITVV---------FSSM--IALMR-PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVE 343
Cdd:PLN03232 537 VTLVSFGVFVLLggdltparaFTSLslFAVLRsPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAIS 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 344 FRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITrfydideGEIlmdghDLREYTLASLRNQVALV 422
Cdd:PLN03232 617 IKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL-----SHAETSSVVIRGSVAYV 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNDTVANNIAYA---RTEQYSREQieEAARMAYAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PLN03232 685 PQVSWIFNATVRENILFGsdfESERYWRAI--DVTALQHDLDLLPGRDL---TEIGERGVNISGGQKQRVSMARAVYSNS 759
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 500 PILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-557 |
4.33e-28 |
|
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: 111.58 E-value: 4.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYpGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlASLRNQVALVSQN 425
Cdd:cd03226 4 NISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 V--HLFNDTVANNIAYARTEQY-SREQIEEAARmayamdfinKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd03226 80 VdyQLFTDSVREELLLGLKELDaGNEQAETVLK---------DLD--LYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 503 ILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEK-ADEIVVVEDGVIV 557
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-560 |
6.66e-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: 111.43 E-value: 6.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 364 LKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReyTLASLRNQVALVSQNVHLFND-TVANNIAYAR- 441
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFAHlTVEQNVGLGLs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 442 -----TEQySREQIEEAARMayaMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:cd03298 97 pglklTAE-DRQAIEVALAR---VGLAGLEKRLPGE--------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
3B5W_D 517 RAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03298 165 AEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
342-554 |
2.59e-27 |
|
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: 109.73 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL----MDGHDLREYTLASLRN 417
Cdd:cd03290 1 VQVTNGYFSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFNDTVANNIAYARTEQYSR-EQIEEAARMAYAMDFinkMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03290 80 SVAYAAQKPWLLNATVEENITFGSPFNKQRyKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 497 RDSPILILDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEKADEIVVVEDG 554
Cdd:cd03290 157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
317-554 |
2.95e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 116.06 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 317 TLFTILDSEQEKDEGKRVIERATGD-VEFRNVTFTYP-GRdvPALRNINLKIPAGKTVALVGRSGSGKST----IASLit 390
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGaLALEDLTLRTPdGR--PLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 391 rfYDIDEGEILMDGHDlreytlaslrnQVALVSQNVHLFNDTVANNIAY-ARTEQYSREQIEEAARMAYAMDFINKMDNG 469
Cdd:COG4178 413 --WPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 470 LDTvigenGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIV 549
Cdd:COG4178 480 ADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVL 554
|
....*
3B5W_D 550 VVEDG 554
Cdd:COG4178 555 ELTGD 559
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-558 |
3.61e-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: 109.83 E-value: 3.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRD--VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR---EYTLASLR 416
Cdd:COG4181 9 IELRGLTKTVGTGAgeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQ-VALVSQNVHLF-NDTVANNIAYARTEQYSREQIEEAARMayamdfinkmdngLDTVigenGV---------LLSGGQ 485
Cdd:COG4181 89 ARhVGFVFQSFQLLpTLTALENVMLPLELAGRRDARARARAL-------------LERV----GLghrldhypaQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIA-HRLSTIEKADEIVVVEDGVIVE 558
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
346-566 |
5.30e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.29 E-value: 5.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYpgrDVPALRnINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAslRNQVALVSQN 425
Cdd:PRK10771 6 DITWLY---HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 VHLFND-TVANNIAYA-----RTEQYSREQIEEAARMAYAMDFINKMDngldtviGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:PRK10771 80 NNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 500 PILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
342-575 |
1.03e-26 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 115.99 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITrfydideGEI--LMDGHdlreytlASLRNQ 418
Cdd:PLN03130 615 ISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAML-------GELppRSDAS-------VVIRGT 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFNDTVANNIAYARTeqYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSP--FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 499 SPILILDEATSALDTESERAI--QAALDELQkNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQL 575
Cdd:PLN03130 759 SDVYIFDDPLSALDAHVGRQVfdKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
342-561 |
1.05e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGR--DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL--REYTLASLR 416
Cdd:PRK13637 3 IKIENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQ--NVHLFNDTVANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLD--TVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13637 83 KKVGLVFQypEYQLFEETIEKDIAFGpINLGLSEEEIEN--RVKRAMNIV-----GLDyeDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-566 |
1.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 109.69 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT-LASLRNQVA 420
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQN--VHLFNDTVANNIAYArTEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFG-PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-568 |
2.02e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.58 E-value: 2.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpGRDVpALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLreyTLASLRNQ-VA 420
Cdd:PRK11432 7 VVLKNITKRF-GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRdIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLF-NDTVANNIAYA-RTEQYSREQIEEAARMAYAM-DFINKMDNGLDTVigengvllSGGQRQRIAIARALLR 497
Cdd:PRK11432 82 MVFQSYALFpHMSLGENVGYGlKMLGVPKEERKQRVKEALELvDLAGFEDRYVDQI--------SGGQQQRVALARALIL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-560 |
7.35e-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: 105.38 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQV-A 420
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSqnVHLFND---TVANNIAYARTEQYSREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03268 77 LIE--APGFYPnltARENLRLLARLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
352-574 |
8.89e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.13 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 352 PGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREY---TLASLRNQVALVSQNvhl 428
Cdd:PRK11308 24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQN--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 fndtvanniAYA--RTEQYSREQIEE----------AARMAYAMDFINKMdnGLDTvigENGV----LLSGGQRQRIAIA 492
Cdd:PRK11308 101 ---------PYGslNPRKKVGQILEEpllintslsaAERREKALAMMAKV--GLRP---EHYDryphMFSGGQRQRIAIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 493 RALLRDSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK11308 167 RALMLDPDVVVADEPVSALDV----SVQAQvlnlMMDLQQElGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
|
250
....*....|
3B5W_D 566 LEH-RGVYAQ 574
Cdd:PRK11308 243 FNNpRHPYTQ 252
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
14-325 |
1.21e-25 |
|
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: 107.54 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 14 RRLWPTIApfkAGLIVAGVALILNAASdTFMLS-LLKPLLDDGFGKTDRSVLVWMpLVVIGLMILRGITSYVSSYCISWV 92
Cdd:cd18578 5 KPEWPLLL---LGLIGAIIAGAVFPVF-AILFSkLISVFSLPDDDELRSEANFWA-LMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQ--STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSII 170
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPenSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 171 LIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSI 250
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 251 SDPIIQLIASLALAFVLYA---------ASFPSVMDSLTAgtitVVFSSMIALMrplksLTNVNAQFQRGMAACQTLFTI 321
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYggrlvangeYTFEQFFIVFMA----LIFGAQSAGQ-----AFSFAPDIAKAKAAAARIFRL 310
|
....
3B5W_D 322 LDSE 325
Cdd:cd18578 311 LDRK 314
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
346-568 |
1.68e-25 |
|
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: 110.54 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKS----TIASLITRFYDIDEGEILMDGHDLREYTLASLR----N 417
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQ------N-VHlfndTVANNI--------------AYART-EQYSREQIEEAARM--AYAMDfinkmdngldtv 473
Cdd:COG4172 93 RIAMIFQepmtslNpLH----TIGKQIaevlrlhrglsgaaARARAlELLERVGIPDPERRldAYPHQ------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 474 igengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEK-ADEIVV 550
Cdd:COG4172 157 -------LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLlITHDLGVVRRfADRVAV 229
|
250
....*....|....*...
3B5W_D 551 VEDGVIVERGTHNDLLEH 568
Cdd:COG4172 230 MRQGEIVEQGPTAELFAA 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-563 |
1.79e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLAS----LRN 417
Cdd:COG3845 6 LELRGITKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSprdaIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQNVHLFND-TVANNIAYARTEQYS--------REQIEEAARmAYAMDfINkmdngLDTVIGEngvlLSGGQRQR 488
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkaaRARIRELSE-RYGLD-VD-----PDAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 489 IAIARALLRDSPILILDEATSAL-DTESERAIqAALDELQKNRTSLV-IAHRLSTI-EKADEIVVVEDGVIVerGTHN 563
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVmAIADRVTVLRRGKVV--GTVD 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
342-563 |
2.56e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH------DLREYTLASL 415
Cdd:COG4161 3 IQLKNINCFYGS--HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQVALVSQNVHLF-NDTVANNIAYA--RTEQYSREQ-IEEAARMAYAMDFINKMDngldtvigENGVLLSGGQRQRIAI 491
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLIEApcKVLGLSKEQaREKAMKLLARLRLTDKAD--------RFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHN 563
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
355-567 |
2.73e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 104.05 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReyTLAS---LRNQVALVSQNVHLFND 431
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPherARAGIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 -TVANNI---AYARTEQYSREQIEEaarmAYAMdFINkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:cd03224 90 lTVEENLllgAYARRRAKRKARLER----VYEL-FPR-----LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 508 TSALDTESERAIQAALDELQKNRTSLVI----AHRLSTIekADEIVVVEDGVIVERGTHNDLLE 567
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-576 |
6.27e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPgRDVP----ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDG----HDLREYTLA 413
Cdd:PRK13646 3 IRFDNVSYTYQ-KGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQVALVSQ--NVHLFNDTVANNIAYArtEQYSREQIEEAArmAYAMDFInkMDNGLD-TVIGENGVLLSGGQRQRIA 490
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFG--PKNFKMNLDEVK--NYAHRLL--MDLGFSrDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
....*....
3B5W_D 568 HRGVYAQLH 576
Cdd:PRK13646 236 DKKKLADWH 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
342-566 |
6.89e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.62 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHlFND--TVANNIAYAR--------TEQySREQIEEAarMAYaMDFINKMDNGLDTvigengvlLSGGQRQRIAI 491
Cdd:COG4604 80 LRQENH-INSrlTVRELVAFGRfpyskgrlTAE-DREIIDEA--IAY-LDLEDLADRYLDE--------LSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAAL----DELqkNRTSLVIAHRL---STIekADEIVVVEDGVIVERGTHND 564
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLrrlaDEL--GKTVVIVLHDInfaSCY--ADHIVAMKDGRVVAQGTPEE 222
|
..
3B5W_D 565 LL 566
Cdd:COG4604 223 II 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
346-560 |
7.15e-25 |
|
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: 102.66 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYPGRDvpALRNINLKIPAGKTvALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAsLRNQVALVSQN 425
Cdd:cd03264 5 NLTKRYGKKR--ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 VHLF-NDTVANNIAYARTeQYSREQIEEAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
Cdd:cd03264 81 FGVYpNFTVREFLDYIAW-LKGIPSKEVKARVDEVLELVN-LGDRAKKKIGS----LSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
342-560 |
1.11e-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: 101.47 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVPA----LRNINLKIPAGKTVALVGRSGSGKSTIASLIT--RFYDIDEGEILMDGHDLReytLASL 415
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQVALVSQNVHLF-NDTVanniayarteqysREqieeaarmayAMDFINKMDNgldtvigengvlLSGGQRQRIAIARA 494
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTV-------------RE----------TLMFAAKLRG------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEIVVVEDGVIVERG 560
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-566 |
1.37e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGEILMDGHDLREYTLASLRNQVALVSQ----- 424
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 -NVHLFnDTVA-----NNIAYARTEQYSReqIEEAARMAYAMDfinKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:PRK14247 95 pNLSIF-ENVAlglklNRLVKSKKELQER--VRWALEKAQLWD---EVKDRLDAPAGK----LSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWGPTREVF 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-565 |
1.72e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 103.27 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVA 420
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNV--HLFNDTVANNIAYARTEQ-----YSREQIEEAARMAYAMDFINKmdngldtvigeNGVLLSGGQRQRIAIAR 493
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKgipheEMKERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 494 ALLRDSPILILDEATSALDTESE----RAIQAALDELQknRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDYQ--MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-554 |
4.87e-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: 100.59 E-value: 4.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 353 GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDgHDLREYTLASL---------RNQVALVS 423
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQAspreilalrRRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QNVH--------------LFNDTVANNIAYARTEQY-SREQIEEAARMAYAMDFinkmdngldtvigengvllSGGQRQR 488
Cdd:COG4778 100 QFLRviprvsaldvvaepLLERGVDREEARARARELlARLNLPERLWDLPPATF-------------------SGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEIVVVEDG 554
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
359-565 |
6.28e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 6.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQVALVSQNVHLFND-TVANNI 437
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRKVGFVFQHYALFRHmTVFDNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 438 AYARTEQYSREQIEEAARMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
Cdd:PRK10851 96 AFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRK 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 518 AIQAALDELQKNR--TSLVIAH-RLSTIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK10851 174 ELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
345-561 |
8.45e-24 |
|
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: 100.20 E-value: 8.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRnqVAL 421
Cdd:cd03219 4 RGLTKRFGG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG--IGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAYARTEQYSREQI------EEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03219 80 TFQIPRLFPElTVLENVMVAAQARTGSGLLlararrEEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 495 LLRDSPILILDEATSAL-DTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:cd03219 158 LATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-574 |
9.24e-24 |
|
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: 101.08 E-value: 9.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 340 GDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIdEGEILMDGHDLREYTLASLRNQV 419
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD--PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQ 574
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
51-314 |
9.90e-24 |
|
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: 101.37 E-value: 9.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 51 LLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITy 130
Cdd:cd18570 28 LIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 131 DSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQM 210
Cdd:cd18570 107 DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 211 LKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVM-DSLTAGTItVVFS 289
Cdd:cd18570 187 LKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSY-LVIkGQLSLGQL-IAFN 264
|
250 260
....*....|....*....|....*.
3B5W_D 290 SMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18570 265 ALLGyFLGPIENLINLQPKIQEAKVA 290
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
359-566 |
1.26e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQnVHLFND--TVANN 436
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHLTPEgiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 437 IAYARTEQYS---REQIEEAARMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:PRK11231 97 VAYGRSPWLSlwgRLSAEDNARVNQAME-----QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 514 ESERAIQAALDELQKN-RTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK11231 172 NHQVELMRLMRELNTQgKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEVM 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-574 |
1.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.58 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK13647 5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNV--HLFNDTVANNIAYA-RTEQYSREQIEEAARMAYAM----DFINKMDNGLdtvigengvllSGGQRQRIAIARA 494
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEALKAvrmwDFRDKPPYHL-----------SYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEKADEIVVVEDGVIVERGThNDLLEHRGVY 572
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDEDIV 231
|
..
