|
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: 1263.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 1 MQNDKDLSTWQTFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGV 80
Cdd:PRK11176 1 MHNDKDLSTWQTFRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 81 TSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMM 160
Cdd:PRK11176 81 TSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 161 FYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQ 240
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 241 GMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
Cdd:PRK11176 241 GMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 321 ILDSEQEKDEGKLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI 400
Cdd:PRK11176 321 ILDLEQEKDEGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 401 LLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVL 480
Cdd:PRK11176 401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
|
570 580
....*....|....*....|..
gi 1336523670 561 SHADLLEHRGVYAQLHKMQFGQ 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: 897.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 12 TFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISW 91
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 92 VSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLIL 171
Cdd:TIGR02203 81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 172 IVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSIS 251
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 252 DPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEG 331
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDTG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 332 KLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT 411
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 412 LASLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGL 560
|
570
....*....|.
gi 1336523670 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: 675.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 8 STWQTFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSY 87
Cdd:COG1132 4 SPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 88 CISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQL 167
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 168 SLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSA 247
Cdd:COG1132 164 ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 248 SSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQE 327
Cdd:COG1132 244 SALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 328 KDE--GKLVIERAKGNLEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH 405
Cdd:COG1132 324 IPDppGAVPLPPVRGEIEFENVSFSYPG-DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 406 DLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQ 485
Cdd:COG1132 403 DIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQ 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADL 565
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEEL 561
|
570
....*....|....*..
gi 1336523670 566 LEHRGVYAQLHKMQFGQ 582
Cdd:COG1132 562 LARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-579 |
1.14e-167 |
|
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: 493.58 E-value: 1.14e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 12 TFRRLWPLIAPFKTGLIVAAVALVFNAasdtfMLSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISS 86
Cdd:COG2274 143 GLRWFLRLLRRYRRLLLQVLLASLLIN-----LLALATPLFtqvviDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRS 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 87 YCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQ 166
Cdd:COG2274 218 YLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPP 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 167 LSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVS 246
Cdd:COG2274 297 LALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRR 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 247 ASSISDPVIQLIASLALAFVLYAASFpSVME-TLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFAILDS 324
Cdd:COG2274 377 LSNLLSTLSGLLQQLATVALLWLGAY-LVIDgQLTLGQL-IAFNILSGrFLAPVAQLIGLLQRFQDAKIALERLDDILDL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 325 EQEKDEG--KLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILL 402
Cdd:COG2274 455 PPEREEGrsKLSLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 403 DGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLS 482
Cdd:COG2274 535 DGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD-PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLS 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 483 GGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSH 562
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTH 693
|
570
....*....|....*..
gi 1336523670 563 ADLLEHRGVYAQLHKMQ 579
Cdd:COG2274 694 EELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
342-576 |
1.19e-146 |
|
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: 422.02 E-value: 1.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGA-TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLH 576
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
14-580 |
6.34e-140 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 417.95 E-value: 6.34e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 14 RRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVS 93
Cdd:TIGR02204 7 AALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 94 GKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIV 173
Cdd:TIGR02204 87 ERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 174 LAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:TIGR02204 167 AVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 254 VIQLIASLALAFVLYAASFPSVMETLTAGTIT-VVFSSMIALMrPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDE-- 330
Cdd:TIGR02204 247 IVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGqFVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKApa 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 331 -GKLVIERAKGNLEFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR 408
Cdd:TIGR02204 326 hPKTLPVPLRGEIEFEQVNFAYPARpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 409 EYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQR 488
Cdd:TIGR02204 406 QLDPAELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:TIGR02204 485 IAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK 564
|
570
....*....|..
gi 1336523670 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 |
5.06e-133 |
|
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: 401.12 E-value: 5.06e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 6 DLSTWQTFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDrsVLLWMPlvvIGLMLLRGVTSYIS 85
Cdd:COG5265 17 DLLLRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLSGAA--ALLVVP---VGLLLAYGLLRLLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 86 SYCISW---VSGKVVM-TMRR---RLFSHMMGMPVSF-FDKQSTGtlLSRI----TYDSEQVASSSSSALITVVREGASI 153
Cdd:COG5265 92 VLFGELrdaLFARVTQrAVRRlalEVFRHLHALSLRFhLERQTGG--LSRDiergTKGIEFLLRFLLFNILPTLLEIALV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 154 IGLFVmmFYYSWQLSLILIV-LAPIVSMAIRVVSKRFRnISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDK 232
Cdd:COG5265 170 AGILL--VKYDWWFALITLVtVVLYIAFTVVVTEWRTK-FRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 233 VSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGM 312
Cdd:COG5265 247 ALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQAL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 313 AACQTLFAILDSEQE----KDEGKLVIERakGNLEFKDVTFTY-PGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIAS 387
Cdd:COG5265 327 ADMERMFDLLDQPPEvadaPDAPPLVVGG--GEVRFENVSFGYdPER--PILKGVSFEVPAGKTVAIVGPSGAGKSTLAR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 388 LITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMD 467
Cdd:COG5265 403 LLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGR-PDASEEEVEAAARAAQIHDFIESLP 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 468 NGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADE 547
Cdd:COG5265 482 DGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADE 561
|
570 580 590
....*....|....*....|....*....|..
gi 1336523670 548 IVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:COG5265 562 ILVLEAGRIVERGTHAELLAQGGLYAQMWARQ 593
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-570 |
7.72e-128 |
|
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: 386.42 E-value: 7.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 14 RRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGF-GKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWV 92
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIiGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 93 SGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILI 172
Cdd:COG4988 86 AARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 173 VLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISD 252
Cdd:COG4988 166 VTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLSS 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 253 PVIQLIASLALAFVLYAASFpsvmeTLTAGTITVvFSSMIALM------RPLKSLtnvNAQF---QRGMAACQTLFAILD 323
Cdd:COG4988 246 AVLEFFASLSIALVAVYIGF-----RLLGGSLTL-FAALFVLLlapeffLPLRDL---GSFYharANGIAAAEKIFALLD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 324 SEQEKDEGKLVIERAKGN--LEFKDVTFTYPGREtPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQIL 401
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPpsIELEDVSFSYPGGR-PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 402 LDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLL 481
Cdd:COG4988 396 INGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR-PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 482 SGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGS 561
Cdd:COG4988 475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554
|
....*....
gi 1336523670 562 HADLLEHRG 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 |
2.19e-122 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 360.32 E-value: 2.19e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03249 2 EFKNVSFRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDA-TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
12-577 |
8.78e-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: 360.62 E-value: 8.78e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 12 TFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSL---------LKPLLDDgfgktdrsvlLWMPLV-VIGLMLLRGVT 81
Cdd:COG4987 2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGIGLLALsgwliaaaaLAPPILN----------LFVPIVgVRAFAIGRTVF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 82 SYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMF 161
Cdd:COG4987 72 RYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 162 YYSWQLSLIL-------IVLAPIVSMAIRvvskrfRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVS 234
Cdd:COG4987 152 FFSPALALVLalglllaGLLLPLLAARLG------RRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 235 NKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:COG4987 226 ARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 315 CQTLFAILDSE-QEKDEGKLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFY 393
Cdd:COG4987 306 ARRLNELLDAPpAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 394 DIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTV 473
Cdd:COG4987 386 DPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLAR-PDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 474 IGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVED 553
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
570 580
....*....|....*....|....
gi 1336523670 554 GRIVERGSHADLLEHRGVYAQLHK 577
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-575 |
1.95e-113 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 354.03 E-value: 1.95e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 14 RRLWPLiapfktgLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTD-----RSVLLwMPLVVIGLMLLRGVtsyiSSYC 88
Cdd:TIGR00958 157 GRDWPW-------LISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGppalaSAIFF-MCLLSIASSVSAGL----RGGS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 89 ISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLS 168
Cdd:TIGR00958 225 FNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLT 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 169 LILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSAS 248
Cdd:TIGR00958 305 MVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAY 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 249 SISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSE-QE 327
Cdd:TIGR00958 385 AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKpNI 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 328 KDEGKLVIERAKGNLEFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD 406
Cdd:TIGR00958 465 PLTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 407 LREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEeYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQR 486
Cdd:TIGR00958 545 LVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD-TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQK 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAalDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLL 566
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLM 701
|
....*....
gi 1336523670 567 EHRGVYAQL 575
Cdd:TIGR00958 702 EDQGCYKHL 710
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-579 |
1.82e-111 |
|
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: 332.66 E-value: 1.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTY-PGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVA 420
Cdd:cd03253 1 IEFENVTFAYdPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSP 500
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGR-PDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 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 |
4.10e-104 |
|
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: 315.52 E-value: 4.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 267 LYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 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 |
6.06e-103 |
|
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: 310.31 E-value: 6.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYpGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGR-PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRG 570
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
69-581 |
3.04e-95 |
|
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: 305.90 E-value: 3.04e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 69 LVVIGL-MLLRGVT----SYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSAL 143
Cdd:TIGR01846 178 LSVLALaMLAVAIFepalGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVR-ELEQIRNFLTGSA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 144 ITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFR-----NISKNMQNTMGQV-TTSAEQMLKGhkev 217
Cdd:TIGR01846 257 LTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRkrvedKFERSAAATSFLVeSVTGIETIKA---- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 218 lmfggQAVE---TKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTItVVFSsMIA- 293
Cdd:TIGR01846 333 -----TATEpqfQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQL-VAFN-MLAg 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 294 -LMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQE-KDEGKLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKT 371
Cdd:TIGR01846 406 rVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEpRSAGLAALPELRGAITFENIRFRYAPDSPEVLSNLNLDIKPGEF 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 372 VALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEeYSREQIE 451
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG-APFEHVI 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 452 EAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRT 531
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRT 644
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 532 SLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQFG 581
Cdd:TIGR01846 645 VIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
101-580 |
3.10e-95 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 302.65 E-value: 3.10e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 101 RRRL------FSHMMGMPVSFFDKQSTGTLLsritydseQVASSSSSALITV----VREG-ASIIGLFVMM---FYYSWQ 166
Cdd:PRK13657 86 RRRLavlteyFERIIQLPLAWHSQRGSGRAL--------HTLLRGTDALFGLwlefMREHlATLVALVVLLplaLFMNWR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 167 LSLILIVLAPIVSMAIRVVSKRfrniSKNMQNTMGQVTTSaeqmLKGHKEvlmfggqavetkrfDKVSNKMRLQGMKMVS 246
Cdd:PRK13657 158 LSLVLVVLGIVYTLITTLVMRK----TKDGQAAVEEHYHD----LFAHVS--------------DAIGNVSVVQSYNRIE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 247 A--SSISDPVIQLIAS-------LALAFVL-YAASFPSVMETLTAGTI-----------TVVFSSMIALM-RPLKSLTN- 303
Cdd:PRK13657 216 AetQALRDIADNLLAAqmpvlswWALASVLnRAASTITMLAILVLGAAlvqkgqlrvgeVVAFVGFATLLiGRLDQVVAf 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 304 VNAQFQRGmAACQTLFAILDSEQEKDE--GKLVIERAKGNLEFKDVTFTYPGReTPALRNIDLNIQEGKTVALVGRSGSG 381
Cdd:PRK13657 296 INQVFMAA-PKLEEFFEVEDAVPDVRDppGAIDLGRVKGAVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 382 KSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMD 461
Cdd:PRK13657 374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR-PDATDEEMRAAAERAQAHD 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 462 FISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLST 541
Cdd:PRK13657 453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532
|
490 500 510
....*....|....*....|....*....|....*....
