|
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: 1287.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 1 MHNDKDLSTWQTFRRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGL 80
Cdd:PRK11176 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 81 TSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
Cdd:PRK11176 81 TSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 161 FYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQ 240
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFT 320
Cdd:PRK11176 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 321 ILDSEQEKDEGKRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI 400
Cdd:PRK11176 321 ILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 401 LMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVL 480
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERG 560
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
570 580
....*....|....*....|..
gi 740854059 561 THNELIEQRGVYAQLHKMQFGQ 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: 929.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 12 TFRRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISW 91
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 92 VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIL 171
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 172 IVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSIS 251
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 252 DPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEG 331
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 332 KRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT 411
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 412 LASLRDQVALVSQNVHLFNDTVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGV 571
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
570
....*....|.
gi 740854059 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: 674.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 8 STWQTFRRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSY 87
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQL 167
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 168 SLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSA 247
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 248 SSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQE 327
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 328 KDE--GKRVIERATGDLEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH 405
Cdd:COG1132 324 IPDppGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 406 DLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD-ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
gi 740854059 566 IEQRGVYAQLHKMQFGQ 582
Cdd:COG1132 562 LARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-579 |
5.91e-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: 5.91e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 12 TFRRLWPTIAPFKSGLI-VAGIALILNaasdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVS 85
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLqVLLASLLIN------LLALATPLFtqvviDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 86 SYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSW 165
Cdd:COG2274 217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSP 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 166 QLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMV 245
Cdd:COG2274 296 PLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 246 SASSISDPIIQLIASLALAFVLYAASFpSVMEN-LTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFTILD 323
Cdd:COG2274 376 RLSNLLSTLSGLLQQLATVALLWLGAY-LVIDGqLTLGQL-IAFNILSGrFLAPVAQLIGLLQRFQDAKIALERLDDILD 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 324 SEQEKDEGKRVIERAT--GDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQIL 401
Cdd:COG2274 454 LPPEREEGRSKLSLPRlkGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 402 MDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLL 481
Cdd:COG2274 534 IDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDA-TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNL 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGT 561
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGT 692
|
570
....*....|....*...
gi 740854059 562 HNELIEQRGVYAQLHKMQ 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 |
1.61e-147 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 424.34 E-value: 1.61e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLH 576
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-580 |
7.87e-140 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 417.56 E-value: 7.87e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 14 RRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVS 93
Cdd:TIGR02204 7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIV 173
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 174 LAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:TIGR02204 167 AVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 254 IIQLIASLALAFVLYAASFPSVMENLTAGTIT-VVFSSMIALMrPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDE-- 330
Cdd:TIGR02204 247 IVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGqFVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKApa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 331 -GKRVIERATGDLEFRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR 408
Cdd:TIGR02204 326 hPKTLPVPLRGEIEFEQVNFAYPARpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 409 EYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQR 488
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|..
gi 740854059 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 |
1.97e-131 |
|
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: 396.88 E-value: 1.97e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 6 DLSTWQTFRRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDrsVLLWMPlvvIGLMIVRGLTSYVS 85
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAA--ALLVVP---VGLLLAYGLLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 86 SYCISW---VSGKVVM-TMRR---RLFGHMMGMPVSF-FDKQSTGtlLSRityDSEQvASSSSGALI---------TVVr 148
Cdd:COG5265 92 VLFGELrdaLFARVTQrAVRRlalEVFRHLHALSLRFhLERQTGG--LSR---DIER-GTKGIEFLLrfllfnilpTLL- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 149 EGASIIGlfIMMFYYSWQLSLILIV-LAPIVSVAIRVVSKRFRsISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:COG5265 165 EIALVAG--ILLVKYDWWFALITLVtVVLYIAFTVVVTEWRTK-FRREMNEADSEANTRAVDSLLNYETVKYFGNEAREA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 228 KRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:COG5265 242 RRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYRE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 308 FQRGMAACQTLFTILDSEQE-KD-EGKRVIERATGDLEFRNVTFTY-PGReaPALRNINLNIPAGKTVALVGRSGSGKST 384
Cdd:COG5265 322 IRQALADMERMFDLLDQPPEvADaPDAPPLVVGGGEVRFENVSFGYdPER--PILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 385 IASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFIN 464
Cdd:COG5265 400 LARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDA-SEEEVEAAARAAQIHDFIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 465 KMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ 544
Cdd:COG5265 479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVD 558
|
570 580 590
....*....|....*....|....*....|....*
gi 740854059 545 ADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQ 579
Cdd:COG5265 559 ADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-570 |
1.43e-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: 390.66 E-value: 1.43e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 14 RRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGF-GKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWV 92
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILI 172
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 173 VLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISD 252
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 253 PIIQLIASLALAFVLYAASFpsvmeNLTAGTITVvFSSMIALM------RPLKSLtnvNAQF---QRGMAACQTLFTILD 323
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGF-----RLLGGSLTL-FAALFVLLlapeffLPLRDL---GSFYharANGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 324 S-EQEKDEGKRVIERATG-DLEFRNVTFTYPGREaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQIL 401
Cdd:COG4988 317 ApEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 402 MDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLL 481
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPD-ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGT 561
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
gi 740854059 562 HNELIEQRG 570
Cdd:COG4988 555 HEELLAKNG 563
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
343-579 |
2.91e-123 |
|
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: 362.63 E-value: 2.91e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03249 2 EFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQ 579
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
95-577 |
1.85e-118 |
|
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: 362.55 E-value: 1.85e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 95 KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQ-------VASSSSGALITvvregasIIGLFIMMFYYSWQL 167
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDAldnlylrVLLPLLVALLV-------ILAAVAFLAFFSPAL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 168 SLILIVLAPIVSVAIRVVSKRF-RSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVS 246
Cdd:COG4987 158 ALVLALGLLLAGLLLPLLAARLgRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 247 ASSISDPIIQLIASLALAFVLYAASfpsvmENLTAGTITVVFSSMIALMrPLKS---LTNVNAQFQ---RGMAACQTLFT 320
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAA-----PLVAAGALSGPLLALLVLA-ALALfeaLAPLPAAAQhlgRVRAAARRLNE 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 321 ILDSE-QEKDEGKRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQ 399
Cdd:COG4987 312 LLDAPpAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 400 ILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGV 479
Cdd:COG4987 392 ITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDA-TDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVER 559
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
490
....*....|....*...
gi 740854059 560 GTHNELIEQRGVYAQLHK 577
Cdd:COG4987 551 GTHEELLAQNGRYRQLYQ 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
72-575 |
5.36e-115 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 357.88 E-value: 5.36e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 72 IGLMIVRGLTSYVSSY----CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVV 147
Cdd:TIGR00958 204 IFFMCLLSIASSVSAGlrggSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 148 REGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:TIGR00958 284 RNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 228 KRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQ 307
Cdd:TIGR00958 364 SRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 308 FQRGMAACQTLFTILDSE-QEKDEGKRVIERATGDLEFRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTI 385
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKpNIPLTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTV 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 386 ASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDlYSREQIEKAAQMAYAMDFINK 465
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIME 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAalDELQKNRTSLVIAHRLSTIEQA 545
Cdd:TIGR00958 603 FPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERA 680
|
490 500 510
....*....|....*....|....*....|
gi 740854059 546 DEIIVVEDGVIVERGTHNELIEQRGVYAQL 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 |
5.65e-115 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 341.52 E-value: 5.65e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY-PGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVA 420
Cdd:cd03253 1 IEFENVTFAYdPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDA-TDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQ 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 |
2.52e-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: 323.99 E-value: 2.52e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 740854059 267 LYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 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 |
5.42e-106 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 318.02 E-value: 5.42e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYpGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQV 419
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNA-TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRG 570
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-580 |
6.19e-99 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 312.28 E-value: 6.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 101 RRRL------FGHMMGMPVSFFDKQSTGTLLSRITydseQVASSSSGALITVVREG-ASIIGLFIMM---FYYSWQLSLI 170
Cdd:PRK13657 86 RRRLavlteyFERIIQLPLAWHSQRGSGRALHTLL----RGTDALFGLWLEFMREHlATLVALVVLLplaLFMNWRLSLV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 171 LIVLAPIVSVAIRVVSKRfrsiSKNMQNTM-GQVTTSAEQMLKGHKEVLI---FGGQEVETKRFDKVSNKMR------LQ 240
Cdd:PRK13657 162 LVVLGIVYTLITTLVMRK----TKDGQAAVeEHYHDLFAHVSDAIGNVSVvqsYNRIEAETQALRDIADNLLaaqmpvLS 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTagtiTVVFSSMiaLMRPLKSLTN-VNAQFQRGmAACQTLF 319
Cdd:PRK13657 238 WWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVA----FVGFATL--LIGRLDQVVAfINQVFMAA-PKLEEFF 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 320 TILDSEQEKDE--GKRVIERATGDLEFRNVTFTYPGReAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDE 397
Cdd:PRK13657 311 EVEDAVPDVRDppGAIDLGRVKGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 398 GQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGEN 477
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDA-TDEEMRAAAERAQAHDFIERKPDGYDTVVGER 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 GVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIV 557
Cdd:PRK13657 469 GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVV 548
|
490 500
....*....|....*....|...
gi 740854059 558 ERGTHNELIEQRGVYAQLHKMQF 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 ... |
69-581 |
1.21e-98 |
|
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: 314.76 E-value: 1.21e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 69 LVVIGL-MIVRGLT----SYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGAL 143
Cdd:TIGR01846 178 LSVLALaMLAVAIFepalGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 144 ITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQ 223
Cdd:TIGR01846 257 LTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 224 EVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTItVVFSsMIA--LMRPLKSL 301
Cdd:TIGR01846 337 PQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQL-VAFN-MLAgrVTQPVLRL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 302 TNVNAQFQRGMAACQTLFTILDSEQE-KDEGKRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGS 380
Cdd:TIGR01846 415 AQLWQDFQQTGIALERLGDILNSPTEpRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 381 GKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAM 460
Cdd:TIGR01846 495 GKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGA-PFEHVIHAAKLAGAH 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
Cdd:TIGR01846 574 DFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLS 653
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 740854059 541 TIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQFG 581
Cdd:TIGR01846 654 TVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
27-575 |
1.05e-95 |
|
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: 307.64 E-value: 1.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILN-----AASDTFM--------LSLLKPLLddgfgktdrsvllwmpLVVIGLMIVRGLTSYVSSYCISWVS 93
Cdd:TIGR03796 159 LLLAGLLLVLPglvipAFSQIFVdeilvqgrQDWLRPLL----------------LGMGLTALLQGVLTWLQLYYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDsEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIV 173
Cdd:TIGR03796 223 IKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 174 LAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAeqmlkghkevlIFGGQEVETKR--------FDKVSN---KMRLQGM 242
Cdd:TIGR03796 302 FAAINVLALQLVSRRRVDANRRLQQDAGKLTGVA-----------ISGLQSIETLKasglesdfFSRWAGyqaKLLNAQQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 243 KMVSASSISDPIIQLIASLALAFVLYAASFpSVME-NLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTI 321
Cdd:TIGR03796 371 ELGVLTQILGVLPTLLTSLNSALILVVGGL-RVMEgQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDV 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 322 LDSEQEKDEGKRVI--------ERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFY 393
Cdd:TIGR03796 450 LRNPVDPLLEEPEGsaatseppRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 394 DIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTV 473
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTI-PDADLVRACKDAAIHDVITSRPGGYDAE 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIEQADEIIVVED 553
Cdd:TIGR03796 609 LAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLER 686
|
570 580
....*....|....*....|..
gi 740854059 554 GVIVERGTHNELIEQRGVYAQL 575
Cdd:TIGR03796 687 GKVVQRGTHEELWAVGGAYARL 708
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
342-579 |
3.94e-92 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 282.84 E-value: 3.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGM-SMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQ 579
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-554 |
4.30e-92 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 280.04 E-value: 4.30e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDG 554
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
56-551 |
1.55e-88 |
|
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: 283.41 E-value: 1.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 56 FGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV 135
Cdd:TIGR02857 35 SAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 136 ASSSSGALITVVRegASIIGLFIM--MFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKG 213
Cdd:TIGR02857 115 DGYFARYLPQLVL--AVIVPLAILaaVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 214 HKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpsvmeNLTAGTITVVFSSMIA 293
Cdd:TIGR02857 193 LPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGF-----RLLAGDLDLATGLFVL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 294 LMRP--LKSLTNVNAQF---QRGMAACQTLFTILDS-EQEKDEGKRVIERATGDLEFRNVTFTYPGREaPALRNINLNIP 367
Cdd:TIGR02857 268 LLAPefYLPLRQLGAQYharADGVAAAEALFAVLDAaPRPLAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 368 AGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySR 447
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA-SD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 448 EQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ 527
Cdd:TIGR02857 426 AEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
490 500
....*....|....*....|....
gi 740854059 528 KNRTSLVIAHRLSTIEQADEIIVV 551
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-579 |
4.95e-87 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 281.61 E-value: 4.95e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 13 FRRLWPTI-------APFKSGLIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVV--IGLMIVRGLTSY 83
Cdd:PRK10790 4 FSQLWPTLkrllaygSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayVGLQLLAAGLHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 84 VSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
Cdd:PRK10790 84 AQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 164 SWQLSLILIVLAPIVSVaIRVVSKRFRS-ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN---KMRL 239
Cdd:PRK10790 164 DWRMALVAIMIFPAVLV-VMVIYQRYSTpIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRshyMARM 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 240 QGMKMvsASSISDPIIQLIASLALAFVLYAASFPSVmenltaGTITV-VFSSMIA----LMRPLKSLTNVNAQFQRGMAA 314
Cdd:PRK10790 243 QTLRL--DGFLLRPLLSLFSALILCGLLMLFGFSAS------GTIEVgVLYAFISylgrLNEPLIELTTQQSMLQQAVVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 315 CQTLFTILDSEQEkDEGKRVIERATGDLEFRNVTFTYpGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYD 394
Cdd:PRK10790 315 GERVFELMDGPRQ-QYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 395 IDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTdlYSREQIEKAAQMAYAMDFINKMDNGLDTVI 474
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD--ISEEQVWQALETVQLAELARSLPDGLYTPL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 475 GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDG 554
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRG 550
|
570 580
....*....|....*....|....*
gi 740854059 555 VIVERGTHNELIEQRGVYAQLHKMQ 579
Cdd:PRK10790 551 QAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-576 |
8.38e-85 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 275.17 E-value: 8.38e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 151 ASIIGLFIMMFYYSW---QLSLILIVLAPIVSVAIRVVSKRF-RSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVE 226
Cdd:PRK11160 143 AALVVILVLTIGLSFfdlTLALTLGGILLLLLLLLPLLFYRLgKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRY 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 227 TKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMENLTAGTIT--VVFSSMIALmrplKSLTNV 304
Cdd:PRK11160 223 RQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAG-GVGGNAQPGALIalFVFAALAAF----EALMPV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 305 NAQFQ---RGMAACQTLFTILdsEQEKD---EGKRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRS 378
Cdd:PRK11160 298 AGAFQhlgQVIASARRINEIT--EQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 379 GSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQ--- 455
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA-SDEALIEVLQqvg 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 456 MAYAMDfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI 535
Cdd:PRK11160 455 LEKLLE----DDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI 530
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 740854059 536 AHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLH 576
Cdd:PRK11160 531 THRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-579 |
4.44e-83 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 270.43 E-value: 4.44e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 44 MLSLLKPLLD----DGF---GKTDRSVLLWmplvvIGLMIVRGLTSYVSSYCisW------VSGKVVMTMRRRLFGHMMG 110
Cdd:PRK10789 9 MLQLIPPKVVgiivDGVteqHMTTGQILMW-----IGTMVLIAVVVYLLRYV--WrvllfgASYQLAVELREDFYRQLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 111 MPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRE---GASIigLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:PRK10789 82 QHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmGCAV--LIVMSTQISWQLTLLALLPMPVMAIMIKRYGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 188 RFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 268 YAASFPSVMENLTAGTIT---VVFSSMIALMRPLKSLTNVnaqFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDLEF 344
Cdd:PRK10789 240 GGGSWMVVNGSLTLGQLTsfvMYLGLMIWPMLALAWMFNI---VERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQ 424
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDA-TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLHKMQ 579
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
32-579 |
2.08e-81 |
|
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: 269.13 E-value: 2.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 32 IALILNAASDTFMLSLLKP-----LLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:TIGR03797 138 LLAILAMGLLGTLLGMLVPiatgiLIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWD 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSR---ITYDSEQVASSSSGALITvvregaSIIGLF--IMMFYYSWQLSLILIVLAPIVSVA 181
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASRamgISQIRRILSGSTLTTLLS------GIFALLnlGLMFYYSWKLALVAVALALVAIAV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 182 IRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQE----VETKRFDKvSNKMRLQGMKMVSASSISDPIIQL 257
Cdd:TIGR03797 292 TLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENrafaRWAKLFSR-QRKLELSAQRIENLLTVFNAVLPV 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 258 IASLALafvLYAASFPSVMENLTAGTI---TVVFSSMIALMRPL-KSLTNVNA---QFQRgmaaCQTlftILDSEQEKDE 330
Cdd:TIGR03797 371 LTSAAL---FAAAISLLGGAGLSLGSFlafNTAFGSFSGAVTQLsNTLISILAvipLWER----AKP---ILEALPEVDE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 331 GKRVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREY 410
Cdd:TIGR03797 441 AKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 411 TLASLRDQVALVSQNVHLFNDTVANNIAyaRTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA 490
Cdd:TIGR03797 521 DVQAVRRQLGVVLQNGRLMSGSIFENIA--GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRtsLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRG 570
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676
|
....*....
gi 740854059 571 VYAQLHKMQ 579
Cdd:TIGR03797 677 LFAQLARRQ 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
340-556 |
1.50e-78 |
|
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: 247.38 E-value: 1.50e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQ 418
Cdd:cd03248 10 GIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNIAYGLQSC-SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVI 556
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
98-577 |
5.05e-76 |
|
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: 252.50 E-value: 5.05e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 98 MTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEqvasSSSGALITVVREG-ASIIGLFIMM---FYYSWQLSLILIV 173
Cdd:TIGR01192 89 ATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATE----TLFGLWLEFMRQHlATFVALFLLIptaFAMDWRLSIVLMV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 174 LAPIVSVAIRVVSKRFR----SISKNMQNTMGQVTTSAEQMLKGHKEVLIfggqEVETKRFDKVSNKMRLQGMKMVSASS 249
Cdd:TIGR01192 165 LGILYILIAKLVMQRTKngqaAVEHHYHNVFKHVSDSISNVSVVHSYNRI----EAETSALKQFTNNLLSAQYPVLDWWA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 250 ISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKD 329
Cdd:TIGR01192 241 LASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQRE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 330 E--GKRVIERATGDLEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL 407
Cdd:TIGR01192 321 EpaDAPELPNVKGAVEFRHITFEFAN-SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDI 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 408 REYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQ 487
Cdd:TIGR01192 400 NTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGA-TDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQ 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIE 567
Cdd:TIGR01192 479 RLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQ 558
|
490
....*....|
gi 740854059 568 QRGVYAQLHK 577
Cdd:TIGR01192 559 KDGRFYKLLR 568
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-560 |
1.99e-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: 239.03 E-value: 1.99e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQV 419
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERG 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 |
8.10e-72 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 229.69 E-value: 8.10e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQV 419
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNIAyaRTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGT 561
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
27-314 |
6.00e-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: 222.04 E-value: 6.00e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 740854059 267 LYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-575 |
1.04e-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: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 28 IVAGIALILNAASDTFmlslLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGH 107
Cdd:TIGR01193 163 IAAIIVTLISIAGSYY----LQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKH 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 108 MMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:TIGR01193 239 LFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFKR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 188 RFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:TIGR01193 318 TFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVIL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 268 YAASFPSVMENLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFTIL--DSEQEKDEGKRVIERATGDLEF 344
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQL-ITFNALLSyFLTPLENIINLQPKLQAARVANNRLNEVYlvDSEFINKKKRTELNNLNGDIVI 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYpGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQ 424
Cdd:TIGR01193 477 NDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFNDTVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 505 DEATSALDTESERAIQAALDELQkNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
279-568 |
2.27e-64 |
|
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: 220.78 E-value: 2.27e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 279 LTAGTItvvFSSMIALMR---PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRvIERATGDLEFRNVTFTYPGRE 355
Cdd:COG4618 269 ITPGAM---IAASILMGRalaPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMP-LPRPKGRLSVENLTVVPPGSK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 356 APALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVAN 435
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 436 NIAyaRTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:COG4618 425 NIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 516 ERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG4618 503 EAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
77-539 |
7.47e-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: 218.38 E-value: 7.47e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 77 VR--GLTSYVSSYCISWVSGKVVMT----MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREG 150
Cdd:TIGR02868 59 VRafGIGRAVFRYLERLVGHDAALRslgaLRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVAL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 151 ASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF-RSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKR 229
Cdd:TIGR02868 139 VVGAAAVAAIAVLSVPAALILAAGLLLAGFVAPLVSLRAaRAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQ 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 230 FDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASfPSVMENLTAGTITVVFSSM-IALMRPLKSLTNVNAQF 308
Cdd:TIGR02868 219 VEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGG-PAVADGRLAPVTLAVLVLLpLAAFEAFAALPAAAQQL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 309 QRGMAACQTLFTILDSEQEKDEGkrVIERATG------DLEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGK 382
Cdd:TIGR02868 298 TRVRAAAERIVEVLDAAGPVAEG--SAPAAGAvglgkpTLELRDLSAGYPG-APPVLDGVSLDLPPGERVAILGPSGSGK 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 383 STIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQMAYAMDF 462
Cdd:TIGR02868 375 STLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDA-TDEELWAALERVGLADW 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 463 INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:TIGR02868 454 LRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-575 |
7.08e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 217.02 E-value: 7.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 151 ASIIGLFIMM--FYYSWQLSLILIVLAPIVSVAIRVV------SKRfrsisKNMQnTMGQVttSAEQM--LKGHKEVLIF 220
Cdd:PRK11174 147 AVLVPLLILIavFPINWAAGLILLGTAPLIPLFMALVgmgaadANR-----RNFL-ALARL--SGHFLdrLRGLETLRLF 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 221 GGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASL--ALAFVLYAASFPSVMENLTAGTITVVFSSMIALM--- 295
Cdd:PRK11174 219 NRGEAETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASIsiALVAVYFGFSYLGELNFGHYGTGVTLFAGFFVLIlap 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 296 ---RPLKSL-TNVNAQFQrGMAACQTLFTILDSEQE--KDEGKRVIERATGDLEFRN-VTFTYPGreAPALRNINLNIPA 368
Cdd:PRK11174 299 efyQPLRDLgTFYHAKAQ-AVGAAESLVTFLETPLAhpQQGEKELASNDPVTIEAEDlEILSPDG--KTLAGPLNFTLPA 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 369 GKTVALVGRSGSGKSTIASLITRF--YdidEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLyS 446
Cdd:PRK11174 376 GQRIALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDA-S 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 447 REQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
Cdd:PRK11174 452 DEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA 531
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 740854059 527 QKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:PRK11174 532 SRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
27-298 |
2.62e-59 |
|
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: 198.64 E-value: 2.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRL 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 105 FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 185 VSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 740854059 265 FVLYAASFPSVMENLTAGTITVVFSSMIALMRPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-553 |
3.13e-59 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 214.12 E-value: 3.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 8 STWQTFRRL----WPTIAPFK-------SGLIVAGIALILNAASDTFMLSLLKPLLDD-GFGKTDRSVLLwmPLVVIGlm 75
Cdd:PTZ00265 32 GTFELYKKIktqkIPFFLPFKclpashrKLLGVSFVCATISGGTLPFFVSVFGVIMKNmNLGENVNDIIF--SLVLIG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 76 IVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIG 155
Cdd:PTZ00265 108 IFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 156 LFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNM----QNTMGQVttsaEQMLKGHKEVLIFGGQEVETKRFD 231
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSllynNNTMSII----EEALVGIRTVVSYCGEKTILKKFN 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 232 kVSNKmrLQGMKMVSASSISDPIIQLIASLALAFvlYAASF----PSVMENLT----------AGTITVVFSSMIALMRP 297
Cdd:PTZ00265 264 -LSEK--LYSKYILKANFMESLHIGMINGFILAS--YAFGFwygtRIIISDLSnqqpnndfhgGSVISILLGVLISMFML 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 298 LKSLTNVNaQFQRGMAACQTLFTILDSE---QEKDEGKRVieRATGDLEFRNVTFTYPGR-EAPALRNINLNIPAGKTVA 373
Cdd:PTZ00265 339 TIILPNIT-EYMKSLEATNSLYEIINRKplvENNDDGKKL--KDIKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 374 LVGRSGSGKSTIASLITRFYDIDEGQILM-DGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYArtdLYSREQIEK 452
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYS---LYSLKDLEA 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 453 AAQ-----------------------------MAYAM------------------------------DFINKMDNGLDTV 473
Cdd:PTZ00265 493 LSNyynedgndsqenknkrnscrakcagdlndMSNTTdsneliemrknyqtikdsevvdvskkvlihDFVSALPDKYETL 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIIVV 551
Cdd:PTZ00265 573 VGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
|
..