3B5W_D 573 AQ 574
Cdd:PRK13647 232 EQ 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
343-565 |
1.50e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 104.22 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR-EYTLASLRNQVAL 421
Cdd:PRK11288 6 SFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLD--TVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:PRK11288 84 IYQELHLVPEmTVAENLYLGQLPH-KGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALARN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 499 SPILILDEATSALdteSERAIQ---AALDEL-QKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVErgTHNDL 565
Cdd:PRK11288 159 ARVIAFDEPTSSL---SAREIEqlfRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-561 |
1.52e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReYTLASL---RNQ 418
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNV--HLFNDTVANNIAYAR-----TEQYSREQIEEAARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAI 491
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGT 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
343-561 |
1.53e-23 |
|
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: 100.11 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRnqV 419
Cdd:COG0411 6 EVRGLTKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHRIARLG--I 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNI--------------AYARTEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGG 484
Cdd:COG0411 82 ARTFQNPRLFPElTVLENVlvaaharlgrgllaALLRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-574 |
1.66e-23 |
|
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: 105.76 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLL-----KPLLDDGFGKTDRSVLVWMPLVVIGLM 75
Cdd:TIGR01271 844 RENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLItdnpsAPNYVDQQHANASSPDVQKPVIITPTS 923
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 76 ILRGITSYV----SSYCISWVSG----KVVMTMRRRLFGHMMGM----PVSFFDKQSTGTLLSRITYDSEQVASSSSGAL 143
Cdd:TIGR01271 924 AYYIFYIYVgtadSVLALGFFRGlplvHTLLTVSKRLHEQMLHSvlqaPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTL 1003
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 144 ITVVREGASIIGlfiMMFYYSWQLSIILIVLAPIVSIAIrVVSKRFRNISKNMQNTMGQ----VTTSAEQMLKGHKEVLI 219
Cdd:TIGR01271 1004 FDFIQLTLIVLG---AIFVVSVLQPYIFIAAIPVAVIFI-MLRAYFLRTSQQLKQLESEarspIFSHLITSLKGLWTIRA 1079
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 220 FGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIaslalaFVLY--AASFPSVM-DSLTAGTITVVFSSMIALMR 296
Cdd:TIGR01271 1080 FGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII------FVFFfiAVTFIAIGtNQDGEGEVGIILTLAMNILS 1153
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 297 PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKR-----------VIER--------ATGDVEFRNVT--FTYPGRD 355
Cdd:TIGR01271 1154 TLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGgggkyqlstvlVIENphaqkcwpSGGQMDVQGLTakYTEAGRA 1233
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 356 VpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIdEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVAN 435
Cdd:TIGR01271 1234 V--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRK 1310
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 436 NIAyaRTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:TIGR01271 1311 NLD--PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVT 1388
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRGVYAQ 574
Cdd:TIGR01271 1389 LQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-549 |
1.69e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 351 YPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDlreytlaslrnQVALVSQNVHL-- 428
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 -FNDTVANNIA---YARTEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:NF040873 69 sLPLTVRDLVAmgrWARRGLWRRLTRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
3B5W_D 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIV 549
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
342-568 |
2.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.20 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR---DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT----LAS 414
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQ--NVHLFNDTVANNIAYA-RTEQYSREQIEEAARMAYAMDFINkmdnglDTVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL--STIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
346-569 |
2.18e-23 |
|
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: 100.32 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFT-YPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlreytlaslrnQVALVSQ 424
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFNDTVANNIAYART-EQYSREQIEEAARMAYAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSyDEYRYKSVVKACQLEEDITKFPEKDN---TVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 504 LDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHR 569
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
343-549 |
2.21e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 98.63 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALV 422
Cdd:PRK10247 9 QLQNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFNDTVANNIAYARteQYSREQIEEAARMAYAMDFiNKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:PRK10247 87 AQTPTLFGDTVYDNLIFPW--QIRNQQPDPAIFLDDLERF-ALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
3B5W_D 503 ILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEIV 549
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
357-566 |
2.42e-23 |
|
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: 99.88 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 357 PALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAS---LRNQVALVSQN-VHLFN-- 430
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 511 LDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
358-562 |
2.82e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 2.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH--DLR----EYTLASLRNQVALVSQNVHLF-N 430
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRELRRNVGMVFQQYNLWpH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVANNIAYA--RTEQYSREQIeeaarMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:PRK11124 97 LTVQQNLIEApcRVLGLSKDQA-----LARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 509 SALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTH 562
Cdd:PRK11124 170 AALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-560 |
3.07e-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: 98.21 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 348 TFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNqVALVSQNVH 427
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-LGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 428 LFND-TVANNIAY-------ARTEQYSReqIEEAARMAYAMDFINKMDNGLDTvigengvllsgGQRQRIAIARALLRDS 499
Cdd:cd03266 89 LYDRlTARENLEYfaglyglKGDELTAR--LEELADRLGMEELLDRRVGGFST-----------GMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-539 |
3.37e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGEILMDGHDL--REYTLASLRNQVALVSQNVHLFN 430
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVANNIAY-ARTEQYS---REQIEEAARMAYAMDFINKMdngldtvIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
Cdd:PRK14243 105 KSIYDNIAYgARINGYKgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
3B5W_D 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
343-571 |
4.85e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.13 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRnqV 419
Cdd:COG0410 5 EVENLHAGYG--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIARLG--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNI---AYARTeqySREQIEEAARMAYAM-----DFINKMdngldtvigenGVLLSGGQRQRIA 490
Cdd:COG0410 81 GYVPEGRRIFPSlTVEENLllgAYARR---DRAEVRADLERVYELfprlkERRRQR-----------AGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 491 IARALLRDSPILILDEATSALdteserA------IQAALDELQKNRTSLVI----AHRLSTIekADEIVVVEDGVIVERG 560
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGL------ApliveeIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEG 218
|
250
....*....|.
3B5W_D 561 THNDLLEHRGV 571
Cdd:COG0410 219 TAAELLADPEV 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-515 |
5.65e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 102.45 E-value: 5.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 344 FRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhDLReytlaslrnqVALVS 423
Cdd:COG0488 1 LENLSKSFGGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QNVHLFND-TVANNIAYARTEQYS----REQIEEA--------ARMAYAMDFINKMD------------NGL-------D 471
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAELRAleaeLEELEAKlaepdedlERLAELQEEFEALGgweaearaeeilSGLgfpeedlD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
3B5W_D 472 TVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
343-554 |
5.85e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 5.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGEILMDGHDLREYTLA-SLRNQV 419
Cdd:PRK13549 7 EMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRdTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFND-TVANNIayarteqYSREQIEEAARMAYAMDFIN--------KMDNGLDTVIGEngvlLSGGQRQRIA 490
Cdd:PRK13549 85 AIIHQELALVKElSVLENI-------FLGNEITPGGIMDYDAMYLRaqkllaqlKLDINPATPVGN----LGLGQQQLVE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 491 IARALLRDSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEK-ADEIVVVEDG 554
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-569 |
6.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 99.32 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPGRdVP----ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL----REYTL 412
Cdd:PRK13634 2 DITFQKVEHRYQYK-TPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 413 ASLRNQVALVSQ--NVHLFNDTVANNIAYARTE-QYSREQIEEAARMAYAMdfinkmdNGLD-TVIGENGVLLSGGQRQR 488
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEEDAKQKAREMIEL-------VGLPeELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
....
3B5W_D 566 LEHR 569
Cdd:PRK13634 234 FADP 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
346-568 |
8.43e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFtYPG--RDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLrnqVA 420
Cdd:COG1101 8 SKTF-NPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRAKY---IG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHL---FNDTVANN--IAYARTEQYSREQIEEAARMAYAMDFINKMDNGL----DTVIGengvLLSGGQRQRIAI 491
Cdd:COG1101 84 RVFQDPMMgtaPSMTIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEIVVVEDGVIV--------ERG 560
Cdd:COG1101 160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRIIldvsgeekKKL 239
|
....*...
3B5W_D 561 THNDLLEH 568
Cdd:COG1101 240 TVEDLLEL 247
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
374-568 |
8.46e-23 |
|
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: 99.49 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 374 LVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQVALVSQNVHLF-NDTVANNIAYA-RTEQYSREQIe 451
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 452 eAARMAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR- 530
Cdd:TIGR01187 78 -KPRVLEALRLVQLEEFADRKPHQ-----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
3B5W_D 531 -TSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:TIGR01187 152 iTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-567 |
8.58e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 98.32 E-value: 8.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQ 424
Cdd:PRK10575 15 RNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFNDTVANNI----------AYARTEQYSREQIEEAARMAYAMDFINKMdngLDTvigengvlLSGGQRQRIAIARA 494
Cdd:PRK10575 93 QLPAAEGMTVRELvaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhRLSTIEKA----DEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
345-556 |
9.64e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.83 E-value: 9.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDghdlrEYTLASLRNQVALVSQ 424
Cdd:PRK11247 16 NAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFN-DTVANNIAYARTEQYsREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK11247 89 DARLLPwKKVIDNVGLGLKGQW-RDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 504 LDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEKADEIVVVEDGVI 556
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
1.01e-22 |
|
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: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASD---TFMLSL-----------LKPLLDDGFGKTDR-SVLVWMPLVVIGLMILRGITSYVSSYCISW 91
Cdd:cd18565 1 LVLGLLASILNRLFDlapPLLIGVaidavfngeasFLPLVPASLGPADPrGQLWLLGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 92 VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIIL 171
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 172 IVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSIS 251
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 252 DPIIQLIASLALAFVLYAASF------PSVMDSLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYwvldgpPLFTGTLTVGTL-VTFLFYTQrLLWPLTRLGDLIDQYQRAMAS 309
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-561 |
1.01e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.15 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIAS-----LITRFYDIDEGEILMDGHDLREYTLAS-----------LRNQ 418
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQ--NVHLFNDTVANNIAYARTeQYSREQIEEAARMAYamdFINKMdnGLD-TVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKF---YLNKM--GLDdSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 496 LRDSPILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGT 561
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-569 |
1.61e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.98 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGRDVPA--LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT----LAS 414
Cdd:PRK13641 3 IKFENVDYIYsPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQ--NVHLFNDTVANNIAYAR-----TEQYSREQieeaarmayAMDFINKMdnGLDT-VIGENGVLLSGGQR 486
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPknfgfSEDEAKEK---------ALKWLKKV--GLSEdLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGTHND 564
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*
3B5W_D 565 LLEHR 569
Cdd:PRK13641 232 IFSDK 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-567 |
1.94e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 102.55 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDghdlreytlaslrNQVALVSQNVHLFNDTVANNIA 438
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 439 YARTEQYSReqIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SER 517
Cdd:PTZ00243 743 FFDEEDAAR--LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
3B5W_D 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
67-316 |
2.11e-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: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 67 MPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITV 146
Cdd:cd18554 48 IGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 147 VREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVE 226
Cdd:cd18554 128 WLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 227 TKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNA 306
Cdd:cd18554 208 QKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFT 287
|
250
....*....|
3B5W_D 307 QFQRGMAACQ 316
Cdd:cd18554 288 TLTQSFASMD 297
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
357-565 |
2.65e-22 |
|
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: 101.91 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 357 PALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlreytlaslrnQVALVSQNVHLFNDTVANN 436
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 437 IAYART-EQYSREQIEEAARMAYAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:TIGR01271 507 IIFGLSyDEYRYTSVIKACQLEEDIALFPEKDK---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 516 ERAI-QAALDELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:TIGR01271 584 EKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
331-568 |
2.84e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.52 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 331 GKRVIEratgdveFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMdGHDLRey 410
Cdd:COG0488 312 GKKVLE-------LEGLSKSYGDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 411 tlaslrnqVALVSQNVHLF--NDTVANNIAyarteQYSREQIEEAARmAY--AMDFINKMdngLDTVIGEngvlLSGGQR 486
Cdd:COG0488 380 --------IGYFDQHQEELdpDKTVLDELR-----DGAPGGTEQEVR-GYlgRFLFSGDD---AFKPVGV----LSGGEK 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIekADEIVVVEDGVIVER-GTH 562
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGY 514
|
....*.
3B5W_D 563 NDLLEH 568
Cdd:COG0488 515 DDYLEK 520
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
343-559 |
3.85e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.08 E-value: 3.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGR--DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReyTLASLRnqvA 420
Cdd:COG4525 5 TVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFN-DTVANNIAYARTEQysreQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:COG4525 80 VVFQKDALLPwLNVLDNVAFGLRLR----GVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 500 PILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEKA----DEIVVVED--GVIVER 559
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-566 |
4.46e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 4.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH------DLREYTLASLRNQVALVSQNVHL 428
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 F-NDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTvIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:PRK14246 102 FpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 508 TSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-568 |
4.62e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 95.59 E-value: 4.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYD-----IDEGEILMDGH---DLREYTLA 413
Cdd:PRK11264 4 IEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtIRVGDITIDTArslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQVALVSQNVHLF-NDTVANNIAYART--EQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvLLSGGQRQRIA 490
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFpHRTVLENIIEGPVivKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-579 |
8.14e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY----PGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD-LREYTLASLR 416
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQNVHlfNDTVAN----NIAYArTEQYSREQIEEAARMAYAMDFINKMDngldtVIGENGVLLSGGQRQRIAIA 492
Cdd:PRK13633 85 NKAGMVFQNPD--NQIVATiveeDVAFG-PENLGIPPEEIRERVDESLKKVGMYE-----YRRHAPHLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEIVVVEDGVIVERGThndlleHRG 570
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT------PKE 230
|
....*....
3B5W_D 571 VYAQLHKMQ 579
Cdd:PRK13633 231 IFKEVEMMK 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
342-566 |
8.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.54 E-value: 8.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR-DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVA 420
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNV--HLFNDTVANNIAYARTEQ-YSREQIeeAARMAYAMDFINKMDngldtVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQgIPREEM--IKRVDEALLAVNMLD-----FKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
345-561 |
1.24e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 1.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQ 424
Cdd:PRK13548 6 RNLSVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHL-FNDTVanniayarteqysreqiEEAARM-AYAMDFINKMDNGL-DTVIGENGVL---------LSGGQRQRIAIA 492
Cdd:PRK13548 84 HSSLsFPFTV-----------------EEVVAMgRAPHGLSRAEDDALvAAALAQVDLAhlagrdypqLSGGEQQRVQLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 493 RALLR------DSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLS-TIEKADEIVVVEDGVIVER 559
Cdd:PRK13548 147 RVLAQlwepdgPPRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVAD 222
|
..
3B5W_D 560 GT 561
Cdd:PRK13548 223 GT 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
359-566 |
1.46e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 94.75 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLA---SLRNQVALVSQN-VHLFN--DT 432
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsISAVNprKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 513 TESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK10419 184 LVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKL 240
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-560 |
2.26e-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: 92.73 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReytlASLRNQVAL 421
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNIAY-ARTEQYSREQIEEAARmayamDFINKMD--NGLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlAQLKGLKKEEARRRID-----EWLERLElsEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
343-575 |
2.26e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGEILMDGHDLREYT--------- 411
Cdd:COG0396 2 EIKNLHVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpderaragi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 412 -LA----------SLRNQVALVSQNVHLFNDTVANNIAYARteqysreqiEEAARMAYAMDFINKmdnGLDtvigengVL 480
Cdd:COG0396 80 fLAfqypveipgvSVSNFLRTALNARRGEELSAREFLKLLK---------EKMKELGLDEDFLDR---YVN-------EG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAH--RLSTIEKADEIVVVEDGVIV 557
Cdd:COG0396 141 FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIV 220
|
250 260
....*....|....*....|
3B5W_D 558 ERGTHN--DLLEHRGvYAQL 575
Cdd:COG0396 221 KSGGKElaLELEEEG-YDWL 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
343-514 |
2.73e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 92.16 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID---EGEILMDGHDLReyTLASLRNQV 419
Cdd:COG4136 3 SLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLF-NDTVANNIAYARTEQYSREQIEEAARMAYAmdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:COG4136 79 GILFQDDLLFpHLSVGENLAFALPPTIGRAQRRARVEQALE-------EAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170
....*....|....*.