gi 1336523670 542 IEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQF 580
Cdd:PRK13657 533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-575 |
5.68e-93 |
|
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: 300.32 E-value: 5.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 19 LIAPfktGLIVAAVALVFnaaSDTFML----SLLKPLLddgfgktdrsvllwmpLVVIGLMLLRGVTSYISSYCISWVSG 94
Cdd:TIGR03796 166 LVLP---GLVIPAFSQIF---VDEILVqgrqDWLRPLL----------------LGMGLTALLQGVLTWLQLYYLRRLEI 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 95 KVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDsEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVL 174
Cdd:TIGR03796 224 KLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQLN-DQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 175 APIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAeqmlkghkevlMFGGQAVETKR--------FDKVSN---KMRLQGMK 243
Cdd:TIGR03796 303 AAINVLALQLVSRRRVDANRRLQQDAGKLTGVA-----------ISGLQSIETLKasglesdfFSRWAGyqaKLLNAQQE 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 244 MVSASSISDPVIQLIASLALAFVLYAASFpSVME-TLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIL 322
Cdd:TIGR03796 372 LGVLTQILGVLPTLLTSLNSALILVVGGL-RVMEgQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVL 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 323 DSEQEKDEGKLVI--------ERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYD 394
Cdd:TIGR03796 451 RNPVDPLLEEPEGsaatseppRRLSGYVELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 395 IDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIA-YARTeeYSREQIEEAARMAYAMDFISKMDNGLDTV 473
Cdd:TIGR03796 531 PWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTlWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAE 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 474 IGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAHRLSTIEQADEIVVVED 553
Cdd:TIGR03796 609 LAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEIIVLER 686
|
570 580
....*....|....*....|..
gi 1336523670 554 GRIVERGSHADLLEHRGVYAQL 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 |
1.22e-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: 284.38 E-value: 1.22e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03252 81 VLQENVLFNRSIRDNIALAD-PGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
342-555 |
1.25e-91 |
|
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: 278.88 E-value: 1.25e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03228 81 VPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGR 555
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-579 |
1.99e-85 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 277.37 E-value: 1.99e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 1 MQNDKDLstWQTFRRLWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVV--IGLMLLR 78
Cdd:PRK10790 1 MRSFSQL--WPTLKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKGNLPLGLVAGLAAayVGLQLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 79 GVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFV 158
Cdd:PRK10790 79 AGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 159 MMFYYSWQLSLILIVLAPIVsMAIRVVSKRFRN-ISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSN-- 235
Cdd:PRK10790 159 AMFSLDWRMALVAIMIFPAV-LVVMVIYQRYSTpIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRsh 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 236 -KMRLQGMKMvsASSISDPVIQLIASLALAFVLYAASFPSVmETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:PRK10790 238 yMARMQTLRL--DGFLLRPLLSLFSALILCGLLMLFGFSAS-GTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 315 CQTLFAILDSEQEkDEGKLVIERAKGNLEFKDVTFTYpGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYD 394
Cdd:PRK10790 315 GERVFELMDGPRQ-QYGNDDRPLQSGRIDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 395 IDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARteEYSREQIEEAARMAYAMDFISKMDNGLDTVI 474
Cdd:PRK10790 393 LTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR--DISEEQVWQALETVQLAELARSLPDGLYTPL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 475 GENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDG 554
Cdd:PRK10790 471 GEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRG 550
|
570 580
....*....|....*....|....*
gi 1336523670 555 RIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:PRK10790 551 QAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
44-579 |
7.10e-85 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 275.05 E-value: 7.10e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 44 MLSLLKPLLD----DGF---GKTDRSVLLWmplvvIGLMLLRGVTSYISSYCisW------VSGKVVMTMRRRLFSHMMG 110
Cdd:PRK10789 9 MLQLIPPKVVgiivDGVteqHMTTGQILMW-----IGTMVLIAVVVYLLRYV--WrvllfgASYQLAVELREDFYRQLSR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 111 MPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRE---GASIigLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSK 187
Cdd:PRK10789 82 QHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSlvmGCAV--LIVMSTQISWQLTLLALLPMPVMAIMIKRYGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVL 267
Cdd:PRK10789 160 QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 268 YAASFPSVMETLTAGTIT---VVFSSMIALMRPLKSLTNVnaqFQRGMAACQTLFAILDSEQEKDEGKLVIERAKGNLEF 344
Cdd:PRK10789 240 GGGSWMVVNGSLTLGQLTsfvMYLGLMIWPMLALAWMFNI---VERGSAAYSRIRAMLAEAPVVKDGSEPVPEGRGELDV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQ 424
Cdd:PRK10789 317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 NVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDA-TQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILIL 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 505 DEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
151-576 |
6.81e-83 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 270.16 E-value: 6.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 151 ASIIGLFVMMFYYSW---QLSLILIVLAPIVSMAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVE 226
Cdd:PRK11160 143 AALVVILVLTIGLSFfdlTLALTLGGILLLLLLLLPLLFYRLgKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRY 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 227 TKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFpSVMETLTAGTIT--VVFSSMIALmrplKSLTNV 304
Cdd:PRK11160 223 RQQLEQTEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAAG-GVGGNAQPGALIalFVFAALAAF----EALMPV 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 305 NAQFQ---RGMAACQTLFAILdsEQEKD---EGKLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRS 378
Cdd:PRK11160 298 AGAFQhlgQVIASARRINEIT--EQKPEvtfPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRT 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 379 GSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYArTEEYSREQIEEAARMAy 458
Cdd:PRK11160 376 GCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLA-APNASDEALIEVLQQV- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 459 AMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
Cdd:PRK11160 454 GLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHR 533
|
410 420 430
....*....|....*....|....*....|....*...
gi 1336523670 539 LSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLH 576
Cdd:PRK11160 534 LTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
56-551 |
1.77e-82 |
|
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: 267.62 E-value: 1.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 56 FGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQV 135
Cdd:TIGR02857 35 SAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 136 ASSSSSALITVVRegASIIGLFVM--MFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKG 213
Cdd:TIGR02857 115 DGYFARYLPQLVL--AVIVPLAILaaVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 214 HKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFpsvmeTLTAGTITVVFSSMIA 293
Cdd:TIGR02857 193 LPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGF-----RLLAGDLDLATGLFVL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 294 LMRP--LKSLTNVNAQF---QRGMAACQTLFAILDS-EQEKDEGKLVIERAKGNLEFKDVTFTYPGReTPALRNIDLNIQ 367
Cdd:TIGR02857 268 LLAPefYLPLRQLGAQYharADGVAAAEALFAVLDAaPRPLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVP 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 368 EGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEySR 447
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDA-SD 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 448 EQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ 527
Cdd:TIGR02857 426 AEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
|
490 500
....*....|....*....|....
gi 1336523670 528 KNRTSLVIAHRLSTIEQADEIVVV 551
Cdd:TIGR02857 506 QGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
331-556 |
5.30e-82 |
|
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: 256.24 E-value: 5.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 331 GKLVIERAKGNLEFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLRE 409
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 410 YTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRI 489
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSC-SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
44-579 |
5.11e-79 |
|
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: 262.59 E-value: 5.11e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 44 MLSLLKP-----LLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDK 118
Cdd:TIGR03797 150 LLGMLVPiatgiLIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLRLPVSFFRQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 119 QSTGTLLSRITYDSEQVASSSSSALITVVregASIIGLF--VMMFYYSWQLSLILIVLApIVSMAIRVVSKrFRNISKN- 195
Cdd:TIGR03797 230 YSTGDLASRAMGISQIRRILSGSTLTTLL---SGIFALLnlGLMFYYSWKLALVAVALA-LVAIAVTLVLG-LLQVRKEr 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 196 -MQNTMGQVTTSAEQMLKGHKEVLMFGGQ----AVETKRFDKvSNKMRLQGMKMVSASSISDPVIQLIASLALafvLYAA 270
Cdd:TIGR03797 305 rLLELSGKISGLTVQLINGISKLRVAGAEnrafARWAKLFSR-QRKLELSAQRIENLLTVFNAVLPVLTSAAL---FAAA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 271 SFPSVMETLTAGTI---TVVFSSMIALMRPL-KSLTNVNA---QFQRgmaaCQtlfAILDSEQEKDEGKLVIERAKGNLE 343
Cdd:TIGR03797 381 ISLLGGAGLSLGSFlafNTAFGSFSGAVTQLsNTLISILAvipLWER----AK---PILEALPEVDEAKTDPGKLSGAIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 344 FKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVS 423
Cdd:TIGR03797 454 VDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILI 503
Cdd:TIGR03797 534 QNGRLMSGSIFENIA--GGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILL 611
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 504 LDEATSALDTESERAIQAALDELQKNRtsLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHKMQ 579
Cdd:TIGR03797 612 FDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
340-560 |
2.01e-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: 2.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAYARTEeYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPL-ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
98-577 |
7.89e-73 |
|
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: 244.03 E-value: 7.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 98 MTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPI 177
Cdd:TIGR01192 89 ATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIVLMVLGIL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 178 VSMAIRVVSKRFRN----ISKNMQNTMGQVTTSAEQMLKGHKevlmFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDP 253
Cdd:TIGR01192 169 YILIAKLVMQRTKNgqaaVEHHYHNVFKHVSDSISNVSVVHS----YNRIEAETSALKQFTNNLLSAQYPVLDWWALASG 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 254 VIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGKL 333
Cdd:TIGR01192 245 LNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPAD 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 334 VIE--RAKGNLEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT 411
Cdd:TIGR01192 325 APElpNVKGAVEFRHITFEFAN-SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVT 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 412 LASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:TIGR01192 404 RESLRKSIATVFQDAGLFNRSIRENIRLGR-EGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAI 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:TIGR01192 483 ARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGR 562
|
....*.
gi 1336523670 572 YAQLHK 577
Cdd:TIGR01192 563 FYKLLR 568
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
340-561 |
2.25e-71 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 228.53 E-value: 2.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD--PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGS 561
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
279-568 |
4.89e-66 |
|
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: 225.01 E-value: 4.89e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 279 LTAGTItvvFSSMIALMR---PLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGkLVIERAKGNLEFKDVTFTYPGRE 355
Cdd:COG4618 269 ITPGAM---IAASILMGRalaPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPER-MPLPRPKGRLSVENLTVVPPGSK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVAN 435
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 436 NIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:COG4618 425 NIA--RFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 516 ERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG4618 503 EAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
27-314 |
1.18e-65 |
|
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: 215.88 E-value: 1.18e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1336523670 267 LYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALAS 288
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-575 |
2.02e-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: 226.54 E-value: 2.02e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 16 LWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLKPLLDdgfgktdrsvllwmpLVVIGLM---LLRGVTSYISSYCISWV 92
Cdd:TIGR01193 159 VNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKMMGTLG---------------IISIGLIiayIIQQILSYIQIFLLNVL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 93 SGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILI 172
Cdd:TIGR01193 224 GQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 173 VLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISD 252
Cdd:TIGR01193 303 LSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQ 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 253 P---VIQLIASLalaFVLYAASFPSVMETLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAACQTLFAIL--DSEQ 326
Cdd:TIGR01193 383 AikaVTKLILNV---VILWTGAYLVMRGKLTLGQL-ITFNALLSyFLTPLENIINLQPKLQAARVANNRLNEVYlvDSEF 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 327 EKDEGKLVIERAKGNLEFKDVTFTYpGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD 406
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 407 LREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQR 486
Cdd:TIGR01193 538 LKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQkNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLL 566
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL 696
|
....*....