gi 740854059 552 ED 553
Cdd:PTZ00265 653 SN 654
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-568 |
1.93e-57 |
|
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: 201.42 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 20 IAPFKSGLIVAGIAL----ILNAASDTFMLSLLKPLLDDGFGKTdrsvLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGK 95
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSfvinILMLAPPLYMLQVYDRVLTSGSVPT----LLMLTVLALGLYLFLGLLDALRSFVLVRIGEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 96 VVMTMRRRLFGHMMGMPVSFFDKQSTGTLlsritYDSEQVAS-SSSGALITVVREGASIIGLFIMMFYYSWqlSLILIVL 174
Cdd:TIGR01842 77 LDGALNQPIFAASFSATLRRGSGDGLQAL-----RDLDQLRQfLTGPGLFAFFDAPWMPIYLLVCFLLHPW--IGILALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 175 APIVSVAIRVVSKRF--RSISKNMQNTMgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMK------MVS 246
Cdd:TIGR01842 150 GAVVLVGLALLNNRAtkKPLKEATEASI-RANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAasdragMLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 247 ASSISDPIIQLIASLALAFVLyaasfpSVMENLTAGTItvVFSSMIA--LMRPLKSLTNVNAQFQRGMAACQTLFTILDS 324
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLGAYL------AIDGEITPGMM--IAGSILVgrALAPIDGAIGGWKQFSGARQAYKRLNELLAN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 325 EQEKDEGKRvIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDG 404
Cdd:TIGR01842 301 YPSRDPAMP-LPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 405 HDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLYSREQIEkAAQMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPEKIIE-AAKLAGVHELILRLPDGYDTVIGPGGATLSGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQADEIIVVEDGVIVERGTHN 563
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERD 538
|
....*
gi 740854059 564 ELIEQ 568
Cdd:TIGR01842 539 EVLAK 543
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-560 |
1.19e-55 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 185.59 E-value: 1.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTlASLRDQVAL 421
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIayartdlysreqiekaaqmayamdfinkmdngldtvigenGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERG 560
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-578 |
1.83e-55 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 202.95 E-value: 1.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 65 LWMPLVVIGLMIVRGLTSYVSSYciswVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDseqVASSSSGA 142
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNV----IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRD---VHLLKTGL 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 143 LITVVregasIIGLFIMMFYYSWQLS-----LILIVLAPIVSVAIRVVSKRFR-----SISKNMQNTMGQV--TTSAEQM 210
Cdd:PTZ00265 943 VNNIV-----IFTHFIVLFLVSMVMSfyfcpIVAAVLTGTYFIFMRVFAIRARltankDVEKKEINQPGTVfaYNSDDEI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 211 LK-----------GHKEVLIFGGQEVETKRFDK-VSNKMRLQGMKMVSASSI---SDPIIQLIASLALAFVLYAASFPSV 275
Cdd:PTZ00265 1018 FKdpsfliqeafyNMNTVIIYGLEDYFCNLIEKaIDYSNKGQKRKTLVNSMLwgfSQSAQLFINSFAYWFGSFLIRRGTI 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 276 -MENLTAGTITVVFSSMIA--LMRPLKSLTNVNAQFQR--GMAACQTLFTILDSEQEKDEGKRVIEratGDLEFRNVTFT 350
Cdd:PTZ00265 1098 lVDDFMKSLFTFLFTGSYAgkLMSLKGDSENAKLSFEKyyPLIIRKSNIDVRDNGGIRIKNKNDIK---GKIEIMDVNFR 1174
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 351 YPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDI---------------------------------- 395
Cdd:PTZ00265 1175 YISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 396 --------------------DEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTDLySREQIEKAAQ 455
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA-TREDVKRACK 1333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 456 MAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSL 533
Cdd:PTZ00265 1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTII 1413
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 740854059 534 VIAHRLSTIEQADEIIVVED----GVIVE-RGTHNELIE-QRGVYAQLHKM 578
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-315 |
4.46e-53 |
|
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: 182.97 E-value: 4.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRL 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 105 FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 185 VSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 740854059 265 FVLYAASFPSVMENLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVL-YAFIQYIQrFFRPIRDLAEKFNILQSAMASA 291
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-569 |
4.56e-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: 180.61 E-value: 4.56e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVH--LFNDTVANNIAYARTDL-YSREQIEKAAQmaYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGPENLgLPREEIRERVE--EALELV-----GLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-554 |
6.52e-53 |
|
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: 179.59 E-value: 6.52e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALV 422
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQN--VHLFNDTVANNIAYA-RTDLYSREQIEKAAqmAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:cd03225 81 FQNpdDQFFGPTVEEEVAFGlENLGLPEEEIEERV--EEALELVG-LEGLRDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI-EQADEIIVVEDG 554
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDG 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-556 |
9.93e-53 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 177.79 E-value: 9.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 502 LILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQADEIIVVEDGVI 556
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
1.69e-51 |
|
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: 184.72 E-value: 1.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREA---PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD- 417
Cdd:COG1123 261 LEVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 --QVALVSQN-VHLFN--DTVANNIAYA--RTDLYSREQIEKAAqmAYAMDFInkmdnGLDT-VIGENGVLLSGGQRQRI 489
Cdd:COG1123 341 rrRVQMVFQDpYSSLNprMTVGDIIAEPlrLHGLLSRAERRERV--AELLERV-----GLPPdLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELI 566
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
..
gi 740854059 567 EQ 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 |
2.87e-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: 177.98 E-value: 2.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDD------GFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTM 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 101 RRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSV 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 181 AIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 261 LALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAG 294
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-316 |
1.31e-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: 173.39 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 740854059 267 LYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAE 290
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
342-556 |
6.89e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 168.84 E-value: 6.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYA---RTDLYSREQIEKA-AQMAYAMDFinkmdngLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKFDRERALELlERLGLPPDI-------LDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
112-577 |
1.74e-48 |
|
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: 182.07 E-value: 1.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS----- 186
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVassrq 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 -KRFRSISKNmqntmgQVTTSAEQMLKGHKEVLIFGGQEvetkRFDKVSNKMRLQGMKMVSASSISDPIIQL-IASLALA 264
Cdd:TIGR00957 1132 lKRLESVSRS------PVYSHFNETLLGVSVIRAFEEQE----RFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNC 1201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 265 FVLYAASFPSV-MENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTIldSEQEKDEGKRVIERA----- 338
Cdd:TIGR00957 1202 IVLFAALFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY--SETEKEAPWQIQETAppsgw 1279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 339 --TGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLR 416
Cdd:TIGR00957 1280 ppRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR 1359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQNVHLFNDTVANNIAYARTdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:TIGR00957 1360 FKITIIPQDPVLFSGSLRMNLDPFSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALL 1437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQLH 576
Cdd:TIGR00957 1438 RKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMA 1517
|
.
gi 740854059 577 K 577
Cdd:TIGR00957 1518 K 1518
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
2.16e-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: 165.38 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAAsdtfmLSLLKP--------------------LLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSS 86
Cdd:cd18564 1 LALALLALLLETA-----LRLLEPwplkvviddvlgdkplpgllGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 87 YCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQ 166
Cdd:cd18564 76 YLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 167 LSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVS 246
Cdd:cd18564 156 LALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAAR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 247 ASSISDPIIQLIASLALAFVLYAASFpSVMEN-LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18564 236 LQALLSPVVDVLVAVGTALVLWFGAW-LVLAGrLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAE 305
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
2.28e-46 |
|
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: 170.47 E-value: 2.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID---EGQILMDGHDLREYTLASLRDQ 418
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQN--VHLFNDTVANNIAYA-RTDLYSREQIEKAAQMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlENLGLSRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-554 |
1.61e-45 |
|
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: 159.56 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGRE---APALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHdlreytlaslrdq 418
Cdd:cd03250 1 ISVEDASFTWDSGEqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFNDTVANNIAYART---DLYsrEQIEKAAQMAYamDfINKMDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdeERY--EKVIKACALEP--D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 496 LRDSPILILDEATSALDTESERAI--QAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDG 554
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
359-509 |
2.52e-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: 157.04 E-value: 2.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFND-TVANNI 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 438 AYARtDLYSREQIEKAAQMAYAMDFINkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:pfam00005 81 RLGL-LLKGLSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
338-561 |
4.13e-45 |
|
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: 158.73 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 338 ATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD 417
Cdd:cd03369 3 EHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFNDTVANNIAyaRTDLYSREQIEKAAQmayamdfinkmdngldtvIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGT 561
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-568 |
5.63e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.07 E-value: 5.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAsLRDQVAL 421
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAYARtDLYSREQIEKAAQMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFFA-RLYGLPRKEARERIDELLELFG-LTDAADRKVGT----LSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
2.59e-44 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 159.19 E-value: 2.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 30 AGIALILNAAsdTFMLS--LLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGH 107
Cdd:cd18576 1 GLILLLLSSA--IGLVFplLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 108 MMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSK 187
Cdd:cd18576 79 LQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 188 RFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVL 267
Cdd:cd18576 159 RIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVL 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 740854059 268 YAASFPSVMENLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18576 239 WYGGRLVLAGELTAGDLVafLLYTLFIA--GSIGSLADLYGQLQKALGA 285
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-565 |
2.72e-44 |
|
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: 156.96 E-value: 2.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGQILMDGHDLRE--YTLAS 414
Cdd:cd03260 1 IELRDLNVYYGDKHA--LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTDLYSREQIEKAAQMAYAMDFINKMDNGLDtvigengvlLSGGQRQR 488
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQA----DEIIVVEDGVIVERGTHNE 564
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH---NMQQAarvaDRTAFLLNGRLVEFGPTEQ 226
|
.
gi 740854059 565 L 565
Cdd:cd03260 227 I 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
342-560 |
9.12e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 155.74 E-value: 9.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLR 416
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQNVHL-FND--TVANNIA---YARTDLYSREQIEKAAQMAyamdfinkmdngLDTVIGENGVL------LSGG 484
Cdd:cd03257 82 KEIQMVFQDPMSsLNPrmTIGEQIAeplRIHGKLSKKEARKEAVLLL------------LVGVGLPEEVLnrypheLSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-558 |
2.15e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 154.43 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP--GREAPALRNINLNIPAGKTVALVGRSGSGKST---IASLITRFydiDEGQILMDGHD---LREYTLA 413
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDRP---TSGEVLIDGQDissLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLR-DQVALVSQNVHLFND-TVANNIAYARtdLYSREQIEKAAQMAYAM-------DFINKMdngldtvIGEngvlLSGG 484
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPElTALENVALPL--LLAGVSRKERRERARELlervglgDRLDHR-------PSQ----LSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIIVVEDGVIVE 558
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-554 |
2.34e-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: 152.01 E-value: 2.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALV 422
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQnvhlfndtvanniayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 503 ILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQA-DEIIVVEDG 554
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-560 |
8.13e-43 |
|
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: 152.67 E-value: 8.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLreYTLASLRDQVAL 421
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYA-RTDLYSREQIEKAAQMAYAMdfiNKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGlKLRGVPKAEIRARVRELLEL---VGLEGLLNRYPHE----LSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIIVVEDGVIVERG 560
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-566 |
1.27e-42 |
|
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: 152.74 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPG--REAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLR 416
Cdd:cd03258 2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQNVHLFND-TVANNIAY----ARTDlySREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAI 491
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALpleiAGVP--KAEIEERVLELLELVGLEDKADAYPAQ--------LSGGQKQRVGI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELI 566
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
4.17e-42 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 153.43 E-value: 4.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDD----GFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRR 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 183 RVVSKR--------FRSISKnMQNTMGQVttsaeqmLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPI 254
Cdd:cd18563 161 YFFWKKirrlfhrqWRRWSR-LNSVLNDT-------LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 255 IQLIASLALAFVLYAASfPSVMEN-LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18563 233 LTFLTSLGTLIVWYFGG-RQVLSGtMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAE 294
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-565 |
1.16e-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: 151.04 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD-LREYTLASLRDQVA 420
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQN-----VhlfNDTVANNIAYARTDL-YSREQIEKAAQMAYAM----DFINKmdngldtvigeNGVLLSGGQRQRIA 490
Cdd:TIGR04520 81 MVFQNpdnqfV---GATVEDDVAFGLENLgVPREEMRKRVDEALKLvgmeDFRDR-----------EPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREI 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-570 |
1.54e-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: 150.01 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAsLRDQVAL 421
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYART--DLYSREQIEKAAQMAYAMDfinkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYFAElyGLFDEELKKRIEELIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQRG 570
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-566 |
1.87e-41 |
|
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: 149.76 E-value: 1.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYARTDL-YSREQIEKAAQMAYAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALVPKLLkWPKEKIRERADELLAL-----VGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEQADEIIVVEDGVIVERGTHNELI 566
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-567 |
3.00e-41 |
|
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: 149.36 E-value: 3.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIAYA---RTDLySREQIEKAAQMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRIA 490
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPlreHTDL-SEAEIRELVLEKLELvglpGAADKM-------PSE----LSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIE 567
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-556 |
4.14e-41 |
|
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: 148.02 E-value: 4.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP--GREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT---LASLR 416
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 -DQVALVSQNVHLFND-TVANNIAYArtDLYSReqIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELP--LLLAG--VPKKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIIVVEDGVI 556
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
27-314 |
1.30e-40 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 149.12 E-value: 1.30e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAAsdtfmLSLLKPLL-----DDGFGKtdrSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMR 101
Cdd:cd18551 1 LILALLLSLLGTA-----ASLAQPLLvknliDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 102 RRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVA 181
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 182 IRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 262 ALAFVL-YAASFpsvmenLTAGTITVvfSSMIA-------LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18551 233 ALLVVLgVGGAR------VASGALTV--GTLVAfllylfqLITPLSQLSSFFTQLQKALGA 285
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
32-314 |
7.00e-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: 146.94 E-value: 7.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 32 IALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRS 191
Cdd:cd18557 83 EIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 192 ISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAAS 271
Cdd:cd18557 163 LSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 740854059 272 FPSVMENLTAGTIT--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 |
1.17e-39 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 146.47 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLK--GHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALA 264
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 740854059 265 FVLYAASFPSVMENLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTL-VAFTALLGrLYGPLTQLLNIQVDLMTSLA 289
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-565 |
1.35e-39 |
|
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: 144.95 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP--GREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQV 419
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQN----VHLFNdTVANNIAYARTDLYSREQIEKAAQMAYAMdfinkmdnGLDTvigenGVL------LSGGQRQRI 489
Cdd:COG1124 82 QMVFQDpyasLHPRH-TVDRILAEPLRIHGLPDREERIAELLEQV--------GLPP-----SFLdryphqLSGGQRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-566 |
1.63e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 144.80 E-value: 1.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHL-FNDTVANNIAYART------------DlysREQIEKAAQMAYAMDFINKMdngLDTvigengvlLSGGQRQR 488
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRYphlglfgrpsaeD---REAVEEALERTGLEHLADRP---VDE--------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 740854059 566 I 566
Cdd:COG1120 226 L 226
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
27-314 |
1.72e-39 |
|
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: 146.07 E-value: 1.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 740854059 267 LYAASFPSVMENLTAGTItVVFSSMIALM-RPLKSLTNVNAQFQRGMAA 314
Cdd:cd18545 242 YWYGGKLVLGGAITVGVL-VAFIGYVGRFwQPIRNLSNFYNQLQSAMAS 289
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-554 |
2.21e-39 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 141.94 E-value: 2.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAS--LRDQV 419
Cdd:cd03229 1 LELKNVSKRYGQKTV--LNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLF-NDTVANNIAYArtdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRD 498
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
342-569 |
5.08e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApalrNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREyTLASLRdQVAL 421
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAER-PVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAYA-RTDL-YSREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRD 498
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPGLkLTAEQRAQVEQALERVGLAGLLDRLPGQ--------LSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-558 |
8.80e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.73 E-value: 8.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIAYArtdL----YSREQIEKAAQMAYAM----DFINKMdngldtvIGEngvlLSGGQRQRI 489
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALP---LrvtgKSRKEIRRRVREVLDLvglsDKAKAL-------PHE----LSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADE-IIVVEDGVIVE 558
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-556 |
1.57e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlasLRDQVAL 421
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND---TVANNIA---YARTDL---YSREQIEKAAQmayAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDVVLmgrYGRRGLfrrPSRADREAVDE---ALERVG-LEDLADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-561 |
4.76e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 143.29 E-value: 4.76e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLR 416
Cdd:COG1135 2 IELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQNVHLFND-TVANNIAYArtdL----YSREQIEKaaqmayamdfinKMDNGLDTVigenGvL----------L 481
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALP---LeiagVPKAEIRK------------RVAELLELV----G-LsdkadaypsqL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 740854059 557 VERGT 561
Cdd:COG1135 220 VEQGP 224
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
102-570 |
5.56e-38 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 150.51 E-value: 5.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 102 RRLFGHMMG----MPVSFFDKQSTGTLLSRITYDSEQVAssssgalitvvREGASIIGLFIMMFyysWQL--SLILIVLA 175
Cdd:PLN03232 983 KRLHDAMLNsilrAPMLFFHTNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---WQLlsTFALIGTV 1048
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 176 PIVSV-AIRVVSKRFRSISKNMQNT------MGQVTTSA-----EQMLKGHKEVLIFGGQEvetkRFDKVSNKMRLQGMK 243
Cdd:PLN03232 1049 STISLwAIMPLLILFYAAYLYYQSTsrevrrLDSVTRSPiyaqfGEALNGLSSIRAYKAYD----RMAKINGKSMDNNIR 1124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 244 MVSASSISDPIIQL-IASLALAFVLYAASFpSVMENLTAGTiTVVFSSMIALMRPLKS-----LTNVNAQFQRG---MAA 314
Cdd:PLN03232 1125 FTLANTSSNRWLTIrLETLGGVMIWLTATF-AVLRNGNAEN-QAGFASTMGLLLSYTLnittlLSGVLRQASKAensLNS 1202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 315 CQTLFTILDSEQEK---DEGKRVIER--ATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLI 389
Cdd:PLN03232 1203 VERVGNYIDLPSEAtaiIENNRPVSGwpSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNAL 1282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 390 TRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIayartDLYSREQ---IEKAAQMAYAMDFINKM 466
Cdd:PLN03232 1283 FRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPFSEHNdadLWEALERAHIKDVIDRN 1357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQAD 546
Cdd:PLN03232 1358 PFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCD 1437
|
490 500
....*....|....*....|....
gi 740854059 547 EIIVVEDGVIVERGTHNELIEQRG 570
Cdd:PLN03232 1438 KILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-575 |
6.96e-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: 140.43 E-value: 6.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQV 419
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNIAYARTdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK--CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQR-GVYAQL 575
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASL 252
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-550 |
9.67e-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: 138.76 E-value: 9.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlasLRDQV 419
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFN-DTVANNIAYArtdlYSREQIEKAAQMAYAMDFINKMdnGLDtvigenGVL------LSGGQRQRIAIA 492
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG----LELQGVPKAEARERAEELLELV--GLS------GFEnayphqLSGGMRQRVALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIIV 550
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVV 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
342-568 |
1.10e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 139.36 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL--REYTLASLRDQV 419
Cdd:COG1126 2 IEIENLHKSFGDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFND-TVANNIAYA--RTDLYSREQIEKAAqMAYamdfinkmdngLDTVigenGVL---------LSGGQRQ 487
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApiKVKKMSKAEAEERA-MEL-----------LERV----GLAdkadaypaqLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH-----RlstiEQADEIIVVEDGVIVERGT 561
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHemgfaR----EVADRVVFMDGGRIVEEGP 219
|
....*..
gi 740854059 562 HNELIEQ 568
Cdd:COG1126 220 PEEFFEN 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
27-314 |
1.14e-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: 141.01 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAAsdtfmLSLLKPLL-----DD-GFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTM 100
Cdd:cd18541 1 YLLGILFLILVDL-----LQLLIPRIigraiDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 101 RRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSV 180
Cdd:cd18541 76 RNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 181 AIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIAS 260
Cdd:cd18541 156 LVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 261 LALAFVLYAASFPSVMENLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAA 314
Cdd:cd18541 236 LSFLIVLWYGGRLVIRGTITLGDL-VAFNSYLGMLIwPMMALGWVINLIQRGAAS 289
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
1.47e-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: 141.34 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRN--VTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYD---IDEGQILMDGHDLREYTLASLR 416
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 D----QVALVSQN-------VHlfndTVANNIAYArtdLYSREQIEKAAQMAYAMDFINKMdnGLDtviGENGVL----- 480
Cdd:COG0444 82 KirgrEIQMIFQDpmtslnpVM----TVGDQIAEP---LRIHGGLSKAEARERAIELLERV--GLP---DPERRLdryph 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 -LSGGQRQRIAIARALLRDSPILILDEATSALD-TeseraIQAA----LDELQKNR-TSLV-IAHRLSTIEQ-ADEIIVV 551
Cdd:COG0444 150 eLSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELgLAILfITHDLGVVAEiADRVAVM 224
|
250
....*....|....*..
gi 740854059 552 EDGVIVERGTHNELIEQ 568
Cdd:COG0444 225 YAGRIVEEGPVEELFEN 241
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-565 |
2.75e-37 |
|
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: 138.02 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIA---YARTDLySREQIEKAAQMAYAM----DFINKMDngldtviGEngvlLSGGQRQRIA 490
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAfplREHTRL-SEEEIREIVLEKLEAvglrGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
338-570 |
3.28e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 148.35 E-value: 3.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 338 ATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD 417
Cdd:PLN03130 1234 SSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFNDTVANNI----AYARTDLYsrEQIEKAaqmaYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIAR 493
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdpfnEHNDADLW--ESLERA----HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRG 570
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
4.64e-37 |
|
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: 139.16 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 30 AGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 110 GMPVSFFDKQSTGTLLSRITYDSEQ----VASSSSGALitvvREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVV 185
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLiqtvVGSSLSIAL----RNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 186 SKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAF 265
Cdd:cd18575 157 GRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVF 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 740854059 266 VLYAASFpSVME-NLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18575 237 VLWLGAH-DVLAgRMSAGELSqfVFYAVLAA--GSVGALSEVWGDLQRAAGA 285
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-561 |
5.30e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 140.62 E-value: 5.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 338 ATGDLEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlreytLASL-- 415
Cdd:COG3842 2 AMPALELENVSKRYGDV--TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-----VTGLpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 -RDQVALVSQNVHLF-NDTVANNIAYA-RTDLYSREQIEKAAQMAYAM----DFINKMdngldtvIGEngvlLSGGQRQR 488
Cdd:COG3842 75 eKRNVGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRARVAELLELvgleGLADRY-------PHQ----LSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS---TIeqADEIIVVEDGVIVERGT 561
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-556 |
1.03e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 134.45 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTlASLRDQVAL 421
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIayartdlysreqiekaaqmayamdfinkmdngldtvigengvLLSGGQRQRIAIARALLRDSP 500
Cdd:cd03230 78 LPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
13-558 |
1.21e-36 |
|
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: 143.79 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 13 FRRLWptiAPFKSGLIVAGIALILNAASDTFMLSLLkpllDDGFGKTDrSVLLWMPLVVIGLMIVRGLTSYVSSYCISWV 92
Cdd:COG4615 4 LRLLL---RESRWLLLLALLLGLLSGLANAGLIALI----NQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVaSSSSGALITVVREGASIIGLFIMMFYYSWQLSLILI 172
Cdd:COG4615 76 GQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFLLTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 173 VLAPIVSVAIRVVSKRFR---SISKNMQNTMGQVTTSaeqMLKGHKEVLIFG--GQEVETKRFDKVSNKMRLQGMKMVSA 247
Cdd:COG4615 155 VLLGLGVAGYRLLVRRARrhlRRAREAEDRLFKHFRA---LLEGFKELKLNRrrRRAFFDEDLQPTAERYRDLRIRADTI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 248 SSISDPIIQLIASLALAFVLYAA-SFPSV-MENLTAGTITVVF--SSMIALMRPLKSLTNVNAQFQRgMAACQTLFTILD 323
Cdd:COG4615 232 FALANNWGNLLFFALIGLILFLLpALGWAdPAVLSGFVLVLLFlrGPLSQLVGALPTLSRANVALRK-IEELELALAAAE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 324 SEQEKDEGKRVIeRATGDLEFRNVTFTYPGREAP---ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI 400
Cdd:COG4615 311 PAAADAAAPPAP-ADFQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 401 LMDGHDLREYTLASLRDQVALVSQNVHLFNdtvanniayartDLYSREQIEKAAQmayAMDFINKMDngLDTVIG-ENGV 479
Cdd:COG4615 390 LLDGQPVTADNREAYRQLFSAVFSDFHLFD------------RLLGLDGEADPAR---ARELLERLE--LDHKVSvEDGR 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 L----LSGGQRQRIAIARALLRDSPILILDEatsaldteseraiQAA--------------LDEL-QKNRTSLVIAHRLS 540
Cdd:COG4615 453 FsttdLSQGQRKRLALLVALLEDRPILVFDE-------------WAAdqdpefrrvfytelLPELkARGKTVIAISHDDR 519
|
570
....*....|....*...