3B5W_D 499 SPILILDEATSALDTE 514
Cdd:COG4136 152 PRALLLDEPFSKLDAA 167
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
358-539 |
3.22e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 3.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGEILMDGHDL---REYTLaSLRNQVALVSQNVHLF 429
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTV-DLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 430 NDTVANNIAYA------RTEQYSREQIEEAARMAYAMDFINkmDNGLDTVIGengvlLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWDEVK--DRLHDSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190
....*....|....*....|....*....|....*.
3B5W_D 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
349-568 |
3.75e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 94.77 E-value: 3.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 349 FTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRN---------QV 419
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqmifQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLfndTVANNIAYA-RT--EQYSREQIEEAARmayAMdfinKMDNGL-DTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK15079 107 PLASLNPRM---TIGEIIAEPlRTyhPKLSRQEVKDRVK---AM----MLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 496 LRDSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK15079 177 ILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREmGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
362-581 |
4.24e-21 |
|
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: 95.18 E-value: 4.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 362 INLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLRE----YTLASLRNQVALVSQNVHLFND-TVANN 436
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 437 IAYARTE---QYSREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:TIGR02142 96 LRYGMKRarpSERRISFERVIELL-----------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEhRGVYAQLHKMQFG 581
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA-SPDLPWLAREDQG 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
342-568 |
7.39e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 7.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQVAL 421
Cdd:PRK11607 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLF-NDTVANNIAY-------ARTEQYSReqIEEAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIAR 493
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFglkqdklPKAEIASR--VNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 494 ALLRDSPILILDEATSALDTE-SERAIQAALDELQK-NRTSLVIAH-RLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-566 |
7.41e-21 |
|
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: 94.40 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 361 NINLKIPAGKTVALVGRSGSGKST----IASLITrfydIDEGEILMDGHDL----REYTLASLRNQVALVSQNVHLFND- 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTllraIAGLER----PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 TVANNIAYAR---TEQYSREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:COG4148 93 SVRGNLLYGRkraPRAERRISFDEVVELL-----------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 509 SALDTESERAIqaaLDELQKNRTSLVI-----AHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:COG4148 162 AALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
342-568 |
7.81e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 94.14 E-value: 7.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASlRNqVAL 421
Cdd:PRK11650 4 LKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLF-NDTVANNIAY----ARTEQYSREQ-IEEAARMAYAMDFinkmdngLDTVIGEngvlLSGGQRQRIAIARAL 495
Cdd:PRK11650 81 VFQNYALYpHMSVRENMAYglkiRGMPKAEIEErVAEAARILELEPL-------LDRKPRE----LSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-561 |
9.31e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 9.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 339 TGDVEFRNVTFTYPGR---DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL-----REY 410
Cdd:PRK13645 4 SKDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 411 TLASLRNQVALVSQ--NVHLFNDTVANNIAYARTEQYSREQiEEAARMAYAMDFINKMDNgldtVIGENGVLLSGGQRQR 488
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLPED----YVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEK-ADEIVVVEDGVIVERGT 561
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
343-557 |
1.10e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 95.95 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRD--VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREY---TLASLRN 417
Cdd:PRK10535 6 ELKDIRRSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 Q-VALVSQNVHLFND-TVANNI----AYArteqysreQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:PRK10535 86 EhFGFIFQRYHLLSHlTAAQNVevpaVYA--------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIVVVEDGVIV 557
Cdd:PRK10535 156 ARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-560 |
1.33e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.94 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytLASLRNQVA 420
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLF-NDTVANNIAY-------ARTEQYSR-EQIEEAARMAYAMDFINKMdngldtvigengvlLSGGQRQRIAI 491
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFglklagaKKEEINQRvNQVAEVLQLAHLLDRKPKA--------------LSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEKADEIVVVEDGVIVERG 560
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-566 |
1.34e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHL-FNDTV 433
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNIAYARTEQYSR-EQIEEAARMAY--AMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
Cdd:PRK09536 95 RQVVEMGRTPHRSRfDTWTETDRAAVerAME-----RTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 511 LDTESE-RAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
44-289 |
1.57e-20 |
|
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: 92.14 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 44 MLSLLKPL-----LDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK 118
Cdd:cd18567 16 LFALASPLylqlvIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 119 QSTGTLLSRItyDS-EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIIlIVLAPIVSIAIRVVS-KRFRNIsknm 196
Cdd:cd18567 96 RHLGDIVSRF--GSlDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALI-VLAAVALYALLRLALyPPLRRA---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 197 qnTMGQVTTSAEQ------MLKGHKEVLIFGGQEVETKRF-----DKVSNRMRLQGMKMVSASsisdpIIQLIASLALAF 265
Cdd:cd18567 169 --TEEQIVASAKEqshfleTIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQILFSA-----ANGLLFGLENIL 241
|
250 260
....*....|....*....|....*
3B5W_D 266 VLYAASFpSVMD-SLTAGTITVVFS 289
Cdd:cd18567 242 VIYLGAL-LVLDgEFTVGMLFAFLA 265
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
343-568 |
2.24e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.05 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGR-------DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLrEYTLASL 415
Cdd:COG4167 6 EVRNLSKTFKYRtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQ-VALVSQNVhlfNDTVANNIAYAR------------TEQYSREQIEEAARMA-----YAMDFINkmdngldtvigen 477
Cdd:COG4167 85 RCKhIRMIFQDP---NTSLNPRLNIGQileeplrlntdlTAEEREERIFATLRLVgllpeHANFYPH------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 478 gvLLSGGQRQRIAIARALLRDSPILILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVED 553
Cdd:COG4167 149 --MLSSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqIINLMLELQEKLgiSYIYVSQHLGIVKHiSDKVLVMHQ 225
|
250
....*....|....*
3B5W_D 554 GVIVERGTHNDLLEH 568
Cdd:COG4167 226 GEVVEYGKTAEVFAN 240
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-568 |
4.44e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.79 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLR----NQVALVSQNVHLF-NDT 432
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANNIAYArteqYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PRK10070 123 VLDNTAFG----MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 513 TESERAIQAALDELQ--KNRTSLVIAHRL-STIEKADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
355-565 |
5.09e-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: 88.97 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTlASLRNQVALVSQNVHLFNDTVA 434
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGIVFQDLSVDDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 435 --NNIAYARTEQYSREQIEEaaRMAYAMDFINKMDNGlDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:cd03265 91 weNLYIHARLYGVPGAERRE--RIDELLDFVGLLEAA-DRLVKT----YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 513 TESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:cd03265 164 PQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
360-566 |
6.23e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.66 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 360 RNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFND-TVANNIA 438
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 439 ---YARTEQYSREQIEEAARMAYAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:PRK10253 104 rgrYPHQPLFTRWRKEDEEAVTKAM-----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 516 ERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK10253 179 QIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
358-560 |
7.00e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDiDEGEILMDGHDLREYT---LASLRNQVALVSQ------NVHL 428
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQdpnsslNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 fndTVANNIAYA-RTEQYSREQIEEAARMAYAMdfinkMDNGLDTVI-----GEngvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:PRK15134 380 ---NVLQIIEEGlRVHQPTLSAAQREQQVIAVM-----EEVGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 503 ILDEATSALDTESERAIQAALDELQ-KNRTS-LVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQqKHQLAyLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-576 |
1.11e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNV--HLFNDTVANNIAYART-----EQYSREQIEEAARMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARA 494
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPInlgldEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTI-EKADEIVVVEDGVIVERGTHNDLLEHRGV 571
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
....*
3B5W_D 572 YAQLH 576
Cdd:PRK13652 232 LARVH 236
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
358-569 |
1.29e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.97 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLAslRNQVALVSQNVHLFND-TV 433
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERA--RAGIAYVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNI--AYARTEQYSREQIEEAarmaYAMDFInkmdngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
Cdd:TIGR03410 93 EENLltGLAALPRRSRKIPDEI----YELFPV------LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 512 DTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEHR 569
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-565 |
2.70e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.63 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLReytlASLRNQVA- 420
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 ------LVSQNvhlfndTVANNIAY-ARTEQYSREQIEEAAR--------MAYAMDFINKmdngldtvigengvlLSGGQ 485
Cdd:COG4152 76 lpeergLYPKM------KVGEQLVYlARLKGLSKAEAKRRADewlerlglGDRANKKVEE---------------LSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSlVI--AHRLSTIEK-ADEIVVVEDGVIVERGTH 562
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVLSGSV 213
|
...
3B5W_D 563 NDL 565
Cdd:COG4152 214 DEI 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
341-566 |
3.12e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRF-------YDidEGEILMDGHDL---REY 410
Cdd:PRK15134 7 AIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLlhaSEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 411 TLASLR-NQVAL------VSQN-VHLFNDTVANNIAY--------ARTEQYS---REQIEEAA-RMAyamDFINKmdngl 470
Cdd:PRK15134 85 TLRGVRgNKIAMifqepmVSLNpLHTLEKQLYEVLSLhrgmrreaARGEILNcldRVGIRQAAkRLT---DYPHQ----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 471 dtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADE 547
Cdd:PRK15134 157 ----------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADR 226
|
250
....*....|....*....
3B5W_D 548 IVVVEDGVIVERGTHNDLL 566
Cdd:PRK15134 227 VAVMQNGRCVEQNRAATLF 245
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
355-560 |
3.58e-19 |
|
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: 86.04 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGEILMDGHDLREYTlaslrnqvalvsqnvhlfndt 432
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP--------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 vanniayarteqysreqIEEAARMAYAMDFIN-------KMDNGLDTVigenGVLLSGGQRQRIAIARALLRDSPILILD 505
Cdd:cd03217 71 -----------------PEERARLGIFLAFQYppeipgvKNADFLRYV----NEGFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEKADEIVVVEDGVIVERG 560
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
359-566 |
6.71e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.56 E-value: 6.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR-------------EYTLASLRNQVALVSQN 425
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 VHLFND-TVANNIAYARTEQYSREQIEEAARmayAMDFINKMdnGLD-TVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK10619 101 FNLWSHmTVLENVMEAPIQVLGLSKQEARER---AVKYLAKV--GIDeRAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 504 LDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
343-558 |
7.87e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.85 E-value: 7.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGEILMDG-----HDLREytlaSL 415
Cdd:NF040905 3 EMRGITKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGevcrfKDIRD----SE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQVALVSQNVHLFND-TVANNIaYARTEQYSREQIEEAARMAYAMDFINKMdnGL----DTVIGENGVllsgGQRQRIA 490
Cdd:NF040905 77 ALGIVIIHQELALIPYlSIAENI-FLGNERAKRGVIDWNETNRRARELLAKV--GLdespDTLVTDIGV----GKQQLVE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEIVVVEDGVIVE 558
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-565 |
7.91e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 89.72 E-value: 7.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAsLRNQVA- 420
Cdd:PRK15439 12 LCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 -LVSQNVHLF-NDTVANNIAY--ARTEQYSREQIEEAARMAYAMDfinkmdngLDTVIGengvLLSGGQRQRIAIARALL 496
Cdd:PRK15439 89 yLVPQEPLLFpNLSVKENILFglPKRQASMQKMKQLLAALGCQLD--------LDSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
342-565 |
1.53e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.52 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTypgRDVPALRNINLKIPAGKTVALVGRSGSGKS-TIASL-------ITRFydidEGEILMDGhdlREYTLA 413
Cdd:PRK10418 5 IELRNIALQ---AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAlgilpagVRQT----AGRVLLDG---KPVAPC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQ-VALVSQNVH-LFNdTVANNIAYARTEQYSREQIEEAARMAYAMDFInkmdnGLD---TVIGENGVLLSGGQRQR 488
Cdd:PRK10418 75 ALRGRkIATIMQNPRsAFN-PLHTMHTHARETCLALGKPADDATLTAALEAV-----GLEnaaRVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-568 |
1.81e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--------------------GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL 401
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 402 MDGhdlreyTLASLrnqVAL---------VSQNVHLfndtvanniaYARTEQYSREQIEEaaRMAYAMDF--INKMdngL 470
Cdd:COG1134 85 VNG------RVSAL---LELgagfhpeltGRENIYL----------NGRLLGLSRKEIDE--KFDEIVEFaeLGDF---I 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 471 DTVIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SERAiQAALDELQKNRTSLVIA-HRLSTIEK-ADE 547
Cdd:COG1134 141 DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKC-LARIRELRESGRTVIFVsHSMGAVRRlCDR 215
|
250 260
....*....|....*....|.
3B5W_D 548 IVVVEDGVIVERGTHNDLLEH 568
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEVIAA 236
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-570 |
1.89e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.81 E-value: 1.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL-REYTLAslRNQVA 420
Cdd:PRK13536 42 IDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFND-TVANN-IAYARTEQYSREQIEEAarMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEAV--IPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 499 SPILILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEK-ADEIVVVEDGV-IVERGTHNDLLEHRG 570
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-554 |
4.25e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.96 E-value: 4.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILmdghdlreytlaslrnqval 421
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVhlfndtvanNIAYarTEQysreqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03221 59 WGSTV---------KIGY--FEQ------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 502 LILDEATSALDTESERAIQAALDELQknRTSLVIAH-R--LSTIekADEIVVVEDG 554
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-560 |
5.99e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.15 E-value: 5.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 333 RVIERATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTL 412
Cdd:cd03267 11 RVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 413 ASLRNQVALVSQNVHLFNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
Cdd:cd03267 91 KFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLD-LEELLDTPVRQ----LSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
66-309 |
6.55e-18 |
|
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: 84.45 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 66 WMPLVVIGL---MILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYdSEQVASSSSGA 142
Cdd:cd18569 40 WLRPLLLGMaltALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQS-NDRVANLLSGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 143 LITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQ---VTTSAEQMLkghkEVLI 219
Cdd:cd18569 119 LATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKltgTTMSGLQMI----ETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 220 FGGQEVETkrFDKVSN---RMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMD-SLTAGTItVVFSS-MIAL 294
Cdd:cd18569 195 ASGAESDF--FSRWAGyqaKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGL-LVMDgALTIGML-VAFQSlMASF 270
|
250
....*....|....*
3B5W_D 295 MRPLKSLTNVNAQFQ 309
Cdd:cd18569 271 LAPVNSLVGLGGTLQ 285
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
71-292 |
6.67e-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: 84.64 E-value: 6.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 71 VIGLMILrgITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREG 150
Cdd:cd18558 67 IIGAIVL--ITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNI 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 151 ASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF 230
Cdd:cd18558 145 ATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRY 224
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 231 DKVSNRMRLQGMKMVSASSISDPIIQLI--ASLALAFvLYAASFPSVMDSLTAGTITVVFSSMI 292
Cdd:cd18558 225 AQNLEIAKRNGIKKAITFNISMGAAFLLiyASYALAF-WYGTYLVTQQEYSIGEVLTVFFSVLI 287
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
341-568 |
6.94e-18 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.16 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIA----SLITRFYDIdEGEILMDGHD---LREYTLA 413
Cdd:PRK09473 14 DVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAANGRI-GGSATFNGREilnLPEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLR-NQVALVsqnvhlFNDTVANNIAYART-EQY-----------SREQIEEAARMAYAMdfinKMDNGLDTvIGENGVL 480
Cdd:PRK09473 93 KLRaEQISMI------FQDPMTSLNPYMRVgEQLmevlmlhkgmsKAEAFEESVRMLDAV----KMPEARKR-MKMYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIV 557
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTM 241
|
250
....*....|.