gi 1336523670 567 EHRGVYAQL 575
Cdd:TIGR01193 697 DRNGFYASL 705
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
100-539 |
5.08e-62 |
|
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: 213.38 E-value: 5.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 100 MRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVS 179
Cdd:TIGR02868 88 LRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAG 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 180 MAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLI 258
Cdd:TIGR02868 168 FVAPLVSLRAaRAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 259 ASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSEQEKDEGklVIERA 338
Cdd:TIGR02868 248 AGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEG--SAPAA 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 339 KG------NLEFKDVTFTYPGREtPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL 412
Cdd:TIGR02868 326 GAvglgkpTLELRDLSAGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQ 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 413 ASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:TIGR02868 405 DEVRRRVSVCAQDAHLFDTTVRENLRLAR-PDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL 539
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-565 |
6.30e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 219.13 E-value: 6.30e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 8 STWQTFRRL----WPLIAPFK-------TGLIVAAVALVFNAASDTFMLSLLKPLLDD-GFGKTDRSVLLwmPLVVIGLM 75
Cdd:PTZ00265 32 GTFELYKKIktqkIPFFLPFKclpashrKLLGVSFVCATISGGTLPFFVSVFGVIMKNmNLGENVNDIIF--SLVLIGIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 76 LLrgVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIG 155
Cdd:PTZ00265 110 QF--ILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 156 LFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRnISKNM-----QNTMGQVttsaEQMLKGHKEVLMFGGQAVETKRF 230
Cdd:PTZ00265 188 LYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-INKKTsllynNNTMSII----EEALVGIRTVVSYCGEKTILKKF 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 231 DkVSNKmrLQGMKMVSASSISDPVIQLIASLALAFvlYAASF----PSVMETLT----------AGTITVVFSSMIALMR 296
Cdd:PTZ00265 263 N-LSEK--LYSKYILKANFMESLHIGMINGFILAS--YAFGFwygtRIIISDLSnqqpnndfhgGSVISILLGVLISMFM 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 297 PLKSLTNVNaQFQRGMAACQTLFAILDSE---QEKDEGKLVIERAKgnLEFKDVTFTYPGRETPAL-RNIDLNIQEGKTV 372
Cdd:PTZ00265 338 LTIILPNIT-EYMKSLEATNSLYEIINRKplvENNDDGKKLKDIKK--IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 373 ALVGRSGSGKSTIASLITRFYDIDNGQILL-DGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYA----RTEEYSR 447
Cdd:PTZ00265 415 AFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslKDLEALS 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 448 EQIEE------------------------------------AARMAYAM----------------DFISKMDNGLDTVIG 475
Cdd:PTZ00265 495 NYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTikdsevvdvskkvlihDFVSALPDKYETLVG 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 476 ENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIVVVED 553
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
|
650
....*....|..
gi 1336523670 554 GrivERGSHADL 565
Cdd:PTZ00265 655 R---ERGSTVDV 663
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
153-575 |
4.16e-59 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 207.00 E-value: 4.16e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 153 IIGLFVmmFYYSWQLSLILIVLAPIVSMAIRVV------SKRfrnisKNMQnTMGQVttSAEQM--LKGHKEVLMFGGQA 224
Cdd:PRK11174 153 LILIAV--FPINWAAGLILLGTAPLIPLFMALVgmgaadANR-----RNFL-ALARL--SGHFLdrLRGLETLRLFNRGE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 225 VETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASL--ALAFVLYAASFPSVMETLTAGTITVVFSSMIALM------R 296
Cdd:PRK11174 223 AETESIRSASEDFRQRTMEVLRMAFLSSAVLEFFASIsiALVAVYFGFSYLGELNFGHYGTGVTLFAGFFVLIlapefyQ 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 297 PLKSL-TNVNAQFQrGMAACQTLFAILDSE-QEKDEGKLVIERAKGN-LEFKD-VTFTYPGreTPALRNIDLNIQEGKTV 372
Cdd:PRK11174 303 PLRDLgTFYHAKAQ-AVGAAESLVTFLETPlAHPQQGEKELASNDPVtIEAEDlEILSPDG--KTLAGPLNFTLPAGQRI 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 373 ALVGRSGSGKSTIASLITRF--YdidNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQI 450
Cdd:PRK11174 380 ALVGPSGAGKTSLLNALLGFlpY---QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN-PDASDEQL 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 451 EEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR 530
Cdd:PRK11174 456 QQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ 535
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1336523670 531 TSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQL 575
Cdd:PRK11174 536 TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
342-560 |
5.39e-57 |
|
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: 189.06 E-value: 5.39e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTlASLRDQVAL 421
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfiskmdngldtvigenGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03247 80 LNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
27-298 |
2.65e-56 |
|
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: 190.93 E-value: 2.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRL 104
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLpdGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 105 FSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRV 184
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALA 264
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1336523670 265 FVLYAASFPSVMETLTAGTITVVFSSMIALMRPL 298
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
2.20e-54 |
|
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: 192.43 E-value: 2.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR---ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRD- 417
Cdd:COG1123 261 LEVRNLSKRYPVRgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREl 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 --QVALVSQN-VHLFN--DTVANNIAYA--RTEEYSREQIEEaaRMAYAMDFIskmdnGLDT-VIGENGVLLSGGQRQRI 489
Cdd:COG1123 341 rrRVQMVFQDpYSSLNprMTVGDIIAEPlrLHGLLSRAERRE--RVAELLERV-----GLPPdLADRYPHELSGGQRQRV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVF 493
|
..
gi 1336523670 567 EH 568
Cdd:COG1123 494 AN 495
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-568 |
3.76e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 192.56 E-value: 3.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 20 IAPFKTGLIVAAVALVF----NAASDTFMLSLLKPLLDDGFGKTdrsvLLWMPLVVIGLMLLRGVTSYISSYCISWVSGK 95
Cdd:TIGR01842 1 LAKVKRTFIIVGLFSFVinilMLAPPLYMLQVYDRVLTSGSVPT----LLMLTVLALGLYLFLGLLDALRSFVLVRIGEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 96 VVMTMRRRLFSHMMGMPVSFFDKQSTGTLlsritYDSEQVAS-SSSSALITVVREGASIIGLFVMMFYYSWqlSLILIVL 174
Cdd:TIGR01842 77 LDGALNQPIFAASFSATLRRGSGDGLQAL-----RDLDQLRQfLTGPGLFAFFDAPWMPIYLLVCFLLHPW--IGILALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 175 APIVSMAIRVVSKRF--RNISKNMQNTMgQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMK------MVS 246
Cdd:TIGR01842 150 GAVVLVGLALLNNRAtkKPLKEATEASI-RANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAasdragMLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 247 ASSISDPVIQLIASLALAFVLyaasfpSVMETLTAGTItvVFSSMIA--LMRPLKSLTNVNAQFQRGMAACQTLFAILDS 324
Cdd:TIGR01842 229 NLSKYFRIVLQSLVLGLGAYL------AIDGEITPGMM--IAGSILVgrALAPIDGAIGGWKQFSGARQAYKRLNELLAN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 325 EQEKDEgKLVIERAKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDG 404
Cdd:TIGR01842 301 YPSRDP-AMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 405 HDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGG 484
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG-ENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQADEIVVVEDGRIVERGSHA 563
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERD 538
|
....*
gi 1336523670 564 DLLEH 568
Cdd:TIGR01842 539 EVLAK 543
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
342-569 |
4.10e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 183.30 E-value: 4.10e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVH--LFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRN 498
Cdd:COG1122 80 VFQNPDdqLFAPTVEEDVAFGpENLGLPREEIRE--RVEEALELV-----GLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEHR 569
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
65-578 |
1.43e-53 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 197.17 E-value: 1.43e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 65 LWMPLVVIGLMLLRGVTSYISSYciswVSGKVVMTMRRRLFSHMMGMPVSFFD--KQSTGTLLSRITYDSEqvasssssA 142
Cdd:PTZ00265 870 LYILVIAIAMFISETLKNYYNNV----IGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH--------L 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 143 LITVVREGASIIGLFVMMFYYSWQLS-----LILIVLAPIVSMAIRVVSKRFR-----NISKNMQNTMGQV--TTSAEQM 210
Cdd:PTZ00265 938 LKTGLVNNIVIFTHFIVLFLVSMVMSfyfcpIVAAVLTGTYFIFMRVFAIRARltankDVEKKEINQPGTVfaYNSDDEI 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 211 LK-----------GHKEVLMFGGQAVETKRFDK-VSNKMRLQGMKMVSASSI---SDPVIQLIASLALAFVLYAASFPSV 275
Cdd:PTZ00265 1018 FKdpsfliqeafyNMNTVIIYGLEDYFCNLIEKaIDYSNKGQKRKTLVNSMLwgfSQSAQLFINSFAYWFGSFLIRRGTI 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 276 -METLTAGTITVVFSSMIA--LMRPLKSLTNVNAQFQRgMAACQTLFAILDSeqeKDEGKLVIERA---KGNLEFKDVTF 349
Cdd:PTZ00265 1098 lVDDFMKSLFTFLFTGSYAgkLMSLKGDSENAKLSFEK-YYPLIIRKSNIDV---RDNGGIRIKNKndiKGKIEIMDVNF 1173
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 350 TYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDN------------------------------- 397
Cdd:PTZ00265 1174 RYISRpNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmk 1253
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 398 -----------------------GQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARtEEYSREQIEEAA 454
Cdd:PTZ00265 1254 nvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-EDATREDVKRAC 1332
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 455 RMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTS 532
Cdd:PTZ00265 1333 KFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTI 1412
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 533 LVIAHRLSTIEQADEIVVVED----GRIVE-RGSHADLLE-HRGVYAQLHKM 578
Cdd:PTZ00265 1413 ITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
343-555 |
3.01e-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: 180.36 E-value: 3.01e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQN--VHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfiSKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:cd03225 81 FQNpdDQFFGPTVEEEVAFGlENLGLPEEEIEERVEEALEL---VGLEGLRDRSPFT----LSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI-EQADEIVVVEDGR 555
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLlELADRVIVLEDGK 211
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
27-315 |
1.18e-51 |
|
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: 179.12 E-value: 1.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGF--GKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRL 104
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDDYIvpGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 105 FSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRV 184
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALA 264
Cdd:cd18544 161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 265 FVLYAASFPSVMETLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18544 241 LVLWYGGGQVLSGAVTLGVL-YAFIQYIQrFFRPIRDLAEKFNILQSAMASA 291
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
342-556 |
1.76e-51 |
|
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: 174.33 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03246 81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
342-556 |
1.70e-49 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.38 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:COG4619 1 LELEGLSFRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIAYA---RTEEYSREQIEEA-ARMAYAMDFiskmdngLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPfqlRERKFDRERALELlERLGLPPDI-------LDKPVER----LSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
27-316 |
3.11e-49 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 172.62 E-value: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 267 LYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAE 290
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
27-314 |
5.70e-49 |
|
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: 171.82 E-value: 5.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDD------GFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTM 100
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIDLiieglgGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 101 RRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSM 180
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 181 AIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIAS 260
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 261 LALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAG 294
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
342-568 |
7.41e-48 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 174.71 E-value: 7.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID---NGQILLDGHDLREYTLASLRDQ 418
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQN--VHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfiskmdNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:COG1123 85 IGMVFQDpmTQLNPVTVGDQIAEAlENLGLSRAEARARVLELLEA-------VGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
8.78e-47 |
|
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: 166.15 E-value: 8.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDD---------------GFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISW 91
Cdd:cd18564 1 LALALLALLLETALRLLEPWPLKVVIDDvlgdkplpgllglapLLGPDPLALLLLAAAALVGIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 92 VSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLIL 171