gi 740854059 541 TIEQADEIIVVEDGVIVE 558
Cdd:COG4615 520 YFDLADRVLKMDYGKLVE 537
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-557 |
1.92e-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: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI-----AYART-----DLYSREQIEKAAQMayamdfinkmdngLDTVigenGVL------- 480
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlGRTSTwrsllGLFPPEDRERALEA-------------LERV----GLAdkayqra 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 --LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGV 555
Cdd:COG3638 145 dqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
..
gi 740854059 556 IV 557
Cdd:COG3638 225 VV 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
343-567 |
2.84e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 136.66 E-value: 2.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALV 422
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQNV--HLFNDTVANNIAYA-RTDLYSREQ----IEKAAQMAyamdfinKMDNGLDtvigENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13632 89 FQNPdnQFIGATVEDDIAFGlENKKVPPKKmkdiIDDLAKKV-------GMEDYLD----KEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA--HRLSTIEQADEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-569 |
2.90e-36 |
|
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: 135.39 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT---LASLRDQ 418
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIAYARTD----------LYSREQIEKAaqmAYAMDfinkmDNGLDTVIGENGVLLSGGQRQ 487
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGrrstwrslfgLFPKEEKQRA---LAALE-----RVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNE 564
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAE 231
|
....*
gi 740854059 565 LIEQR 569
Cdd:cd03256 232 LTDEV 236
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
343-560 |
1.55e-35 |
|
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: 131.40 E-value: 1.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALV 422
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQnvhlfndtvanniAYARTDLYsreqiekaaqmayamDFINKmdnGLDTvigengvlLSGGQRQRIAIARALLRDSPIL 502
Cdd:cd03214 79 PQ-------------ALELLGLA---------------HLADR---PFNE--------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 503 ILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIIVVEDGVIVERG 560
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
27-313 |
1.81e-35 |
|
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: 134.88 E-value: 1.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALIlnaasdtFMLsLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18549 12 VLIAALDLV-------FPL-IVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGA----LITVVRegasIIGLFIMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDLFDISELAHHGpedlFISIIT----IIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 183 RVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 740854059 263 LAFVLYAASFPSVMENLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDL-VAFLLYVNvFIKPIRRLVNFTEQYQKGMA 290
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-556 |
1.82e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 132.27 E-value: 1.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL--REYTLASLRDQV 419
Cdd:cd03262 1 IEIKNLHKSFGDFHV--LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLF-NDTVANNIAYArtdLYSREQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLA---PIKVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIIVVEDGVI 556
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-568 |
3.78e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 133.77 E-value: 3.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFY---DIDEGQILMDGHDLREYTLASLRDQ 418
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNV--HLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAmdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGLENRaVPRPEMIKIVRDVLA-------DVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
342-568 |
6.39e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 134.89 E-value: 6.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKST----IASLITrfydIDEGQILMDGHDLreYTLASLRD 417
Cdd:COG1118 3 IEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLET----PDSGRIVLNGRDL--FTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 -QVALVSQNVHLF-NDTVANNIAYA-RTDLYSREQI-EKAAQMayamdfinkmdngLDTV-IGEngvL-------LSGGQ 485
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEIrARVEEL-------------LELVqLEG---LadrypsqLSGGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALDT----ESERAIQAALDELQknRTSLVIAH------RLstieqADEIIVVEDGV 555
Cdd:COG1118 139 RQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELG--GTTVFVTHdqeealEL-----ADRVVVMNQGR 211
|
250
....*....|...
gi 740854059 556 IVERGTHNELIEQ 568
Cdd:COG1118 212 IEQVGTPDEVYDR 224
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
28-318 |
7.26e-35 |
|
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: 133.37 E-value: 7.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 28 IVAGIALILNA-----ASDTFMLSLLKPLLDDGFGKTDRSVLLWMplvvIGLMIVRGLTSYVSSYCISWVSGKVVMTMRR 102
Cdd:cd18577 9 IAAGAALPLMTivfgdLFDAFTDFGSGESSPDEFLDDVNKYALYF----VYLGIGSFVLSYIQTACWTITGERQARRIRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18577 85 RYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 183 RVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18577 165 GIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAM 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 263 LAFVLYAASFPSVMENLTAGTI-TVVFSSMIALMrplkSLTNVNAQ---FQRGMAACQTL 318
Cdd:cd18577 245 YALAFWYGSRLVRDGEISPGDVlTVFFAVLIGAF----SLGQIAPNlqaFAKARAAAAKI 300
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-550 |
1.17e-34 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 131.75 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREA--PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlasLRDQV 419
Cdd:COG1116 8 LELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFN-DTVANNIAYARtdlySREQIEKAAQMAYAMDFINKMdnGLDtvigenGVL------LSGGQRQRIAIA 492
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGL----ELRGVPKAERRERARELLELV--GLA------GFEdayphqLSGGMRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH------RLstieqADEIIV 550
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVV 211
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
342-568 |
1.26e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 133.70 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP------GREAPALR---NINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LRE 409
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 410 YTLASLRDQVALVsqnvhlFND---------TVANNIAYA---RTDLYSREQIEKAAQMayamdfinkmdngLDTVigen 477
Cdd:COG4608 88 RELRPLRRRMQMV------FQDpyaslnprmTVGDIIAEPlriHGLASKAERRERVAEL-------------LELV---- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 GVL----------LSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQK--NRTSLVIAHRLST 541
Cdd:COG4608 145 GLRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIQAQvlnlLEDLQDelGLTYLFISHDLSV 220
|
250 260
....*....|....*....|....*...
gi 740854059 542 IEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG4608 221 VRHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-556 |
1.92e-34 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 129.58 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlasLRDQVALV 422
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQNvHLFN--------DTVANNIaYARTDL---YSREQIEKAAQmayAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAI 491
Cdd:cd03235 74 PQR-RSIDrdfpisvrDVVLMGL-YGHKGLfrrLSKADKAKVDE---ALERVG-LSELADRQIGE----LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-568 |
6.27e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 130.14 E-value: 6.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNV--HLFNDTVANNIAYA-------RTDLYSReqIEKAAQMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIA 492
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGlenigvpREEMVER--VDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-316 |
1.01e-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: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 740854059 267 LYAASFPSVMENLTAGTITVVFS-SMIALMrPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINyLMQILM-SLMMLSMVFVMLPRASASAK 290
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
343-561 |
1.06e-33 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 131.46 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYP--GREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRD 417
Cdd:PRK11153 3 ELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQnvHlFN----DTVANNIAYA-RTDLYSREQIEKaaqmayamdfinKMDNGLDTVigenGVL---------LSG 483
Cdd:PRK11153 83 QIGMIFQ--H-FNllssRTVFDNVALPlELAGTPKAEIKA------------RVTELLELV----GLSdkadrypaqLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
.
gi 740854059 561 T 561
Cdd:PRK11153 224 T 224
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
27-316 |
2.46e-33 |
|
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: 128.75 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVReGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVS 186
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGN-LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 740854059 267 LYAASFPSVMENLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18543 240 LALGGWLVANGSLTLGTL-VAFSAYLTMLVwPVRMLGWLLAMAQRARAAAE 289
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-569 |
5.47e-33 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 135.29 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 10 WQTFRRLWPtiapFKSGLIVAGIALILNAASDTFMLS---LLKPLLDDGFGKTDRSVLLwmplVVIGLMIVRGLTS---Y 83
Cdd:PTZ00243 948 WSTYVAYLR----FCGGLHAAGFVLATFAVTELVTVSsgvWLSMWSTRSFKLSAATYLY----VYLGIVLLGTFSVplrF 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 84 VSSYCISWVSGKvvmTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYY 163
Cdd:PTZ00243 1020 FLSYEAMRRGSR---NMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSAS 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 164 SwqlSLILIVLAPIVSVAIRVV---------SKRFRSISKNmqntmgQVTTSAEQMLKGHKEVLIFGGQEV----ETKRF 230
Cdd:PTZ00243 1097 Q---PFVLVALVPCGYLYYRLMqfynsanreIRRIKSVAKS------PVFTLLEEALQGSATITAYGKAHLvmqeALRRL 1167
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 231 DKVSNKMRLQGM---------------------------KMVSASSISDPIIQLiaSLALAFVLYAasfpsvMENLTAGT 283
Cdd:PTZ00243 1168 DVVYSCSYLENVanrwlgvrveflsnivvtvialigvigTMLRATSQEIGLVSL--SLTMAMQTTA------TLNWLVRQ 1239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 284 ITVVFSSMIALMRPLKSLTNVN-----------AQFQR--GMAACQTlftildseqekdeGKRVIERAT----------- 339
Cdd:PTZ00243 1240 VATVEADMNSVERLLYYTDEVPhedmpeldeevDALERrtGMAADVT-------------GTVVIEPASptsaaphpvqa 1306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYpgREA-P-ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD 417
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGlPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFNDTVANNIayartDLY---SREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV-----DPFleaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 495 LL-RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:PTZ00243 1460 LLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-315 |
8.03e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 127.65 E-value: 8.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKT-DRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLF 105
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 106 GHMMGMPVSFFDKQSTGTLLSRITYDSEQV----ASSSSGALITVVRegasIIGLFIMMFYYSWQLSLILIVLAPIVSVA 181
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVerliADGIPQGITNVLT----LVGVAIILFSINPKLALLTLIPIPFLALG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 182 IRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASL 261
Cdd:cd18778 157 AWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSL 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 262 ALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18778 237 GTVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-567 |
8.04e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 131.68 E-value: 8.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlREYTLASLRD---- 417
Cdd:COG1129 5 LEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFND-TVANNIA----YARTDLYSREQIEKAAQMAyaMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIA 492
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFlgrePRRGGLIDWRAMRRRAREL--LARLG-LDIDPDTPVGD----LSVAQQQLVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 493 RALLRDSPILILDEATSAL-DTESER--AIqaaLDELQKNRTSLV-IAHRLSTIEQ-ADEIIVVEDGVIVERG-----TH 562
Cdd:COG1129 153 RALSRDARVLILDEPTASLtEREVERlfRI---IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGpvaelTE 229
|
....*
gi 740854059 563 NELIE 567
Cdd:COG1129 230 DELVR 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-567 |
1.24e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 126.40 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNV--HLFNDTVANNIAYARTD--LYSREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLR 497
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEALKQVDMLERADYEPNA--------LSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-568 |
5.00e-32 |
|
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: 123.60 E-value: 5.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLreyTLASLRD-QVA 420
Cdd:cd03296 3 IEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQErNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-560 |
1.45e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYD-ID----EGQILMDGHDL--REYTLAS 414
Cdd:COG1117 12 IEVRNLNVYYGDKQA--LKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPgarvEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQNVHLFNDTVANNIAYA--------RTDLysREQIEKAAQMAyamdfinkmdnGL-DTV---IGENGVLLS 482
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiksKSEL--DEIVEESLRKA-----------ALwDEVkdrLKKSALGLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLStieQA----DEIIVVEDGVIVE 558
Cdd:COG1117 157 GGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQ---QAarvsDYTAFFYLGELVE 233
|
..
gi 740854059 559 RG 560
Cdd:COG1117 234 FG 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-568 |
1.72e-31 |
|
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: 121.96 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytLASLRDQVAL 421
Cdd:cd03300 1 IELENVSKFYGGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAYARTDLYSREQIEKAaQMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGLRLKKLPKAEIKE-RVAEALDLV-QLEGYANRKPSQ----LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 501 ILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
1.86e-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: 123.74 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAI---- 182
Cdd:cd18540 84 HLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSiyfq 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 183 RVVSKRFRSISKnmQNTmgQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLA 262
Cdd:cd18540 164 KKILKAYRKVRK--INS--RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 740854059 263 LAFVLYAASFpSVMEN-LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18540 240 TALVLWYGGI-LVLAGaITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
270-575 |
2.51e-31 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 130.07 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 270 ASFPSVMEN--LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEG--KRVIERATGD-LEF 344
Cdd:TIGR00957 560 AVYVTVDENniLDAEKAFVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSieRRTIKPGEGNsITV 639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlreytlaslrdQVALVSQ 424
Cdd:TIGR00957 640 HNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQ 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFNDTVANNIAYAR--TDLYSREQIEKAAQMAYamdfINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPIL 502
Cdd:TIGR00957 707 QAWIQNDSLRENILFGKalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 503 ILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-557 |
4.70e-31 |
|
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: 118.30 E-value: 4.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlREYTLASLRDQ--- 418
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDArra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 -VALVSQnvhlfndtvanniayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLR 497
Cdd:cd03216 76 gIAMVYQ--------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 498 DSPILILDEATSAL-DTESERAIqAALDELQKN-RTSLVIAHRLSTIEQ-ADEIIVVEDGVIV 557
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-316 |
4.93e-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: 122.62 E-value: 4.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 64 LLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGAL 143
Cdd:cd18573 40 LKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 144 ITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQ 223
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 224 EVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMEN-LTAGTIT-------VVFSSMIalm 295
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGS-LVASGeLTVGDLTsflmyavYVGSSVS--- 275
|
250 260
....*....|....*....|.
gi 740854059 296 rplkSLTNVNAQFQRGMAACQ 316
Cdd:cd18573 276 ----GLSSFYSELMKGLGASS 292
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
357-568 |
5.14e-31 |
|
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: 121.60 E-value: 5.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 357 PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASL----RDQVALVSQNVHLF-ND 431
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIAYArtdlYSREQIEKAAQMAYAMDFINKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:cd03294 118 TVLENVAFG----LEVQGVPRAEREERAAEALELVGLEgwEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 510 ALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
53-285 |
5.36e-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: 122.36 E-value: 5.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 53 DDGFGKTDRSVLLWMPLVVIGlmivrGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDS 132
Cdd:cd18780 35 EEALRALNQAVLILLGVVLIG-----SIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 133 EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLK 212
Cdd:cd18780 110 QVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESIS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 213 GHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTIT 285
Cdd:cd18780 190 NIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLT 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
7.60e-31 |
|
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: 126.34 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREA---------PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFydID-EGQILMDGHDLREYT 411
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL--IPsEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 412 ---LASLRDQVALVsqnvhlFND---------TVANNIAYA----RTDLYSREQIEKAAQmayAMDfinkmDNGLDTVIG 475
Cdd:COG4172 354 rraLRPLRRRMQVV------FQDpfgslsprmTVGQIIAEGlrvhGPGLSAAERRARVAE---ALE-----EVGLDPAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 476 -----EngvlLSGGQRQRIAIARALLRDSPILILDEATSALDteseRAIQAA----LDELQKNR--TSLVIAHRLSTIEQ 544
Cdd:COG4172 420 hryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 740854059 545 -ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
359-567 |
8.85e-31 |
|
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: 120.13 E-value: 8.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReyTLASLRDQVALVSQNVHLF-NDTVANNI 437
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 438 AYA-RTDLYSREQIE-KAAQMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03299 93 AYGlKKRKVDKKEIErKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 516 ERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIE 567
Cdd:cd03299 165 KEKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
30-314 |
1.23e-30 |
|
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: 121.11 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 30 AGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMM 109
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 110 GMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF 189
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 190 RSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYA 269
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 740854059 270 ASFPSVMENLTAGT-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 |
1.47e-30 |
|
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: 118.90 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLrEYTLASLRDqVAL 421
Cdd:cd03301 1 VELENVTKRFGNV--TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYA-RTDLYSREQIEK----AAQMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDErvreVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH-RLSTIEQADEIIVVEDGVIVERG 560
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-556 |
7.64e-30 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 116.74 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIAYA-RTDLYSREQIEKAAQMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFAlEVTGVPPREIRKRVPAALEL-------VGLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQA--DEIIVVEDGVI 556
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-548 |
1.63e-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: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKST----IASLITrfydIDEGQILMDGHDLREyTLASLRD 417
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFND-TVANNIAYART---DLYSREQIEKA-AQMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWAAlygLRADREAIDEAlEAV------------GLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADEI 548
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-565 |
1.89e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 115.68 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReYTLASLRDQVAL 421
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIA-YAR-TDLYSREQIEKAAQMAYAMDFINKMdnglDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARlKGLPKSEIKEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
340-565 |
4.16e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 118.25 E-value: 4.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL-----REytlas 414
Cdd:COG3839 2 ASLELENVSKSYGGVEA--LKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppKD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 lRDqVALVSQNV----HLfndTVANNIAYArtdL----YSREQIEKAAQMAYAMdfinkmdngLDtvIGEngVL------ 480
Cdd:COG3839 75 -RN-IAMVFQSYalypHM---TVYENIAFP---LklrkVPKAEIDRRVREAAEL---------LG--LED--LLdrkpkq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAhrlsTIEQ------ADEIIVVED 553
Cdd:COG3839 134 LSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV----THDQveamtlADRIAVMND 209
|
250
....*....|..
gi 740854059 554 GVIVERGTHNEL 565
Cdd:COG3839 210 GRIQQVGTPEEL 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
120-575 |
4.83e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 123.16 E-value: 4.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 120 STGTLLSRITYDS---EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRvvskRFRSISKN- 195
Cdd:PLN03232 396 ASGKVTNMITTDAnalQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVR----KMRKLTKEg 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 196 MQNTMGQVTTSAEqMLKGHKEVLIFGGQEvetkrfdkvSNKMRLQGMKMVSASSISDPiiQLIASLAlAFVLyaASFPSV 275
Cdd:PLN03232 472 LQWTDKRVGIINE-ILASMDTVKCYAWEK---------SFESRIQGIRNEELSWFRKA--QLLSAFN-SFIL--NSIPVV 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 276 MENLTAGTITVV---------FSSM--IALMR-PLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDLE 343
Cdd:PLN03232 537 VTLVSFGVFVLLggdltparaFTSLslFAVLRsPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQNPPLQPGAPAIS 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 344 FRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITrfydideGQIlmdghDLREYTLASLRDQVALV 422
Cdd:PLN03232 617 IKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML-------GEL-----SHAETSSVVIRGSVAYV 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQNVHLFNDTVANNIAYARTdlYSREQIEKA---AQMAYAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PLN03232 685 PQVSWIFNATVRENILFGSD--FESERYWRAidvTALQHDLDLLPGRDL---TEIGERGVNISGGQKQRVSMARAVYSNS 759
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 500 PILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:PLN03232 760 DIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-567 |
5.32e-29 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 5.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR--EYTLASLRDQV 419
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFND-TVANNIAYA--RTDLYSREQIEKAaqmayAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:PRK09493 80 GMVFQQFYLFPHlTALENVMFGplRVRGASKEEAEKQ-----ARELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
28-314 |
6.50e-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: 116.43 E-value: 6.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 28 IVAGIALILNAAsdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRR 102
Cdd:cd18546 1 LALALLLVVVDT----AASLAGPLLvrygiDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 103 RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAI 182
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 183 RVvskrFRSISKN----MQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLI 258
Cdd:cd18546 157 RW----FRRRSSRayrrARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 259 ASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18546 233 GNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
364-560 |
1.11e-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: 113.36 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 364 LNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlreYTLASLRDQ-VALVSQNVHLFND-TVANNIAYAR 441
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRpVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 442 T-DLYSREQIEKAAQMAYA-MDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI 519
Cdd:cd03298 96 SpGLKLTAEDRQAIEVALArVGLAGLEKRLPGE--------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 740854059 520 QAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
361-560 |
2.42e-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: 112.39 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 361 NINLNIPAGkTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLRE----YTLASLRDQVALVSQNVHLF-NDTVAN 435
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 436 NIAYARTDLYSREQIEKAAQMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740854059 516 ERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-575 |
2.75e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.00 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTY-PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLItrfydIDEGQILMDGHdlreytlASLRDQVALVS 423
Cdd:PLN03130 618 KNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM-----LGELPPRSDAS-------VVIRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVHLFNDTVANNIAYARTdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:PLN03130 686 QVSWIFNATVRDNILFGSP--FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 504 LDEATSALDTESERAI--QAALDELQkNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:PLN03130 764 FDDPLSALDAHVGRQVfdKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-566 |
4.85e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 112.87 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQ---ILmdGHDLREYTLASLRDQ 418
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLF--GERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLF---NDTVANNI---AYARTDLY---SREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRI 489
Cdd:COG1119 80 IGLVSPALQLRfprDETVLDVVlsgFFDSIGLYrepTDEQRERARELLELLGLAHLADRPFGT--------LSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQA-DEIIVVEDGVIVERGTHNELI 566
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-557 |
5.70e-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: 111.19 E-value: 5.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTYpGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlASLRDQVALVSQN 425
Cdd:cd03226 4 NISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 426 V--HLFNDTVANNIAYaRTDLYSREQIEKAAQMAyamdfinKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:cd03226 80 VdyQLFTDSVREELLL-GLKELDAGNEQAETVLK-------DLD--LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 504 LDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIIVVEDGVIV 557
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
363-556 |
9.65e-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: 110.72 E-value: 9.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 363 NLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlrEYTLASLRDQVALVSQNVHLFND-TVANNIAYA- 440
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 441 ----RTDLYSREQIEKAAQMAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:TIGR01277 96 hpglKLNAEQQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740854059 517 RAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIIVVEDGVI 556
Cdd:TIGR01277 165 EEMLALVKQLcsERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
342-574 |
1.17e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.52 E-value: 1.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--------ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREY--- 410
Cdd:PRK11308 6 LQAIDLKKHYPVKRGLfkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 411 TLASLRDQVALVSQNVH-----------LFNDTVANNiayarTDLYSREQIEKAAQMayaMDFInkmdnGLDTvigENGV 479
Cdd:PRK11308 86 AQKLLRQKIQIVFQNPYgslnprkkvgqILEEPLLIN-----TSLSAAERREKALAM---MAKV-----GLRP---EHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 ----LLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEI 548
Cdd:PRK11308 150 ryphMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV----SVQAQvlnlMMDLQQElGLSYVfISHDLSVVEHiADEV 225
|
250 260
....*....|....*....|....*..
gi 740854059 549 IVVEDGVIVERGTHNELIEQ-RGVYAQ 574
Cdd:PRK11308 226 MVMYLGRCVEKGTKEQIFNNpRHPYTQ 252
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-561 |
1.53e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 112.00 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT-LASLRDQVA 420
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQN--VHLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAmdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFGPENLcLPPIEIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGT 561
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-566 |
2.08e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.44 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpgrEAPALRnINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAslRDQVAL 421
Cdd:PRK10771 2 LKLTDITWLY---HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAYA-----RTDLYSREQIEKAAQMAYAMDFINKMDngldtviGEngvlLSGGQRQRIAIARAL 495
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELI 566
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-558 |
2.42e-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: 110.22 E-value: 2.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR---EYTLASLR 416
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 -DQVALVSQNVHLF-NDTVANNIA----YARTdlysREQIEKAAQMayamdfinkmdngLDTVigenGV---------LL 481
Cdd:COG4181 89 aRHVGFVFQSFQLLpTLTALENVMlpleLAGR----RDARARARAL-------------LERV----GLghrldhypaQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIA-HRLSTIEQADEIIVVEDGVIVE 558
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
346-564 |
3.56e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 3.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTY-PGR--EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL--REYTLASLRDQVA 420
Cdd:PRK13637 7 NLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQ--NVHLFNDTVANNIAYARTDL-YSREQIEKaaQMAYAMDFInkmdnGLD--TVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13637 87 LVFQypEYQLFEETIEKDIAFGPINLgLSEEEIEN--RVKRAMNIV-----GLDyeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNE 564
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
317-554 |
3.70e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 115.67 E-value: 3.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 317 TLFTILDSEQEKDEGKRVIERATGD-LEFRNVTFTYPGREaPALRNINLNIPAGKTVALVGRSGSGKST----IASLitr 391
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGaLALEDLTLRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 392 fYDIDEGQILMDGHDlreytlaslrdQVALVSQNVHLFNDTVANNIAY-ARTDLYSREQIEKAAQMAYAMDFINKMDNGL 470
Cdd:COG4178 413 -WPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 471 DTvigenGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIV 550
Cdd:COG4178 481 DW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLE 555
|
....