3B5W_D 558 ERGTHNDLLEH 568
Cdd:PRK09473 242 EYGNARDVFYQ 252
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-554 |
9.46e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 9.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTL---ASLRNQ-VALVSQNVHLFND-TV 433
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNIAYAR-TEQYSREQIEEAAR-MAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
Cdd:PRK11629 105 LENVAMPLlIGKKKPAEINSRALeMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3B5W_D 512 DTESERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEIVVVEDG 554
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-544 |
1.95e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.46 E-value: 1.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:PRK10908 2 IRFEHVSKAYLG-GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANN------IAYARTEQYSReqieeaaRMAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAI 491
Cdd:PRK10908 81 IGMIFQDHHLLMDrTVYDNvaipliIAGASGDDIRR-------RVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTIEK 544
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISR 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
342-560 |
3.22e-17 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.04 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYP--------------------GRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL 401
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 402 MDGhdlreyTLASLrnqVAL---------VSQNVHLfndtvaNNIAYARTEQYSREQIEEAARMAYAMDFInkmdnglDT 472
Cdd:cd03220 81 VRG------RVSSL---LGLgggfnpeltGRENIYL------NGRLLGLSRKEIDEKIDEIIEFSELGDFI-------DL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 473 VIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEK-ADEIVV 550
Cdd:cd03220 139 PVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALV 214
|
250
....*....|
3B5W_D 551 VEDGVIVERG 560
Cdd:cd03220 215 LEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-561 |
3.59e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLAslRNQVALVSQNVHLFND-TV 433
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQIA--RMGVVRTFQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNIAYA--------------RTEQYSREQIEEAARMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGT 561
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGT 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-544 |
3.90e-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: 3.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHdlreytlaslrNQVAL 421
Cdd:cd03223 1 IELENLSLATPDGRV-LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVanniayarteqysREQIeeaarmAYAMDFInkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03223 69 LPQRPYLPLGTL-------------REQL------IYPWDDV-----------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200
....*....|....*....|....*....|....*....|....
3B5W_D 502 LILDEATSALDTESERAIQAALDELqknRTSLV-IAHRlSTIEK 544
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHR-PSLWK 152
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-566 |
4.18e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGEILMDGHDL--REYTLAS 414
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQNVHLFNDTVANNIAYA------RTEQYSREQIEEAARMAYAMDFI-NKmdngldtvIGENGVLLSGGQRQ 487
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLWDEIkHK--------IHKSALDLSGGQQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALD--ELQKNRTSLVIAHRLSTIEKADEIVVV------EDGVIVER 559
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEF 237
|
....*..
3B5W_D 560 GTHNDLL 566
Cdd:PRK14258 238 GLTKKIF 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-568 |
4.81e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGEILMDGHDL--REYTLAS 414
Cdd:PRK14267 5 IETVNLRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQNVHLF-NDTVANNIA-------YARTEQYSREQIEEAARMAYAMDfinKMDNGLDTVIGEngvlLSGGQR 486
Cdd:PRK14267 83 VRREVGMVFQYPNPFpHLTIYDNVAigvklngLVKSKKELDERVEWALKKAALWD---EVKDRLNDYPSN----LSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKV 235
|
...
3B5W_D 566 LEH 568
Cdd:PRK14267 236 FEN 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-567 |
4.90e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTY-PGRDVP--ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI----LMDGHDLREYTLAS 414
Cdd:PRK13643 2 IKFEKVNYTYqPNSPFAsrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRNQVALVSQ--NVHLFNDTVANNIAYA-RTEQYSREQIEEAArmAYAMDFInkmdnGLDTVIGENGVL-LSGGQRQRIA 490
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpQNFGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPFeLSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
60-309 |
6.76e-17 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 81.45 E-value: 6.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 60 DRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSS 139
Cdd:cd18568 37 NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 140 SGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLI 219
Cdd:cd18568 116 TRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 220 FGgqeVETKRFDKVSNRM------RLQGMKMVSASSIsdpIIQLIASLALAFVL-YAASFpsVMD-SLTAGTItVVFSSM 291
Cdd:cd18568 196 LA---AERPIRWRWENKFakalntRFRGQKLSIVLQL---ISSLINHLGTIAVLwYGAYL--VISgQLTIGQL-VAFNML 266
|
250
....*....|....*....
3B5W_D 292 IA-LMRPLKSLTNVNAQFQ 309
Cdd:cd18568 267 FGsVINPLLALVGLWDELQ 285
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
342-558 |
7.43e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 83.87 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVAL 421
Cdd:PRK10522 323 LELRNVTFAYQDNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFNDTVANNIAYARTEQYsrEQIEEAARMAYAMDFinkmdngldtvigENGVL----LSGGQRQRIAIARALLR 497
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANPALV--EKWLERLKMAHKLEL-------------EDGRIsnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 498 DSPILILDEATSALDTESERAI-QAALDELQ-KNRTSLVIAHRLSTIEKADEIVVVEDGVIVE 558
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
343-559 |
8.24e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 8.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLASLR-NQVAL 421
Cdd:PRK10762 6 QLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKsSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VS---QNVHLF-NDTVANNIAYAR--TEQYSR----EQIEEAARMAYAMdfinKMDNGLDTVIGEngvlLSGGQRQRIAI 491
Cdd:PRK10762 81 IGiihQELNLIpQLTIAENIFLGRefVNRFGRidwkKMYAEADKLLARL----NLRFSSDKLVGE----LSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 492 ARALLRDSPILILDEATSAL-DTESErAIQAALDELQKNRTSLV-IAHRLSTI-EKADEIVVVEDG-VIVER 559
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGqFIAER 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-567 |
1.01e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.75 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 354 RDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH---DLREYTLASLRNQVALVSQNVHLFN 430
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 D---TVANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:PRK10261 415 DprqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 508 TSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLE 567
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
345-571 |
1.11e-16 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.51 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASlRNQVAL--V 422
Cdd:cd03218 4 ENLSKRYGKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK-RARLGIgyL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFND-TVANNI-AYARTEQYSREQIEEaaRMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03218 81 PQEASIFRKlTVEENIlAVLEIRGLSKKEREE--KLEELLE-----EFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEKADEIVVVEDGVIVERGTHNDLLEHRGV 571
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-561 |
2.40e-16 |
|
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: 83.14 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 357 PALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLrEYTLASLRNQVALVSQNVHLFND-TVAN 435
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 436 NIA-YARTEQYSRE--QIEEAARMAyamdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:TIGR01257 1023 HILfYAQLKGRSWEeaQLEMEAMLE---------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
3B5W_D 513 TESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEIVVVEDGVIVERGT 561
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-561 |
2.58e-16 |
|
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: 81.77 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLI--TRFYDIDEGEIL------------------ 401
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 402 ---------------MDGHDLREYTLASLRNQVALVSQNVHLF--NDTVANNIAYARTE-QYSREqieEAARMAYAMDFI 463
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEiGYEGK---EAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 464 NKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST 541
Cdd:TIGR03269 156 VQLSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|.
3B5W_D 542 IEK-ADEIVVVEDGVIVERGT 561
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGT 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-554 |
2.62e-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: 81.79 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGEILMDGHDLREYTLASL-RNQ 418
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYArteqysREQIEEAARMAYAMDFIN--------KMDNGLDT-VIGENGvllsGGQRQR 488
Cdd:TIGR02633 80 IVIIHQELTLVPElSVAENIFLG------NEITLPGGRMAYNAMYLRaknllrelQLDADNVTrPVGDYG----GGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 489 IAIARALLRDSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEK-ADEIVVVEDG 554
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-571 |
3.01e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 79.51 E-value: 3.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH--DLREYTLASLRNQV 419
Cdd:PRK13636 6 LKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNV--HLFNDTVANNIAY-ARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARALL 496
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFgAVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIE-KADEIVVVEDGVIVERGTHNDLLEHRGV 571
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
45-309 |
4.04e-16 |
|
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: 79.09 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 45 LSLLKPLL-----DDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQ 119
Cdd:cd18555 17 LTLLIPILtqyviDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 120 STGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLApIVSIAIRVVSKRfRNISKNMQNT 199
Cdd:cd18555 97 SSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRK-KIKKLNQEEI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 200 MGQVTTSAEQ--MLKGHKEVLIFGgqeVETKRFDKVSNRMrlqgMKMVSA-------SSISDPIIQLIASLALAFVLYAA 270
Cdd:cd18555 174 VAQTKVQSYLteTLYGIETIKSLG---SEKNIYKKWENLF----KKQLKAfkkkerlSNILNSISSSIQFIAPLLILWIG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
3B5W_D 271 SFPSVMDSLTAGTItVVFSSM-IALMRPLKSLTNVNAQFQ 309
Cdd:cd18555 247 AYLVINGELTLGEL-IAFSSLaGSFLTPIVSLINSYNQFI 285
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
336-573 |
4.49e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 4.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 336 ERATGDV--EFRNVTftypgrDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLA 413
Cdd:COG1129 249 AAAPGEVvlEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 S----LRNQVALVSQNVH---LF-NDTVANNIAYARTEQYSREQ-IEEAARMAYAMDFINKMD---NGLDTVIGEngvlL 481
Cdd:COG1129 320 SprdaIRAGIAYVPEDRKgegLVlDLSIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLRiktPSPEQPVGN----L 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhrlST-----IEKADEIVVVEDGVI 556
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRI 472
|
250
....*....|....*..
3B5W_D 557 VERGTHNDLLEHRGVYA 573
Cdd:COG1129 473 VGELDREEATEEAIMAA 489
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-568 |
6.37e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.69 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 339 TGDVEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASlRNQ 418
Cdd:PRK13537 5 VAPIDFRNVEKRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNI-AYARTEQYSREQIEeaARMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
Cdd:PRK13537 82 VGVVPQFDNLDPDfTVRENLlVFGRYFGLSAAAAR--ALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
30-237 |
6.73e-16 |
|
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: 78.51 E-value: 6.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 30 AGVALILNAASDTFMLSLLKPLLDD-----GFGKTDRSVLVwMPLVVIGLMILRGITSYVSSYCISwvsgKVVMTMRRRL 104
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGiviekSQDKFSRAIII-MGLLAIASSVAAGIRGGLFTLAMA----RLNIRIRNLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 105 FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRV 184
Cdd:cd18784 76 FRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
3B5W_D 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRM 237
Cdd:cd18784 156 YGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDT 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
359-554 |
8.13e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 77.12 E-value: 8.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhdlREYTLASLRNQValVSQNVHLFN-DTVANNI 437
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQITEPGPDRMV--VFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 438 AYA---------RTEQysREQIEEAarmayaMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:TIGR01184 76 ALAvdrvlpdlsKSER--RAIVEEH------IALVG-LTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
3B5W_D 509 SALDTESERAIQAALDEL-QKNR-TSLVIAHRL-STIEKADEIVVVEDG 554
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIwEEHRvTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-557 |
8.80e-16 |
|
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: 76.93 E-value: 8.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVT--FTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLIT---RFYDIDEGEILMDGHDLREYTLaslR 416
Cdd:cd03234 4 LPWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQF---Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NQVALVSQ-NVHLFNDTVANNIAYARTEQYSREQIEEAARMayaMDFINKMDNGLDTVIGENGVL-LSGGQRQRIAIARA 494
Cdd:cd03234 81 KCVAYVRQdDILLPGLTVRETLTYTAILRLPRKSSDAIRKK---RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEKADEIVVVEDGVIV 557
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-554 |
9.35e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 75.55 E-value: 9.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQ-VALVSqnvhlfndtvann 436
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 437 iayarteqysreqiEEAARMAYAMDFinkmdngldtVIGEN---GVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:cd03215 82 --------------EDRKREGLVLDL----------SVAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
3B5W_D 514 ESERAIQAALDEL-QKNRTSLVIahrlST-----IEKADEIVVVEDG 554
Cdd:cd03215 138 GAKAEIYRLIRELaDAGKAVLLI----SSeldelLGLCDRILVMYEG 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
358-568 |
1.48e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.98 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTI----ASLITRfYDIDEGEILMDGHDL-REYTLA----SLRNQVALVSQNVHL 428
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITG-DKSAGSHIELLGRTVqREGRLArdirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 FND-TVANNI--------AYART--EQYSREQIEEAARMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLR 497
Cdd:PRK09984 98 VNRlSVLENVligalgstPFWRTcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEIVVVEDG-VIVERGTH---NDLLEH 568
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGhVFYDGSSQqfdNERFDH 247
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
358-560 |
1.61e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 76.85 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlASLRNQVALVSQNVH-------LFN 430
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQSEEvdwsfpvLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVA----NNIAYAR-TEQYSREQIEEAARMAYAMDFINKMdngldtvIGEngvlLSGGQRQRIAIARALLRDSPILILD 505
Cdd:PRK15056 99 DVVMmgryGHMGWLRrAKKRDRQIVTAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 506 EATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEKADEIVVVEDGVIVERG 560
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-559 |
2.14e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 351 YPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHdlreyTLASLRNQVALVSQNVHLFN 430
Cdd:PRK11248 11 YGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 -DTVANNIAYA-RTEQYSREQIEEAARmayamdfinKMDNGLDTVIGENGVL--LSGGQRQRIAIARALLRDSPILILDE 506
Cdd:PRK11248 84 wRNVQDNVAFGlQLAGVEKMQRLEIAH---------QMLKKVGLEGAEKRYIwqLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 507 ATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEK----ADEIVVVE--DGVIVER 559
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwqETGKQVLLITH---DIEEavfmATELVLLSpgPGRVVER 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-565 |
3.16e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLA-SLRNQVA 420
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFND-TVANNIAYAR--TEQYSREQIEEAARM---AYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGRhlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-561 |
3.60e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT--LASLRNQVALVS 423
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QNVH------LFND---------TVANNIAYA-RTEQ-YSREQ-IEEAARMayaMDFINKMDNglDTVIGENGVLLSGGQ 485
Cdd:PRK10261 99 RHVRgadmamIFQEpmtslnpvfTVGEQIAESiRLHQgASREEaMVEAKRM---LDQVRIPEA--QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV--IAHRLSTI-EKADEIVVVEDGVIVERGT 561
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVaEIADRVLVMYQGEAVETGS 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
359-560 |
3.67e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.38 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKST----IASLITRFYDIDEGEILMDGHDLREYtLASLRNQVALVSQN-VHLFNDTV 433
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETdVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNIAYA--------RTEQYSREqiEEAARMA-YAMDfINKMDNGLDTVIGEN---GVllSGGQRQRIAIARALLRDSPI 501
Cdd:TIGR00956 156 GETLDFAarcktpqnRPDGVSRE--EYAKHIAdVYMA-TYGLSHTRNTKVGNDfvrGV--SGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 502 LILDEATSALDT----ESERAIQAALDELqkNRTSLVIAHRLS--TIEKADEIVVVEDGVIVERG 560
Cdd:TIGR00956 231 QCWDNATRGLDSatalEFIRALKTSANIL--DTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
346-546 |
4.03e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.22 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREyTLASLRNQVALVSQN 425
Cdd:PRK13540 6 ELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 VHLF-NDTVANNIAYARTEQYSREQIEEAARmayamdfINKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK13540 83 SGINpYLTLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
3B5W_D 505 DEATSALDtesERAIQAALDELQKNRTS----LVIAHRLSTIEKAD 546
Cdd:PRK13540 152 DEPLVALD---ELSLLTIITKIQEHRAKggavLLTSHQDLPLNKAD 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
355-570 |
6.45e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGEILMDGHDLREYTlASLRNQVALVSQNVHLFNDT 432
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANN-----IAY-ARTEQYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVL--LSGGQRQRIAIARALLRDSPILIL 504
Cdd:CHL00131 98 GVSNadflrLAYnSKRKFQGLPELDPLEFLEIINEKLKLV--GMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 505 DEATSALDTESERAIQAALDELQKNRTSLV-IAH--RLSTIEKADEIVVVEDGVIVERGTHN--DLLEHRG 570
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-566 |
8.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGEILMDGHDLREY-TLASLRNQV 419
Cdd:PRK14271 26 NLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNVHLFNDTVANNIaYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNV-LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
32-314 |
1.08e-14 |
|
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: 74.62 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 32 VALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRN 191
Cdd:cd18561 83 GPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 192 ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAAS 271
Cdd:cd18561 163 TGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGA 242
|
250 260 270 280
....*....|....*....|....*....|....*....|...