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 172 IVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSIS 251
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 252 DPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAE 305
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
340-561 |
2.96e-46 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 161.81 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03369 5 GEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARmayamdfiskmdngldtvIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD--PFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGS 561
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
112-577 |
3.74e-46 |
|
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: 175.13 E-value: 3.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRN 191
Cdd:TIGR00957 1052 PMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQ 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 192 ISKNMQNTMGQVTTSAEQMLKGHKEVLMFGgqavETKRFDKVSNKMRLQGMKMVSASSISDPVIQL-IASLALAFVLYAA 270
Cdd:TIGR00957 1132 LKRLESVSRSPVYSHFNETLLGVSVIRAFE----EQERFIHQSDLKVDENQKAYYPSIVANRWLAVrLECVGNCIVLFAA 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 271 SFPSV-METLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAIldSEQEKDEGKLVIERA-------KGNL 342
Cdd:TIGR00957 1208 LFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEY--SETEKEAPWQIQETAppsgwppRGRV 1285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:TIGR00957 1286 EFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITII 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPIL 502
Cdd:TIGR00957 1366 PQDPVLFSGSLRMNLD--PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKIL 1443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 503 ILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQLHK 577
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
342-560 |
1.06e-45 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 160.75 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLR 416
Cdd:cd03257 2 LEVKNLSVSFPtgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllkLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DQVALVSQNVHL-FND--TVanniayarteeysREQIEEAARMAYAMD----FISKMDNGLDTVIGENGVL------LSG 483
Cdd:cd03257 82 KEIQMVFQDPMSsLNPrmTI-------------GEQIAEPLRIHGKLSkkeaRKEAVLLLLVGVGLPEEVLnrypheLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-555 |
2.78e-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: 158.79 E-value: 2.78e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRET---PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHdlreytlaslrdq 418
Cdd:cd03250 1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFNDTVANNIAYArtEEYSREQIEEAARmAYAMDF-ISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG--KPFDEERYEKVIK-ACALEPdLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 498 NSPILILDEATSALDTESERAI--QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGR 555
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
342-561 |
1.30e-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: 157.73 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDI-----DNGQILLDGHDLRE--YTLAS 414
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFISKMDNGLDtvigengvlLSGGQRQR 488
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQA----DEIVVVEDGRIVERGS 561
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH---NMQQAarvaDRTAFLLNGRLVEFGP 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
342-558 |
1.53e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.51 E-value: 1.53e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKST---IASLITRFydiDNGQILLDGHD---LREYTLA 413
Cdd:COG1136 5 LELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDRP---TSGEVLIDGQDissLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 414 SLR-DQVALVSQNVHLFND-TVANNIAYARteEYSREQIEEAARMAYAMdfiskmdngLDTV---------IGEngvlLS 482
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPElTALENVALPL--LLAGVSRKERRERAREL---------LERVglgdrldhrPSQ----LS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 483 GGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
359-509 |
5.48e-44 |
|
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: 153.57 E-value: 5.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFND-TVANNI 437
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 438 AYARTEEYsREQIEEAARMAYAMDFISkMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:pfam00005 81 RLGLLLKG-LSKREKDARAEEALEKLG-LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
342-568 |
6.84e-44 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 156.20 E-value: 6.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPG--RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLR 416
Cdd:cd03258 2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DQVALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIskmdnGL----DTVIGEngvlLSGGQRQRIA 490
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPlEIAGVPKAEIEE--RVLELLELV-----GLedkaDAYPAQ----LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
.
gi 1336523670 568 H 568
Cdd:cd03258 231 N 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
27-314 |
7.33e-44 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 158.03 E-value: 7.33e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAasdtfmlsLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18576 6 LLSSAIGLVFPL--------LAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18576 78 HLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd18576 158 RRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 267 LYAASFPSVMETLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18576 238 LWYGGRLVLAGELTAGDLVafLLYTLFIA--GSIGSLADLYGQLQKALGA 285
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
342-567 |
8.02e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 155.99 E-value: 8.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAsLRDQVAL 421
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIAY-ARTeeYSREQIEEAARMAYAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:COG1131 78 VPQEPALYPDlTVRENLRFfARL--YGLPRKEARERIDELLELF-GLTDAADRKVGT----LSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
342-560 |
1.44e-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: 154.60 E-value: 1.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLreYTLASLRDQVAL 421
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfiSKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:cd03259 77 VFQDYALFpHLTVAENIAFGlKLRGVPKAEIRARVRELLEL---VGLEGLLNRYPHE----LSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-316 |
4.37e-43 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 156.13 E-value: 4.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDD----GFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRR 102
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIDDvliqLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 103 RLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAI 182
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 183 RVVSKRFRNI-------SKNMQNTMGQVttsaeqmLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVI 255
Cdd:cd18563 161 YFFWKKIRRLfhrqwrrWSRLNSVLNDT-------LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 256 QLIASLALAFVLYAASfPSVME-TLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18563 234 TFLTSLGTLIVWYFGG-RQVLSgTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAE 294
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
343-555 |
6.20e-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: 150.86 E-value: 6.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:cd00267 1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQnvhlfndtvanniayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSPIL 502
Cdd:cd00267 79 PQ--------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 503 ILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQA-DEIVVVEDGR 555
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
342-556 |
1.23e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 152.26 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT---LASLR 416
Cdd:cd03255 1 IELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 -DQVALVSQNVHLFND-TVANNIAYArtEEYSREQIEEAARMAYAMdfISKMdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03255 81 rRHIGFVFQSFNLLPDlTALENVELP--LLLAGVPKKERRERAEEL--LERV--GLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
342-568 |
1.09e-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: 150.53 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:cd03295 1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYART-EEYSREQIEEAARmayamDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALVPKlLKWPKEKIRERAD-----ELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRL-STIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
1.21e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 150.34 E-value: 1.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQN----VHLFNdTVanniayarteeysREQIEEAARMAYAMDFISKMDNGLDTV-IGEnGVL------LSGGQRQR 488
Cdd:COG1124 82 QMVFQDpyasLHPRH-TV-------------DRILAEPLRIHGLPDREERIAELLEQVgLPP-SFLdryphqLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADL 565
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
|
...
gi 1336523670 566 LEH 568
Cdd:COG1124 227 LAG 229
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
342-570 |
1.16e-40 |
|
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: 148.35 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD-LREYTLASLRDQVA 420
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQN-----VhlfNDTVANNIAYA------RTEEYsREQIEEAARMAYAMDFISKmdngldtvigeNGVLLSGGQRQRI 489
Cdd:TIGR04520 81 MVFQNpdnqfV---GATVEDDVAFGlenlgvPREEM-RKRVDEALKLVGMEDFRDR-----------EPHLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 490 AIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERG------S 561
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifS 225
|
....*....
gi 1336523670 562 HADLLEHRG 570
Cdd:TIGR04520 226 QVELLKEIG 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
342-570 |
1.18e-40 |
|
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: 147.70 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAsLRDQVAL 421
Cdd:COG4555 2 IEVENLSKKYGKV--PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAY-ARTEEYSREQIEE-AARMAYAMDfiskMDNGLDTVIGEngvlLSGGQRQRIAIARALLRN 498
Cdd:COG4555 79 LPDERGLYdRLTVRENIRYfAELYGLFDEELKKrIEELIELLG----LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEHRG 570
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
342-568 |
4.46e-40 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 4.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLR 416
Cdd:COG1135 2 IELENLSKTFPtkGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDltaLSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DQVALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaarmayamdfisKMDNGLDTVigenGvL----------LSGG 484
Cdd:COG1135 82 RKIGMIFQHFNLLSSrTVAENVALPlEIAGVPKAEIRK------------RVAELLELV----G-LsdkadaypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEQ-ADEIVVVEDGRIVER 559
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
....*....
gi 1336523670 560 GSHADLLEH 568
Cdd:COG1135 223 GPVLDVFAN 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
342-567 |
4.53e-40 |
|
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: 145.89 E-value: 4.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:COG1127 6 IEVRNLTKSFGDR--VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNIAYARTE--EYSREQIEEAARMAYAM----DFISKMdngldtvIGEngvlLSGGQRQRIAI 491
Cdd:COG1127 84 IGMLFQGGALFDSlTVFENVAFPLREhtDLSEAEIRELVLEKLELvglpGAADKM-------PSE----LSGGMRKRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
342-566 |
6.54e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.96 E-value: 6.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:COG1120 2 LEAENLSVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHL-FNDTVANNIAYAR----------TEEySREQIEEAARMAYAMDFISKMdngLDTvigengvlLSGGQRQRIA 490
Cdd:COG1120 80 VPQEPPApFGLTVRELVALGRyphlglfgrpSAE-DREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLL 566
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
342-558 |
7.50e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.81 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:COG2884 2 IRFENVSKRYPG-GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEAARMAyamdfiskmdngLDTVigenGVL---------LSGGQRQ 487
Cdd:COG2884 81 IGVVFQDFRLLPDrTVYENVALPlRVTGKSRKEIRRRVREV------------LDLV----GLSdkakalpheLSGGEQQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADE-IVVVEDGRIVE 558
Cdd:COG2884 145 RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
342-568 |
1.23e-39 |
|
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: 147.12 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKD--VTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYD---IDNGQILLDGHDLREYTLASLR 416
Cdd:COG0444 2 LEVRNlkVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 D----QVALVSQN-------VHlfndTVANNIA--YARTEEYSREQIEEaaRMAYAMDFIskmdnGLDtviGENGVL--- 480
Cdd:COG0444 82 KirgrEIQMIFQDpmtslnpVM----TVGDQIAepLRIHGGLSKAEARE--RAIELLERV-----GLP---DPERRLdry 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 ---LSGGQRQRIAIARALLRNSPILILDEATSALD-TeseraIQAA----LDELQKNR-TSLV-IAHRLSTIEQ-ADEIV 549
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDvT-----IQAQilnlLKDLQRELgLAILfITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 1336523670 550 VVEDGRIVERGSHADLLEH 568
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
330-570 |
2.27e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 154.90 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 330 EGKLVIER--------AKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQIL 401
Cdd:PLN03130 1218 EAPLVIENnrpppgwpSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 402 LDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLL 481
Cdd:PLN03130 1298 IDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD--PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENF 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 482 SGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGS 561
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDT 1455
|
....*....