gi 740854059 551 VEDG 554
Cdd:COG4178 556 LTGD 559
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
332-567 |
6.45e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 6.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 332 KRVIERATGD--LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLRE 409
Cdd:PRK09452 3 KLNKQPSSLSplVELRGISKSFDGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 410 ytLASLRDQVALVSQNVHLF-NDTVANNIAYA-RTDLYSREQIEKAAQMAYAM----DFINKmdngldtvigeNGVLLSG 483
Cdd:PRK09452 81 --VPAENRHVNTVFQSYALFpHMTVFENVAFGlRMQKTPAAEITPRVMEALRMvqleEFAQR-----------KPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLstiEQA----DEIIVVEDGVIV 557
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQ---EEAltmsDRIVVMRDGRIE 224
|
250
....*....|
gi 740854059 558 ERGTHNELIE 567
Cdd:PRK09452 225 QDGTPREIYE 234
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
359-565 |
1.87e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.94 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLreyTLASLRD-QVALVSQNVHLFND-TVANN 436
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDrKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 437 IAYARTDLYSREQIEKAAQMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:PRK10851 95 IAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740854059 517 RAIQAALDELQKNR--TSLVIAH-RLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK10851 173 KELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
14-325 |
1.89e-26 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 109.85 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 14 RRLWPTIAPfksGLIVAGIALILNAASdTFMLS-LLKPLLDDGFGKTDRSVLLWMpLVVIGLMIVRGLTSYVSSYCISWV 92
Cdd:cd18578 5 KPEWPLLLL---GLIGAIIAGAVFPVF-AILFSkLISVFSLPDDDELRSEANFWA-LMFLVLAIVAGIAYFLQGYLFGIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQ--STGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLI 170
Cdd:cd18578 80 GERLTRRLRKLAFRAILRQDIAWFDDPenSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 171 LIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSI 250
Cdd:cd18578 160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 251 SDPIIQLIASLALAFVLYA---------ASFPSVMENLTAgtitVVFSSMIALMrplksLTNVNAQFQRGMAACQTLFTI 321
Cdd:cd18578 240 GFGLSQSLTFFAYALAFWYggrlvangeYTFEQFFIVFMA----LIFGAQSAGQ-----AFSFAPDIAKAKAAAARIFRL 310
|
....
gi 740854059 322 LDSE 325
Cdd:cd18578 311 LDRK 314
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
349-554 |
3.33e-26 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 106.65 E-value: 3.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 349 FTYpGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQIL----MDGHDLREYTLASLRDQVALVSQ 424
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFNDTVANNIAYARTdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:cd03290 87 KPWLLNATVEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740854059 505 DEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEQADEIIVVEDG 554
Cdd:cd03290 165 DDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-568 |
3.78e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 109.81 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASlRDqVAL 421
Cdd:PRK11432 7 VVLKNITKRFG--SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYA-RTDLYSREQIEKAAQMAYAM-DFINKMDNGLDTVigengvllSGGQRQRIAIARALLRD 498
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGlKMLGVPKEERKQRVKEALELvDLAGFEDRYVDQI--------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-565 |
5.31e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 107.90 E-value: 5.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY-PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVA 420
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNV--HLFNDTVANNIAY-------ARTDLysREQIEKAAQMAYAMDFINKmdngldtvigeNGVLLSGGQRQRIAI 491
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFglenkgiPHEEM--KERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 492 ARALLRDSPILILDEATSALDTESE----RAIQAALDELQknRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDYQ--MTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
342-560 |
5.35e-26 |
|
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: 105.74 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTvALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAsLRDQVAL 421
Cdd:cd03264 1 LQLENLTKRYGKKRA--LDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYARTdLYSREQIEKAAQMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYIAW-LKGIPSKEVKARVDEVLELVN-LGDRAKKKIGS----LSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
346-569 |
9.95e-26 |
|
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: 107.25 E-value: 9.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFT-YPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlreytlaslrdQVALVSQ 424
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFNDTVANNIAYART-DLYSREQIEKAAQMAYAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSyDEYRYKSVVKACQLEEDITKFPEKDN---TVLGEGGITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 504 LDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:cd03291 183 LDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-576 |
1.33e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.79 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPG---REAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDG----HDLREYTLAS 414
Cdd:PRK13646 3 IRFDNVSYTYQKgtpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTDLysREQIEKAAQMAYAMdfinKMDNGLD-TVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNF--KMNLDEVKNYAHRL----LMDLGFSrDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236
|
....*...
gi 740854059 569 RGVYAQLH 576
Cdd:PRK13646 237 KKKLADWH 244
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-565 |
2.31e-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: 104.44 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReyTLAS---LRDQ 418
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI---AYARTDLYSREQIEKaaqmAYAMdFINkmdngLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLER----VYEL-FPR-----LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIahrlstIEQ--------ADEIIVVEDGVIVERGTHNEL 565
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILL------VEQnarfaleiADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
341-565 |
3.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.87 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 341 DLEFRNVTFTYPGR---EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL----REYTLA 413
Cdd:PRK13634 2 DITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQVALVSQ--NVHLFNDTVANNIAYARTDL-YSREQIE-KAAQMAYAMdfinkmdnGLD-TVIGENGVLLSGGQRQR 488
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFgVSEEDAKqKAREMIELV--------GLPeELLARSPFELSGGQMRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
342-554 |
1.17e-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: 102.51 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNV--TFTY---PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDgHDLREYTLASL- 415
Cdd:COG4778 5 LEVENLskTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 -RDQVAL-------VSQNVH--------------LFNDTVANNIAYART-DLYSREQIEKAAQMAYAMDFinkmdngldt 472
Cdd:COG4778 84 pREILALrrrtigyVSQFLRviprvsaldvvaepLLERGVDREEARARArELLARLNLPERLWDLPPATF---------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 473 vigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIIV 550
Cdd:COG4778 154 ---------SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVD 224
|
....
gi 740854059 551 VEDG 554
Cdd:COG4778 225 VTPF 228
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
1.55e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 107.46 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRN--VTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKS----TIASLITRFYDIDEGQILMDGHDLREYTLASL 415
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 R----DQVALVSQ------N-VHlfndTVANNI--------------AYART-DLYSREQIEKAAQM--AYAMDfinkmd 467
Cdd:COG4172 87 RrirgNRIAMIFQepmtslNpLH----TIGKQIaevlrlhrglsgaaARARAlELLERVGIPDPERRldAYPHQ------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 468 ngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEQ- 544
Cdd:COG4172 157 -------------LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLlITHDLGVVRRf 223
|
250 260
....*....|....*....|....
gi 740854059 545 ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG4172 224 ADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
342-563 |
1.76e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH------DLREYTLASL 415
Cdd:COG4161 3 IQLKNINCFYGSHQA--LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 RDQVALVSQNVHLF-NDTVANNIAYARTDLYSreqIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:COG4161 81 RQKVGMVFQQYNLWpHLTVMENLIEAPCKVLG---LSKEQAREKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHN 563
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
343-566 |
1.88e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.47 E-value: 1.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALV 422
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQNVHlFND--TVANNIAYARTDlYSREQIEKA--AQMAYAMDFINKM---DNGLDTvigengvlLSGGQRQRIAIARAL 495
Cdd:COG4604 81 RQENH-INSrlTVRELVAFGRFP-YSKGRLTAEdrEIIDEAIAYLDLEdlaDRYLDE--------LSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAAL----DELqkNRTSLVIAHrlsTIEQA----DEIIVVEDGVIVERGTHNELI 566
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLrrlaDEL--GKTVVIVLH---DINFAscyaDHIVAMKDGRVVAQGTPEEII 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-560 |
3.43e-24 |
|
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: 100.75 E-value: 3.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytLASLRDQV-A 420
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSqnVHLFND---TVANNIAYARTDLYSREQIEKAAQMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03268 77 LIE--APGFYPnltARENLRLLARLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
359-576 |
3.93e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 101.63 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQnVHLFND--TVANN 436
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHLTPEgiTVREL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 437 IAYART---DLYSREQIEKAAQMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:PRK11231 97 VAYGRSpwlSLWGRLSAEDNARVNQAME-----QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 514 ESERAIQAALDELQKN-RTSLVIAHRLStieQA----DEIIVVEDGVIVERGTHNELIEQR------GVYAQLH 576
Cdd:PRK11231 172 NHQVELMRLMRELNTQgKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGTPEEVMTPGllrtvfDVEAEIH 242
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-571 |
5.56e-24 |
|
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: 100.83 E-value: 5.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRdq 418
Cdd:COG0410 4 LEVENLHAGYG--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIARLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI---AYARTDlysREQIEKAAQMAYAM-----DFINKMdngldtvigenGVLLSGGQRQRI 489
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYARRD---RAEVRADLERVYELfprlkERRRQR-----------AGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 490 AIARALLRDSPILILDEATSALdteserA------IQAALDELQKNRTSLVIahrlstIEQ--------ADEIIVVEDGV 555
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL------ApliveeIFEIIRRLNREGVTILL------VEQnarfaleiADRAYVLERGR 213
|
250
....*....|....*.
gi 740854059 556 IVERGTHNELIEQRGV 571
Cdd:COG0410 214 IVLEGTAAELLADPEV 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-563 |
6.02e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.49 E-value: 6.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlREYTLASLRDQVAL 421
Cdd:COG3845 6 LELRGITKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 ----VSQNVHLFND-TVANNIAYARTDLYS--------REQIEKAAQmAYAMDfINkmdngLDTVIGEngvlLSGGQRQR 488
Cdd:COG3845 81 gigmVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkaaRARIRELSE-RYGLD-VD-----PDAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 489 IAIARALLRDSPILILDEATSAL-DTESERAIqAALDELQKNRTSLV-IAHRLSTIEQ-ADEIIVVEDGVIVerGTHN 563
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV--GTVD 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-557 |
7.93e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 7.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFT-YPG--REAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASL 415
Cdd:COG1101 2 LELKNLSKTfNPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 rdqVALVSQNVHL---FNDTVANN--IAYARTDLYSREQIEKAAQMAYAMDFINKMDNGL----DTVIGengvLLSGGQR 486
Cdd:COG1101 82 ---IGRVFQDPMMgtaPSMTIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLstiEQA----DEIIVVEDGVIV 557
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
342-561 |
8.82e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 101.36 E-value: 8.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGR---EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT----LAS 414
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAMDFINkmdnglDTVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL--STIEQADEIIVVEDGVIVERGT 561
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-574 |
9.51e-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: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 340 GDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIdEGQILMDGHDLREYTLASLRDQV 419
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNI-AYARtdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLdPYGK---WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQ 574
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
342-558 |
1.16e-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: 100.65 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY-------PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAS 414
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 ---LRDQVALVSQN-VHLFN--DTVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQR 488
Cdd:TIGR02769 83 rraFRRDVQLVFQDsPSAVNprMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVE 558
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
342-549 |
1.19e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.40 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK10247 8 LQLQNVGYLAGDA--KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYArtdlYS-REQIEKAAQMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP 500
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFP----WQiRNQQPDPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 740854059 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEII 549
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-574 |
1.25e-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: 106.15 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 1 MHNDKDLSTWQTFRRLWPTIAPFKSGLIVAGIALILNAASDTFMLSLL-----KPLLDDGFGKTDRSvllwmPLVVIGLM 75
Cdd:TIGR01271 844 RENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLAEVAASLLGLWLItdnpsAPNYVDQQHANASS-----PDVQKPVI 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 76 IVRGLTSYV---------SSYCISWVSG----KVVMTMRRRLFGHMMGM----PVSFFDKQSTGTLLSRITYDSEQVASS 138
Cdd:TIGR01271 919 ITPTSAYYIfyiyvgtadSVLALGFFRGlplvHTLLTVSKRLHEQMLHSvlqaPMAVLNTMKAGRILNRFTKDMAIIDDM 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 139 SSGALITVVREGASIIGlfiMMFYYSWQLSLILIVLAPiVSVAIRVVSKRFRSISKNMQNTMGQ----VTTSAEQMLKGH 214
Cdd:TIGR01271 999 LPLTLFDFIQLTLIVLG---AIFVVSVLQPYIFIAAIP-VAVIFIMLRAYFLRTSQQLKQLESEarspIFSHLITSLKGL 1074
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 215 KEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIaslalaFVLY--AASFPSVMEN-LTAGTITVVFSSM 291
Cdd:TIGR01271 1075 WTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDII------FVFFfiAVTFIAIGTNqDGEGEVGIILTLA 1148
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 292 IALMRPLKSLTNVNAQFQRGMAACQTLFTILDSEQEKDEGKR-----------VIER--------ATGDLEFRNVTFTYP 352
Cdd:TIGR01271 1149 MNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGgggkyqlstvlVIENphaqkcwpSGGQMDVQGLTAKYT 1228
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 353 GREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIdEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDT 432
Cdd:TIGR01271 1229 EAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGT 1307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNI-AYARtdlYSREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
Cdd:TIGR01271 1308 FRKNLdPYEQ---WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 512 DTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGVYAQ 574
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-565 |
1.59e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.54 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP-GREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReYTLASL---RD 417
Cdd:PRK13639 2 LETRDLKYSYPdGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNV--HLFNDTVANNIAYARTDL-YSREQIE---KAAQMAYAM-DFINKMDNGLdtvigengvllSGGQRQRIA 490
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGPLNLgLSKEEVEkrvKEALKAVGMeGFENKPPHHL-----------SGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIE-QADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-565 |
1.96e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 99.60 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGQILMDGHDLREYTLASLRDQVALVSQ----- 424
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 -NVHLFnDTVA-----NNIAYARTDLYSR--EQIEKAaqmayamDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
Cdd:PRK14247 95 pNLSIF-ENVAlglklNRLVKSKKELQERvrWALEKA-------QLWDEVKDRLDAPAGK----LSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStieqaDEIIVVEDGVIVERGTHNEL 565
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
358-561 |
1.97e-23 |
|
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: 99.05 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRdqVALVSQNVHLFND-TV 433
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG--IGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYA------RTDLYSREQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:cd03219 93 LENVMVAaqartgSGLLLARARREEREARERAEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 508 TSAL-DTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGT 561
Cdd:cd03219 171 AAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-565 |
1.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.47 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTIAS-----LITRFYDIDEGQILMDGHDLREYTLAS-----------LRDQ 418
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQ--NVHLFNDTVANNIAYARTDLySREQIEKAAQMAYamdFINKMdnGLD-TVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKF---YLNKM--GLDdSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 496 LRDSPILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
342-560 |
2.87e-23 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 97.62 E-value: 2.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAPA----LRNINLNIPAGKTVALVGRSGSGKSTIASLIT--RFYDIDEGQILMDGHDLReytLASL 415
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 RDQVALVSQNVHLF-NDTVanniayartdlysREqiekaaqmayAMDFINKMDNgldtvigengvlLSGGQRQRIAIARA 494
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTV-------------RE----------TLMFAAKLRG------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIIVVEDGVIVERG 560
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
3.23e-23 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 100.33 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASD---TFMLSL-----------LKPLLDDGFGKTDRSVLLWM-PLVVIGLMIVRGLTSYVSSYCISW 91
Cdd:cd18565 1 LVLGLLASILNRLFDlapPLLIGVaidavfngeasFLPLVPASLGPADPRGQLWLlGGLTVAAFLLESLFQYLSGVLWRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 92 VSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIL 171
Cdd:cd18565 81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 172 IVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSIS 251
Cdd:cd18565 161 LLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAF 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 252 DPIIQLIASLALAFVLYAASF------PSVMENLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18565 241 FPVIRLVAGAGFVATFVVGGYwvldgpPLFTGTLTVGTL-VTFLFYTQrLLWPLTRLGDLIDQYQRAMAS 309
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
301-565 |
3.37e-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: 104.99 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 301 LTNVNAQFQRGMAAcqtLFTilDSEQEKDEGKRvierATGD--LEFRNVTFTYpgreAPALRNINLNIPAGKTVALVGRS 378
Cdd:TIGR01271 395 MVNVTASWDEGIGE---LFE--KIKQNNKARKQ----PNGDdgLFFSNFSLYV----TPVLKNISFKLEKGQLLAVAGST 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 379 GSGKSTIASLITRFYDIDEGQILMDGhdlreytlaslrdQVALVSQNVHLFNDTVANNIAYART-DLYSREQIEKAAQMA 457
Cdd:TIGR01271 462 GSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFGLSyDEYRYTSVIKACQLE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 458 YAMDFINKMDNgldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIA 536
Cdd:TIGR01271 529 EDIALFPEKDK---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVT 605
|
250 260
....*....|....*....|....*....
gi 740854059 537 HRLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:TIGR01271 606 SKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-569 |
3.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 3.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY-PGR--EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT----LAS 414
Cdd:PRK13641 3 IKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTDLYSREQIEKAAqmayAMDFINKMdnGLDT-VIGENGVLLSGGQRQRIAI 491
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK----ALKWLKKV--GLSEdLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-549 |
4.37e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 4.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 351 YPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlreytlaslrdQVALVSQNVHL-- 428
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 429 -FNDTVANNIA---YARTDLYSREQIEKAAQMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:NF040873 69 sLPLTVRDLVAmgrWARRGLWRRLTRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 740854059 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEII 549
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-556 |
6.27e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDghdlrEYTLASLRDQVAL 421
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFN-DTVANNIAyartdLYSREQIEKAAQMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVG-----LGLKGQWRDAALQALAA-------VGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIIVVEDGVI 556
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
342-561 |
7.35e-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: 98.19 E-value: 7.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRdq 418
Cdd:COG0411 5 LEVRGLTKRFGGLVA--VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHRIARLG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI--------------AYARTDLYSREQIEKAAQMAYAMDFInkmdnGLDTVIGENGVLLSG 483
Cdd:COG0411 81 IARTFQNPRLFPElTVLENVlvaaharlgrgllaALLRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEG 235
|
.
gi 740854059 561 T 561
Cdd:COG0411 236 T 236
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
51-314 |
9.80e-23 |
|
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: 98.67 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 51 LLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITy 130
Cdd:cd18570 28 LIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 131 DSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQM 210
Cdd:cd18570 107 DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 211 LKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMEN-LTAGTItVVFS 289
Cdd:cd18570 187 LKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSY-LVIKGqLSLGQL-IAFN 264
|
250 260
....*....|....*....|....*.
gi 740854059 290 SMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18570 265 ALLGyFLGPIENLINLQPKIQEAKVA 290
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-574 |
9.82e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.27 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP-GREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVA 420
Cdd:PRK13647 5 IEVEDLHFRYKdGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNV--HLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAM----DFINKMDNGLdtvigengvllSGGQRQRIAIAR 493
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMgLDKDEVERRVEEALKAvrmwDFRDKPPYHL-----------SYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIIVVEDGVIVERGThNELIEQRGV 571
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDEDI 230
|
...
gi 740854059 572 YAQ 574
Cdd:PRK13647 231 VEQ 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
342-572 |
9.95e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.92 E-value: 9.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHL-FNDTVANNIAYARTDLYSREQIEKAAqmayamdfinkmdngLDTVIGENGVL---------LSGGQRQRIAI 491
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDAL---------------VAAALAQVDLAhlagrdypqLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 492 ARALLR------DSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLS-TIEQADEIIVVEDGVIVE 558
Cdd:PRK13548 146 ARVLAQlwepdgPPRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVA 221
|
250
....*....|....*....
gi 740854059 559 RGT-----HNELIEQrgVY 572
Cdd:PRK13548 222 DGTpaevlTPETLRR--VY 238
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
67-316 |
1.28e-22 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 98.26 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 67 MPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITV 146
Cdd:cd18554 48 IGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 147 VREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVE 226
Cdd:cd18554 128 WLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 227 TKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRPLKSLTNVNA 306
Cdd:cd18554 208 QKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFT 287
|
250
....*....|
gi 740854059 307 QFQRGMAACQ 316
Cdd:cd18554 288 TLTQSFASMD 297
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-539 |
1.35e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGQILMDGHDL--REYTLASLRDQVALVSQNVHLFN 430
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 431 DTVANNIAY-ARTDLYS---REQIEKAAQMAYAMDFINKMdngldtvIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
Cdd:PRK14243 105 KSIYDNIAYgARINGYKgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|...
gi 740854059 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
359-558 |
1.49e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.45 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL----REYTLASLRDqVALVSQN-VHLFN--D 431
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRD-IQMVFQDsISAVNprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIAYAR---TDLYSREQIEKAAQMAYAMDFinkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEAT 508
Cdd:PRK10419 107 TVREIIREPLrhlLSLDKAERLARASEMLRAVDL---DDSVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 740854059 509 SALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIIVVEDGVIVE 558
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
358-562 |
2.31e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH--DLR----EYTLASLRDQVALVSQNVHLF-N 430
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIRELRRNVGMVFQQYNLWpH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 431 DTVANNIAYARTDLYSreqIEKAAQMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSA 510
Cdd:PRK11124 97 LTVQQNLIEAPCRVLG---LSKDQALARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 511 LDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTH 562
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-568 |
2.58e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGQILMDGHDLREYT-------- 411
Cdd:COG0396 1 LEIKNLHVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 412 --LA----------SLRDqvalvsqnvhlFNDTVANNIAYARTDLY-SREQI-EKAAQMAYAMDFINKmdnGLDtvigen 477
Cdd:COG0396 79 ifLAfqypveipgvSVSN-----------FLRTALNARRGEELSAReFLKLLkEKMKELGLDEDFLDR---YVN------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 gVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAH--RLSTIEQADEIIVVEDG 554
Cdd:COG0396 139 -EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDG 217
|
250
....*....|....
gi 740854059 555 VIVERGTHnELIEQ 568
Cdd:COG0396 218 RIVKSGGK-ELALE 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-560 |
2.68e-22 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 95.51 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 348 TFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRdQVALVSQNVH 427
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 428 LFND-TVANNIAY-------ARTDLYSReqIEKAAQMAYAMDFINKMDNGLDTvigengvllsgGQRQRIAIARALLRDS 499
Cdd:cd03266 89 LYDRlTARENLEYfaglyglKGDELTAR--LEELADRLGMEELLDRRVGGFST-----------GMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
342-559 |
3.19e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREA--PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReyTLASLRdqv 419
Cdd:COG4525 4 LTVRHVSVRYPGGGQpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFN-DTVANNIAYArtdLYSReQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFG---LRLR-GVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 499 SPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQA----DEIIVVED--GVIVER 559
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-568 |
3.30e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY----PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD-LREYTLASLR 416
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQNVHlfNDTVAN----NIAYARTDL-YSREQIEKaaqmayamdfinKMDNGLDTVigenGV---------LLS 482
Cdd:PRK13633 85 NKAGMVFQNPD--NQIVATiveeDVAFGPENLgIPPEEIRE------------RVDESLKKV----GMyeyrrhaphLLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIIVVEDGVIVERG 560
Cdd:PRK13633 147 GGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
....*...