3B5W_D 272 FPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18561 243 LRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-566 |
1.25e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR-------DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLrEYTLAS 414
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 LRnqvalvSQNVHL-FNDtvanniayARTEQYSREQIEEAarmayaMDFINKMDNGLDTVIGENGV-------------- 479
Cdd:PRK15112 84 YR------SQRIRMiFQD--------PSTSLNPRQRISQI------LDFPLRLNTDLEPEQREKQIietlrqvgllpdha 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 -----LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVV 551
Cdd:PRK15112 144 syyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVM 223
|
250
....*....|....*
3B5W_D 552 EDGVIVERGTHNDLL 566
Cdd:PRK15112 224 HQGEVVERGSTADVL 238
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
342-565 |
2.40e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 73.26 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHD---LREYTLASLRNQ 418
Cdd:PRK11831 8 VDMRGVSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 419 VALVSQNVHLFND-TVANNIAYARTEQysrEQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPLREH---TQLPAPLLHSTVMMKLEAV--GLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEKADEIVVVEDGVIVERGTHNDL 565
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
368-580 |
3.35e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.66 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 368 AGKTVALVGRSGSGKST----IASLITrfydiDEGEILMDGHDLREYTLASLRNQVALVSQNVH-LFNDTV----ANNIA 438
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVfqylTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 439 YARTEQYSREQIEEAARMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARALLRDSP-------ILILDEATSAL 511
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----------LSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 512 DTeserAIQAALDEL-----QKNRTSLVIAHRLS-TIEKADEIVVVEDGVIVERGTHNDLLEHRGVyAQLHKMQF 580
Cdd:PRK03695 165 DV----AQQAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFGVNF 234
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
72-279 |
4.02e-14 |
|
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: 73.27 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSS------YCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT 145
Cdd:cd18589 39 ITVMSLLTIASAVSEfvcdliYNIT--MSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 146 VVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEV 225
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEG 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 226 ETKRFdkvsnRMRLQGMKMVS------------ASSISDPII---------QLIASLAL------AFVLYAASFPSVMDS 278
Cdd:cd18589 197 EAQRY-----RQRLQKTYRLNkkeaaayavsmwTSSFSGLALkvgilyyggQLVTAGTVssgdlvTFVLYELQFTSAVEV 271
|
.
3B5W_D 279 L 279
Cdd:cd18589 272 L 272
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-567 |
5.32e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGR---DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI---LMDGHDLREYTLAS- 414
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 415 --------------------LRNQVALVSQ--NVHLFNDTVANNIAY-ARTEQYSREQIEEAARmayamDFINKMdnGLD 471
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFgPVSMGVSKEEAKKRAA-----KYIELV--GLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 472 -TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL-STIEKADEI 548
Cdd:PRK13651 156 eSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*....
3B5W_D 549 VVVEDGVIVERGTHNDLLE 567
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILS 254
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-560 |
6.10e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 72.35 E-value: 6.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 338 ATGDVEFRNvtftypgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGH--DLREYTLASL 415
Cdd:PRK13638 3 ATSDLWFRY-------QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 416 RNQVALVSQN--VHLFNDTVANNIAYARTEQYSREqiEEAARmayamdfinKMDNGLdTVIGENGV------LLSGGQRQ 487
Cdd:PRK13638 76 RQQVATVFQDpeQQIFYTDIDSDIAFSLRNLGVPE--AEITR---------RVDEAL-TLVDAQHFrhqpiqCLSHGQKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVERG 560
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHG 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
353-565 |
6.57e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 353 GRDVPALR-------NINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDlreYTLASLRNQVALVS-Q 424
Cdd:PRK13539 5 GEDLACVRggrvlfsGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLGhR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFNDTVANNIAY-ARTEQYSREQIEEAArmaYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK13539 82 NAMKPALTVAENLEFwAAFLGGEELDIAAAL---EAV--------GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 504 LDEATSALDteseRAIQAALDELqknrtslvIAHRLstiekadeivvvEDGVIVERGTHNDL 565
Cdd:PRK13539 151 LDEPTAALD----AAAVALFAEL--------IRAHL------------AQGGIVIAATHIPL 188
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-571 |
8.99e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.06 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpGRdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLAS-LRNQVA 420
Cdd:PRK11614 6 LSFDKVSAHY-GK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 421 LVSQNVHLFND-TVANNIA----YARTEQYSReqieeaaRMAYAMDFINKMdngLDTVIGENGVLlSGGQRQRIAIARAL 495
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAmggfFAERDQFQE-------RIKWVYELFPRL---HERRIQRAGTM-SGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 496 LRDSPILILDEATSALdteSERAIQAALDELQKNRTS-----LVIAHRLSTIEKADEIVVVEDGVIVERGTHNDLLEHRG 570
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
3B5W_D 571 V 571
Cdd:PRK11614 230 V 230
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
72-238 |
1.01e-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: 71.99 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSSYC----ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVV 147
Cdd:cd18590 39 IGLMCLFSLGSSLSAGLrgglFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 148 REGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEA 198
|
170
....*....|.
3B5W_D 228 KRFDKVSNRMR 238
Cdd:cd18590 199 CRYSEALERTY 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
345-554 |
1.06e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.61 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGrdVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR-EYTLASLRNQVALVS 423
Cdd:PRK10982 2 SNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QNVHLFND-TVANNIAYARteqYSREQ--IEEAARMAYAMDFINKMDNGLDTviGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:PRK10982 80 QELNLVLQrSVMDNMWLGR---YPTKGmfVDQDKMYRDTKAIFDELDIDIDP--RAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 501 ILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEK-ADEIVVVEDG 554
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-557 |
2.14e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.75 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 336 ERATGDV--EFRNVTFTyPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDL------ 407
Cdd:COG3845 250 PAEPGEVvlEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglspr 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 408 --REYTLASL---RNQVALVSqnvhlfNDTVANNIA--YARTEQYSRE-QIEEAARMAYAMDFINKMD---NGLDTVIGe 476
Cdd:COG3845 329 erRRLGVAYIpedRLGRGLVP------DMSVAENLIlgRYRRPPFSRGgFLDRKAIRAFAEELIEEFDvrtPGPDTPAR- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 477 ngvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EKADEIVVVEDG 554
Cdd:COG3845 402 ---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAvLLISEDLDEIlALSDRIAVMYEG 478
|
...
3B5W_D 555 VIV 557
Cdd:COG3845 479 RIV 481
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
346-571 |
2.38e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 346 NVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTL-ASLRNQVALVSQ 424
Cdd:PRK10895 8 NLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFND-TVANNIAYART--EQYSREQIEEAARMAYAMDFINKMDNGLdtvigenGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:PRK10895 86 EASIFRRlSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRL-STIEKADEIVVVEDGVIVERGTHNDLLEHRGV 571
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
343-525 |
2.99e-13 |
|
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: 68.54 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNqVALV 422
Cdd:TIGR01189 2 AARNLACSRGER--MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-ILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFND-TVANNIA-YARTEQYSREQIEEA-ARMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:TIGR01189 79 GHLPGLKPElSALENLHfWAAIHGGAQRTIEDAlAAV------------GLTGFEDLPAAQLSAGQQRRLALARLWLSRR 146
|
170 180
....*....|....*....|....*.
3B5W_D 500 PILILDEATSALDTESERAIQAALDE 525
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-560 |
4.85e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 361 NINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHdlreyTLASLRNQVAL---------VSQNVHLF-N 430
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR-----VLFDAEKGICLppekrrigyVFQDARLFpH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 431 DTVANNIAYArteqysreqieeaarMAyamdfiNKMDNGLDTVIGENGV---------LLSGGQRQRIAIARALLRDSPI 501
Cdd:PRK11144 91 YKVRGNLRYG---------------MA------KSMVAQFDKIVALLGIeplldrypgSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 502 LILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERG 560
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAReiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
363-555 |
6.51e-13 |
|
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: 71.35 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 363 NLKIP-AGKTVALVGRSGSGKSTIAS-----LITRFYDIDEG----EIL--MDGHDLREYtLASLRNQ---VALVSQNVH 427
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrFRGTELQDY-FKKLANGeikVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 428 L----FNDTVanniayarteqysREQIEEAARMAYAMDFINK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPI 501
Cdd:COG1245 171 LipkvFKGTV-------------RELLEKVDERGKLDELAEKlgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 502 LILDEATSALD----TESERAIQaalDELQKNRTSLVIAHRLSTIEK-ADEIVVV--EDGV 555
Cdd:COG1245 234 YFFDEPSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAILDYlADYVHILygEPGV 291
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
359-561 |
7.77e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 71.23 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKST----IASLITRFYDIDeGEILMDGH--DLREYTLASlrnqvALVSQNVHLFND- 431
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnaLAFRSPKGVKGS-GSVLLNGMpiDAKEMRAIS-----AYVQQDDLFIPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 TVANNIAY-AR---TEQYSREQieeaaRMAYAMDFINKMdnGL----DTVIGENGVL--LSGGQRQRIAIARALLRDSPI 501
Cdd:TIGR00955 115 TVREHLMFqAHlrmPRRVTKKE-----KRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 502 LILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEIVVVEDGVIVERGT 561
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
72-314 |
2.29e-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: 67.96 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASS-----SSGalitv 146
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSfkqcvSQG----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 147 VREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVE 226
Cdd:cd18574 124 LRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 227 TKRFDKVSNRMRlqgmKMVSASSISDPIIQLIASLALA----FVLYAASFPSVMDSLTAGTITvvfSSMIALMRPLKSLT 302
Cdd:cd18574 204 LELYEEEVEKAA----KLNEKLGLGIGIFQGLSNLALNgivlGVLYYGGSLVSRGELTAGDLM---SFLVATQTIQRSLA 276
|
250
....*....|....*
3B5W_D 303 NVNA---QFQRGMAA 314
Cdd:cd18574 277 QLSVlfgQYVKGKSA 291
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
344-557 |
2.56e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 2.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 344 FRNVTFTYPGRDV--PALRNINLKIPAGKTVALVGRSGSGKST----IASLITRFYDIdEGEILMDGHDLREyTLASLRN 417
Cdd:cd03233 6 WRNISFTTGKGRSkiPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE-FAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 418 QVALVSQN-VHLFNDTVanniayarteqysREQIEEAARMayamdfinkmdNGLDTVIGengvlLSGGQRQRIAIARALL 496
Cdd:cd03233 84 EIIYVSEEdVHFPTLTV-------------RETLDFALRC-----------KGNEFVRG-----ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 497 RDSPILILDEATSALDTESeraiqaALDELQKNRTslvIAH--RLSTI-----------EKADEIVVVEDGVIV 557
Cdd:cd03233 135 SRASVLCWDNSTRGLDSST------ALEILKCIRT---MADvlKTTTFvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
345-506 |
2.88e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 66.59 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTL---AslRNQVAL 421
Cdd:COG1137 7 ENLVKSYGKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrA--RLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLFND-TVANNI-AYARTEQYSREQIEEaaRMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:COG1137 83 LPQEASIFRKlTVEDNIlAVLELRKLSKKEREE--RLEELLE-----EFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
....*..
3B5W_D 500 PILILDE 506
Cdd:COG1137 156 KFILLDE 162
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
62-190 |
6.03e-12 |
|
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: 66.77 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 62 SVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSSSG 141
Cdd:cd18783 39 STLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTG 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
3B5W_D 142 ALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFR 190
Cdd:cd18783 118 QLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFR 166
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-567 |
6.32e-12 |
|
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: 68.29 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 324 SEQEKDegkRVIERATGDVEFRNVTFTYPGRD---VPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEI 400
Cdd:TIGR03269 265 SEVEKE---CEVEVGEPIIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 401 -------LMDGHDLREYTLASLRNQVALVSQNVHLF-NDTVANNIayarTEQYSREQIEEAARMA-------------YA 459
Cdd:TIGR03269 342 nvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMKavitlkmvgfdeeKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 460 MDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERA----IQAALDELqkNRTSLVI 535
Cdd:TIGR03269 418 EEILDKYPDEL-----------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEM--EQTFIIV 484
|
250 260 270
....*....|....*....|....*....|...
3B5W_D 536 AHRLSTI-EKADEIVVVEDGVIVERGTHNDLLE 567
Cdd:TIGR03269 485 SHDMDFVlDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
362-523 |
6.89e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.82 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 362 INLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQNVHLFNDTVANNIAYAR 441
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 442 TEqYSREQIEEAarmayamdfinkmdngLDTViGENGV------LLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03231 99 AD-HSDEQVEEA----------------LARV-GLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
3B5W_D 516 ERAIQAAL 523
Cdd:cd03231 161 VARFAEAM 168
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
341-565 |
7.59e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 66.69 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKS----TIASLITRFYDIDEGEILMDGHDLREYTLASLR 416
Cdd:PRK11022 5 NVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 NqvaLVSQNVHL-FNDTVAN-NIAYarTEQYsreQIEEA----------ARMAYAMDFINKM-----DNGLDTVIGEngv 479
Cdd:PRK11022 85 N---LVGAEVAMiFQDPMTSlNPCY--TVGF---QIMEAikvhqggnkkTRRQRAIDLLNQVgipdpASRLDVYPHQ--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 lLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEIVVVEDGVI 556
Cdd:PRK11022 154 -LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*....