gi 1336523670 562 HADLLEHRG 570
Cdd:PLN03130 1456 PENLLSNEG 1464
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
342-555 |
2.45e-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: 2.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAS--LRDQV 419
Cdd:cd03229 1 LELKNVSKRYGQKT--VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLF-NDTVANNIAYArteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRN 498
Cdd:cd03229 79 GMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDELQKN--RTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
27-314 |
4.42e-39 |
|
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: 144.88 E-value: 4.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAAsdtfmLSLLKPLL-----DDGFGKtdrSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMR 101
Cdd:cd18551 1 LILALLLSLLGTA-----ASLAQPLLvknliDALSAG---GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 102 RRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMA 181
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 182 IRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASL 261
Cdd:cd18551 153 ILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 262 ALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18551 233 ALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGA 285
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
338-570 |
7.59e-39 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 153.21 E-value: 7.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 338 AKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRD 417
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 QVALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNID--PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLR 1388
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRG 570
Cdd:PLN03232 1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
27-314 |
2.77e-38 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 142.61 E-value: 2.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd18545 162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1336523670 267 LYAASFPSVMETLTAGTItVVFSSMIALM-RPLKSLTNVNAQFQRGMAA 314
Cdd:cd18545 242 YWYGGKLVLGGAITVGVL-VAFIGYVGRFwQPIRNLSNFYNQLQSAMAS 289
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
341-569 |
3.17e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 3.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVTFTYPGRetpALRnIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREyTLASLRdQVA 420
Cdd:COG3840 1 MLRLDDLTYRYGDF---PLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAER-PVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIAYAR------TEEySREQIEEAARmayamdfisKMdnGLDtvigenGVL------LSGGQRQ 487
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLrpglklTAE-QRAQVEQALE---------RV--GLA------GLLdrlpgqLSGGQRQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHAD 564
Cdd:COG3840 137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAA 216
|
....*
gi 1336523670 565 LLEHR 569
Cdd:COG3840 217 LLDGE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
342-568 |
3.43e-38 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 140.90 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL--REYTLASLRDQV 419
Cdd:COG1126 2 IEIENLHKSFGDLE--VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFND-TVANNIAYA--RTEEYSREQIEEAArMAYamdfiskmdngLDTVigenGVL---------LSGGQRQ 487
Cdd:COG1126 80 GMVFQQFNLFPHlTVLENVTLApiKVKKMSKAEAEERA-MEL-----------LERV----GLAdkadaypaqLSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH-----RlstiEQADEIVVVEDGRIVERGS 561
Cdd:COG1126 144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHemgfaR----EVADRVVFMDGGRIVEEGP 219
|
....*..
gi 1336523670 562 HADLLEH 568
Cdd:COG1126 220 PEEFFEN 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
342-568 |
4.66e-38 |
|
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: 140.33 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:cd03261 1 IELRGLTKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNIAYARTE--EYSREQIEEAARMAYAM----DFISKMDngldtviGEngvlLSGGQRQRIAI 491
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPLREhtRLSEEEIREIVLEKLEAvglrGAEDLYP-------AE----LSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
342-568 |
7.54e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 143.31 E-value: 7.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlreytLASL---RDQ 418
Cdd:COG3842 6 LELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-----VTGLppeKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFISKMdngldtvIGEngvlLSGGQRQRIAIA 492
Cdd:COG3842 79 VGMVFQDYALFpHLTVAENVAFGlRMRGVPKAEIRARVAELLELvgleGLADRY-------PHQ----LSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS---TIeqADEIVVVEDGRIVERGSHADLLE 567
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEIYE 225
|
.
gi 1336523670 568 H 568
Cdd:COG3842 226 R 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
343-567 |
1.36e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.13 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNV--HLFNDTVANNIAYA-RTEEYSREQ----IEEAARMAyamdfisKMDNGLDtvigENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13632 89 FQNPdnQFIGATVEDDIAFGlENKKVPPKKmkdiIDDLAKKV-------GMEDYLD----KEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 496 LRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA--HRLSTIEQADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISitHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
340-575 |
3.48e-37 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 138.50 E-value: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03288 18 GEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAYARTeeYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03288 98 SIILQDPILFSGSIRFNLDPECK--CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHR-GVYAQL 575
Cdd:cd03288 176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASL 252
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
30-314 |
3.71e-37 |
|
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: 139.62 E-value: 3.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 30 AAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMM 109
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 110 GMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRF 189
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYA 269
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1336523670 270 ASFPSVMETLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18557 241 GGYLVLSGQLTVGELTsfILYTIMVA--SSVGGLSSLLADIMKALGA 285
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-313 |
5.68e-37 |
|
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: 139.15 E-value: 5.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLK--GHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALA 264
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETLSvsGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 265 FVLYAASFPSVMETLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTL-VAFTALLGrLYGPLTQLLNIQVDLMTSLA 289
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
342-568 |
1.14e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 139.90 E-value: 1.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKST----IASLITrfydIDNGQILLDGHDLreYTLASLRD 417
Cdd:COG1118 3 IEVRNISKRFGSF--TLLDDVSLEIASGELVALLGPSGSGKTTllriIAGLET----PDSGRIVLNGRDL--FTNLPPRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 -QVALVSQNVHLF-NDTVANNIAYA-RTEEYSREQIeeAARmayAMDFISKMdnGLDTvigengvL-------LSGGQRQ 487
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIAFGlRVRPPSKAEI--RAR---VEELLELV--QLEG-------LadrypsqLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDT----ESERAIQAALDELQknRTSLVIAH------RLstieqADEIVVVEDGRIV 557
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELG--GTTVFVTHdqeealEL-----ADRVVVMNQGRIE 213
|
250
....*....|.
gi 1336523670 558 ERGSHADLLEH 568
Cdd:COG1118 214 QVGTPDEVYDR 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
342-559 |
1.19e-36 |
|
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: 136.06 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlasLRDQV 419
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFN-DTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFISKMdngldtvIGEngvlLSGGQRQRIAIAR 493
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGlELQGVPKAEARERAEELLELvglsGFENAY-------PHQ----LSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 494 ALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVE--DGRIVER 559
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLSarPGRIVAE 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
342-556 |
1.65e-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: 134.06 E-value: 1.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTlASLRDQVAL 421
Cdd:cd03230 1 IEVRNLSKRYGKK--TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVanniayarteeysREQIEeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSP 500
Cdd:cd03230 78 LPEEPSLYENlTV-------------RENLK-----------------------------LSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
30-314 |
3.04e-36 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 136.84 E-value: 3.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 30 AAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMM 109
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 110 GMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRF 189
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYA 269
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1336523670 270 ASFpSVME-TLTAGTIT--VVFSSMIAlmRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18575 241 GAH-DVLAgRMSAGELSqfVFYAVLAA--GSVGALSEVWGDLQRAAGA 285
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
57-314 |
7.37e-36 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 136.00 E-value: 7.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 57 GKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVA 136
Cdd:cd18541 32 GTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 137 SSSSSALITVVRegASIIGLFV--MMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGH 214
Cdd:cd18541 112 MALGPGILYLVD--ALFLGVLVlvMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 215 KEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTItVVFSSMIAL 294
Cdd:cd18541 190 RVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDL-VAFNSYLGM 268
|
250 260
....*....|....*....|.
gi 1336523670 295 MR-PLKSLTNVNAQFQRGMAA 314
Cdd:cd18541 269 LIwPMMALGWVINLIQRGAAS 289
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-568 |
8.50e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.45 E-value: 8.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlasLRDQVAL 421
Cdd:COG1121 7 IELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND---TVANNIAYARTEE------YSREQIEEAARmayAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIA 492
Cdd:COG1121 80 VPQRAEVDWDfpiTVRDVVLMGRYGRrglfrrPSRADREAVDE---ALERV-GLEDLADRPIGE----LSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVErGSHADLLEH 568
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVLTP 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
342-565 |
1.15e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.03 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGReTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNI-----AYART-----EEYSREQIEEAARMayamdfiskmdngLDTVigenGVL------- 480
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagrlGRTSTwrsllGLFPPEDRERALEA-------------LERV----GLAdkayqra 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 --LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:COG3638 145 dqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 1336523670 556 IVERGSHADL 565
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-569 |
1.23e-35 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 133.85 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT---LASLRDQ 418
Cdd:cd03256 1 IEVENLSKTYPN-GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNIAYARTEE----------YSREQIEEAarmAYAMDfiskmDNGLDTVIGENGVLLSGGQRQ 487
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglFPKEEKQRA---LAALE-----RVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGSHAD 564
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAE 231
|
....*
gi 1336523670 565 LLEHR 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 |
1.68e-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: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:cd03214 1 EVENLSVGYGGR--TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHLFNdtvanniayarTEEYSREQIEEaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSPIL 502
Cdd:cd03214 79 PQALELLG-----------LAHLADRPFNE----------------------------LSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 503 ILDEATSALDTeserAIQAALDEL------QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:cd03214 120 LLDEPTSHLDI----AHQIELLELlrrlarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
342-558 |
1.83e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 134.06 E-value: 1.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR--ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlasLRDQV 419
Cdd:COG1116 8 LELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFN-DTVANNIAYA-RTEEYSREQIEEAARmayamDFISKMdnGLDtvigenGVL------LSGGQRQRIAI 491
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGlELRGVPKAERRERAR-----ELLELV--GLA------GFEdayphqLSGGMRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAH------RLstieqADEIVVVED--GRIVE 558
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
342-567 |
2.12e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.54 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFY---DIDNGQILLDGHDLREYTLASLRDQ 418
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNV--HLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAmdfiskmDNGLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13640 86 VGIVFQNPdnQFVGATVGDDVAFGlENRAVPRPEMIKIVRDVLA-------DVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 496 LRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-568 |
2.13e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 134.37 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNV--HLFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIsKMDNGLDtvigENGVLLSGGQRQRIAIARALLRN 498
Cdd:PRK13635 86 VFQNPdnQFVGATVQDDVAFGlENIGVPREEMVE--RVDQALRQV-GMEDFLN----REPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
342-556 |
2.16e-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: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL--REYTLASLRDQV 419
Cdd:cd03262 1 IEIKNLHKSFGDFH--VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLF-NDTVANNIAYA--RTEEYSREQIEEAArmayaMDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03262 79 GMVFQQFNLFpHLTVLENITLApiKVKGMSKAEAEERA-----LELLEKV--GLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRI 556
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
16-565 |
2.18e-35 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 139.93 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 16 LWPLIAPFKTGLIVAAVALVFNAASDTFMLSLLkpllDDGFGKTDrSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGK 95
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLLSGLANAGLIALI----NQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 96 VVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSaLITVVREGASIIGLFVMMFYYSWQLSLILIVLA 175
Cdd:COG4615 79 AVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 176 PIVSMAIRVVSKRFR---NISKNMQNTMGQVTTSaeqMLKGHKEVLMFG--GQAVETKRFDKVSNKMRLQGMKMVSASSI 250
Cdd:COG4615 158 GLGVAGYRLLVRRARrhlRRAREAEDRLFKHFRA---LLEGFKELKLNRrrRRAFFDEDLQPTAERYRDLRIRADTIFAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 251 SDPVIQLIASLALAFVLYAA-SFPSV-METLTAGTITVVFssmiaLMRPLKSLTNVNAQFQRGMAACQ---TLFAILDSE 325
Cdd:COG4615 235 ANNWGNLLFFALIGLILFLLpALGWAdPAVLSGFVLVLLF-----LRGPLSQLVGALPTLSRANVALRkieELELALAAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 326 QEkDEGKLVIERAKGN---LEFKDVTFTYPGRETP---ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQ 399
Cdd:COG4615 310 EP-AAADAAAPPAPADfqtLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 400 ILLDGHDLREYTLASLRDQVALVSQNVHLFNDTvanniaYARTEEYSREQIEEaarmayamdFISKMDngLDTVIG-ENG 478
Cdd:COG4615 389 ILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPARARE---------LLERLE--LDHKVSvEDG 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 479 VL----LSGGQRQRIAIARALLRNSPILILDEatsaldteseraiQAA--------------LDEL-QKNRTSLVIAHRL 539
Cdd:COG4615 452 RFsttdLSQGQRKRLALLVALLEDRPILVFDE-------------WAAdqdpefrrvfytelLPELkARGKTVIAISHDD 518
|
570 580
....*....|....*....|....*.