gi 740854059 561 THNELIEQ 568
Cdd:PRK13633 227 TPKEIFKE 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
342-558 |
3.40e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMdGHDLReytlaslrdqVAL 421
Cdd:COG0488 316 LELEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF--NDTVANNIAYARTDLYSREqiekAAQMAYAMDFINKMdngLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:COG0488 383 FDQHQEELdpDKTVLDELRDGAPGGTEQE----VRGYLGRFLFSGDD---AFKPVGV----LSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEIIVVEDGVIVE 558
Cdd:COG0488 452 NVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
360-566 |
3.72e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.21 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 360 RNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFND-TVANNIA 438
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 439 ---YARTDLYSREQIEKAAQMAYAMdfinkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:PRK10253 104 rgrYPHQPLFTRWRKEDEEAVTKAM-----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 516 ERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELI 566
Cdd:PRK10253 179 QIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-515 |
4.87e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 4.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 344 FRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhDLReytlaslrdqVALVS 423
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVHLFND-TVANNIAYARTDLYS-REQIEKA-AQMAYAMDFINKMD----------------------NGL-------D 471
Cdd:COG0488 68 QEPPLDDDlTVLDTVLDGDAELRAlEAELEELeAKLAEPDEDLERLAelqeefealggweaearaeeilSGLgfpeedlD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 740854059 472 TVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-565 |
5.96e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.22 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR-EYTLASLRDQVA 420
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNIAYARtdLYSREQ-IEKAAQMAYAMDFINKMDNGLD--TVIGEngvlLSGGQRQRIAIARALL 496
Cdd:PRK11288 83 IIYQELHLVPEmTVAENLYLGQ--LPHKGGiVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 497 RDSPILILDEATSALdteSERAIQ---AALDEL-QKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVErgTHNEL 565
Cdd:PRK11288 157 RNARVIAFDEPTSSL---SAREIEqlfRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
339-565 |
7.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 96.23 E-value: 7.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 339 TGDLEFRNVTFTYPGR---EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL-----REY 410
Cdd:PRK13645 4 SKDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 411 TLASLRDQVALVSQ--NVHLFNDTVANNIAYARTDLYSREQiEKAAQMAYAMDFINKMDNgldtVIGENGVLLSGGQRQR 488
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLPED----YVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVLRiADEVIVMHEGKVISIGSPFEI 238
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
374-568 |
8.25e-22 |
|
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: 96.79 E-value: 8.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 374 LVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytLASLRDQVALVSQNVHLF-NDTVANNIAYA-RTDLYSREQIe 451
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 452 kAAQMAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR- 530
Cdd:TIGR01187 78 -KPRVLEALRLVQLEEFADRKPHQ-----LSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 740854059 531 -TSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:TIGR01187 152 iTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-567 |
1.02e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.85 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQ 424
Cdd:PRK10575 15 RNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHLFND-TVANNIAYARTDLY---------SREQIEKAAQMAYAMDFINKMdngLDTvigengvlLSGGQRQRIAIARA 494
Cdd:PRK10575 93 QLPAAEGmTVRELVAIGRYPWHgalgrfgaaDREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhRLSTIEQA----DEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-557 |
1.50e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREY---TLASLR 416
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 -DQVALVSQNVHLFND-TVANNI----AYArtdlysreQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIA 490
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHlTAAQNVevpaVYA--------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIIVVEDGVIV 557
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
358-548 |
2.06e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGQILMDGHDL---REYTLaSLRDQVALVSQNVHLF 429
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTV-DLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 430 NDTVANNIAY----------ARTDlysrEQIEKAAQMAYAMDFINkmDNGLDTVIGengvlLSGGQRQRIAIARALLRDS 499
Cdd:PRK14239 99 PMSIYENVVYglrlkgikdkQVLD----EAVEKSLKGASIWDEVK--DRLHDSALG-----LSGGQQQRVCIARVLATSP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQADEI 548
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
342-567 |
4.20e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 95.29 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytLASLRDQVAL 421
Cdd:PRK11607 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYA-RTDLYSREQI----EKAAQMAYAMDFINKMDNGldtvigengvlLSGGQRQRIAIARAL 495
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFGlKQDKLPKAEIasrvNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 496 LRDSPILILDEATSALDTE-SERAIQAALDELQK-NRTSLVIAH-RLSTIEQADEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-565 |
5.07e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 92.51 E-value: 5.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI-----LMDGH---DLREYTLA 413
Cdd:PRK11264 4 IEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQVALVSQNVHLF-NDTVANNIAYARTDLysrEQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFpHRTVLENIIEGPVIV---KGEPKEEATARARELLAKV--GLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 493 RALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-565 |
5.90e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 92.80 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH------DLREYTLASLRDQVALVSQNVHLF-ND 431
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNGLDTvIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 512 DTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
342-565 |
7.68e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.85 E-value: 7.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGR-EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVA 420
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNV--HLFNDTVANNIAYARTD--LYSREQIEKAAQMAYAMdfinkmdNGLDTVIGENGvLLSGGQRQRIAIARALL 496
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEALLAV-------NMLDFKTREPA-RLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
44-289 |
1.26e-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: 92.52 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 44 MLSLLKPL-----LDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDK 118
Cdd:cd18567 16 LFALASPLylqlvIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 119 QSTGTLLSRItyDS-EQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIlIVLAPIVSVAIRVVS-KRFRsisknm 196
Cdd:cd18567 96 RHLGDIVSRF--GSlDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALI-VLAAVALYALLRLALyPPLR------ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 197 QNTMGQVTTSAEQ------MLKGHKEVLIFGGQEVETKRF-----DKVSNKMRLQGMKMVSASsisdpIIQLIASLALAF 265
Cdd:cd18567 167 RATEEQIVASAKEqshfleTIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQILFSA-----ANGLLFGLENIL 241
|
250 260
....*....|....*....|....*
gi 740854059 266 VLYAASFpSVMEN-LTAGTITVVFS 289
Cdd:cd18567 242 VIYLGAL-LVLDGeFTVGMLFAFLA 265
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
362-581 |
1.46e-20 |
|
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: 93.25 E-value: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 362 INLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLRE----YTLASLRDQVALVSQNVHLFND-TVANN 436
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 437 IAYARTDL---YSREQIEKAAQMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:TIGR02142 96 LRYGMKRArpsERRISFERVIELL-----------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNElIEQRGVYAQLHKMQFG 581
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAE-VWASPDLPWLAREDQG 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
342-514 |
1.52e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID---EGQILMDGHDLReyTLASLRDQ 418
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLF-NDTVANNIAYARTDLYSREQIEKAAQMAYAmdfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:COG4136 78 IGILFQDDLLFpHLSVGENLAFALPPTIGRAQRRARVEQALE-------EAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170
....*....|....*..
gi 740854059 498 DSPILILDEATSALDTE 514
Cdd:COG4136 151 EPRALLLDEPFSKLDAA 167
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
358-565 |
1.85e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.85 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD---------QVALVSQNVHL 428
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqmifQDPLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 429 fndTVANNIAYARTDLY---SREQI-EKAAQMayaMDFINKMDNgldtVIGENGVLLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK15079 116 ---TIGEIIAEPLRTYHpklSRQEVkDRVKAM---MLKVGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 505 DEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK15079 186 DEPVSALDV----SIQAQvvnlLQQLQREmGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-554 |
2.69e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 94.23 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGQILMDGHDLREYTLA-SLRDQ 418
Cdd:PRK13549 6 LEMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRdTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIayartdlYSREQIEKAAQMAYAMDFIN--------KMDNGLDTVIGEngvlLSGGQRQRI 489
Cdd:PRK13549 84 IAIIHQELALVKElSVLENI-------FLGNEITPGGIMDYDAMYLRaqkllaqlKLDINPATPVGN----LGLGQQQLV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 490 AIARALLRDSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-565 |
2.92e-20 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 89.74 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTlASLRDQVAL 421
Cdd:cd03265 1 IEVENLVKKYGDFEA--VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFNDTVANNIAYARTDLY---SREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRD 498
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYgvpGAERRERIDELLDFVGLLEAADRLVKT--------YSGGMRRRLEIARSLVHR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:cd03265 150 PEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-565 |
4.28e-20 |
|
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: 92.09 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 361 NINLNIPAGKTVALVGRSGSGKST----IASLITrfydIDEGQILMDGHDL----REYTLASLRDQVALVSQNVHLFND- 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTllraIAGLER----PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIAYARTDLysreqieKAAQMAYAMDFINKMdngLDtvIGEngvL-------LSGGQRQRIAIARALLRDSPILIL 504
Cdd:COG4148 93 SVRGNLLYGRKRA-------PRAERRISFDEVVEL---LG--IGH---LldrrpatLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 505 DEATSALDTESERAIqaaLDELQKNRTSLVI-----AHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:COG4148 158 DEPLAALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEV 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
342-561 |
4.47e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 90.28 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP-------ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLrEYTLAS 414
Cdd:COG4167 5 LEVRNLSKTFKYRTGLfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQ-VALVSQNVhlfNDTVANNIAYAR---------TDLYSREQIEKAAQ-------MAYAMDFINKMdngldtvigen 477
Cdd:COG4167 84 YRCKhIRMIFQDP---NTSLNPRLNIGQileeplrlnTDLTAEEREERIFAtlrlvglLPEHANFYPHM----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 gvlLSGGQRQRIAIARALLRDSPILILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVED 553
Cdd:COG4167 150 ---LSSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqIINLMLELQEKLgiSYIYVSQHLGIVKHiSDKVLVMHQ 225
|
....*...
gi 740854059 554 GVIVERGT 561
Cdd:COG4167 226 GEVVEYGK 233
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-560 |
6.00e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 94.46 E-value: 6.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDghdlreytlaslrDQVALVSQNVHLFNDTVANNIa 438
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI- 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 439 yartdLYSREqiEKAAQMAYAMDF------INKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PTZ00243 742 -----LFFDE--EDAARLADAVRVsqleadLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740854059 513 TE-SERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVERG 560
Cdd:PTZ00243 815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-566 |
6.23e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.02 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRD----QVALVSQNVHLF-NDT 432
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNIAYArtdlYSREQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PRK10070 123 VLDNTAFG----MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 513 TESERAIQAALDELQ--KNRTSLVIAHRL-STIEQADEIIVVEDGVIVERGTHNELI 566
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-576 |
9.09e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.48 E-value: 9.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNV--HLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAMdfinkmdNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPINLgLDEETVAHRVSSALHM-------LGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTI-EQADEIIVVEDGVIVERGTHNELIEQRGVYAQL 575
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARV 235
|
.
gi 740854059 576 H 576
Cdd:PRK13652 236 H 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
342-568 |
9.64e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 91.06 E-value: 9.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASlRDqVAL 421
Cdd:PRK11650 4 LKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYA-------RTDLysREQIEKAAQMAYAMDFinkmdngLDTVIGEngvlLSGGQRQRIAIAR 493
Cdd:PRK11650 81 VFQNYALYpHMSVRENMAYGlkirgmpKAEI--EERVAEAARILELEPL-------LDRKPRE----LSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 494 ALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
342-565 |
1.13e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.60 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreaPALRNINLNIPAGKTVALVGRSGSGKS-TIASL-------ITRFydidEGQILMDGhdlREYTLA 413
Cdd:PRK10418 5 IELRNIALQAAQ---PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAlgilpagVRQT----AGRVLLDG---KPVAPC 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQ-VALVSQNVH-LFNdTVANNIAYARTDLYSREQIEKAAQMAYAMDFInkmdnGLD---TVIGENGVLLSGGQRQR 488
Cdd:PRK10418 75 ALRGRkIATIMQNPRsAFN-PLHTMHTHARETCLALGKPADDATLTAALEAV-----GLEnaaRVLKLYPFEMSGGMLQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK10418 149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-560 |
1.51e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 87.34 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReytlASLRDQVAL 421
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAY-ARTDLYSREQIEKAAQmayamDFINKMD--NGLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlAQLKGLKKEEARRRID-----EWLERLElsEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-568 |
1.76e-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: 86.81 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGQILMDGHDLREYTlaslrdqv 419
Cdd:cd03217 1 LEIKDLHVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 alvsqnvhlfndtvanniayarTDLYSREQIEKAAQMAYA------MDFINKMDNGldtvigengvlLSGGQRQRIAIAR 493
Cdd:cd03217 71 ----------------------PEERARLGIFLAFQYPPEipgvknADFLRYVNEG-----------FSGGEKKRNEILQ 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 494 ALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIIVVEDGVIVERGThNELIEQ 568
Cdd:cd03217 118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
314-560 |
1.81e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.69 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 314 ACQTLFT---------ILDSEQEkDEGKRVIERATGDLEFRNVTFTYPGR---------EAPALRNINLNIPAGKTVALV 375
Cdd:PRK15134 240 RAATLFSapthpytqkLLNSEPS-GDPVPLPEPASPLLDVEQLQVAFPIRkgilkrtvdHNVVVKNISFTLRPGETLGLV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 376 GRSGSGKSTIASLITRFYDiDEGQILMDGHDLREYT---LASLRDQVALVSQ------NVHL-FNDTVANNIAYARTDLY 445
Cdd:PRK15134 319 GESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQdpnsslNPRLnVLQIIEEGLRVHQPTLS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 446 SREQiekAAQMAYAMdfinkMDNGLDTVI-----GEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQ 520
Cdd:PRK15134 398 AAQR---EQQVIAVM-----EEVGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIL 465
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 740854059 521 AALDELQ-KNRTS-LVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:PRK15134 466 ALLKSLQqKHQLAyLFISHDLHVVRAlCHQVIVLRQGEVVEQG 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-565 |
5.90e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAsLRDQVA- 420
Cdd:PRK15439 12 LCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 -LVSQNVHLF-NDTVANNIAY--ARTDLYSREQIEKAAQMAYAMDfinkmdngLDTVIGengvLLSGGQRQRIAIARALL 496
Cdd:PRK15439 89 yLVPQEPLLFpNLSVKENILFglPKRQASMQKMKQLLAALGCQLD--------LDSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
355-565 |
5.93e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.95 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR-------------EYTLASLRDQVAL 421
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFND-TVANNIAYARTDLYSreqIEKAAQMAYAMDFINKMdnGLD-TVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMEAPIQVLG---LSKQEARERAVKYLAKV--GIDeRAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-565 |
6.47e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLreytlaslrdqval 421
Cdd:COG4152 2 LELKGLTKRFGDK--TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 vsqnvhlfNDTVANNIAY---ARtDLYSR----EQI---------EKAAQMAYAMDFINKMDNG--LDTVIGEngvlLSG 483
Cdd:COG4152 66 --------DPEDRRRIGYlpeER-GLYPKmkvgEQLvylarlkglSKAEAKRRADEWLERLGLGdrANKKVEE----LSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 484 GQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSlVI--AHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVLSG 211
|
....*
gi 740854059 561 THNEL 565
Cdd:COG4152 212 SVDEI 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
342-569 |
9.06e-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: 85.65 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpGReAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLAslRDQ 418
Cdd:TIGR03410 1 LEVSNLNVYY-GQ-SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERA--RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIayaRTDLYSREQIEKAAQmayamDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENL---LTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
69-292 |
1.20e-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: 86.95 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 69 LVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVR 148
Cdd:cd18558 63 YYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 149 EGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
Cdd:cd18558 143 NIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEET 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 229 RFDKVSNKMRLQGMKMVSASSISDPIIQLI--ASLALAFvLYAASFPSVMENLTAGTITVVFSSMI 292
Cdd:cd18558 223 RYAQNLEIAKRNGIKKAITFNISMGAAFLLiyASYALAF-WYGTYLVTQQEYSIGEVLTVFFSVLI 287
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-571 |
1.77e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.05 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP-GREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH--DLREYTLASLRDQ 418
Cdd:PRK13636 6 LKVEELNYNYSdGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNV--HLFNDTVANNIAYARTDL-YSREQIEKAAQMAYAMDFINKMDNgldtvigENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLkLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIE-QADEIIVVEDGVIVERGTHNELIEQRGV 571
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEM 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
344-565 |
2.58e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 87.01 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 344 FRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytLASLRDQVALVS 423
Cdd:PRK11000 6 LRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVHLF-NDTVANNIAY-------ARTDLYSR-EQIEKAAQMAYAMDFINKMdngldtvigengvlLSGGQRQRIAIARA 494
Cdd:PRK11000 82 QSYALYpHLSVAENMSFglklagaKKEEINQRvNQVAEVLQLAHLLDRKPKA--------------LSGGQRQRVAIGRT 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK11000 148 LVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-554 |
4.21e-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: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGqILMDGHDLReytlaslrdqVAL 421
Cdd:cd03221 1 IELENLSKTYGGK--LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQnvhlfndtvanniayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPI 501
Cdd:cd03221 68 FEQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 740854059 502 LILDEATSALDTESERAIQAALDELQknRTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-567 |
4.97e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 4.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLI--TRFYDIDEGQIL------------------ 401
Cdd:TIGR03269 1 IEVKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 402 ---------------MDGHDLREYTLASLRDQVALVSQNVHLF--NDTVANNIAYARTDL-YS-REQIEKAAQMAYAMDF 462
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIgYEgKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 463 INKMdngldTVIGENgvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVI-AHRLS 540
Cdd:TIGR03269 159 SHRI-----THIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgISMVLtSHWPE 230
|
250 260
....*....|....*....|....*...
gi 740854059 541 TIEQ-ADEIIVVEDGVIVERGTHNELIE 567
Cdd:TIGR03269 231 VIEDlSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
342-558 |
5.69e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.33 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVAL 421
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFndtvanniayarTDLYSREQIEKAAQMAYAMDFINKMDNGLDTvigENGVL----LSGGQRQRIAIARALLR 497
Cdd:PRK10522 402 VFTDFHLF------------DQLLGPEGKPANPALVEKWLERLKMAHKLEL---EDGRIsnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 498 DSPILILDEATSALDTESERAI-QAALDELQ-KNRTSLVIAHRLSTIEQADEIIVVEDGVIVE 558
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-567 |
6.38e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.98 E-value: 6.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlREYTLASLRD-QVA 420
Cdd:PRK10762 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSsQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVS---QNVHLF-NDTVANNIAYAR--TDLYSREQIEKAAQMAYAMDFINKMDNGLDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:PRK10762 80 GIGiihQELNLIpQLTIAENIFLGRefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 495 LLRDSPILILDEATSAL-DTESErAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIIVVEDG-VIVERG----THNELI 566
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGqFIAEREvadlTEDSLI 234
|
.
gi 740854059 567 E 567
Cdd:PRK10762 235 E 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-568 |
6.39e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL-REYTLAslRDQVA 420
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVpARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANN-IAYARTDLYSREQIEkaAQMAYAMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENlLVFGRYFGMSTREIE--AVIPSLLEFA-RLESKADARVSD----LSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 499 SPILILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
342-568 |
9.17e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.82 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--------------------ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQIL 401
Cdd:COG1134 5 IEVENVSKSYRLYHEPsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 402 MDGhdlreyTLASLrdqVAL---------VSQNVHLfndtvanniaYARtdLY--SREQIEKaaqmayAMDFI------- 463
Cdd:COG1134 85 VNG------RVSAL---LELgagfhpeltGRENIYL----------NGR--LLglSRKEIDE------KFDEIvefaelg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 464 NKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTE-SERAiQAALDELQKNRTSLVIA-HRLST 541
Cdd:COG1134 138 DFIDQPVKT--------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKC-LARIRELRESGRTVIFVsHSMGA 208
|
250 260
....*....|....*....|....*...
gi 740854059 542 IEQ-ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG1134 209 VRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
355-560 |
1.11e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHL-FNDTV 433
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYARTDLYSR---------EQIEKAAQMAYAMDFInkmDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK09536 95 RQVVEMGRTPHRSRfdtwtetdrAAVERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 740854059 505 DEATSALDTESE-RAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:PRK09536 164 DEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-538 |
1.33e-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: 80.28 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILM-DGHDL-----REY-TLAS 414
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLlflpqRPYlPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQNVhlfndtvanniayartdlysreqiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARA 494
Cdd:cd03223 80 LREQLIYPWDDV------------------------------------------------------LSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDELqknRTSLV-IAHR 538
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHR 147
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
342-571 |
1.50e-17 |
|
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: 82.21 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTL-ASLRDQVA 420
Cdd:cd03218 1 LRAENLSKRYGKR--KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNI--AYARTDLYSREQIEKAAQMAYamDFinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03218 79 YLPQEASIFRKlTVEENIlaVLEIRGLSKKEREEKLEELLE--EF------HITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIIVVEDGVIVERGTHNELIEQRGV 571
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-568 |
1.72e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.24 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGRE---APALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI----LMDGHDLREYTLAS 414
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTDL-YSREQIEKAAqmAYAMDFInkmdnGLDTVIGENGVL-LSGGQRQRIA 490
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFgIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPFeLSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQE 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
342-557 |
2.06e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.55 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVT--FTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLIT---RFYDIDEGQILMDGHDLREYTLaslR 416
Cdd:cd03234 4 LPWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQF---Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 DQVALVSQ-NVHLFNDTVANNIAYARTDLYSREQIEKAAQMayaMDFINKMDNGLDTVIGENGVL-LSGGQRQRIAIARA 494
Cdd:cd03234 81 KCVAYVRQdDILLPGLTVRETLTYTAILRLPRKSSDAIRKK---RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIIVVEDGVIV 557
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-565 |
2.35e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.14 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 347 VTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRF-------YDidEGQILMDGHDL---REYTLASLR 416
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLlhaSEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 417 -DQVAL------VSQN-VHLFNDTVANNIAY--------ARTDLYS---REQIEKAAQMAyaMDFINKmdngldtvigen 477
Cdd:PRK15134 91 gNKIAMifqepmVSLNpLHTLEKQLYEVLSLhrgmrreaARGEILNcldRVGIRQAAKRL--TDYPHQ------------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 gvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:PRK15134 157 ---LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
250
....*....|.
gi 740854059 555 VIVERGTHNEL 565
Cdd:PRK15134 234 RCVEQNRAATL 244
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
66-309 |
3.03e-17 |
|
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: 82.52 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 66 WMPLVVIGL---MIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYdSEQVASSSSGA 142
Cdd:cd18569 40 WLRPLLLGMaltALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQS-NDRVANLLSGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 143 LITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQ---VTTSAEQMLkghkEVLI 219
Cdd:cd18569 119 LATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKltgTTMSGLQMI----ETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 220 FGGQEVETkrFDKVSN---KMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVME-NLTAGTItVVFSS-MIAL 294
Cdd:cd18569 195 ASGAESDF--FSRWAGyqaKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGL-LVMDgALTIGML-VAFQSlMASF 270
|
250
....*....|....*
gi 740854059 295 MRPLKSLTNVNAQFQ 309
Cdd:cd18569 271 LAPVNSLVGLGGTLQ 285
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-565 |
4.46e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 4.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGQILMDGHDL--REYTLAS 414
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQNVHLFNDTVANNIAYARTDLYSREQIEKAAQMAYAMDFINKMDNgLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDE-IKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 495 LLRDSPILILDEATSALDTESERAIQAALD--ELQKNRTSLVIAHRLSTIEQADEIIVV------EDGVIVERGTHNEL 565
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFfkgnenRIGQLVEFGLTKKI 243
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-558 |
4.81e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 84.07 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGQILMDGhDLREYtlASLRD-- 417
Cdd:NF040905 2 LEMRGITKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG-EVCRF--KDIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 ---------QVALVSQ-----NVHLFNDTVANN-IAYARTDLYSREQIEKAaqmayamdfinkmdnGL----DTVIGENG 478
Cdd:NF040905 77 algiviihqELALIPYlsiaeNIFLGNERAKRGvIDWNETNRRARELLAKV---------------GLdespDTLVTDIG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 479 VllsgGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:NF040905 142 V----GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRT 217
|
..
gi 740854059 557 VE 558
Cdd:NF040905 218 IE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-564 |
5.72e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY-PGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRD 417
Cdd:PRK10908 2 IRFEHVSKAYlGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQNVHLFND-TVANNIAYARTDL-YSREQIEKaaQMAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAIARAL 495
Cdd:PRK10908 80 QIGMIFQDHHLLMDrTVYDNVAIPLIIAgASGDDIRR--RVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 496 LRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTIEQAD-EIIVVEDGVIVErGTHNE 564
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-565 |
9.06e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.42 E-value: 9.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLAslRDQVALVSQNVHLFND-TV 433
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQIA--RMGVVRTFQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYA--------------RTDLYSREQIEKAAQMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-560 |
1.03e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 79.68 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 333 RVIERATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTL 412
Cdd:cd03267 11 RVYSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 413 ASLRDQVALVSQNVHLFNDTVANNIAYARTDLYS------REQIEKAAQMayamdfinkMDNG--LDTVIGEngvlLSGG 484
Cdd:cd03267 91 KFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDlpparfKKRLDELSEL---------LDLEelLDTPVRQ----LSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-561 |
1.08e-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: 84.29 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 357 PALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLrEYTLASLRDQVALVSQNVHLFND-TVAN 435
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 436 NIAYaRTDLYSREQIEKAAQMAYAMDfinkmDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:TIGR01257 1023 HILF-YAQLKGRSWEEAQLEMEAMLE-----DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740854059 516 ERAIQAALDELQKNRTSLVIAHRLSTIE-QADEIIVVEDGVIVERGT 561
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
45-309 |
1.26e-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: 80.63 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 45 LSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQ 119
Cdd:cd18555 17 LTLLIPILtqyviDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 120 STGTLLSRITyDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLApIVSVAIRVVSKRfRSISKNMQNT 199
Cdd:cd18555 97 SSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRK-KIKKLNQEEI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 200 MGQVTTSAEQ--MLKGHKEVLIFGgqeVETKRFDKVSNKMrlqgMKMVSA-------SSISDPIIQLIASLALAFVLYAA 270
Cdd:cd18555 174 VAQTKVQSYLteTLYGIETIKSLG---SEKNIYKKWENLF----KKQLKAfkkkerlSNILNSISSSIQFIAPLLILWIG 246
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 740854059 271 SFPSVMENLTAGTItVVFSSM-IALMRPLKSLTNVNAQFQ 309
Cdd:cd18555 247 AYLVINGELTLGEL-IAFSSLaGSFLTPIVSLINSYNQFI 285
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
60-309 |
1.48e-16 |
|
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: 80.30 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 60 DRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSS 139
Cdd:cd18568 37 NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 140 SGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLI 219
Cdd:cd18568 116 TRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 220 FGgqeVETKRFDKVSNKM------RLQGMKMVSASSIsdpIIQLIASLALAFVL-YAASFpsVM-ENLTAGTItVVFSSM 291
Cdd:cd18568 196 LA---AERPIRWRWENKFakalntRFRGQKLSIVLQL---ISSLINHLGTIAVLwYGAYL--VIsGQLTIGQL-VAFNML 266
|
250
....*....|....*....