3B5W_D 557 VERGTHNDL 565
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-576 |
9.33e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 9.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 354 RDVPALRNINLKIPAGKTVALVGRSGSGKST----IASLITRfydiDEGEILMDGHD--LREYTLASlrnQVALV----S 423
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVpfKRRKEFAR---RIGVVfgqrS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QnvhLFND-TVANNIAYAR------TEQYsREQIEEAARMayaMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
Cdd:COG4586 106 Q---LWWDlPAIDSFRLLKaiyripDAEY-KKRLDELVEL---LD----LGELLDTPVRQ----LSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEHRGVYA 573
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
3B5W_D 574 QLH 576
Cdd:COG4586 251 TIV 253
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-551 |
9.84e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.53 E-value: 9.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 363 NLKIP-AGKTVALVGRSGSGKSTIAS-----LITRFYDIDEG----EIL--MDGHDLREYtLASLRNQ---VALVSQNVH 427
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEpswdEVLkrFRGTELQNY-FKKLYNGeikVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 428 L----FNDTVANNIayarteqysrEQIEEAARMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK13409 171 LipkvFKGKVRELL----------KKVDERGKLDEVVERLG-LENILDRDISE----LSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
3B5W_D 504 LDEATSALD----TESERAIQaaldELQKNRTSLVIAHRLSTIEK-ADEIVVV 551
Cdd:PRK13409 236 FDEPTSYLDirqrLNVARLIR----ELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
359-535 |
1.07e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR---EYTLASLRNQ-VALVSQNVHLFNDTVA 434
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 435 -NNI---AYAR--TEQYSREQieeaarmayAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:PRK10584 106 lENVelpALLRgeSSRQSRNG---------AKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180
....*....|....*....|....*..
3B5W_D 509 SALDTESERAIQAALDELQKNRTSLVI 535
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
359-566 |
1.24e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTI---------ASLITRFYDIdEGEILMDGHDLREY---TLASLRNQVALVSQNV 426
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARV-TGDVTLNGEPLAAIdapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 427 HLFNdtvANNIA------YAR----TEQYSREQIEEAARMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARAL- 495
Cdd:PRK13547 96 FAFS---AREIVllgrypHARragaLTHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 496 --------LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHND 564
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPAD 241
|
..
3B5W_D 565 LL 566
Cdd:PRK13547 242 VL 243
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
369-559 |
4.85e-11 |
|
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: 61.24 E-value: 4.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 369 GKTVALVGRSGSGKSTIASLITRFYDIDEGEILM-DGHDLREYTLASLRNqvalvsqnvhlfndtvanniayarteqysr 447
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 448 eqieeaarmayamdfinkmdngldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD--- 524
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*...
3B5W_D 525 ---ELQKNRTSLVIAHRLSTIEKADEIVVVEDGVIVER 559
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
355-557 |
5.26e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGhDLreyTLASL-----RNqvalVSQNVHlf 429
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL---IVARLqqdppRN----VEGTVY-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 430 nDTVANNIA--------YART-----EQYSREQIEEAARMAYAMDFIN--KMDNGLDTVIGENGV-------LLSGGQRQ 487
Cdd:PRK11147 85 -DFVAEGIEeqaeylkrYHDIshlveTDPSEKNLNELAKLQEQLDHHNlwQLENRINEVLAQLGLdpdaalsSLSGGWLR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTEserAIQaALDELQKN-RTSLV-IAHRLSTIEK-ADEIVVVEDGVIV 557
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIE---TIE-WLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
72-182 |
7.60e-11 |
|
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: 63.29 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREGA 151
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTLVLDLV 127
|
90 100 110
....*....|....*....|....*....|.
3B5W_D 152 SIIGLFIMMFYYSWQLSiiLIVLAPIVSIAI 182
Cdd:cd18588 128 FSVVFLAVMFYYSPTLT--LIVLASLPLYAL 156
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-554 |
1.65e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.36 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 323 DSEQEKDEgkrviERATGDVEF--RNVTFTYP--GRDVPALRNINLKIPAGKTVALVGRSGSGKST----IASLITRFYd 394
Cdd:TIGR00956 744 DVNDEKDM-----EKESGEDIFhwRNLTYEVKikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnvLAERVTTGV- 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 395 IDEGEILMDGHDLREytlaSLRNQVALVSQN-VHLFNDTVANNIAY-ARTEQYSREQIEEaaRMAYAMDFIN--KMDNGL 470
Cdd:TIGR00956 818 ITGGDRLVNGRPLDS----SFQRSIGYVQQQdLHLPTSTVRESLRFsAYLRQPKSVSKSE--KMEYVEEVIKllEMESYA 891
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 471 DTVIGENGVLLSGGQRQRIAIARALLRDSPILI-LDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTI--EKAD 546
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAIlfEEFD 971
|
....*...
3B5W_D 547 EIVVVEDG 554
Cdd:TIGR00956 972 RLLLLQKG 979
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
2.23e-10 |
|
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: 61.48 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTI------ASLITRFYdidEGEILMDGHDlREYTLASLrNQVALVSQNvhLFNDT 432
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlyPALARRLH---LKKEQPGNHD-RIEGLEHI-DKVIVIDQS--PIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANNIA-YA--------------RTEQYSRE-----------------QIEEAA-------RMAYAMDFInkMDNGLDTV 473
Cdd:cd03271 84 PRSNPAtYTgvfdeirelfcevcKGKRYNREtlevrykgksiadvldmTVEEALeffenipKIARKLQTL--CDVGLGYI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 474 -IGENGVLLSGGQRQRIAIARALLRDSP---ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEI 548
Cdd:cd03271 162 kLGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWI 241
|
.
3B5W_D 549 V 549
Cdd:cd03271 242 I 242
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
355-570 |
3.01e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 355 DVPALRNINLKIPAGKTVALVGRSGSGKSTI-ASLITRF-YDIDEGEILMDGHDLREYT---------LASLRNQVALVS 423
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSpedragegiFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 424 QNVHLFNDTVANNIayartEQYsREQiEEAARMAYAmDFINK----MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PRK09580 93 VSNQFFLQTALNAV-----RSY-RGQ-EPLDRFDFQ-DLMEEkialLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA---HRLSTIEKADEIVVVEDGVIVERGTHN--DLLEHRG 570
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQG 240
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
27-197 |
5.02e-10 |
|
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: 60.98 E-value: 5.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFMLSLLKPLLDDGFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLApivsIAIRVVS 186
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL----VVYYLLQ 156
|
170
....*....|.
3B5W_D 187 KRFRNISKNMQ 197
Cdd:cd18580 157 RYYLRTSRQLR 167
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-554 |
7.62e-10 |
|
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: 59.73 E-value: 7.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 369 GKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR---EYTLASLRNQV-ALVSQNVHLFNdtvanNIAYARTEQ 444
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKADYEGTVrDLLSSITKDFY-----THPYFKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 445 YSREQIEEAarmayamdfinkMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQ 520
Cdd:cd03237 100 AKPLQIEQI------------LDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasKVIR 159
|
170 180 190
....*....|....*....|....*....|....
3B5W_D 521 AALDELQKnrTSLVIAHRLSTIEKADEIVVVEDG 554
Cdd:cd03237 160 RFAENNEK--TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
70-309 |
1.09e-09 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 59.90 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 70 VVIGLMILRGITSYVssycISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVRE 149
Cdd:cd18566 51 AILLESLLRLLRSYI----LAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 150 GASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKR 229
Cdd:cd18566 126 LPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 230 FDKVSNRMRLQGMKMVSASSISDPIIQLIASLA-LAFVLYAASFpsVMD-SLTAGTItvVFSSMIA--LMRPLKSLTNVN 305
Cdd:cd18566 206 YERLQANAAYAGFKVAKINAVAQTLGQLFSQVSmVAVVAFGALL--VINgDLTVGAL--IACTMLSgrVLQPLQRAFGLW 281
|
....
3B5W_D 306 AQFQ 309
Cdd:cd18566 282 TRFQ 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
342-570 |
1.79e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlASLRNQV-- 419
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 --ALVSQ----NvhLFND-TVANNIAY-ARteQYSREQIEEAARMAYAMDfinkmDNGL----DTVIGEngvlLSGGQRQ 487
Cdd:NF033858 77 riAYMPQglgkN--LYPTlSVFENLDFfGR--LFGQDAAERRRRIDELLR-----ATGLapfaDRPAGK----LSGGMKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIahrLST--IEKA---DEIVVVEDGVIVERGT 561
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMsVL---VATayMEEAerfDWLVAMDAGRVLATGT 220
|
....*....
3B5W_D 562 HNDLLEHRG 570
Cdd:NF033858 221 PAELLARTG 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
344-554 |
1.98e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 57.25 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 344 FRNVTFTY--PGRDVPALRNINLKIPAGKTVALVGRSGSGKST---------IASLITrfydideGEILMDGHDLREytl 412
Cdd:cd03232 6 WKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVIT-------GEILINGRPLDK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 413 aSLRNQVALVSQN-VHLFNDTVanniayarteqysREQIEEAARMayamdfinkmdNGldtvigengvlLSGGQRQRIAI 491
Cdd:cd03232 76 -NFQRSTGYVEQQdVHSPNLTV-------------REALRFSALL-----------RG-----------LSVEQRKRLTI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS--TIEKADEIVVVEDG 554
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-555 |
3.17e-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: 57.76 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 364 LKIPA-GKTVALVGRSGSGKSTIASLIT--------RFYDIDEGEILMD---GHDLREYtLASLRN---QVALVSQNVHL 428
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNY-FTKLLEgdvKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 429 FNDTVANNIAYARTEQYSREQIEEAARmayAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDELVD---QLELRHVLDRNIDQ--------LSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
3B5W_D 509 SALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIVVVEDGV 555
Cdd:cd03236 168 SYLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-294 |
3.53e-09 |
|
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: 58.26 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 122 GTLLSRITYDSEQ-------VASSSSGALITvvregasIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRF-RNIS 193
Cdd:cd18585 92 GDLLNRIVADIDTldnlylrVLSPPVVALLV-------ILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLgKKIG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 194 KNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASfp 273
Cdd:cd18585 165 QQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGA-- 242
|
170 180
....*....|....*....|.
3B5W_D 274 svmDSLTAGTITVVFSSMIAL 294
Cdd:cd18585 243 ---PLVQNGALDGALLAMLVF 260
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-191 |
3.76e-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: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 69 LVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVR 148
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|...
3B5W_D 149 EGASIIGLFIMMFYYSWQLSIILIVLAPIVSIAIRVVSKRFRN 191
Cdd:cd18782 125 DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
336-552 |
6.36e-09 |
|
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: 58.64 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 336 ERATGDVEFRNVTFTYPgRDVPALRNINLKIPAGK-----TVALVGRSGSGKSTIASLITRFYDIDEGEILMDghdlrey 410
Cdd:COG1245 329 VHAPRREKEEETLVEYP-DLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 411 tlasLRnqVALVSQNV-HLFNDTVANNIAYARTEQY--SREQIEEAARMAyamdfINK-MDNGLDTvigengvlLSGGQR 486
Cdd:COG1245 401 ----LK--ISYKPQYIsPDYDGTVEEFLRSANTDDFgsSYYKTEIIKPLG-----LEKlLDKNVKD--------LSGGEL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 487 QRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDElqKNRTSLVIAHRLSTIEK-ADEIVVVE 552
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRFAEN--RGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
363-575 |
6.55e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 363 NLKIPAGKTVALVGRSGSGKSTIASLItrfydidEGE-ILMDGH---DLREYTLASLRNQVALVSQ-----NVHLFND-- 431
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGElPLLSGErqsQFSHITRLSFEQLQKLVSDewqrnNTDMLSPge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 -----TVANNIayarteqysREQIEEAAR-MAYAMDFinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILD 505
Cdd:PRK10938 96 ddtgrTTAEII---------QDEVKDPARcEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 506 EATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EKADEIVVVEDGVIVERGTHNDLLEhRGVYAQL 575
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ-QALVAQL 231
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
342-566 |
1.09e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.12 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVT--FTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLIT--------------RFYDIDEgeilmdgh 405
Cdd:PRK15093 4 LDIRNLTieFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDIDL-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 406 dLReytlASLRNQVALVSQNVHL-FNDTVAnniAYARTEQYSREQIEEAARMAY--------------AMDFINKMdnGL 470
Cdd:PRK15093 76 -LR----LSPRERRKLVGHNVSMiFQEPQS---CLDPSERVGRQLMQNIPGWTYkgrwwqrfgwrkrrAIELLHRV--GI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 471 ---DTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK- 544
Cdd:PRK15093 146 kdhKDAMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQw 225
|
250 260
....*....|....*....|..
3B5W_D 545 ADEIVVVEDGVIVERGTHNDLL 566
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELV 247
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-564 |
1.43e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTftypGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT-LASLRNQVAL 421
Cdd:PRK09700 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVH---LF-NDTVANNIAYARTEQYSR--------EQIEEAARMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRI 489
Cdd:PRK09700 343 ITESRRdngFFpNFSIAQNMAISRSLKDGGykgamglfHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQQKV 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EKADEIVVVEDGVIVERGTHND 564
Cdd:PRK09700 419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQILTNRD 495
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
350-549 |
2.50e-08 |
|
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: 53.87 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 350 TYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASlitrfydidegEILMDGHDLREYTLASL--RNQVALVSQNVH 427
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKfsRNKLIFIDQLQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 428 LfndtVANNIAYARTEQysreqieeaarmayamdfinKMDNgldtvigengvlLSGGQRQRIAIARALLRDSP--ILILD 505
Cdd:cd03238 71 L----IDVGLGYLTLGQ--------------------KLST------------LSGGELQRVKLASELFSEPPgtLFILD 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3B5W_D 506 EATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEIV 549
Cdd:cd03238 115 EPSTGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWII 159
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
345-560 |
2.67e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGRDvpALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNqvalvSQ 424
Cdd:PRK11701 10 RGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE-----AE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 425 NVHLFndtvanniayaRTE-----QYSReqieEAARMA------------------Y------AMDFINKMDNGLDTvIG 475
Cdd:PRK11701 83 RRRLL-----------RTEwgfvhQHPR----DGLRMQvsaggnigerlmavgarhYgdiratAGDWLERVEIDAAR-ID 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 476 ENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLSTIE-KADEI 548
Cdd:PRK11701 147 DLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDLAVARlLAHRL 222
|
250
....*....|..
3B5W_D 549 VVVEDGVIVERG 560
Cdd:PRK11701 223 LVMKQGRVVESG 234
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
481-552 |
2.92e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 2.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESE----RAIQAALDElqKNRTSLVIAHRLSTIEK-ADEIVVVE 552
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaKAIRRIAEE--REATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
357-538 |
3.05e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 357 PALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVSQnvhlFNDTVAnn 436
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----FKDAVE-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 437 iayarteqysreqIEEAARMAYAMDFINKMDNgldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:COG2401 118 -------------LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|....
3B5W_D 517 RAIQAALDEL-QKNRTSLVIA-HR 538
Cdd:COG2401 173 KRVARNLQKLaRRAGITLVVAtHH 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-515 |
3.40e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 56.28 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVTFTYPGrDVPALRNINLKIPAGKTVALVGRSGSGKSTI----ASLITRFydidEGE-ILMDG--------------- 404
Cdd:PRK11819 10 NRVSKVVPP-KKQILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKEF----EGEaRPAPGikvgylpqepqldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 405 HDLREYTLASLRNQVALVSQnvhlFNDTvanNIAYARTEQYSREQIEEAARMAYAMDFIN--KMDNGL------------ 470
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDR----FNEI---YAAYAEPDADFDALAAEQGELQEIIDAADawDLDSQLeiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
3B5W_D 471 DTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
360-525 |
3.66e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 360 RNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREytlasLRNQVAlvsQNV----HL--FND-- 431
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYH---QDLlylgHQpgIKTel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 TVANNIA-YAR-TEQYSREQIEEA-ARMayamdfinkmdnGL----DTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK13538 90 TALENLRfYQRlHGPGDDEALWEAlAQV------------GLagfeDVPVRQ----LSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|.