gi 1336523670 540 STIEQADEIVVVEDGRIVERGSHADL 565
Cdd:COG4615 519 RYFDLADRVLKMDYGKLVELTGPAAL 544
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
27-313 |
6.85e-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: 133.34 E-value: 6.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNaasdtfmlSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18549 12 VLIAALDLVFP--------LIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYD----SEQVASSSSSALITVVRegasIIGLFVMMFYYSWQLSLILIVLAPIVSMAI 182
Cdd:cd18549 84 HLQKLSFSFFDNNKTGQLMSRITNDlfdiSELAHHGPEDLFISIIT----IIGSFIILLTINVPLTLIVFALLPLMIIFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 183 RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLA 262
Cdd:cd18549 160 IYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 263 LAFVLYAASFPSVMETLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMA 313
Cdd:cd18549 240 NLVVLVAGGYFIIKGEITLGDL-VAFLLYVNvFIKPIRRLVNFTEQYQKGMA 290
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
342-568 |
8.65e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.09 E-value: 8.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYP------GRETPALR---NIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LRE 409
Cdd:COG4608 8 LEVRDLKKHFPvrgglfGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 410 YTLASLRDQVALVsqnvhlFND---------TVANNIAYART--EEYSREQIEEAARmayAMdfiskmdngLDTVigenG 478
Cdd:COG4608 88 RELRPLRRRMQMV------FQDpyaslnprmTVGDIIAEPLRihGLASKAERRERVA---EL---------LELV----G 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 479 VL----------LSGGQRQRIAIARALLRNSPILILDEATSALDTeserAIQAA----LDELQK--NRTSLVIAHRLSTI 542
Cdd:COG4608 146 LRpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVSALDV----SIQAQvlnlLEDLQDelGLTYLFISHDLSVV 221
|
250 260
....*....|....*....|....*..
gi 1336523670 543 EQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG4608 222 RHiSDRVAVMYLGKIVEIAPRDELYAR 248
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
343-568 |
1.73e-34 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 133.39 E-value: 1.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRD 417
Cdd:PRK11153 3 ELKNISKVFPqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 QVALVSQnvHlFN----DTVANNIAYA-RTEEYSREQIEeaARMAYAMDFIskmdnGL----DTVIGEngvlLSGGQRQR 488
Cdd:PRK11153 83 QIGMIFQ--H-FNllssRTVFDNVALPlELAGTPKAEIK--ARVTELLELV-----GLsdkaDRYPAQ----LSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIqaaLDELQK-NR----TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSH 562
Cdd:PRK11153 149 VAIARALASNPKVLLCDEATSALDPATTRSI---LELLKDiNRelglTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
....*.
gi 1336523670 563 ADLLEH 568
Cdd:PRK11153 226 SEVFSH 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
359-568 |
4.51e-34 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 129.38 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReyTLASLRDQVALVSQNVHLF-NDTVANNI 437
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 438 AYA-RTEEYSREQIEEAARMayamdfISKMdNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESE 516
Cdd:cd03299 93 AYGlKKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 517 RAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03299 166 EKLREELKKIRKEFgvTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
342-569 |
6.17e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 135.15 E-value: 6.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRD---- 417
Cdd:COG1129 5 LEMRGISKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRFRSPRDaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 QVALVSQNVHLFND-TVANNIAYARteEYSR-------EQIEEAARMAYAMDFisKMDngLDTVIGEngvlLSGGQRQRI 489
Cdd:COG1129 80 GIAIIHQELNLVPNlSVAENIFLGR--EPRRgglidwrAMRRRARELLARLGL--DID--PDTPVGD----LSVAQQQLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 490 AIARALLRNSPILILDEATSAL-DTESER--AIqaaLDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHAD 564
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLtEREVERlfRI---IRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLVGTGPVAE 226
|
....*
gi 1336523670 565 LLEHR 569
Cdd:COG1129 227 LTEDE 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
342-568 |
6.58e-34 |
|
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: 128.89 E-value: 6.58e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQVAL 421
Cdd:cd03300 1 IELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:cd03300 77 VFQNYALFPHlTVFENIAFGlRLKKLPKAEIKE--RVAEALDLV-QLEGYANRKPSQ----LSGGQQQRVAIARALVNEP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03300 150 KVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
25-318 |
1.68e-33 |
|
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: 129.52 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 25 TGLIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMplvvIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRL 104
Cdd:cd18577 11 AGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYF----VYLGIGSFVLSYIQTACWTITGERQARRIRKRY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 105 FSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRV 184
Cdd:cd18577 87 LKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALA 264
Cdd:cd18577 167 MGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYA 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 265 FVLYAASFPSVMETLTAGTI-TVVFSSMIALMrplkSLTNVNAQ---FQRGMAACQTL 318
Cdd:cd18577 247 LAFWYGSRLVRDGEISPGDVlTVFFAVLIGAF----SLGQIAPNlqaFAKARAAAAKI 300
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
31-316 |
2.63e-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: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 31 AVALVFNAASDTFMLS---LLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSH 107
Cdd:cd18543 2 ILALLAALLATLAGLAiplLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 108 MMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVReGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSK 187
Cdd:cd18543 82 LQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPFLLGN-LLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 188 RFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVL 267
Cdd:cd18543 161 RYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 268 YAASFPSVMETLTAGTItVVFSSMIALMR-PLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18543 241 ALGGWLVANGSLTLGTL-VAFSAYLTMLVwPVRMLGWLLAMAQRARAAAE 289
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
27-316 |
2.89e-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: 128.67 E-value: 2.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVS 186
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 KRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFV 266
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 267 LYAASFPSVMETLTAGTITVVFS-SMIALMrPLKSLTNVNAQFQRGMAACQ 316
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINyLMQILM-SLMMLSMVFVMLPRASASAK 290
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
4.77e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 132.89 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR---------ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDnGQILLDGHDLREYT- 411
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 412 --LASLRDQVALVsqnvhlFND---------TVANNIAyartE-------EYSREQIEEaaRMAYAMDfiskmDNGLDTV 473
Cdd:COG4172 355 raLRPLRRRMQVV------FQDpfgslsprmTVGQIIA----EglrvhgpGLSAAERRA--RVAEALE-----EVGLDPA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 474 IG-----EngvlLSGGQRQRIAIARALLRNSPILILDEATSALDteseRAIQAA----LDELQKNR--TSLVIAHRLSTI 542
Cdd:COG4172 418 ARhryphE----FSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQildlLRDLQREHglAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*..
gi 1336523670 543 EQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
343-557 |
9.55e-33 |
|
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: 124.95 E-value: 9.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlasLRDQVALV 422
Cdd:cd03235 1 EVEDLTVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNvHLFN--------DTVANNIaYARTEEYSREQIEEAARMAYAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:cd03235 74 PQR-RSIDrdfpisvrDVVLMGL-YGHKGLFRRLSKADKAKVDEALERV-GLSELADRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIV 557
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
342-561 |
1.09e-32 |
|
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: 124.92 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReYTLASLRDQVAL 421
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIA-YARTEEYSREQI-EEAARMAYAMDFISKMdnglDTVIGEngvlLSGGQRQRIAIARALLRN 498
Cdd:cd03263 80 CPQFDALFDElTVREHLRfYARLKGLPKSEIkEEVELLLRVLGLTDKA----NKRART----LSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGS 561
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
342-568 |
1.54e-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: 125.14 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLreyTLASLRD-QVA 420
Cdd:cd03296 3 IEVRNVSKRFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA---TDVPVQErNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIAYARTEEYSREQIEEAARMAYAMDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03296 78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLV--QLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
356-568 |
2.13e-32 |
|
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: 125.83 E-value: 2.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASL----RDQVALVSQNVHLF-N 430
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 DTVANNIAYArteeYSREQIEEAARMAYAMDFISKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:cd03294 117 RTVLENVAFG----LEVQGVPRAEREERAAEALELVGLEgwEHKYPDE----LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 509 SALDTESERAIQAALDELQKN--RTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
30-285 |
1.36e-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: 124.28 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 30 AAVALVFNAASDTFMLSLLKPLLD------DGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRR 103
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDavtnhsGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 104 LFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIR 183
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 184 VVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLAL 263
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260
....*....|....*....|..