gi 740854059 292 IA-LMRPLKSLTNVNAQFQ 309
Cdd:cd18568 267 FGsVINPLLALVGLWDELQ 285
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
358-569 |
2.37e-16 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTI----ASLITRfYDIDEGQILMDGHDL-REYTLA----SLRDQVALVSQNVHL 428
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITG-DKSAGSHIELLGRTVqREGRLArdirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 429 FND-TVANNI--------AYARTDL--YSREQIEKAAQMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLR 497
Cdd:PRK09984 98 VNRlSVLENVligalgstPFWRTCFswFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQR 569
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
359-557 |
4.14e-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: 77.89 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLrdqvaLVSQNVHLFN-DTVANNI 437
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 438 AYA-RTDLYSREQIEKAAQMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
Cdd:TIGR01184 76 ALAvDRVLPDLSKSERRAIVEEHIALVG-LTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740854059 517 RAIQAALDEL-QKNR-TSLVIAHRLstieqaDEIIVVEDGVIV 557
Cdd:TIGR01184 151 GNLQEELMQIwEEHRvTVLMVTHDV------DEALLLSDRVVM 187
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-554 |
6.13e-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: 75.93 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFtypgreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQ-VA 420
Cdd:cd03215 5 LEVRGLSV------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVH---LFND-TVANNIAyartdlysreqiekaaqmayamdfinkmdngldtvigeNGVLLSGGQRQRIAIARALL 496
Cdd:cd03215 79 YVPEDRKregLVLDlSVAENIA--------------------------------------LSSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
336-557 |
6.18e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.45 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 336 ERATGD--LEFRNVTFtypgreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhdlREYTLA 413
Cdd:COG1129 249 AAAPGEvvLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQ----VALVSQNVH---LF-NDTVANNIAYARTDLYSREQ-IEKAAQMAYAMDFINKMD---NGLDTVIGEngvlL 481
Cdd:COG1129 320 SPRDAiragIAYVPEDRKgegLVlDLSIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLRiktPSPEQPVGN----L 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhrlST-----IEQADEIIVVEDGVI 556
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRI 472
|
.
gi 740854059 557 V 557
Cdd:COG1129 473 V 473
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
359-554 |
7.80e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.16 E-value: 7.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTL---ASLRDQ-VALVSQNVHLFND-TV 433
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPDfTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYART--DLYSREQIEKAAQMAYAMdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSAL 511
Cdd:PRK11629 105 LENVAMPLLigKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740854059 512 DTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIIVVEDG 554
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
354-560 |
1.14e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.42 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 354 REAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlreytlaslrdqVALVSQNVHLFND-T 432
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------------SSLLGLGGGFNPElT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNIaYARTDLY--SREQIEKaaqmayAMDFI---NKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:cd03220 101 GRENI-YLNGRLLglSRKEIDE------KIDEIiefSELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 508 TSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
359-560 |
1.29e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 80.54 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKST----IASLITRFYDIDEGQILMDGHDLREYtLASLRDQVALVSQN-VHLFNDTV 433
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETdVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYA--------RTDLYSREqiEKAAQMA-YAMDfINKMDNGLDTVIGEN---GVllSGGQRQRIAIARALLRDSPI 501
Cdd:TIGR00956 156 GETLDFAarcktpqnRPDGVSRE--EYAKHIAdVYMA-TYGLSHTRNTKVGNDfvrGV--SGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 502 LILDEATSALDT----ESERAIQAALDELqkNRTSLVIAHRLS--TIEQADEIIVVEDGVIVERG 560
Cdd:TIGR00956 231 QCWDNATRGLDSatalEFIRALKTSANIL--DTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFG 293
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-571 |
1.47e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.97 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 338 ATGDLEFRNvtftypgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH--DLREYTLASL 415
Cdd:PRK13638 3 ATSDLWFRY-------QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 RDQVALVSQN--VHLFNDTVANNIAYARTDLYSREQiekaaqmayamDFINKMDNGLdTVIGENGV------LLSGGQRQ 487
Cdd:PRK13638 76 RQQVATVFQDpeQQIFYTDIDSDIAFSLRNLGVPEA-----------EITRRVDEAL-TLVDAQHFrhqpiqCLSHGQKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVERG----- 560
Cdd:PRK13638 144 RVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgev 223
|
250
....*....|..
gi 740854059 561 -THNELIEQRGV 571
Cdd:PRK13638 224 fACTEAMEQAGL 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-567 |
1.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.42 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID-----EGQILMDGHDL--REYTLAS 414
Cdd:PRK14267 5 IETVNLRVYYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRDQVALVSQNVHLFN-----DTVA-----NNIAYARTDLysREQIEKAAQMAYAMDfinKMDNGLDTVIGEngvlLSGG 484
Cdd:PRK14267 83 VRREVGMVFQYPNPFPhltiyDNVAigvklNGLVKSKKEL--DERVEWALKKAALWD---EVKDRLNDYPSN----LSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHN 563
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTR 233
|
....
gi 740854059 564 ELIE 567
Cdd:PRK14267 234 KVFE 237
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
76-232 |
1.68e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 77.35 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 76 IVRGLTSYVSSYCISWVSGKVVMTM-------RRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVR 148
Cdd:cd18784 40 IIMGLLAIASSVAAGIRGGLFTLAMarlniriRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 149 EGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
Cdd:cd18784 120 SLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEAN 199
|
....
gi 740854059 229 RFDK 232
Cdd:cd18784 200 RYSE 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
342-545 |
2.12e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.28 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHdlreyTLASLRDQVAL 421
Cdd:PRK11248 2 LQISHLYADYGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLFN-DTVANNIAYArtdlYSREQIEKAAQMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:PRK11248 75 VFQNEGLLPwRNVQDNVAFG----LQLAGVEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740854059 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQA 545
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKLwqETGKQVLLITH---DIEEA 192
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-554 |
3.06e-15 |
|
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: 78.33 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGQILMDGHDLREytlASLRDQ- 418
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKA---SNIRDTe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 ---VALVSQNVHLFND-TVANNIayartdLYSREQIEKAAQMAYAMDFIN--------KMDNGLDT-VIGENGvllsGGQ 485
Cdd:TIGR02633 77 ragIVIIHQELTLVPElSVAENI------FLGNEITLPGGRMAYNAMYLRaknllrelQLDADNVTrPVGDYG----GGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDG 554
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
339-567 |
3.34e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.77 E-value: 3.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 339 TGDLEFRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASlRDQ 418
Cdd:PRK13537 5 VAPIDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI-AYARTDLYSREQIEKAAQMAyaMDFInKMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
Cdd:PRK13537 82 VGVVPQFDNLDPDfTVRENLlVFGRYFGLSAAAARALVPPL--LEFA-KLENKADAKVGE----LSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIE 567
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
34-314 |
3.92e-15 |
|
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: 76.16 E-value: 3.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 34 LILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPV 113
Cdd:cd18561 5 GLLITALYIAQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 114 SFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSIS 193
Cdd:cd18561 85 GYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 194 KNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFP 273
Cdd:cd18561 165 RRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 740854059 274 SVMENLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18561 245 VLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
342-567 |
4.06e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 4.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYP---------GREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGH---DLRE 409
Cdd:PRK10261 314 LQVRNLVTRFPlrsgllnrvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSP 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 410 YTLASLRDQVALVSQNVHLFND---TVANNI--------------AYARTD-LYSREQIEKAAQMAYAMDFinkmdngld 471
Cdd:PRK10261 394 GKLQALRRDIQFIFQDPYASLDprqTVGDSImeplrvhgllpgkaAAARVAwLLERVGLLPEHAWRYPHEF--------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 472 tvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEI 548
Cdd:PRK10261 465 ----------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRV 534
|
250
....*....|....*....
gi 740854059 549 IVVEDGVIVERGTHNELIE 567
Cdd:PRK10261 535 AVMYLGQIVEIGPRRAVFE 553
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
342-566 |
9.00e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 9.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGR-------EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLrEYTLAS 414
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRdqvalvSQNVHL-FNDtvanniayARTDLYSREQIEKAaqmayaMDFINKMDNGLDTVIGENGV-------------- 479
Cdd:PRK15112 84 YR------SQRIRMiFQD--------PSTSLNPRQRISQI------LDFPLRLNTDLEPEQREKQIietlrqvgllpdha 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 -----LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVV 551
Cdd:PRK15112 144 syyphMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVM 223
|
250
....*....|....*
gi 740854059 552 EDGVIVERGTHNELI 566
Cdd:PRK15112 224 HQGEVVERGSTADVL 238
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
346-568 |
1.06e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 75.53 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIA----SLITRFYDIdEGQILMDGHD---LREYTLASLR-D 417
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAANGRI-GGSATFNGREilnLPEKELNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVsqnvhlFNDTVANNIAYAR--TDLYSREQIEKAAQMAYAMDFINKMdngLDTV--------IGENGVLLSGGQRQ 487
Cdd:PRK09473 98 QISMI------FQDPMTSLNPYMRvgEQLMEVLMLHKGMSKAEAFEESVRM---LDAVkmpearkrMKMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNE 564
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248
|
....
gi 740854059 565 LIEQ 568
Cdd:PRK09473 249 VFYQ 252
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-565 |
1.11e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDI-----DEGQILMDGHDLREY-TLASLRDQV 419
Cdd:PRK14271 26 NLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 ALVSQNVHLFNDTVANNI-AYART-DLYSREQIEKAAQMAyaMDFINKMDNGLDTvIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNVlAGVRAhKLVPRKEFRGVAQAR--LTEVGLWDAVKDR-LSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
368-580 |
3.75e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 72.27 E-value: 3.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 368 AGKTVALVGRSGSGKST----IASLITrfydiDEGQILMDGHDLREYTLASLRDQVALVSQNVH-LFNDTVANNIAYART 442
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVFQYLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 443 DLYSREQIEKA-AQMAYAMdfinKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSP-------ILILDEATSALDTe 514
Cdd:PRK03695 96 DKTRTEAVASAlNEVAEAL----GLDDKLGRSVNQ----LSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNSLDV- 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 515 serAIQAALDEL-----QKNRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGTHNELIEQRGVyAQLHKMQF 580
Cdd:PRK03695 167 ---AQQAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFGVNF 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
359-567 |
4.90e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.08 E-value: 4.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKST----IASLITRFYDIDeGQILMDGH--DLREYTLASlrdqvALVSQnVHLFNDT 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnaLAFRSPKGVKGS-GSVLLNGMpiDAKEMRAIS-----AYVQQ-DDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VAnniayARTDLY------SREQIEKAAQMAYAMDFINKMdnGL----DTVIGENGVL--LSGGQRQRIAIARALLRDSP 500
Cdd:TIGR00955 114 LT-----VREHLMfqahlrMPRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIIVVEDGVIVERGTHNELIE 567
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
347-560 |
5.19e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 5.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 347 VTFTYPGREApALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLrdqVALVSQNV 426
Cdd:PRK15056 12 VTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 427 H-------LFNDTVANNiAYARTDLYSREQIEKAAQMAYAMDFINkMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDS 499
Cdd:PRK15056 88 EvdwsfpvLVEDVVMMG-RYGHMGWLRRAKKRDRQIVTAALARVD-MVEFRHRQIGE----LSGGQKKRVFLARAIAQQG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 500 PILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEIIVVEDGVIVERG 560
Cdd:PRK15056 162 QVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-560 |
5.30e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.82 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLA-SLRDQVA 420
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNIAYARTDLYS---------REQIEKAAQMAYAMDFinKMDngLDTVIGEngvlLSGGQRQRIA 490
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGL--KVD--LDEKVAN----LSISHKQMLE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740854059 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
72-279 |
6.16e-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: 72.50 E-value: 6.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 72 IGLMIVRGLTSYVSS------YCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT 145
Cdd:cd18589 39 ITVMSLLTIASAVSEfvcdliYNIT--MSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 146 VVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEV 225
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 226 ETKRF-DKVSNKMRLQGMKMVS------ASSISDPII---------QLIASLAL------AFVLYAASFPSVMENL 279
Cdd:cd18589 197 EAQRYrQRLQKTYRLNKKEAAAyavsmwTSSFSGLALkvgilyyggQLVTAGTVssgdlvTFVLYELQFTSAVEVL 272
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
342-565 |
6.39e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.11 E-value: 6.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD---LREYTLASLRDQ 418
Cdd:PRK11831 8 VDMRGVSFTRGNR--CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNIAYARtdlysREQIEKAAQMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK11831 86 MSMLFQSGALFTDmNVFDNVAYPL-----REHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK11831 161 EPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVpEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-561 |
1.49e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT--LASLRDQVALVS 423
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQSAAQM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVH------LFND---------TVANNIAYA---RTDLYSREQIEKAAQMayaMDFINKMDNglDTVIGENGVLLSGGQ 485
Cdd:PRK10261 99 RHVRgadmamIFQEpmtslnpvfTVGEQIAESirlHQGASREEAMVEAKRM---LDQVRIPEA--QTILSRYPHQLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLV--IAHRLSTI-EQADEIIVVEDGVIVERGT 561
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVaEIADRVLVMYQGEAVETGS 252
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
342-571 |
1.73e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTL-ASLRDQVA 420
Cdd:PRK10895 4 LTAKNLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNIAYA---RTDLYSREQIEKAAQMAYAMDFINKMDNgldtvIGENgvlLSGGQRQRIAIARALL 496
Cdd:PRK10895 82 YLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDS-----MGQS---LSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRL-STIEQADEIIVVEDGVIVERGTHNELIEQRGV 571
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-536 |
2.87e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDlreYTLASLRDQVAL 421
Cdd:PRK13539 3 LEGEDLACVRGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VS-QNVHLFNDTVANNIAYARtDLYSREQIEKAAqmayAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
Cdd:PRK13539 78 LGhRNAMKPALTVAENLEFWA-AFLGGEELDIAA----ALEAV-----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRP 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 740854059 501 ILILDEATSALDTESERAIqAALDELQKNRTSLVIA 536
Cdd:PRK13539 148 IWILDEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-571 |
3.03e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPgrEAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLAS-LRDQVA 420
Cdd:PRK11614 6 LSFDKVSAHYG--KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNVHLFND-TVANNIAYARTdLYSREQIEKAAQMAYAMdfinkMDNGLDTVIGENGVlLSGGQRQRIAIARALLRDS 499
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAMGGF-FAERDQFQERIKWVYEL-----FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 500 PILILDEATSALdteSERAIQAALDELQKNRTS-----LVIAHRLSTIEQADEIIVVEDGVIVERGTHNELIEQRGV 571
Cdd:PRK11614 157 RLLLLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
355-561 |
3.38e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.67 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRF--YDIDEGQILMDGHDLREYTlASLRDQVALVSQNVHLFNDT 432
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNIAYARTDLYSREQIEKAAQMAyAMDFINKMDNGLDtVIGENGVLL--------SGGQRQRIAIARALLRDSPILIL 504
Cdd:CHL00131 98 GVSNADFLRLAYNSKRKFQGLPELD-PLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 505 DEATSALDTESERAIQAALDELQKNRTSLV-IAH--RLSTIEQADEIIVVEDGVIVERGT 561
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
336-557 |
3.59e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.98 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 336 ERATGD--LEFRNVTFTyPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLA 413
Cdd:COG3845 250 PAEPGEvvLEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQ-VALVSQNVH---LFND-TVANNIA--------YARTDLYSREQIEKAAQmayamDFINKMD---NGLDTVIGen 477
Cdd:COG3845 329 ERRRLgVAYIPEDRLgrgLVPDmSVAENLIlgryrrppFSRGGFLDRKAIRAFAE-----ELIEEFDvrtPGPDTPAR-- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 478 gvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EQADEIIVVEDGV 555
Cdd:COG3845 402 --SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAvLLISEDLDEIlALSDRIAVMYEGR 479
|
..
gi 740854059 556 IV 557
Cdd:COG3845 480 IV 481
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
361-560 |
3.63e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.06 E-value: 3.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 361 NINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDL----REYTLASLRDQVALVSQNVHLF-NDTVAN 435
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 436 NIAY--ARTDlysREQIEKAAQMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDT 513
Cdd:PRK11144 96 NLRYgmAKSM---VAQFDKIVALL-----------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740854059 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERG 560
Cdd:PRK11144 162 PRKRELLPYLERLAReiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFG 211
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
72-238 |
3.95e-13 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 70.06 E-value: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 72 IGLMIVRGLTSYVSSYC----ISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVV 147
Cdd:cd18590 39 IGLMCLFSLGSSLSAGLrgglFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 148 REGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVET 227
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEA 198
|
170
....*....|.
gi 740854059 228 KRFDKVSNKMR 238
Cdd:cd18590 199 CRYSEALERTY 209
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-560 |
7.06e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 7.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGR---EAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI---LMDGHDLREYTLAS- 414
Cdd:PRK13651 3 IKVKNIVKIFNKKlptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 --------------------LRDQVALVSQ--NVHLFNDTVANNIAY-ARTDLYSREQIEKAAQmayamDFINKMdnGLD 471
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFgPVSMGVSKEEAKKRAA-----KYIELV--GLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 472 -TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL-STIEQADEI 548
Cdd:PRK13651 156 eSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|..
gi 740854059 549 IVVEDGVIVERG 560
Cdd:PRK13651 236 IFFKDGKIIKDG 247
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
342-525 |
8.11e-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: 67.38 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT------LASL 415
Cdd:TIGR01189 1 LAARNLACSRGER--MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdephenILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 RDQVAL-----VSQNVHLFND---TVANNI--AYARTDLYSREQIeKAAQmayamdfinkmdngldtvigengvlLSGGQ 485
Cdd:TIGR01189 79 GHLPGLkpelsALENLHFWAAihgGAQRTIedALAAVGLTGFEDL-PAAQ-------------------------LSAGQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE 525
Cdd:TIGR01189 133 QRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-546 |
8.37e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 8.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREyTLASLRDQVAL 421
Cdd:PRK13540 2 LDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVHLF-NDTVANNIAYartDLYSREQIEKAAQMAYamdfINKMDNGLDTVIGengvLLSGGQRQRIAIARALLRDSP 500
Cdd:PRK13540 79 VGHRSGINpYLTLRENCLY---DIHFSPGAVGITELCR----LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 740854059 501 ILILDEATSALDtesERAIQAALDELQKNRTS----LVIAHRLSTIEQAD 546
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHRAKggavLLTSHQDLPLNKAD 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
363-555 |
1.38e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 70.20 E-value: 1.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 363 NLNIP-AGKTVALVGRSGSGKSTIAS-----LITRFYDIDEG----QIL--MDGHDLREYtLASLRDQ---VALVSQNVH 427
Cdd:COG1245 92 GLPVPkKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrFRGTELQDY-FKKLANGeikVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 428 L----FNDTVanniayartdlysREQIEKAAQMAYAMDFINK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPI 501
Cdd:COG1245 171 LipkvFKGTV-------------RELLEKVDERGKLDELAEKlgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 502 LILDEATSALD----TESERAIQaalDELQKNRTSLVIAHRLSTIEQ-ADEIIVV--EDGV 555
Cdd:COG1245 234 YFFDEPSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAILDYlADYVHILygEPGV 291
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-576 |
4.23e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 354 REAPALRNINLNIPAGKTVALVGRSGSGKST----IASLITRfydiDEGQILMDGHD--LREYTLASlrdQVALV----S 423
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVpfKRRKEFAR---RIGVVfgqrS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QnvhLFND-TVANNIAYARtDLYsreQIEKAaqmayamDFINKMDNgLDTVIGENGVL------LSGGQRQRIAIARALL 496
Cdd:COG4586 106 Q---LWWDlPAIDSFRLLK-AIY---RIPDA-------EYKKRLDE-LVELLDLGELLdtpvrqLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQRGVYA 573
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 740854059 574 QLH 576
Cdd:COG4586 251 TIV 253
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
72-314 |
9.11e-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: 66.03 E-value: 9.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 72 IGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASS-----SSGalitv 146
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSfkqcvSQG----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 147 VREGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVE 226
Cdd:cd18574 124 LRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 227 TKRFDKVSNKMRlqgmKMVSASSISDPIIQLIASLALA----FVLYAASFPSVMENLTAGTITvvfSSMIALMRPLKSLT 302
Cdd:cd18574 204 LELYEEEVEKAA----KLNEKLGLGIGIFQGLSNLALNgivlGVLYYGGSLVSRGELTAGDLM---SFLVATQTIQRSLA 276
|
250
....*....|....*
gi 740854059 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 |
1.30e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 63.82 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 344 FRNVTFTYPGR--EAPALRNINLNIPAGKTVALVGRSGSGKST----IASLITRFYDIdEGQILMDGHDLREyTLASLRD 417
Cdd:cd03233 6 WRNISFTTGKGrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE-FAEKYPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQN-VHLFNDTVanniayartdlysREQIEKAAQMayamdfinkmdNGLDTVIGengvlLSGGQRQRIAIARALL 496
Cdd:cd03233 84 EIIYVSEEdVHFPTLTV-------------RETLDFALRC-----------KGNEFVRG-----ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 497 RDSPILILDEATSALDTESeraiqaALDELQKNRTslvIAH--RLSTI-----------EQADEIIVVEDGVIV 557
Cdd:cd03233 135 SRASVLCWDNSTRGLDSST------ALEILKCIRT---MADvlKTTTFvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
345-554 |
1.40e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.06 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR-EYTLASLRDQVALVS 423
Cdd:PRK10982 2 SNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVHLFND-TVANNIAYARtdlYSREQIEKAAQMAYAmDFINKMDN-GLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
Cdd:PRK10982 80 QELNLVLQrSVMDNMWLGR---YPTKGMFVDQDKMYR-DTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 502 LILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIIVVEDG 554
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDG 210
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-190 |
1.48e-11 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 65.62 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 69 LVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSSSGALITVVR 148
Cdd:cd18783 46 IGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 740854059 149 EGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFR 190
Cdd:cd18783 125 DATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFR 166
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
358-565 |
1.86e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 65.53 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKS----TIASLITRFYDIDEGQILMDGHDLREYTLASLRDqvaLVSQNVHL-FND- 431
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRN---LVGAEVAMiFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 --------TVANNIAYArtdLYSREQIEKAAQMAYAMDFINKM-----DNGLDTVIGEngvlLSGGQRQRIAIARALLRD 498
Cdd:PRK11022 99 mtslnpcyTVGFQIMEA---IKVHQGGNKKTRRQRAIDLLNQVgipdpASRLDVYPHQ----LSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIIVVEDGVIVERGTHNEL 565
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
2.10e-11 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 64.56 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTI------ASLITRFYdidEGQILMDGHDlREYTLASLrDQVALVSQNvhLFNDT 432
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlyPALARRLH---LKKEQPGNHD-RIEGLEHI-DKVIVIDQS--PIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNIA-YAR--TDL------------YSREQIE---KAAQMAYAMD---------FINK----------MDNGLDTV-I 474
Cdd:cd03271 84 PRSNPAtYTGvfDEIrelfcevckgkrYNRETLEvryKGKSIADVLDmtveealefFENIpkiarklqtlCDVGLGYIkL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 475 GENGVLLSGGQRQRIAIARALLRDSP---ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEII 549
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWII 242
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
369-559 |
2.57e-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: 62.01 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 369 GKTVALVGRSGSGKSTIASLITRFYDIDEGQILM-DGHDLREYTLASLRDqvalvsqnvhlfndtvanniayartdlysr 447
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 448 eqiekaaqmayamdfinkmdngldTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALD--- 524
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 740854059 525 ---ELQKNRTSLVIAHRLSTIEQADEIIVVEDGVIVER 559
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
362-523 |
3.91e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.51 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 362 INLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYAR 441
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 442 tDLYSREQIEKAaqmayamdfinkmdngLDTViGENGV------LLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:cd03231 99 -ADHSDEQVEEA----------------LARV-GLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 740854059 516 ERAIQAAL 523
Cdd:cd03231 161 VARFAEAM 168
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
342-506 |
9.09e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 62.35 E-value: 9.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTL---AslRDQ 418
Cdd:COG1137 4 LEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrA--RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 VALVSQNVHLFND-TVANNI-AYARTDLYSREQIEKaaqmayamdfinKMDN-----GLDTVIGENGVLLSGGQRQRIAI 491
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNIlAVLELRKLSKKEREE------------RLEElleefGITHLRKSKAYSLSGGERRRVEI 147
|
170
....*....|....*
gi 740854059 492 ARALLRDSPILILDE 506
Cdd:COG1137 148 ARALATNPKFILLDE 162
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
70-310 |
9.47e-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: 62.90 E-value: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 70 VVIGLMIV---RGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITV 146
Cdd:cd18588 44 LAIGLLVValfEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 147 VREGASIIGLFIMMFYYSWQLSLILIVLAP---IVSVAI-----RVVSKRFRSISKNmQNTMGQvTTSAEQMLKGHkevl 218
Cdd:cd18588 123 VLDLVFSVVFLAVMFYYSPTLTLIVLASLPlyaLLSLLVtpilrRRLEEKFQRGAEN-QSFLVE-TVTGIETVKSL---- 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 219 ifggqEVE---TKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVMEN-LTAGTItVVFsSMIA- 293
Cdd:cd18588 197 -----AVEpqfQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAY-LVMDGeLTIGQL-IAF-NMLAg 268
|
250
....*....|....*...