3B5W_D 505 DEATSALDTESERAIQAALDE 525
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
479-552 |
4.37e-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: 53.34 E-value: 4.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEK-ADEIVVVE 552
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
342-549 |
5.10e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDgHDLReytlaslrnqVAL 421
Cdd:PRK09544 5 VSLENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR----------IGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQNVHLfNDTVANNIA-YARTEQYSREQ-IEEAARMAYAMDFINK-MDNgldtvigengvlLSGGQRQRIAIARALLRD 498
Cdd:PRK09544 72 VPQKLYL-DTTLPLTVNrFLRLRPGTKKEdILPALKRVQAGHLIDApMQK------------LSGGETQRVLLARALLNR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EKADEIV 549
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVL 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
335-519 |
5.53e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 5.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 335 IERATGDVEFRNVTFTYPGrdvpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLA- 413
Cdd:PRK10762 249 LDKAPGEVRLKVDNLSGPG-----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQVALVSQNVH----LFNDTVANNIAYARTEQYSRE--QIEEAARMAYAMDFInKMDN----GLDTVIGengvLLSG 483
Cdd:PRK10762 324 GLANGIVYISEDRKrdglVLGMSVKENMSLTALRYFSRAggSLKHADEQQAVSDFI-RLFNiktpSMEQAIG----LLSG 398
|
170 180 190
....*....|....*....|....*....|....*.
3B5W_D 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
342-541 |
5.69e-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: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMdGHDLreytlaslrnQVAL 421
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQnvhlFNDTVANNiayaRT--EQYS--REQIE----EAARMAYAMDFINKmdnGLDT--VIGEngvlLSGGQRQRIAI 491
Cdd:TIGR03719 390 VDQ----SRDALDPN----KTvwEEISggLDIIKlgkrEIPSRAYVGRFNFK---GSDQqkKVGQ----LSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
3B5W_D 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST 541
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
103-318 |
5.77e-08 |
|
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: 54.54 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLF-IMMFYYSWQLSIILIV---LAPIV 178
Cdd:cd18560 76 KTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSvVFAFHFGAWLALIVFLsvlLYGVF 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 179 SIAIRVVSKRFRNISKNMQNTMGQVTTSAeqmLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLI 258
Cdd:cd18560 156 TIKVTEWRTKFRRAANKKDNEAHDIAVDS---LLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLI 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 259 ASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTL 318
Cdd:cd18560 233 IQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-556 |
8.02e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 360 RNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTL-----------------------ASLR 416
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyldAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 417 -NQVALVSQNVHLFNDTVANNiayARTEQYSR------EQIEEAARMayamdfinkmdngldtvigengvlLSGGQRQRI 489
Cdd:PRK15439 360 wNVCALTHNRRGFWIKPAREN---AVLERYRRalnikfNHAEQAART------------------------LSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEK-ADEIVVVEDGVI 556
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
345-568 |
8.15e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.53 E-value: 8.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 345 RNVT--FTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLIT--------------RFYDIDegeIL-MDGHDL 407
Cdd:COG4170 7 RNLTieIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICgitkdnwhvtadrfRWNGID---LLkLSPRER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 408 REYTlaslRNQVALVSQnvhlfndtvaNNIAYARTEQYSREQIEEA---------------ARMAYAMDFINKmdngldt 472
Cdd:COG4170 84 RKII----GREIAMIFQ----------EPSSCLDPSAKIGDQLIEAipswtfkgkwwqrfkWRKKRAIELLHR------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 473 vIG---ENGVL------LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST 541
Cdd:COG4170 143 -VGikdHKDIMnsypheLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLES 221
|
250 260
....*....|....*....|....*...
3B5W_D 542 IEK-ADEIVVVEDGVIVERGTHNDLLEH 568
Cdd:COG4170 222 ISQwADTITVLYCGQTVESGPTEQILKS 249
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-515 |
1.05e-07 |
|
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: 54.56 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 352 PGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTI----ASLITRFydidEGE-ILMDG---------------HDLREYT 411
Cdd:TIGR03719 16 PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKDF----NGEaRPQPGikvgylpqepqldptKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 412 LASLRNQVALVSQnvhlFNDTVAnniAYARTEQYSREQIEEAARMAYAMDFIN--KMDNGLDTVI-------GENGV-LL 481
Cdd:TIGR03719 90 EEGVAEIKDALDR----FNEISA---KYAEPDADFDKLAAEQAELQEIIDAADawDLDSQLEIAMdalrcppWDADVtKL 162
|
170 180 190
....*....|....*....|....*....|....
3B5W_D 482 SGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
336-512 |
1.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 336 ERATGDV--EFRNVTFTYP-GRDVPALRNINLKIPAGKTVALVGRSGSGKS-TIASLITRFYDIDEGEILMDGHDLREYT 411
Cdd:PRK13549 252 PHTIGEVilEVRNLTAWDPvNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRN 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 412 LA-SLRNQVALVSQN------VHLFNdtVANNIAYARTEQYS-REQIEEAARMAYAMDFINKMD---NGLDTVIGEngvl 480
Cdd:PRK13549 332 PQqAIAQGIAMVPEDrkrdgiVPVMG--VGKNITLAALDRFTgGSRIDDAAELKTILESIQRLKvktASPELAIAR---- 405
|
170 180 190
....*....|....*....|....*....|..
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-571 |
1.63e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMdghdlreytlaSLRNQVAL 421
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------SENANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQ-NVHLF-ND-TVANNIAYARTEQYSrEQIEEAA--RMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALL 496
Cdd:PRK15064 387 YAQdHAYDFeNDlTLFDWMSQWRQEGDD-EQAVRGTlgRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST--IEkadeivVVEDGVIVERGTHNDLLEH 568
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdrefvsSLATriIE------ITPDGVVDFSGTYEEYLRS 526
|
...
3B5W_D 569 RGV 571
Cdd:PRK15064 527 QGI 529
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
481-549 |
2.14e-07 |
|
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: 50.82 E-value: 2.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3B5W_D 481 LSGGQRQRIAIARAL----LRDSPILILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEKADEIV 549
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
32-187 |
2.34e-07 |
|
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: 52.54 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 32 VALILNAASDTFMLSLLKPLLddgFGKTDRSVLVWMPLVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18781 7 ISLLANIAFVFSIANLLQKLL---EGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSG-------ALItvvregASIIgLFIMMFYYSWQLSIILIVLAPIVSIAIRV 184
Cdd:cd18781 84 GPSYQEKVSTAEVVQLSVEGVEQLEIYFGRylpqffySML------APLT-LFVVLAPINWKAALVLLICVPLIPISIIA 156
|
...
3B5W_D 185 VSK 187
Cdd:cd18781 157 VQK 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
321-543 |
2.44e-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: 54.25 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 321 ILDSEQE-KDEGKRVIE--RATGDVEFRNVTFTYPGRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDE 397
Cdd:TIGR01257 1914 IFDEDDDvAEERQRIISggNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS 1993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 398 GEILMDGHdlreytlaSLRNQVALVSQNV-----------------HLFndtvanniAYARTEQYSREQIEEAARMAyam 460
Cdd:TIGR01257 1994 GDATVAGK--------SILTNISDVHQNMgycpqfdaiddlltgreHLY--------LYARLRGVPAEEIEKVANWS--- 2054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 461 dfINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRL 539
Cdd:TIGR01257 2055 --IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
....
3B5W_D 540 STIE 543
Cdd:TIGR01257 2131 EECE 2134
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
66-188 |
2.81e-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: 52.55 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 66 WMPLVVIGLMIL---RGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRitydseqVASSS--- 139
Cdd:cd18779 40 LLGVLGLGLAALvltQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMR-------LSSNAtir 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
3B5W_D 140 ---SGALITVVREGASIIGLFIMMFYYSWQLSIILIVLApIVSIAIRVVSKR 188
Cdd:cd18779 113 ellTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLA-ALQVALLLATRR 163
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-554 |
3.38e-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: 52.90 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 339 TGDV--EFRNVTFTYP-GRDVPALRNINLKIPAGKTVALVGRSGSGKS-TIASLITRFYDIDEGEILMDGHDLREYTLA- 413
Cdd:TIGR02633 253 IGDVilEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAq 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQVALVSQNVH----LFNDTVANNIAYARTEQYS-REQIEEAARMAYAMDFINKMD---NGLDTVIGEngvlLSGGQ 485
Cdd:TIGR02633 333 AIRAGIAMVPEDRKrhgiVPILGVGKNITLSVLKSFCfKMRIDAAAELQIIGSAIQRLKvktASPFLPIGR----LSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3B5W_D 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTIEK-ADEIVVVEDG 554
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVLGlSDRVLVIGEG 479
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
28-266 |
4.06e-07 |
|
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: 52.03 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 28 IVAGVALILNAAsdtfmlsLLKPLLDDGFGKTDRSVLVWMPLVV-IGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18584 6 LLAALLIIAQAW-------LLARIIAGVFLEGAGLAALLPLLLLlLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegASII--GLFIMMFYYSWQLSIILIVLAPIVSIAIRV 184
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVL--AAIVplLILVAVFPLDWVSALILLVTAPLIPLFMIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMK-----MVSASsisdpIIQLIA 259
Cdd:cd18584 157 IGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKvlrvaFLSSA-----VLEFFA 231
|
....*..
3B5W_D 260 SLALAFV 266
Cdd:cd18584 232 TLSIALV 238
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-540 |
4.57e-07 |
|
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: 52.83 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 27 LIVAGVALILNAASDTFML----SLLKPLLDDGFGKTDRSVLVWMplvVIGLMIlrgitSYVSSYcISWVSGKVVMTMRR 102
Cdd:TIGR00954 98 LILIAFLLVSRTYLSVYVAtldgQIESSIVRRSPRNFAWILFKWF---LIAPPA-----SFINSA-IKYLLKELKLRFRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 103 RLFGHMMGMPVSFFDKQSTGTLLSRI-------TYDSEQVASSSSGALITVVRegaSIIGLFIMMFYY----SWQLSIIL 171
Cdd:TIGR00954 169 RLTRYLYSKYLSGFTFYKVSNLDSRIqnpdqllTQDVEKFCDSVVELYSNLTK---PILDVILYSFKLltalGSVGPAGL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 172 IVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSIS 251
Cdd:TIGR00954 246 FAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETVMSSFYRLVEHLNLIIKFRFSY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 252 DPIIQLIAS-LALAFVLYAASFPSVM----------------DSLTAGTITVVFSSMIA-LMRPLKSLT----------- 302
Cdd:TIGR00954 326 GFLDNIVAKyTWSAVGLVAVSIPIFDkthpaflemseeelmqEFYNNGRLLLKAADALGrLMLAGRDMTrlagftarvdt 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 303 ------NVNA-QFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDVEFRNVTFTYPGRDVpALRNINLKIPAGKTVALV 375
Cdd:TIGR00954 406 llqvldDVKSgNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDV-LIESLSFEVPSGNNLLIC 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 376 GRSGSGKSTIASLITRFYDIDEGEILMDGhdlreytlaslRNQVALVSQNVHLFNDTVANNIAYA-RTEQYSREQIEEAA 454
Cdd:TIGR00954 485 GPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIYPdSSEDMKRRGLSDKD 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 455 RMAY----AMDFINKMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDElqKNR 530
Cdd:TIGR00954 554 LEQIldnvQLTHILEREGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGI 630
|
570
....*....|
3B5W_D 531 TSLVIAHRLS 540
Cdd:TIGR00954 631 TLFSVSHRKS 640
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
7.84e-07 |
|
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: 50.33 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIAslitrFYDI-DEGEilmdghdlREY--TLAS-LRNQVALVSQ-NV-HLFNDT 432
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA-----FDTIyAEGQ--------RRYveSLSAyARQFLGQMDKpDVdSIEGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANNIAYARTEQYSRE------QIEEAARMAYAMDFINK-----MDNGLDTV-IGENGVLLSGGQRQRIAIARAL---Lr 497
Cdd:cd03270 78 PAIAIDQKTTSRNPRStvgtvtEIYDYLRLLFARVGIRErlgflVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIgsgL- 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
3B5W_D 498 DSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEKADEIV 549
Cdd:cd03270 157 TGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-554 |
8.83e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.80 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 369 GKTVALVGRSGSGKSTIASLIT-RFYDID-EGEILMDGHDLREYTLaslrNQVALVSQNVHLF-NDTVANNIAYAR---- 441
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQIL----KRTGFVTQDDILYpHLTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 442 TEQYSREQIEEAARMAYAMDFINKMDNgldTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSALD-TESERAI 519
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*..
3B5W_D 520 QAALDELQKNRTSLVIAHRLST--IEKADEIVVVEDG 554
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
466-549 |
9.13e-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: 51.94 E-value: 9.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQ----KNRTSLVIAH 537
Cdd:TIGR00630 814 CDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDD---IKKLLEVLQrlvdKGNTVVVIEH 890
|
90
....*....|..
3B5W_D 538 RLSTIEKADEIV 549
Cdd:TIGR00630 891 NLDVIKTADYII 902
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
44-295 |
1.21e-06 |
|
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: 50.52 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 44 MLSLLKPLL-----DDGFGKTDRSVLVwmpLVVIGLMILrGITSYVSSYCISW----VSGKVVMTMRRRLFGHMMGMPVS 114
Cdd:cd18571 16 LLQLIFPFLtqsivDKGINNKDLNFIY---LILIAQLVL-FLGSTSIEFIRSWillhISSRINISIISDFLIKLMRLPIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 115 FFDKQSTGTLLSRItYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLApIVSIA-------IRVV-- 185
Cdd:cd18571 92 FFDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGS-VLYILwillflkKRKKld 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 186 SKRFRNISKNMQNTMgqvttsaeQMLKGHKEVLIFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAF 265
Cdd:cd18571 170 YKRFDLSSENQSKLI--------ELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNIL 241
|
250 260 270
....*....|....*....|....*....|
3B5W_D 266 VLYAASFpSVMDsltaGTITvvFSSMIALM 295
Cdd:cd18571 242 ITFLAAK-LVID----GEIT--LGMMLAIQ 264
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-554 |
1.80e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIASLI----TRFYDidEGEILMDGHDLREYTLASLRnqvALVSQN-VHLFNDTV 433
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKKQETFARIS---GYCEQNdIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 434 ANNIAYARTEQYSREqIEEAARMAYA---MDFInKMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:PLN03140 971 RESLIYSAFLRLPKE-VSKEEKMMFVdevMELV-ELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
3B5W_D 510 ALDTESE----RAIQAALDelqKNRTSLVIAHRLS--TIEKADEIVVVEDG 554
Cdd:PLN03140 1049 GLDARAAaivmRTVRNTVD---TGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
480-556 |
2.67e-06 |
|
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: 50.74 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 LLSGGQRQRIAIA--RALL--RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVV---E 552
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVtmvE 1156
|
....