gi 1336523670 264 AFVLYAASFPSVMETLTAGTIT 285
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLT 262
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
359-560 |
2.39e-31 |
|
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: 120.86 E-value: 2.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQ---EGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLRE----YTLASLRDQVALVSQNVHLF-N 430
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 DTVANNIAYARTEEYSREQIEEAARMAYAMdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:cd03297 90 LNVRENLAFGLKRKRNREDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 511 LDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
342-568 |
2.74e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.74 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR--EYTLASLRDQV 419
Cdd:PRK09493 2 IEFKNVSKHFG--PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVA-NNIAYA--RTEEYSREQIEEAARmayamDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:PRK09493 80 GMVFQQFYLFPHLTAlENVMFGplRVRGASKEEAEKQAR-----ELLAKV--GLAERAHHYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
27-569 |
3.12e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 129.90 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFmLSLLKPlldDGFGKTDRSVLLwmplVVIGLMLLRGVTS---YISSYCISWVSGKvvmTMRRR 103
Cdd:PTZ00243 968 LATFAVTELVTVSSGVW-LSMWST---RSFKLSAATYLY----VYLGIVLLGTFSVplrFFLSYEAMRRGSR---NMHRD 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 104 LFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSwqlSLILIVLAPIVSMAIR 183
Cdd:PTZ00243 1037 LLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQ---PFVLVALVPCGYLYYR 1113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 184 VV---SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAV----ETKRFDKVSNKMRLQ-------GMKMVSASS 249
Cdd:PTZ00243 1114 LMqfyNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLvmqeALRRLDVVYSCSYLEnvanrwlGVRVEFLSN 1193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 250 ISDPVIQLI---------ASLALAFVlyaaSFPSVMETLTAGT-------ITVVFSSMIALMRPLKSLTNVN-------- 305
Cdd:PTZ00243 1194 IVVTVIALIgvigtmlraTSQEIGLV----SLSLTMAMQTTATlnwlvrqVATVEADMNSVERLLYYTDEVPhedmpeld 1269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 306 ---AQFQR--GMAACQTlfaildseqekdeGKLVIERAK-----------GNLEFKDVTFTYpgRE-TP-ALRNIDLNIQ 367
Cdd:PTZ00243 1270 eevDALERrtGMAADVT-------------GTVVIEPASptsaaphpvqaGSLVFEGVQMRY--REgLPlVLRGVSFRIA 1334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 368 EGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIayARTEEYSR 447
Cdd:PTZ00243 1335 PREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV--DPFLEASS 1412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 448 EQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALL-RNSPILILDEATSALDTESERAIQAALDEL 526
Cdd:PTZ00243 1413 AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSA 1492
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1336523670 527 QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHR 569
Cdd:PTZ00243 1493 FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
342-560 |
3.39e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.07 E-value: 3.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYD-IDN----GQILLDGHDL--REYTLAS 414
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlIPGarveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAyamdfiskmdnGL-DTV---IGENGVLLSGG 484
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESLRKA-----------ALwDEVkdrLKKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLStieQA----DEIVVVEDGRIVERG 560
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQ---QAarvsDYTAFFYLGELVEFG 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
342-557 |
5.73e-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: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRDQ--- 418
Cdd:cd03216 1 LELRGITKRFGG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---KEVSFASPRDArra 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 -VALVSQnvhlfndtvanniayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLR 497
Cdd:cd03216 76 gIAMVYQ--------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 498 NSPILILDEATSAL-DTESERAIqAALDELQKN-RTSLVIAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:cd03216 100 NARLLILDEPTAALtPAEVERLF-KVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
342-560 |
9.45e-31 |
|
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: 119.28 E-value: 9.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLrEYTLASLRDqVAL 421
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAMdfiskmdNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFGlKLRKVPKDEIDERVREVAEL-------LQIEHLLDRKPKQLSGGQRQRVALGRAIVREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH-RLSTIEQADEIVVVEDGRIVERG 560
Cdd:cd03301 150 KVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
342-568 |
1.01e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.87 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL-----REytlaslR 416
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdlppKD------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DqVALVSQNV----HLfndTVANNIAYA-RTEEYSREQIE----EAARMAyamdfisKMDNGLDTVIGEngvlLSGGQRQ 487
Cdd:COG3839 76 N-IAMVFQSYalypHM---TVYENIAFPlKLRKVPKAEIDrrvrEAAELL-------GLEDLLDRKPKQ----LSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAhrlsTIEQ------ADEIVVVEDGRIVERG 560
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYV----THDQveamtlADRIAVMNDGRIQQVG 216
|
....*...
gi 1336523670 561 SHADLLEH 568
Cdd:COG3839 217 TPEELYDR 224
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
30-314 |
1.25e-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: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 30 AAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMM 109
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 110 GMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRF 189
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 190 RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYA 269
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1336523670 270 ASFPSVMETLTAGT-ITVVFSSMIaLMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18572 241 GGHLVLSGRMSAGQlVTFMLYQQQ-LGEAFQSLGDVFSSLMQAVGA 285
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-315 |
1.39e-30 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 121.10 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKT-DRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLF 105
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSkSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 106 SHMMGMPVSFFDKQSTGTLLSRITYDS---EQVASSSSSALITVVregASIIGLFVMMFYYSWQLSLILIVLAPIVSMAI 182
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVanvERLIADGIPQGITNV---LTLVGVAIILFSINPKLALLTLIPIPFLALGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 183 RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLA 262
Cdd:cd18778 158 WLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 263 LAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315
Cdd:cd18778 238 TVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGA 290
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
342-566 |
1.50e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 119.30 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgrETPALRnIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAslRDQVAL 421
Cdd:PRK10771 2 LKLTDITWLY---HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIAYA-----RTEEYSREQIEEAARMAYAMDFISKMDngldtviGEngvlLSGGQRQRIAIARAL 495
Cdd:PRK10771 76 LFQENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 496 LRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDELL 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
335-575 |
1.69e-30 |
|
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: 127.75 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 335 IERAKGN-LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlreytla 413
Cdd:TIGR00957 629 IKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 414 slrdQVALVSQNVHLFNDTVANNIAYAR--TEEYSREQIEEAARMAYamdfISKMDNGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:TIGR00957 700 ----SVAYVPQQAWIQNDSLRENILFGKalNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAAL---DELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:TIGR00957 772 ARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
....*..
gi 1336523670 569 RGVYAQL 575
Cdd:TIGR00957 852 DGAFAEF 858
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
342-568 |
1.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 120.24 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNV--HLFNDTVANNIAYArTEEYS---REQIEEAARMAYAMDFISKMDNGLDTvigengvlLSGGQRQRIAIARALL 496
Cdd:PRK13648 88 VFQNPdnQFVGSIVKYDVAFG-LENHAvpyDEMHRRVSEALKQVDMLERADYEPNA--------LSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
27-314 |
3.20e-30 |
|
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: 120.29 E-value: 3.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVvs 186
Cdd:cd18546 81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRW-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 187 krFRNISKN----MQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLA 262
Cdd:cd18546 159 --FRRRSSRayrrARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 263 LAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18546 237 TAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAA 288
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
342-556 |
4.86e-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: 117.51 E-value: 4.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:cd03292 1 IEFINVTKTYPN-GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdLRGRAIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03292 80 IGVVFQDFRLLPDrNVYENVAFAlEVTGVPPREIRK--RVPAALELV-----GLSHKHRALPAELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhrlstiEQADEIV--------VVEDGRI 556
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAKELVdttrhrviALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
342-560 |
7.21e-30 |
|
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: 116.82 E-value: 7.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPAlrNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlreYTLASLRDQ-VA 420
Cdd:cd03298 1 VRLDKIRFSY--GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPADRpVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIAYART-----EEYSREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03298 74 MLFQENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEVALARV-----------GLAGLEKRLPGELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
1.31e-29 |
|
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: 118.35 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAP---IVSMAIR 183
Cdd:cd18540 84 HLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPvlaVVSIYFQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 184 V-VSKRFRNISKnmQNTmgQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLA 262
Cdd:cd18540 164 KkILKAYRKVRK--INS--RITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 263 LAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18540 240 TALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQAS 291
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
342-561 |
1.61e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQVAL 421
Cdd:PRK09452 15 VELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH--VPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAMDFISKMDNgldtvigENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK09452 91 VFQSYALFpHMTVFENVAFGlRMQKTPAAEITPRVMEALRMVQLEEFAQ-------RKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLstiEQA----DEIVVVEDGRIVERGS 561
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHDQ---EEAltmsDRIVVMRDGRIEQDGT 228
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
342-550 |
3.92e-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: 114.50 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKST----IASLITrfydIDNGQILLDGHDLREyTLASLRD 417
Cdd:COG4133 3 LEAENLSCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRD-AREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 QVALVSQNVHLFND-TVANNIAYART---EEYSREQIEEA-ARMayamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:COG4133 76 RLAYLGHADGLKPElTVRENLRFWAAlygLRADREAIDEAlEAV------------GLAGLADLPVRQLSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEQADEIVV 550
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
342-566 |
4.43e-29 |
|
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: 115.57 E-value: 4.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRF-YDIDNGQILLDGHDLREYTLASLRDQVA 420
Cdd:COG1119 4 LELRNVTVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlPPTYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLF---NDTVANNI---AYA---RTEEYSREQIEEAARMAYAMDFISKMDNGLDTvigengvlLSGGQRQRIAI 491
Cdd:COG1119 82 LVSPALQLRfprDETVLDVVlsgFFDsigLYREPTDEQRERARELLELLGLAHLADRPFGT--------LSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQA-DEIVVVEDGRIVERGSHADLL 566
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
64-316 |
1.83e-28 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 115.30 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 64 LLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSAL 143
Cdd:cd18573 40 LKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 144 ITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQ 223
Cdd:cd18573 120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 224 AVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTIT-------VVFSSMIalmr 296
Cdd:cd18573 200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTsflmyavYVGSSVS---- 275
|
250 260
....*....|....*....|
gi 1336523670 297 plkSLTNVNAQFQRGMAACQ 316
Cdd:cd18573 276 ---GLSSFYSELMKGLGASS 292
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
363-556 |
2.45e-28 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 112.65 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 363 DLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlrEYTLASLRDQVALVSQNVHLFND-TVANNIAYA- 440
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 441 ----RTEEYSREQIEEAARMAYAMDFISKMDNGLdtvigengvllSGGQRQRIAIARALLRNSPILILDEATSALDTESE 516
Cdd:TIGR01277 96 hpglKLNAEQQEKVVDAAQQVGIADYLDRLPEQL-----------SGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1336523670 517 RAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRI 556
Cdd:TIGR01277 165 EEMLALVKQLcsERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
168-575 |
7.95e-28 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 119.31 E-value: 7.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 168 SLILIVLAPIVSMAIRvvskRFRNISKN-MQNTMGQVTTSAEqmlkghkevLMFGGQAVETKRFDKvSNKMRLQGMKMVS 246
Cdd:PLN03232 447 SLILFLLIPLQTLIVR----KMRKLTKEgLQWTDKRVGIINE---------ILASMDTVKCYAWEK-SFESRIQGIRNEE 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 247 ASSISDPviQLIASLAlAFVLyaASFPSVMETLTAGTITVV---------FSSM--IALMR-PLKSLTNVNAQFQRGMAA 314
Cdd:PLN03232 513 LSWFRKA--QLLSAFN-SFIL--NSIPVVVTLVSFGVFVLLggdltparaFTSLslFAVLRsPLNMLPNLLSQVVNANVS 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 315 CQTLFAILDSEQEKDEGKLVIERAKGNLEFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASlitrfy 393
Cdd:PLN03232 588 LQRIEELLLSEERILAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS------ 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 394 didngqILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYARTEEYSR--EQIEEAArMAYAMDFISKMDNgld 471
Cdd:PLN03232 662 ------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERywRAIDVTA-LQHDLDLLPGRDL--- 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 472 TVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIVV 550
Cdd:PLN03232 732 TEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIIL 811
|
410 420
....*....|....*....|....*
gi 1336523670 551 VEDGRIVERGSHADLLEHRGVYAQL 575
Cdd:PLN03232 812 VSEGMIKEEGTFAELSKSGSLFKKL 836
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
342-568 |
8.49e-28 |
|
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: 117.48 E-value: 8.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKD--VTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKS----TIASLITRFYDIDNGQILLDGHDLREYTLASL 415
Cdd:COG4172 7 LSVEDlsVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 416 R----DQVALVSQ------N-VHlfndTVANNI--------------AYARTEEYSRE-QIEEAARM--AYAMDfiskmd 467
Cdd:COG4172 87 RrirgNRIAMIFQepmtslNpLH----TIGKQIaevlrlhrglsgaaARARALELLERvGIPDPERRldAYPHQ------ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 468 ngldtvigengvlLSGGQRQRIAIARALLrNSP-ILILDEATSALDTESERAIQAALDELQKNR-TSLV-IAHRLSTIEQ 544
Cdd:COG4172 157 -------------LSGGQRQRVMIAMALA-NEPdLLIADEPTTALDVTVQAQILDLLKDLQRELgMALLlITHDLGVVRR 222
|
250 260
....*....|....*....|....*
gi 1336523670 545 -ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
14-325 |
1.46e-27 |
|
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: 113.32 E-value: 1.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 14 RRLWPLIApfkTGLIVAAV--------ALVFNAASDTFMLSLLKPLLDDGfgktdrsvLLWMpLVVIGLMLLRGVTSYIS 85
Cdd:cd18578 5 KPEWPLLL---LGLIGAIIagavfpvfAILFSKLISVFSLPDDDELRSEA--------NFWA-LMFLVLAIVAGIAYFLQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 86 SYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQ--STGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYY 163
Cdd:cd18578 73 GYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPenSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 164 SWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMK 243
Cdd:cd18578 153 GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 244 MVSASSISDPVIQLIASLALAFVLYA---------ASFPSVMETLTAgtitVVFSSMIALMrplksLTNVNAQFQRGMAA 314
Cdd:cd18578 233 RALISGLGFGLSQSLTFFAYALAFWYggrlvangeYTFEQFFIVFMA----LIFGAQSAGQ-----AFSFAPDIAKAKAA 303
|
330
....*....|.