gi 740854059 294 -LMRPLKSLTNVNAQFQR 310
Cdd:cd18588 269 qVSQPVLRLVQLWQDFQQ 286
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-552 |
1.03e-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: 62.04 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 365 NIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR---EYTLAslrDQVALVSQNVHLFNDTVANNiAYAR 441
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKA---DYEGTVRDLLSSITKDFYTH-PYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 442 TDLYSREQIEKAaqmayamdfinkMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----R 517
Cdd:cd03237 97 TEIAKPLQIEQI------------LDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasK 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 740854059 518 AIQAALDELQKnrTSLVIAHRLSTIEQ-ADEIIVVE 552
Cdd:cd03237 157 VIRRFAENNEK--TAFVVEHDIIMIDYlADRLIVFE 190
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
359-535 |
1.45e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLR---EYTLASLRDQ-VALVSQNVHLFNDTVA 434
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 435 -NNI---AYAR--TDLYSREQ-IEKAAQMayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:PRK10584 106 lENVelpALLRgeSSRQSRNGaKALLEQL------------GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180
....*....|....*....|....*...
gi 740854059 508 TSALDTESERAIQAALDELQKNRTSLVI 535
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
363-551 |
1.87e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 363 NLNIP-AGKTVALVGRSGSGKSTIAS-----LITRFYDIDEG----QIL--MDGHDLREYtLASLRDQ---VALVSQNVH 427
Cdd:PRK13409 92 GLPIPkEGKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEEpswdEVLkrFRGTELQNY-FKKLYNGeikVVHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 428 L----FNDTVanniayartdlysREQIEKAAQMAYAMDFINK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPI 501
Cdd:PRK13409 171 LipkvFKGKV-------------RELLKKVDERGKLDEVVERlgLENILDRDISE----LSGGELQRVAIAAALLRDADF 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 502 LILDEATSALD----TESERAIQaaldELQKNRTSLVIAHRLSTIEQ-ADEIIVV 551
Cdd:PRK13409 234 YFFDEPTSYLDirqrLNVARLIR----ELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
246-568 |
2.82e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 246 SASSISDPIIQLIASLALAFVLyAASFPSVMENLTAGTITVVFSSMIALMRPLKsltnVNAQFQRGMaacqtlftildSE 325
Cdd:TIGR03269 203 TAKLVHNALEEAVKASGISMVL-TSHWPEVIEDLSDKAIWLENGEIKEEGTPDE----VVAVFMEGV-----------SE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 326 QEKDegkRVIERATGDLEFRNVTFTYPGRE---APALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQI-- 400
Cdd:TIGR03269 267 VEKE---CEVEVGEPIIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnv 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 401 -----LMDGHDLREYTLASLRDQVALVSQNVHLF-NDTVANNIayarTDLYSREQIEKAAQMA-------------YAMD 461
Cdd:TIGR03269 344 rvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMKavitlkmvgfdeeKAEE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 462 FINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSPILILDEATSALDTESERA----IQAALDELqkNRTSLVIAH 537
Cdd:TIGR03269 420 ILDKYPDEL-----------SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEM--EQTFIIVSH 486
|
330 340 350
....*....|....*....|....*....|..
gi 740854059 538 RLSTI-EQADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:TIGR03269 487 DMDFVlDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
359-561 |
3.20e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTI---------ASLITRFYDIdEGQILMDGHDLREY---TLASLRDQVALVSQNV 426
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARV-TGDVTLNGEPLAAIdapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 427 HLFNdtvANNIA------YAR----TDLYSREQIEKAAQMAyamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARAL- 495
Cdd:PRK13547 96 FAFS---AREIVllgrypHARragaLTHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 496 --------LRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIIVVEDGVIVERGT 561
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
350-549 |
5.00e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.87 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 350 TYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLItrFYDIDEGQiLMDGHDLREYTLASLRDQVALVsqnvhlf 429
Cdd:cd03238 2 TVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKAR-LISFLPKFSRNKLIFIDQLQFL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 430 ndtVANNIAYARtdlysreqiekaaqmayamdfinkmdngldtvIGENGVLLSGGQRQRIAIARALLRDSP--ILILDEA 507
Cdd:cd03238 72 ---IDVGLGYLT--------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 740854059 508 TSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEII 549
Cdd:cd03238 117 STGLHQQDINQLLEVIKGLiDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
364-555 |
5.00e-10 |
|
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: 60.46 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 364 LNIPA-GKTVALVGRSGSGKSTIASLIT--------RFYDIDEGQILMD---GHDLREYTLASLRDQVALV--SQNVHLF 429
Cdd:cd03236 20 LPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIvkPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 430 NDTVANNIayartdlysREQIEKAAQMAYAMDFINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:cd03236 100 PKAVKGKV---------GELLKKKDERGKLDELVDQLE--LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 740854059 510 ALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIIVVEDGV 555
Cdd:cd03236 169 YLDIKQRLNAARLIRELaEDDNYVLVVEHDLAVLDYLSDYIHCLYGE 215
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
27-197 |
5.30e-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: 60.60 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLApivsVAIRVVS 186
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLL----VVYYLLQ 156
|
170
....*....|.
gi 740854059 187 KRFRSISKNMQ 197
Cdd:cd18580 157 RYYLRTSRQLR 167
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
356-557 |
7.09e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.89 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 356 APALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGhDLreyTLASL-RDQVALVSQNVHlfnDTVA 434
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL---IVARLqQDPPRNVEGTVY---DFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 435 NNIA---------YARTDLYSREQIEKA-AQMAYAMDFINKMdNG--LDTVIGENGVL-----------LSGGQRQRIAI 491
Cdd:PRK11147 89 EGIEeqaeylkryHDISHLVETDPSEKNlNELAKLQEQLDHH-NLwqLENRINEVLAQlgldpdaalssLSGGWLRKAAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740854059 492 ARALLRDSPILILDEATSALDTEserAIQaALDELQKN-RTSLV-IAHRLSTIEQ-ADEIIVVEDGVIV 557
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIE---TIE-WLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
350-558 |
9.88e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 350 TYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVSQnvhlF 429
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----F 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 430 NDTVA--NNIAYARTDLYSREQIEkaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:COG2401 113 KDAVEllNAVGLSDAVLWLRRFKE-----------------------------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 508 TSALDTESERAIQAALDEL-QKNRTSLVIA-HRLSTIE--QADEIIVVEDGVIVE 558
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLaRRAGITLVVAtHHYDVIDdlQPDLLIFVGYGGVPE 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-554 |
1.74e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 323 DSEQEKDEgkrviERATGDLEF--RNVTFTYP--GREAPALRNINLNIPAGKTVALVGRSGSGKST----IASLITRFYd 394
Cdd:TIGR00956 744 DVNDEKDM-----EKESGEDIFhwRNLTYEVKikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnvLAERVTTGV- 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 395 IDEGQILMDGHDLREytlaSLRDQVALVSQN-VHLFNDTVANNIAYARtdlYSRE--QIEKAAQMAYAMDFIN--KMDNG 469
Cdd:TIGR00956 818 ITGGDRLVNGRPLDS----SFQRSIGYVQQQdLHLPTSTVRESLRFSA---YLRQpkSVSKSEKMEYVEEVIKllEMESY 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILI-LDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTI--EQA 545
Cdd:TIGR00956 891 ADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAIlfEEF 970
|
....*....
gi 740854059 546 DEIIVVEDG 554
Cdd:TIGR00956 971 DRLLLLQKG 979
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
122-294 |
1.83e-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: 59.03 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 122 GTLLSRITYDSEQ-------VASSSSGALITvvregasIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRF-RSIS 193
Cdd:cd18585 92 GDLLNRIVADIDTldnlylrVLSPPVVALLV-------ILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLgKKIG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 194 KNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFp 273
Cdd:cd18585 165 QQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAP- 243
|
170 180
....*....|....*....|.
gi 740854059 274 svmeNLTAGTITVVFSSMIAL 294
Cdd:cd18585 244 ----LVQNGALDGALLAMLVF 260
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
343-570 |
3.24e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYpgREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlASLRDQV--- 419
Cdd:NF033858 3 RLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcpr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 420 -ALVSQ----NvhLFND-TVANNIAY-ARtdLYSREQIEKAAQMAYAMDfinkmDNGL----DTVIGEngvlLSGGQRQR 488
Cdd:NF033858 78 iAYMPQglgkN--LYPTlSVFENLDFfGR--LFGQDAAERRRRIDELLR-----ATGLapfaDRPAGK----LSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIahrLST--IEQA---DEIIVVEDGVIVERGTH 562
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMsVL---VATayMEEAerfDWLVAMDAGRVLATGTP 221
|
....*...
gi 740854059 563 NELIEQRG 570
Cdd:NF033858 222 AELLARTG 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-552 |
3.31e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 366 IPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDghdLR-----EYTLASLRDQV-ALVSQNVHLFNDTvanniaY 439
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKisykpQYIKPDYDGTVeDLLRSITDDLGSS------Y 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 440 ARTDLYSREQIEKAaqmayamdfinkMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE--- 516
Cdd:PRK13409 433 YKSEIIKPLQLERL------------LDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlav 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 740854059 517 -RAIQAALDElqKNRTSLVIAHRLSTIEQ-ADEIIVVE 552
Cdd:PRK13409 493 aKAIRRIAEE--REATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-554 |
5.39e-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: 56.10 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTY--PGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDID--EGQILMDGHDLREytlaSLRD 417
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 418 QVALVSQN-VHLFNDTVanniayartdlysREQIEKAAQMayamdfinkmdNGldtvigengvlLSGGQRQRIAIARALL 496
Cdd:cd03232 80 STGYVEQQdVHSPNLTV-------------REALRFSALL-----------RG-----------LSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 497 RDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS--TIEQADEIIVVEDG 554
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-190 |
6.09e-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: 57.60 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 69 LVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVR 148
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 740854059 149 EGASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFR 190
Cdd:cd18782 125 DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILR 166
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
342-566 |
6.11e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 57.89 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLIT--------------RFYDIDEGQIlmdgh 405
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDIDLLRL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 406 dlreytlaSLRDQVALVSQNVHLF----------NDTVANNIA------------YARTDLYSREQIE----------KA 453
Cdd:PRK15093 79 --------SPRERRKLVGHNVSMIfqepqscldpSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIEllhrvgikdhKD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 454 AQMAYAMDfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--T 531
Cdd:PRK15093 151 AMRSFPYE-------------------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntT 211
|
250 260 270
....*....|....*....|....*....|....*.
gi 740854059 532 SLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELI 566
Cdd:PRK15093 212 ILLISHDLQMLSQwADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
363-575 |
6.67e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 6.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 363 NLNIPAGKTVALVGRSGSGKSTIASLItrfydidEGQ-ILMDGH---DLREYTLASLRDQVALVSQNvhlFNDtvaNNia 438
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARAL-------AGElPLLSGErqsQFSHITRLSFEQLQKLVSDE---WQR---NN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 439 yarTDLYS----------REQI-----EKAAQMAYAMDFinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
Cdd:PRK10938 88 ---TDMLSpgeddtgrttAEIIqdevkDPARCEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740854059 504 LDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIIVVEDGVIVERGTHNElIEQRGVYAQL 575
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREE-ILQQALVAQL 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
342-575 |
7.17e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.86 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASL------ 415
Cdd:PRK11701 7 LSVRGLTKLYGPRKG--CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 416 ---RDQVALVSQNvhlfndtvanniayARTDLysREQIEKAAQ-----MA-----Y------AMDFINKMDNGLDTvIGE 476
Cdd:PRK11701 85 rllRTEWGFVHQH--------------PRDGL--RMQVSAGGNigerlMAvgarhYgdiratAGDWLERVEIDAAR-IDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 477 NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLSTIEQ-ADEII 549
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLL 223
|
250 260
....*....|....*....|....*..
gi 740854059 550 VVEDGVIVERG-THNELIEQRGVYAQL 575
Cdd:PRK11701 224 VMKQGRVVESGlTDQVLDDPQHPYTQL 250
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
65-318 |
7.71e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 57.23 E-value: 7.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 65 LWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRL----FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSS 140
Cdd:cd18560 34 LESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELslktFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLS 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 141 GALITVVREGASIIGLF-IMMFYYSWQLSLILIV---LAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAeqmLKGHKE 216
Cdd:cd18560 114 YLVFYLVPTLLELIVVSvVFAFHFGAWLALIVFLsvlLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDS---LLNFET 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 217 VLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMR 296
Cdd:cd18560 191 VKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQ 270
|
250 260
....*....|....*....|..
gi 740854059 297 PLKSLTNVNAQFQRGMAACQTL 318
Cdd:cd18560 271 PLNFLGTIYRMIIQSLTDMENL 292
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
360-525 |
8.37e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.97 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 360 RNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREytlasLRDQVAlvsQNV----HL--FND-- 431
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYH---QDLlylgHQpgIKTel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIA-YAR-TDLYSREQIEKA-AQMayamdfinkmdnGL----DTVIGEngvlLSGGQRQRIAIARALLRDSPILIL 504
Cdd:PRK13538 90 TALENLRfYQRlHGPGDDEALWEAlAQV------------GLagfeDVPVRQ----LSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|.
gi 740854059 505 DEATSALDTESERAIQAALDE 525
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQ 174
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-549 |
9.70e-09 |
|
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: 54.67 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 353 GREAPALRNINLNIPAGKTVALVGRSGSGKSTIA---SLITrfydidegqiLMDGHDLREYTLASLRDQVALVSqnVHLf 429
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdaiGLAL----------GGAQSATRRRSGVKAGCIVAAVS--AEL- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 430 ndtvanniayartdLYSREQiekaaqmayamdfinkmdngldtvigengvlLSGGQRQRIAIARAL----LRDSPILILD 505
Cdd:cd03227 72 --------------IFTRLQ-------------------------------LSGGEKELSALALILalasLKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740854059 506 EATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQADEII 549
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
355-568 |
1.30e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 355 EAPALRNINLNIPAGKTVALVGRSGSGKSTI-ASLITRF-YDIDEGQILMDGHDLREYT---------LASLRDQVALVS 423
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSpedragegiFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 424 QNVHLFNDTVANNIAYAR----TDLYSREQI--EKAAQMAYAMDFINKMDNgldtvigengVLLSGGQRQRIAIARALLR 497
Cdd:PRK09580 93 VSNQFFLQTALNAVRSYRgqepLDRFDFQDLmeEKIALLKMPEDLLTRSVN----------VGFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA---HRLSTIEQADEIIVVEDGVIVERGTHN---ELIEQ 568
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFTlvkQLEEQ 239
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
71-190 |
1.48e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 56.44 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 71 VIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSGALITVVREG 150
Cdd:cd18566 48 VVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLDL 126
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 740854059 151 ASIIGLFIMMFYYSWQLSLILIVLAPIVSVAIRVVSKRFR 190
Cdd:cd18566 127 PFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR 166
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
369-552 |
1.52e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 369 GKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDghdLR-----EYTLASLRDQV--ALVSQNVHLFNDTvanniaYAR 441
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKisykpQYISPDYDGTVeeFLRSANTDDFGSS------YYK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 442 TDLYSREQIEKAaqmayamdfinkMDNGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESE----R 517
Cdd:COG1245 437 TEIIKPLGLEKL------------LDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaK 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 740854059 518 AIQAALDElqKNRTSLVIAHRLSTIEQ-ADEIIVVE 552
Cdd:COG1245 497 AIRRFAEN--RGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
479-552 |
1.61e-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: 54.50 E-value: 1.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIIVVE 552
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
2.83e-08 |
|
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: 54.57 E-value: 2.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIAslitrFYDI-DEGQilmdghdlREYtLASL------------RDQVALV--- 422
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA-----FDTIyAEGQ--------RRY-VESLsayarqflgqmdKPDVDSIegl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 -----------SQNVHLFNDTVANNIAYARTdLYSREQIEKAAQMAYamdfinkmDNGLDTV-IGENGVLLSGGQRQRIA 490
Cdd:cd03270 77 spaiaidqkttSRNPRSTVGTVTEIYDYLRL-LFARVGIRERLGFLV--------DVGLGYLtLSRSAPTLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 491 IARAL---LrDSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEII 549
Cdd:cd03270 148 LATQIgsgL-TGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
321-543 |
3.57e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.95 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 321 ILDSEQE-KDEGKRVIE--RATGDLEFRNVTFTYPGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDE 397
Cdd:TIGR01257 1914 IFDEDDDvAEERQRIISggNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTS 1993
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 398 GQILMDGHDLreytLASLRDqvalVSQNV-----------------HLFndtvanniAYARTDLYSREQIEKAAQMAyam 460
Cdd:TIGR01257 1994 GDATVAGKSI----LTNISD----VHQNMgycpqfdaiddlltgreHLY--------LYARLRGVPAEEIEKVANWS--- 2054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 461 dfINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRL 539
Cdd:TIGR01257 2055 --IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
....
gi 740854059 540 STIE 543
Cdd:TIGR01257 2131 EECE 2134
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-515 |
5.20e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGREaPALRNINLNIPAGKTVALVGRSGSGKSTI----ASLITRFydidEGQ-ILMDG--------------- 404
Cdd:PRK11819 10 NRVSKVVPPKK-QILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKEF----EGEaRPAPGikvgylpqepqldpe 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 405 HDLREYTLASLRDQVALVSQnvhlFNDTvanNIAYARTDLYSREQIEKAAQMAYAMDFIN--KMDNGL------------ 470
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDR----FNEI---YAAYAEPDADFDALAAEQGELQEIIDAADawDLDSQLeiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 740854059 471 DTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
466-566 |
5.24e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 56.17 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQ----KNRTSLVIAH 537
Cdd:TIGR00630 814 CDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDD---IKKLLEVLQrlvdKGNTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|....*...
gi 740854059 538 RLSTIEQADEIIvveD---------GVIVERGTHNELI 566
Cdd:TIGR00630 891 NLDVIKTADYII---DlgpeggdggGTVVASGTPEEVA 925
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
32-213 |
5.79e-08 |
|
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: 54.48 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 32 IALILNAASDTFMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18779 4 LGQILLASLLLQLLGLALPLLtgvlvDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRitydseqVASSS------SGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIVSV 180
Cdd:cd18779 84 HLLRLPYRFFQQRSTGDLLMR-------LSSNAtirellTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVA 156
|
170 180 190
....*....|....*....|....*....|...
gi 740854059 181 AIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKG 213
Cdd:cd18779 157 LLLATRRRVRELMARELAAQAEAQSYLVEALSG 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
335-556 |
6.09e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.39 E-value: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 335 IERATGD--LEFRNVTftypgreAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHdlreyTL 412
Cdd:PRK10762 249 LDKAPGEvrLKVDNLS-------GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH-----EV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 413 ASLRDQVALVSQNVHLFND----------TVANNIAYARTDLYSRE--QIEKAAQMAYAMDFInKMDN----GLDTVIGe 476
Cdd:PRK10762 317 VTRSPQDGLANGIVYISEDrkrdglvlgmSVKENMSLTALRYFSRAggSLKHADEQQAVSDFI-RLFNiktpSMEQAIG- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 477 ngvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQADEIIVVEDG 554
Cdd:PRK10762 395 ---LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEG 471
|
..
gi 740854059 555 VI 556
Cdd:PRK10762 472 RI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
346-515 |
7.57e-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: 55.33 E-value: 7.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 346 NVTFTYPGREaPALRNINLNIPAGKTVALVGRSGSGKSTI----ASLITRF-------------YDIDEGQiLMDGHDLR 408
Cdd:TIGR03719 9 RVSKVVPPKK-EILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKDFngearpqpgikvgYLPQEPQ-LDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 409 EYTLASLRDQVALVSQnvhlFNDTVAnniAYARTDLYSREQIEKAAQMAYAMDFIN--KMDNGLDTVI-------GENGV 479
Cdd:TIGR03719 87 ENVEEGVAEIKDALDR----FNEISA---KYAEPDADFDKLAAEQAELQEIIDAADawDLDSQLEIAMdalrcppWDADV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 740854059 480 -LLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
Cdd:TIGR03719 160 tKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-556 |
1.55e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.29 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 360 RNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASlRDQVALV-----SQNVHLFNDT-V 433
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylpedRQSSGLYLDApL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNI---AYARTDLYSREQIEKAAQMAYAMDfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
Cdd:PRK15439 359 AWNVcalTHNRRGFWIKPARENAVLERYRRA-LNIKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 740854059 511 LDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIIVVEDGVI 556
Cdd:PRK15439 434 VDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
336-569 |
1.92e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 336 ERATGDlefrnVTFTYPGREAPALRN-INLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLReytLAS 414
Cdd:PRK11288 250 PRPLGE-----VRLRLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 415 LRD-------------------QVALVSQNVhlfndtvanNIAYARTDLYSREQIEKAAQMAYAMDFINKMD---NGLDT 472
Cdd:PRK11288 322 PRDairagimlcpedrkaegiiPVHSVADNI---------NISARRHHLRAGCLINNRWEAENADRFIRSLNiktPSREQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 473 VIGengvLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIIV 550
Cdd:PRK11288 393 LIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLpEVLGVADRIVV 468
|
250
....*....|....*....
gi 740854059 551 VEDGVIVERGTHNELIEQR 569
Cdd:PRK11288 469 MREGRIAGELAREQATERQ 487
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
342-541 |
3.25e-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: 53.02 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMdGHDLreytlaslrdQVAL 421
Cdd:TIGR03719 323 IEAENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQnvhlFNDTVANN-------------IAYARTDLYSReqiekaaqmAYAMDFINKmdnGLDT--VIGEngvlLSGGQR 486
Cdd:TIGR03719 390 VDQ----SRDALDPNktvweeisggldiIKLGKREIPSR---------AYVGRFNFK---GSDQqkKVGQ----LSGGER 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST 541
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
32-187 |
3.39e-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: 52.16 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 32 IALILNAASDTFMLSLLKPLLddgFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGM 111
Cdd:cd18781 7 ISLLANIAFVFSIANLLQKLL---EGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSG-------ALItvvregASIIgLFIMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:cd18781 84 GPSYQEKVSTAEVVQLSVEGVEQLEIYFGRylpqffySML------APLT-LFVVLAPINWKAALVLLICVPLIPISIIA 156
|
...