3B5W_D 553 DGVI 556
Cdd:pfam02463 1157 NGVS 1160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
342-542 |
3.85e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYpgRDVPALRNINLKIPAGKTVALVGRSGSGKSTIASLIT----RFYDID---------EGEILMDghdlr 408
Cdd:PRK10938 261 IVLNNGVVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYSNDltlfgrrrgSGETIWD----- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 409 eytlasLRNQVALVSQNVHL---FNDTVANNIAYARTEQYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVL-LSGG 484
Cdd:PRK10938 334 ------IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3B5W_D 485 QrQRIA-IARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLV------------IAHRLSTI 542
Cdd:PRK10938 406 Q-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFV 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-537 |
4.51e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 341 DVEFRNVTFTYPGRDVPALRNINLKIpaGKTVALVGRSGSGKSTIASLITrFYDID-----------EGEILMDGHDLRE 409
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAF--GRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkncqilhvEQEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 410 YTLASLRNQVALVSQNVHLF-------------------NDTVANNIAYARTEQ-YSR-EQIEEAARMAYAMDFINKMDN 468
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVaqqrelefetetgkgkganKDGVDKDAVSQRLEEiYKRlELIDAYTAEARAASILAGLSF 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
3B5W_D 469 GLDTVIGENGVLlSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
Cdd:PLN03073 334 TPEMQVKATKTF-SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-554 |
4.92e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRdvPAL-RNINLKIPAGKTVALVGRSGSGKSTIASLITrfydideGEIL-MDGHDLReytlaSLRNQV 419
Cdd:PLN03073 509 ISFSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GELQpSSGTVFR-----SAKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQNvHLFN-DTVANNIAY-ARTEQYSREQieeaarmayamdfinKMDNGLDTvIGENGVL-------LSGGQRQRIA 490
Cdd:PLN03073 575 AVFSQH-HVDGlDLSSNPLLYmMRCFPGVPEQ---------------KLRAHLGS-FGVTGNLalqpmytLSGGQKSRVA 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIE-KADEIVVVEDG 554
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISgSVDELWVVSEG 700
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
343-537 |
5.06e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 343 EFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMdGHDLreytlaslrnQVALV 422
Cdd:PRK11147 321 EMENVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKL----------EVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 423 SQNVHLFN--DTVANNIAYARTEqysreqIEEAAR----MAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAIARALL 496
Cdd:PRK11147 388 DQHRAELDpeKTVMDNLAEGKQE------VMVNGRprhvLGYLQDFLFHPKRAMTPVKA-----LSGGERNRLLLARLFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
3B5W_D 497 RDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
Cdd:PRK11147 457 KPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
358-572 |
6.85e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.73 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYTLASLRNQVALVsQNVHLfndtvaNNI 437
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-ENIEL------KGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 438 AYARTEQYSREQIEEAARMAYAMDFINKmdnGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQ---PVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
3B5W_D 518 AIQAALDELQKN-RTSLVIAHRLSTIEK-ADEIVVVEDGVIVERGTHNDLLEHRGVY 572
Cdd:PRK13545 181 KCLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
342-525 |
9.12e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 342 VEFRNVTFTYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIlmdghDLREyTLaslrnQVAL 421
Cdd:PRK11819 325 IEAENLSKSFGDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIGE-TV-----KLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 422 VSQN-VHLFND-TV-------ANNIAYARTEQYSReqieeaarmAYAMDFINKmdnGLDT--VIGEngvlLSGGQRQRIA 490
Cdd:PRK11819 392 VDQSrDALDPNkTVweeisggLDIIKVGNREIPSR---------AYVGRFNFK---GGDQqkKVGV----LSGGERNRLH 455
|
170 180 190
....*....|....*....|....*....|....*
3B5W_D 491 IARALLRDSPILILDEATSALDTESERAIQAALDE 525
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
72-178 |
9.68e-06 |
|
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: 47.47 E-value: 9.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 72 IGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGA 151
Cdd:cd18606 42 AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLS 121
|
90 100
....*....|....*....|....*..
3B5W_D 152 SIIGLFIMMFYYswqLSIILIVLAPIV 178
Cdd:cd18606 122 SIIGTFILIIIY---LPWFAIALPPLL 145
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
480-555 |
9.76e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 46.69 E-value: 9.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 LLSGGQRQRIAIAR--ALLR--DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVV---E 552
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvrPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVtmqE 192
|
...
3B5W_D 553 DGV 555
Cdd:cd03278 193 SGV 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
481-552 |
1.04e-05 |
|
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: 46.83 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 LSGGQRQ------RIAIARALLRDSPILILDEATSALDTES-ERAIQAALDEL--QKNRTSLVIAHRLSTIEKADEIVVV 551
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERksQKNFQLIVITHDEELVDAADHIYRV 195
|
.
3B5W_D 552 E 552
Cdd:cd03240 196 E 196
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
350-512 |
1.06e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 350 TYPGRDVpaLRNINLKIPAGKTVALVGRSGSGKSTIA-SLITRFYDID-EGEILMDGHDLREYTLA-SLRNQVALVSQN- 425
Cdd:NF040905 269 LHPERKV--VDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDGKEVDVSTVSdAIDAGLAYVTEDr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 426 ----VHLfNDTVANNIAYARTEQYSREQ-IEEAARMAYAMDFINKMD---NGLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:NF040905 347 kgygLNL-IDDIKRNITLANLGKVSRRGvIDENEEIKVAEEYRKKMNiktPSVFQKVGN----LSGGNQQKVVLSKWLFT 421
|
170
....*....|....*
3B5W_D 498 DSPILILDEATSALD 512
Cdd:NF040905 422 DPDVLILDEPTRGID 436
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-569 |
1.51e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.60 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 336 ERATGDVEFRnvtftYPGRDVPALRN-INLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLR-EYTLA 413
Cdd:PRK11288 250 PRPLGEVRLR-----LDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRD 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 414 SLRNQVALVSQN--------VHlfndTVANNIAYARTEQYSREQ--IEEAARMAYAMDFINKMD---NGLDTVIGengvL 480
Cdd:PRK11288 325 AIRAGIMLCPEDrkaegiipVH----SVADNINISARRHHLRAGclINNRWEAENADRFIRSLNiktPSREQLIM----N 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEKADEIVVVEDGVIVE 558
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAG 476
|
250
....*....|.
3B5W_D 559 RGTHNDLLEHR 569
Cdd:PRK11288 477 ELAREQATERQ 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-535 |
2.60e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 357 PALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEILMDGHDLREYT-LASLRNQVALVSQ---------NV 426
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEerrstgiyaYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 427 HL-FNDTVANNIAY-ARTEQYSREQIEEAARmaYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK10982 342 DIgFNSLISNIRNYkNKVGLLDNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190
....*....|....*....|....*....|.
3B5W_D 505 DEATSALDTESERAIQAALDELQKNRTSLVI 535
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIII 446
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
358-512 |
4.06e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 358 ALRNINLKIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGEIL-----MDGHDLreytlaSLRNQVALVSQNVHLFND- 431
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDI------ATRRRVGYMSQAFSLYGEl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 432 TVANNIA-YARTEQYSREQIeeAARMAYAMD-FinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:NF033858 355 TVRQNLElHARLFHLPAAEI--AARVAEMLErF------DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
...
3B5W_D 510 ALD 512
Cdd:NF033858 427 GVD 429
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
26-188 |
4.87e-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: 45.31 E-value: 4.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 26 GLIVAGVALIlnaasdtfMLSLLKPLLddgFGKTDRSVLVW-MPLVVIGLMILRGITSYVSSYCISWVSGKvvMTMRRRL 104
Cdd:cd18562 3 GLALANVALA--------GVQFAEPVL---FGRVVDALSSGgDAFPLLALWAALGLFSILAGVLVALLADR--LAHRRRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 105 ------FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssGALITVVREG-ASIIGLFIMM---FYYSWQLSIILIVL 174
Cdd:cd18562 70 avmasyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALF----GLWLGFFREHlAALVSLIVLLpvaLWMNWRLALLLVVL 145
|
170
....*....|....
3B5W_D 175 APIVSIAIRVVSKR 188
Cdd:cd18562 146 AAVYAALNRLVMRR 159
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
69-235 |
7.53e-05 |
|
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: 44.84 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 69 LVVIGLMILRGITSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVaSSSSGALITVVR 148
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNL-SQVIQSFLFILS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 149 EGASIIGLFIMMFYYSWQLSIIL-IVLAPIVSIAIRVVSKRFRN---ISKNMQNTMGQVTTSAeqmLKGHKEVLIFGGQE 224
Cdd:cd18553 137 EIFVILFIYSLLLYVNWKITLVLtLFLGLNVFFITKIVSKKIKKqgkKREESQKKFYKILSET---FGNFKIIKLKSNEK 213
|
170
....*....|.
3B5W_D 225 VETKRFDKVSN 235
Cdd:cd18553 214 EILKNFSQASL 224
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
26-194 |
1.07e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 44.48 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 26 GLIVAGVAL---ILNAASDTFMLSLLKPLLDDGFGKTDRSV---------------LVWMPLVVIGLMILRGITSYVSSY 87
Cdd:cd18599 1 GYVVFLFVLllfILSVGSTVFSDWWLSYWLKQGSGNTTNNVdnstvdsgnisdnpdLNFYQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIG-LFIMMFYYSW- 165
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFsLIIIAIVFPWf 160
|
170 180 190
....*....|....*....|....*....|....
3B5W_D 166 -----QLSIILIVLAPIVSIAIRVVsKRFRNISK 194
Cdd:cd18599 161 lialiPLAIIFVFLSKIFRRAIREL-KRLENISR 193
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
67-301 |
1.29e-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: 44.03 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 67 MPLVVIGLMILRGITSYVSSYCI---SWVSGKVVM-TMRR---RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSS 139
Cdd:cd18582 33 LLAVPLLLLLAYGLARILSSLFNelrDALFARVSQrAVRRlalRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 140 SGALITVVREGASIIGLFIMMFY-YSWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVL 218
Cdd:cd18582 113 RFLLFNILPTILELLLVCGILWYlYGWSYALITLVTVALYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 219 IFGGQEVETKRFDKVSNRMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDSLTAGTITVVFSSMIALMRPL 298
Cdd:cd18582 193 YFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPL 272
|
...
3B5W_D 299 KSL 301
Cdd:cd18582 273 NFL 275
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-555 |
1.55e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 480 LLSGGQRQRIAIARA----LLRDSPILILDEATSALD-TESERAIQaALDELQKNRTSLVIAHRLSTIEKADEIVVV--- 551
Cdd:TIGR02168 1089 LLSGGEKALTALALLfaifKVKPAPFCILDEVDAPLDdANVERFAN-LLKEFSKNTQFIVITHNKGTMEVADQLYGVtmq 1167
|
....
3B5W_D 552 EDGV 555
Cdd:TIGR02168 1168 EKGV 1171
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
99-193 |
1.55e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 44.06 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 99 TMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSIILIVLAPIv 178
Cdd:cd18605 76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFI- 154
|
90
....*....|....*
3B5W_D 179 siaIRVVSKRFRNIS 193
Cdd:cd18605 155 ---YYRIQRYYRATS 166
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-567 |
1.75e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIasLITRFYDID-----EGEILMDGHDLREYTLaslRNQVALVSQN-VHLFNDT 432
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTL--LLALAGKLDpslkvSGEITYNGYRLNEFVP---RKTSAYISQNdVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 433 VANNIAYARTEQ---YSREQIEEAARM-----------------AYAM---------DFINK---MDNGLDTVIGENGVL 480
Cdd:PLN03140 256 VKETLDFSARCQgvgTRYDLLSELARRekdagifpeaevdlfmkATAMegvksslitDYTLKilgLDICKDTIVGDEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 481 -LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS----TIEKADEIVVVEDGV 555
Cdd:PLN03140 336 gISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQ 415
|
250
....*....|..
3B5W_D 556 IVERGTHNDLLE 567
Cdd:PLN03140 416 IVYQGPRDHILE 427
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-384 |
2.10e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.10e-04
10 20
....*....|....*....|....*.
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKST 384
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKST 650
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
69-197 |
6.90e-04 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 42.04 E-value: 6.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 69 LVVIGL-MILRgitsYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSfFDKQSTGTLLSRIT-YDS--EQVASSSSGALI 144
Cdd:cd18587 49 LIALLFdFILK----LLRAYFIDVAGKRADVILSSRLFERVLGLRLE-ARPASVGSFANNLReFESvrDFFTSATLTALI 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
3B5W_D 145 TVVregasIIGLFIMMFYY-SWQLSIILIVLAPIVSIAIRVVSKRFRNISKNMQ 197
Cdd:cd18587 124 DLP-----FVLLFLAVIALiGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESM 172
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-384 |
1.33e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 1.33e-03
10 20
....*....|....*....|....*.
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKST 384
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKST 646
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-386 |
1.61e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.55 E-value: 1.61e-03
10 20
....*....|....*....|....*...
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIA 386
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
466-549 |
1.70e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.60 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQK-----NrTSLVIA 536
Cdd:PRK00349 815 VDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFED---IRKLLEVLHRlvdkgN-TVVVIE 890
|
90
....*....|...
3B5W_D 537 HRLSTIEKADEIV 549
Cdd:PRK00349 891 HNLDVIKTADWII 903
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
481-549 |
1.89e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.89e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
3B5W_D 481 LSGGQRQRIAIARALLRDSP---ILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTIEKADEIV 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 |
2.23e-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: 39.21 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 475 GENGVLLSGGQRQRIAIARAL----LRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTIEKADEIV 549
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQfIVITLKKEMFENADKLI 168
|
...
3B5W_D 550 VVE 552
Cdd:cd03239 169 GVL 171
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-386 |
2.45e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 2.45e-03
10 20
....*....|....*....|....*...
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIA 386
Cdd:PRK00349 16 LKNIDLDIPRDKLVVFTGLSGSGKSSLA 43
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
359-386 |
3.15e-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: 40.38 E-value: 3.15e-03
10 20
....*....|....*....|....*...
3B5W_D 359 LRNINLKIPAGKTVALVGRSGSGKSTIA 386
Cdd:TIGR00630 12 LKNIDVEIPRDKLVVITGLSGSGKSSLA 39
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
70-175 |
4.44e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 39.37 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 70 VVIGLM-ILRGITSYVSSYCISWVSGKvvmTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVR 148
Cdd:cd18604 50 ALISLLsVLLGTLRYLLFFFGSLRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLE 126
|
90 100
....*....|....*....|....*..
3B5W_D 149 EGASIIGLFIMMFYYSWQLSIILIVLA 175
Cdd:cd18604 127 STLSLLVILIAIVVVSPAFLLPAVVLA 153
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
372-537 |
8.80e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 372 VALVGRSGSGKSTIASLITR-FY----------------DIDEGEILMD-GHDLREYTLAslRNQ--------------V 419
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYaLYgkarsrsklrsdlinvGSEEASVELEfEHGGKRYRIE--RRQgefaefleakpserK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3B5W_D 420 ALVSQnvhLFNDTVANNIA--YARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVigengVLLSGGQRQRIAIARALLr 497
Cdd:COG0419 104 EALKR---LLGLEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRLALADLLS- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
3B5W_D 498 dspiLILDeaTSALDTESERAIQAALDELQknrtslVIAH 537
Cdd:COG0419 175 ----LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| |