gi 740854059 185 VSK 187
Cdd:cd18781 157 VQK 159
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
27-540 |
3.47e-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: 53.21 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 27 LIVAGIALILNAASDTFML----SLLKPLLDDGFGKTDRSVLLWMplvVIGLMIvrgltSYVSSYcISWVSGKVVMTMRR 102
Cdd:TIGR00954 98 LILIAFLLVSRTYLSVYVAtldgQIESSIVRRSPRNFAWILFKWF---LIAPPA-----SFINSA-IKYLLKELKLRFRV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 103 RLFGHMMGMPVSFFDKQSTGTLLSRI-------TYDSEQVASSSSGALITVVRegaSIIGLFIMMFYY----SWQLSLIL 171
Cdd:TIGR00954 169 RLTRYLYSKYLSGFTFYKVSNLDSRIqnpdqllTQDVEKFCDSVVELYSNLTK---PILDVILYSFKLltalGSVGPAGL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 172 IVLAPIVSVAIRVVSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKR----FDKVSNKMRLQGMKMVSA 247
Cdd:TIGR00954 246 FAYLFATGVVLTKLRPPIGKLTVEEQALEGEYRYVHSRLIMNSEEIAFYQGNKVEKETvmssFYRLVEHLNLIIKFRFSY 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 248 SSISDPIIQLIASlalAFVLYAASFPSVMEN----------------LTAGTITVVFSSMIA-LMRPLKSLT-------- 302
Cdd:TIGR00954 326 GFLDNIVAKYTWS---AVGLVAVSIPIFDKThpaflemseeelmqefYNNGRLLLKAADALGrLMLAGRDMTrlagftar 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 303 ---------NVNA-QFQRGMAACQTLFTILDSEQEKDEGKRVIERATGDLEFRNVTFTYPGREApALRNINLNIPAGKTV 372
Cdd:TIGR00954 403 vdtllqvldDVKSgNFKRPRVEEIESGREGGRNSNLVPGRGIVEYQDNGIKFENIPLVTPNGDV-LIESLSFEVPSGNNL 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 373 ALVGRSGSGKSTIASLITRFYDIDEGQILMDGHD------LREY-TLASLRDQValvsqnvhLFNDTVANNI--AYARTD 443
Cdd:TIGR00954 482 LICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyvpQRPYmTLGTLRDQI--------IYPDSSEDMKrrGLSDKD 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 444 LysrEQIEKAAQMAYamdfINKMDNGLDTVIGENGVLlSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
Cdd:TIGR00954 554 L---EQILDNVQLTH----ILEREGGWSAVQDWMDVL-SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC 625
|
570
....*....|....*..
gi 740854059 524 DElqKNRTSLVIAHRLS 540
Cdd:TIGR00954 626 RE--FGITLFSVSHRKS 640
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
345-576 |
3.70e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 51.65 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 345 RNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDgHDLReytlaslrdqVALVSQ 424
Cdd:PRK09544 8 ENVSVSFGQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR----------IGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 425 NVHL---FNDTVANNI----AYARTDLYSREQIEKAAQMAYAmdfinKMDNgldtvigengvlLSGGQRQRIAIARALLR 497
Cdd:PRK09544 75 KLYLdttLPLTVNRFLrlrpGTKKEDILPALKRVQAGHLIDA-----PMQK------------LSGGETQRVLLARALLN 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 498 DSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIIVVeDGVIVERGT------HNELI-- 566
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVmAKTDEVLCL-NHHICCSGTpevvslHPEFIsm 216
|
250
....*....|....*.
gi 740854059 567 ------EQRGVYAQLH 576
Cdd:PRK09544 217 fgprgaEQLGIYRHHH 232
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
354-554 |
4.83e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.57 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 354 REAPALRNINLNIPAGKTVALVGRSGSGKSTIASLIT-RFYDID-EGQILMDGHDLREYTLAslrdQVALVSQNVHLF-N 430
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 431 DTVANNIAYAR----TDLYSREQIEKAAQMAYAMDFINKMDNgldTVIGENGVL-LSGGQRQRIAIARALLRDSPILILD 505
Cdd:PLN03211 155 LTVRETLVFCSllrlPKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 740854059 506 EATSALD-TESERAIQAALDELQKNRTSLVIAHRLST--IEQADEIIVVEDG 554
Cdd:PLN03211 232 EPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
342-567 |
5.56e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTftypGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT-LASLRDQVA 420
Cdd:PRK10982 251 LEVRNLT----SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQ---------NVHL-FNDTVANNIAY-ARTDLYSREQIEKAAQmaYAMDFINKMDNGLDTVIGEngvlLSGGQRQRI 489
Cdd:PRK10982 327 LVTEerrstgiyaYLDIgFNSLISNIRNYkNKVGLLDNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKV 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIIVVEDGV---IVE--RGTH 562
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMpELLGITDRILVMSNGLvagIVDtkTTTQ 480
|
....*
gi 740854059 563 NELIE 567
Cdd:PRK10982 481 NEILR 485
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
28-266 |
5.71e-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: 51.26 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 28 IVAGIALILNAAsdtfmlsLLKPLLDDGFGKTDRSVLLWMPLVV-IGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFG 106
Cdd:cd18584 6 LLAALLIIAQAW-------LLARIIAGVFLEGAGLAALLPLLLLlLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVRegASII--GLFIMMFYYSWQLSLILIVLAPIVSVAIRV 184
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVL--AAIVplLILVAVFPLDWVSALILLVTAPLIPLFMIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 185 VSKRFRSISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMK-----MVSASsisdpIIQLIA 259
Cdd:cd18584 157 IGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKvlrvaFLSSA-----VLEFFA 231
|
....*..
gi 740854059 260 SLALAFV 266
Cdd:cd18584 232 TLSIALV 238
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
343-546 |
7.02e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRfydiDEGQilmdGH--DLREY--------TL 412
Cdd:PRK10938 262 VLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQ----GYsnDLTLFgrrrgsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 413 ASLRDQVALVSQNVHL---FNDTVANNIAYARTD---LYsreQIEKAAQMAYAMDFINKMdnGLDTVIGENGVL-LSGGQ 485
Cdd:PRK10938 332 WDIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDsigIY---QAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWGQ 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 486 rQRIA-IARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLV------------IAHRLSTIEQAD 546
Cdd:PRK10938 407 -QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-554 |
9.59e-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: 51.75 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 339 TGD--LEFRNVTFTYP-GREAPALRNINLNIPAGKTVALVGRSGSGKS-TIASLITRFYDIDEGQILMDGHDLREYTLA- 413
Cdd:TIGR02633 253 IGDviLEARNLTCWDViNPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAq 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQVALVSQNVH----LFNDTVANNIAYARTDLYS-REQIEKAAQMAYAMDFINKMD---NGLDTVIGEngvlLSGGQ 485
Cdd:TIGR02633 333 AIRAGIAMVPEDRKrhgiVPILGVGKNITLSVLKSFCfKMRIDAAAELQIIGSAIQRLKvktASPFLPIGR----LSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EQADEIIVVEDG 554
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVlGLSDRVLVIGEG 479
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-554 |
1.84e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.01 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGreAPAL-RNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMdghdlreytlaSLRDQVA 420
Cdd:PLN03073 509 ISFSDASFGYPG--GPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR-----------SAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 421 LVSQNvHLfnDTVanniayartDLYSREqiekaaqMAYAMD-FINKMDNGLDTVIGENGV----------LLSGGQRQRI 489
Cdd:PLN03073 576 VFSQH-HV--DGL---------DLSSNP-------LLYMMRcFPGVPEQKLRAHLGSFGVtgnlalqpmyTLSGGQKSRV 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 740854059 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIE-QADEIIVVEDG 554
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISgSVDELWVVSEG 700
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
342-568 |
2.25e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.90 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGREAP--ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDiDEGQILMD-----GHDLreytLA- 413
Cdd:COG4170 4 LDIRNLTIEIDTPQGRvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADrfrwnGIDL----LKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 414 SLRDQVALVSQNVHL-FNDtvanniayARTDLYSREQIEKaaQMAYAMDF--------------------------INKM 466
Cdd:COG4170 79 SPRERRKIIGREIAMiFQE--------PSSCLDPSAKIGD--QLIEAIPSwtfkgkwwqrfkwrkkraiellhrvgIKDH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 467 DNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ 544
Cdd:COG4170 149 KDIMNSYPHE----LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQ 224
|
250 260
....*....|....*....|....*
gi 740854059 545 -ADEIIVVEDGVIVERGTHNELIEQ 568
Cdd:COG4170 225 wADTITVLYCGQTVESGPTEQILKS 249
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-554 |
2.33e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIASLI----TRFYDidEGQILMDGHDLREYTLASLRdqvALVSQN-VHLFNDTV 433
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGFPKKQETFARIS---GYCEQNdIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 434 ANNIAYARTdLYSREQIEKAAQMAYA---MDFInKMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATS 509
Cdd:PLN03140 971 RESLIYSAF-LRLPKEVSKEEKMMFVdevMELV-ELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 740854059 510 ALDTESE----RAIQAALDelqKNRTSLVIAHRLS--TIEQADEIIVVEDG 554
Cdd:PLN03140 1049 GLDARAAaivmRTVRNTVD---TGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-558 |
2.53e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTftypGREAPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYT-LASLRDQVAL 421
Cdd:PRK09700 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 VSQNVH---LF-NDTVANNIAYART----------DLYSREQIEKAAQMAyaMDFINKMDNGLDTVIGEngvlLSGGQRQ 487
Cdd:PRK09700 343 ITESRRdngFFpNFSIAQNMAISRSlkdggykgamGLFHEVDEQRTAENQ--RELLALKCHSVNQNITE----LSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIIVVEDGVIVE 558
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
480-555 |
3.80e-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: 47.84 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 LLSGGQRQRIAIAR--ALLR--DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVV---E 552
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvrPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRLYGVtmqE 192
|
...
gi 740854059 553 DGV 555
Cdd:cd03278 193 SGV 195
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
44-295 |
4.98e-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: 48.59 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 44 MLSLLKPLL-----DDGFGKTDRSVLLwmpLVVIG-LMIVRGLTS--YVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSF 115
Cdd:cd18571 16 LLQLIFPFLtqsivDKGINNKDLNFIY---LILIAqLVLFLGSTSieFIRSWILLHISSRINISIISDFLIKLMRLPISF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 116 FDKQSTGTLLSRItYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLApIVSVA-------IRVV--S 186
Cdd:cd18571 93 FDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGS-VLYILwillflkKRKKldY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 187 KRFRSISKNMQNTMgqvttsaeQMLKGHKEVLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFV 266
Cdd:cd18571 171 KRFDLSSENQSKLI--------ELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNILI 242
|
250 260
....*....|....*....|....*....
gi 740854059 267 LYAASFpSVMEnltaGTITvvFSSMIALM 295
Cdd:cd18571 243 TFLAAK-LVID----GEIT--LGMMLAIQ 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
336-512 |
5.26e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 336 ERATGD--LEFRNVT---FTYPGREApaLRNINLNIPAGKTVALVGRSGSGKS-TIASLITRFYDIDEGQILMDGHDLRE 409
Cdd:PRK13549 252 PHTIGEviLEVRNLTawdPVNPHIKR--VDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 410 YTLA-SLRDQVALVSQN------VHLFNdtVANNIAYARTDLYS-REQIEKAAQMAYAMDFINKMD---NGLDTVIGEng 478
Cdd:PRK13549 330 RNPQqAIAQGIAMVPEDrkrdgiVPVMG--VGKNITLAALDRFTgGSRIDDAAELKTILESIQRLKvktASPELAIAR-- 405
|
170 180 190
....*....|....*....|....*....|....
gi 740854059 479 vlLSGGQRQRIAIARALLRDSPILILDEATSALD 512
Cdd:PRK13549 406 --LSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
343-537 |
5.46e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 5.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 343 EFRNVTFTYPGREApaLRNINLNIPAGKTVALVGRSGSGKSTIASLITrfydideGQILMDGHDLREYTlaslRDQVALV 422
Cdd:PRK11147 321 EMENVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHCGT----KLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 423 SQNVHLFN--DTVANNIAYARTDLYSREQIEKAaqMAYAMDFINKMDNGLDTVIGengvlLSGGQRQRIAIARALLRDSP 500
Cdd:PRK11147 388 DQHRAELDpeKTVMDNLAEGKQEVMVNGRPRHV--LGYLQDFLFHPKRAMTPVKA-----LSGGERNRLLLARLFLKPSN 460
|
170 180 190
....*....|....*....|....*....|....*..
gi 740854059 501 ILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
480-556 |
6.50e-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: 49.20 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 LLSGGQRQRIAIA--RALL--RDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIIVV---E 552
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQkyKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLVGVtmvE 1156
|
....
gi 740854059 553 DGVI 556
Cdd:pfam02463 1157 NGVS 1160
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
481-552 |
1.07e-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: 46.45 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 LSGGQRQ------RIAIARALLRDSPILILDEATSALDTES-ERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIIVV 551
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERksQKNFQLIVITHDEELVDAADHIYRV 195
|
.
gi 740854059 552 E 552
Cdd:cd03240 196 E 196
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
26-188 |
1.48e-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: 47.24 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 26 GLIVAGIALIlnaasdtfMLSLLKPLLddgFGKTDRSVLLW-MPLVVIGLMIVRGLTSYVSSYCISWVSGKvvMTMRRRL 104
Cdd:cd18562 3 GLALANVALA--------GVQFAEPVL---FGRVVDALSSGgDAFPLLALWAALGLFSILAGVLVALLADR--LAHRRRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 105 ------FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAssssGALITVVREG-ASIIGLFIMM---FYYSWQLSLILIVL 174
Cdd:cd18562 70 avmasyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALF----GLWLGFFREHlAALVSLIVLLpvaLWMNWRLALLLVVL 145
|
170
....*....|....
gi 740854059 175 APIVSVAIRVVSKR 188
Cdd:cd18562 146 AAVYAALNRLVMRR 159
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
358-572 |
2.24e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMDGHDLREYTLASLRDQVALVsQNVHLfndtvaNNI 437
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-ENIEL------KGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 438 AYARTDLYSREQIEKAAQMAYAMDFINKmdnGLDTvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQ---PVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 740854059 518 AIQAALDELQKN-RTSLVIAHRLSTIEQ-ADEIIVVEDGVIVERGTHNELIEQRGVY 572
Cdd:PRK13545 181 KCLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEF 237
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-512 |
2.86e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPG-REAPALRNINLNIPAGKTVALVGRSGSGKSTIA-SLITRFYDID-EGQILMDGhdlREYTLASLRDQ 418
Cdd:NF040905 258 FEVKNWTVYHPLhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDG---KEVDVSTVSDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 419 V----ALVSQN-----VHLfNDTVANNIAYARTDLYSREQ-IEKAAQMAYAMDFINKMD---NGLDTVIGEngvlLSGGQ 485
Cdd:NF040905 335 IdaglAYVTEDrkgygLNL-IDDIKRNITLANLGKVSRRGvIDENEEIKVAEEYRKKMNiktPSVFQKVGN----LSGGN 409
|
170 180
....*....|....*....|....*..
gi 740854059 486 RQRIAIARALLRDSPILILDEATSALD 512
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
72-178 |
3.77e-05 |
|
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: 45.93 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 72 IGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGA 151
Cdd:cd18606 42 AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLS 121
|
90 100
....*....|....*....|....*..
gi 740854059 152 SIIGLFIMMFYYswqLSLILIVLAPIV 178
Cdd:cd18606 122 SIIGTFILIIIY---LPWFAIALPPLL 145
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-571 |
5.63e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 342 LEFRNVTFTYPGReaPALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQILMdghdlreytlaslrdqval 421
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 422 vSQNVhlfndtvanNIAYARTDlysreqiekaaqmaYAMDFINKMD-----------NGLDTVIgeNGVL---------- 480
Cdd:PRK15064 379 -SENA---------NIGYYAQD--------------HAYDFENDLTlfdwmsqwrqeGDDEQAV--RGTLgrllfsqddi 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 ------LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEII-V 550
Cdd:PRK15064 433 kksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSL--ATRIIeI 508
|
250 260
....*....|....*....|.
gi 740854059 551 VEDGVIVERGTHNELIEQRGV 571
Cdd:PRK15064 509 TPDGVVDFSGTYEEYLRSQGI 529
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
54-193 |
5.68e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 45.21 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 54 DGFGKTDRSVLLWMPLVVIGLMIVRGLTSYVSSYCISWVsgkvvmtMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSE 133
Cdd:cd18605 38 NDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARR-------LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVY 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 134 QVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPIvsvaIRVVSKRFRSIS 193
Cdd:cd18605 111 TIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFI----YYRIQRYYRATS 166
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
67-301 |
9.39e-05 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 44.41 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 67 MPLVVIGLMIVRGLTSYVSSYCI---SWVSGKVVM-TMRR---RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSS 139
Cdd:cd18582 33 LLAVPLLLLLAYGLARILSSLFNelrDALFARVSQrAVRRlalRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 140 SGALITVVREGASIIGLFIMMFY-YSWQLSLILIV-LAPIVSVAIRVVSKRfRSISKNMQNTMGQVTTSAEQMLKGHKEV 217
Cdd:cd18582 113 RFLLFNILPTILELLLVCGILWYlYGWSYALITLVtVALYVAFTIKVTEWR-TKFRREMNEADNEANAKAVDSLLNYETV 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 218 LIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMENLTAGTITVVFSSMIALMRP 297
Cdd:cd18582 192 KYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQP 271
|
....
gi 740854059 298 LKSL 301
Cdd:cd18582 272 LNFL 275
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-567 |
9.97e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.61 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIasLITRFYDID-----EGQILMDGHDLREYTLaslRDQVALVSQN-VHLFNDT 432
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTL--LLALAGKLDpslkvSGEITYNGYRLNEFVP---RKTSAYISQNdVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 433 VANNIAYA--------RTDLYS----REQ---IEKAAQM-----AYAM---------DFINK---MDNGLDTVIGENGVL 480
Cdd:PLN03140 256 VKETLDFSarcqgvgtRYDLLSelarREKdagIFPEAEVdlfmkATAMegvksslitDYTLKilgLDICKDTIVGDEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 481 -LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS----TIEQADEIIVVEDGV 555
Cdd:PLN03140 336 gISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQ 415
|
250
....*....|..
gi 740854059 556 IVERGTHNELIE 567
Cdd:PLN03140 416 IVYQGPRDHILE 427
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
341-537 |
1.04e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 341 DLEFRNVTFTYPGREAPALRNINLNIpaGKTVALVGRSGSGKSTIASLITrFYDID-----------EGQILMDGHDLRE 409
Cdd:PLN03073 177 DIHMENFSISVGGRDLIVDASVTLAF--GRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkncqilhvEQEVVGDDTTALQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 410 YTLASLRDQVALVSQNVHLF-------------------NDTVANNIAYAR-TDLYSR-EQIE------KAAQMAYAMDF 462
Cdd:PLN03073 254 CVLNTDIERTQLLEEEAQLVaqqrelefetetgkgkganKDGVDKDAVSQRlEEIYKRlELIDaytaeaRAASILAGLSF 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740854059 463 INKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
Cdd:PLN03073 334 TPEMQV-------KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-555 |
1.16e-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: 45.43 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 480 LLSGGQRQRIAIARA----LLRDSPILILDEATSALD-TESERAIQaALDELQKNRTSLVIAHRLSTIEQADEIIVV--- 551
Cdd:TIGR02168 1089 LLSGGEKALTALALLfaifKVKPAPFCILDEVDAPLDdANVERFAN-LLKEFSKNTQFIVITHNKGTMEVADQLYGVtmq 1167
|
....
gi 740854059 552 EDGV 555
Cdd:TIGR02168 1168 EKGV 1171
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
65-318 |
1.34e-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: 43.97 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 65 LWMplVVIGLMIVRG---LTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSfFDKQSTGTLLSRIT-YDS--EQVASS 138
Cdd:cd18587 41 LWV--LAIGVLIALLfdfILKLLRAYFIDVAGKRADVILSSRLFERVLGLRLE-ARPASVGSFANNLReFESvrDFFTSA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 139 SSGALITVVregasIIGLFIMMFYY-SWQLSLILIVLAPIVSVAIRVVSKRF-RSISKNMQNTMGQVTTSAEqMLKGHKE 216
Cdd:cd18587 118 TLTALIDLP-----FVLLFLAVIALiGGPLALVPLVAIPLVLLYGLLLQKPLrRLVEESMRESAQKNALLVE-SLSGLET 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 217 VLIFGGQEVETKRFDKVSNKMRLQGMKMVSASSISDPIIQLIASLALAFVLYAASFpSVME-NLTAGTItvVFSSMIA-- 293
Cdd:cd18587 192 IKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVY-LISDgELTMGGL--IACVILSgr 268
|
250 260
....*....|....*....|....*
gi 740854059 294 LMRPLKSLTNVNAQFQRGMAACQTL 318
Cdd:cd18587 269 ALAPLGQIAGLLTRYQQARTALKSL 293
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
466-549 |
1.47e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 466 MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRDS---PILILDEATSALDTESeraIQAALDELQK-----NrTSLVIA 536
Cdd:PRK00349 815 VDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFED---IRKLLEVLHRlvdkgN-TVVVIE 890
|
90
....*....|...
gi 740854059 537 HRLSTIEQADEII 549
Cdd:PRK00349 891 HNLDVIKTADWII 903
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
481-525 |
1.49e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 740854059 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDE 525
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
69-236 |
2.23e-04 |
|
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group represents the transmembrane (TM) domain of an active lipid-linked oligosaccharides flippase PglK (protein glycosylation K), which is a homodimeric ABC transporter that flips a lipid-linked oligosaccharide that serves as a glycan donor in N-linked protein glycosylation. Pglk mediates the ATP-dependent translocation of the undecaprenylpyrophosphate-linked heptasaccharide intermediate across the cell membrane; this is an essential step during the N-linked protein glycosylation pathway. This TM subunit exhibits the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 349997 Cd Length: 300 Bit Score: 43.30 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 69 LVVIGLMIVRGLTSYVSSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVaSSSSGALITVVR 148
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNL-SQVIQSFLFILS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 149 EGASIIGLFIMMFYYSWQLSLIL-IVLAPIVSVAIRVVSKRFRS---ISKNMQNTMGQVTTSAeqmLKGHKEVLIFGGQE 224
Cdd:cd18553 137 EIFVILFIYSLLLYVNWKITLVLtLFLGLNVFFITKIVSKKIKKqgkKREESQKKFYKILSET---FGNFKIIKLKSNEK 213
|
170
....*....|..
gi 740854059 225 VETKRFDKVSNK 236
Cdd:cd18553 214 EILKNFSQASLK 225
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
26-194 |
2.41e-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: 43.32 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 26 GLIVAGIAL---ILNAASDTFMLSLLKPLLDDGFGKTDRSVL--------------LWM-PLVVIGLMIVRGLTSYVSSY 87
Cdd:cd18599 1 GYVVFLFVLllfILSVGSTVFSDWWLSYWLKQGSGNTTNNVDnstvdsgnisdnpdLNFyQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 88 CISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIG-LFIMMFYYSW- 165
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFsLIIIAIVFPWf 160
|
170 180 190
....*....|....*....|....*....|....
gi 740854059 166 -----QLSLILIVLAPIVSVAIRVVsKRFRSISK 194
Cdd:cd18599 161 lialiPLAIIFVFLSKIFRRAIREL-KRLENISR 193
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-384 |
4.78e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.14 E-value: 4.78e-04
10 20
....*....|....*....|....*.
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKST 384
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKST 650
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
481-549 |
8.34e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 8.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 481 LSGGQRQRIAIARALLRDSP---ILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTIEQADEII 549
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
470-570 |
1.01e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.64 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADE 547
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHE 213
|
90 100
....*....|....*....|...
gi 740854059 548 IIVVEDGVIVERGTHNELIEQRG 570
Cdd:NF000106 214 LTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
358-512 |
2.08e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 358 ALRNINLNIPAGKTVALVGRSGSGKSTIASLITRFYDIDEGQIL-----MDGHDLreytlaSLRDQVALVSQNVHLFND- 431
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWlfgqpVDAGDI------ATRRRVGYMSQAFSLYGEl 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 432 TVANNIA-YARtdLY--SREQIEKA-AQMAyaMDFinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
Cdd:NF033858 355 TVRQNLElHAR--LFhlPAAEIAARvAEML--ERF------DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
....*
gi 740854059 508 TSALD 512
Cdd:NF033858 425 TSGVD 429
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-386 |
2.88e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.78 E-value: 2.88e-03
10 20
....*....|....*....|....*...
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIA 386
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSLA 43
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
359-386 |
2.96e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.83 E-value: 2.96e-03
10 20
....*....|....*....|....*...
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIA 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 |
3.04e-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: 40.77 E-value: 3.04e-03
10 20
....*....|....*....|....*...
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKSTIA 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; ... |
60-194 |
3.15e-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: 39.76 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 60 DRSVLLWMPL-VVIGLM-IVRGLTSYVSSYCISWVSGKvvmTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVAS 137
Cdd:cd18604 39 EVSVLYYLGIyALISLLsVLLGTLRYLLFFFGSLRASR---KLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDS 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740854059 138 SSSGALITVVREGASIIGLFIMMFYYSWQLSLILIVLAPI-VSVAIRVVS-----KRFRSISK 194
Cdd:cd18604 116 ELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALyVYIGRLYLRasrelKRLESVAR 178
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
475-552 |
3.33e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740854059 475 GENGVLLSGGQRQRIAIARAL----LRDSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTIEQADEII 549
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQfIVITLKKEMFENADKLI 168
|
...
gi 740854059 550 VVE 552
Cdd:cd03239 169 GVL 171
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
359-384 |
3.56e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 3.56e-03
10 20
....*....|....*....|....*.
gi 740854059 359 LRNINLNIPAGKTVALVGRSGSGKST 384
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKST 646
|
|
| |