gi 1336523670 315 CQTLFAILDSE 325
Cdd:cd18578 304 AARIFRLLDRK 314
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
342-567 |
2.06e-27 |
|
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: 110.22 E-value: 2.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReyTLAS---LRDQ 418
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPherARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNI---AYARTEEYSREQIEEAarmaYAMDFIskmdngLDTVIGENGVLLSGGQRQRIAIARA 494
Cdd:cd03224 77 IGYVPEGRRIFPElTVEENLllgAYARRRAKRKARLERV----YELFPR------LKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIahrlstIEQ--------ADEIVVVEDGRIVERGSHADLL 566
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILL------VEQnarfaleiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 1336523670 567 E 567
Cdd:cd03224 221 A 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
342-558 |
2.11e-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: 110.60 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETP--ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR---EYTLASLR 416
Cdd:COG4181 9 IELRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 -DQVALVSQNVHLF-NDTVANNIAYARTEEYSREQIEEAARMayamdfiskmdngLDTVigenGV---------LLSGGQ 485
Cdd:COG4181 89 aRHVGFVFQSFQLLpTLTALENVMLPLELAGRRDARARARAL-------------LERV----GLghrldhypaQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIA-HRLSTIEQADEIVVVEDGRIVE 558
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-576 |
2.25e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 111.80 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgRETP----ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDG----HDLREYTLA 413
Cdd:PRK13646 3 IRFDNVSYTYQ-KGTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 414 SLRDQVALVSQ--NVHLFNDTVANNIAYArtEEYSREQIEEAArmAYAMDFIskMDNGLD-TVIGENGVLLSGGQRQRIA 490
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFG--PKNFKMNLDEVK--NYAHRLL--MDLGFSrDVMSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFK 235
|
....*....
gi 1336523670 568 HRGVYAQLH 576
Cdd:PRK13646 236 DKKKLADWH 244
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
345-557 |
2.78e-27 |
|
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: 109.27 E-value: 2.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTYpGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlASLRDQVALVSQ 424
Cdd:cd03226 3 ENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 NV--HLFNDTVANNIAY-ARTEEYSREQIEEAarmayamdfISKMDngLDTVIGENGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03226 79 DVdyQLFTDSVREELLLgLKELDAGNEQAETV---------LKDLD--LYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIVVVEDGRIV 557
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYEFLaKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
345-570 |
3.05e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.68 E-value: 3.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTY-PGR--ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL--REYTLASLRDQV 419
Cdd:PRK13637 6 ENLTHIYmEGTpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEaaRMAYAMDFIskmdnGLD--TVIGENGVLLSGGQRQRIAIARA 494
Cdd:PRK13637 86 GLVFQypEYQLFEETIEKDIAFGpINLGLSEEEIEN--RVKRAMNIV-----GLDyeDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGS------HADL 565
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTprevfkEVET 238
|
....*
gi 1336523670 566 LEHRG 570
Cdd:PRK13637 239 LESIG 243
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
342-566 |
6.66e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 6.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT-LASLRDQVA 420
Cdd:PRK13644 2 IRLENVSYSYPD-GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQN--VHLFNDTVANNIAYArTEEYSREQIEEAARMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRN 498
Cdd:PRK13644 81 IVFQNpeTQFVGRTVEEDLAFG-PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
358-574 |
1.13e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 110.82 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREY---TLASLRDQVALVSQNvhlfndtva 434
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeAQKLLRQKIQIVFQN--------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 435 nniAYARTEEYSR--EQIEE----------AARMAYAMDFISKMdnGLDTvigENGV----LLSGGQRQRIAIARALLRN 498
Cdd:PRK11308 101 ---PYGSLNPRKKvgQILEEpllintslsaAERREKALAMMAKV--GLRP---EHYDryphMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 499 SPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH-RG 570
Cdd:PRK11308 173 PDVVVADEPVSALDV----SVQAQvlnlMMDLQQElGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNpRH 248
|
....
gi 1336523670 571 VYAQ 574
Cdd:PRK11308 249 PYTQ 252
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-557 |
2.15e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 108.63 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFT-YPG--RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASL 415
Cdd:COG1101 2 LELKNLSKTfNPGtvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 416 rdqVALVSQNVHL---FNDTVANN--IAYARTEEYSREQIEEAARMAYAMDFISKMDNGL----DTVIGengvLLSGGQR 486
Cdd:COG1101 82 ---IGRVFQDPMMgtaPSMTIEENlaLAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLstiEQA----DEIVVVEDGRIV 557
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM---EQAldygNRLIMMHEGRII 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
317-554 |
2.20e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.36 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 317 TLFAILDSEQEKDEGKLVIERAKGN-LEFKDVTFTYPgRETPALRNIDLNIQEGKTVALVGRSGSGKST----IASLitr 391
Cdd:COG4178 337 GFEEALEAADALPEAASRIETSEDGaLALEDLTLRTP-DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL--- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 392 fYDIDNGQILLDGHDlreytlaslrdQVALVSQNVHLFNDTVANNIAY-ARTEEYSREQIEEAARMAYAMDFISKMDNGL 470
Cdd:COG4178 413 -WPYGSGRIARPAGA-----------RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERLDEEA 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 471 DTvigenGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVV 550
Cdd:COG4178 481 DW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLE 555
|
....
gi 1336523670 551 VEDG 554
Cdd:COG4178 556 LTGD 559
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
342-570 |
3.90e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 108.28 E-value: 3.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTY-PGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVA 420
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNV--HLFNDTVANNIAYARTE-----EYSREQIEEAARMAYAMDFISKmdngldtvigeNGVLLSGGQRQRIAIAR 493
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgiphEEMKERVNEALELVGMQDFKER-----------EPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 494 ALLRNSPILILDEATSALDTESE----RAIQAALDELQknRTSLVIAHRLSTIEQADEIVVVEDGRiVERGSHADLLEHR 569
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDDYQ--MTVISITHDLDEVALSDRVLVMKNGQ-VESTSTPRELFSR 230
|
.
gi 1336523670 570 G 570
Cdd:PRK13650 231 G 231
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
342-568 |
7.67e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.52 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR---ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT----LAS 414
Cdd:PRK13649 3 INLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMDFISkmdnglDTVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpQNFGVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRL--STIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLmdDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
342-568 |
8.38e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpGRETpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASlRDqVAL 421
Cdd:PRK11432 7 VVLKNITKRF-GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYA-RTEEYSREQIEEAARMAYAM-DFISKMDNGLDTVigengvllSGGQRQRIAIARALLRN 498
Cdd:PRK11432 83 VFQSYALFpHMSLGENVGYGlKMLGVPKEERKQRVKEALELvDLAGFEDRYVDQI--------SGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
357-566 |
2.93e-25 |
|
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: 105.27 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAS---LRDQVALVSQN-VHLFN-- 430
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDsPSAVNpr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 DTVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 511 LDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:TIGR02769 181 LDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
342-560 |
2.97e-25 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 103.01 E-value: 2.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPA----LRNIDLNIQEGKTVALVGRSGSGKSTIASLIT--RFYDIDNGQILLDGHDLReytLASL 415
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 416 RDQVALVSQNVHLF-NDTVanniayarteeysREqieeaarmayAMDFISKMDNgldtvigengvlLSGGQRQRIAIARA 494
Cdd:cd03213 81 RKIIGYVPQDDILHpTLTV-------------RE----------TLMFAAKLRG------------LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIVVVEDGRIVERG 560
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
342-560 |
3.02e-25 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 103.81 E-value: 3.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTvALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAsLRDQVAL 421
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK-LRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAY-ARTEEYSREQIEEAARMAyamdfISKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:cd03264 77 LPQEFGVYpNFTVREFLDYiAWLKGIPSKEVKARVDEV-----LELVNLGdrAKKKIGS----LSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
342-571 |
3.07e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 104.29 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRdq 418
Cdd:COG0410 4 LEVENLHAGYG--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitgLPPHRIARLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNI---AYARTeeySREQIEEAARMAYAM-----DFISKMdngldtvigenGVLLSGGQRQRI 489
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENLllgAYARR---DRAEVRADLERVYELfprlkERRRQR-----------AGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 490 AIARALLRNSPILILDEATSALdteserA------IQAALDELQKNRTSLVIahrlstIEQ--------ADEIVVVEDGR 555
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL------ApliveeIFEIIRRLNREGVTILL------VEQnarfaleiADRAYVLERGR 213
|
250
....*....|....*.
gi 1336523670 556 IVERGSHADLLEHRGV 571
Cdd:COG0410 214 IVLEGTAAELLADPEV 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
342-560 |
6.42e-25 |
|
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: 102.68 E-value: 6.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQV-A 420
Cdd:cd03268 1 LKTNDLTKTYGKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSqnVHLFND---TVANNIAYARTEEYSREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:cd03268 77 LIE--APGFYPnltARENLRLLARLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSLRDQgITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
349-554 |
6.56e-25 |
|
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: 103.18 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 349 FTYpGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQIL----LDGHDLREYTLASLRDQVALVSQ 424
Cdd:cd03290 8 FSW-GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 NVHLFNDTVANNIAYARTEEYSR-EQIEEAARMAYAMDFISKMDNgldTVIGENGVLLSGGQRQRIAIARALLRNSPILI 503
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRyKAVTDACSLQPDIDLLPFGDQ---TEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 504 LDEATSALDTE-SERAIQAALDELQKN--RTSLVIAHRLSTIEQADEIVVVEDG 554
Cdd:cd03290 164 LDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
342-560 |
8.55e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.05 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK13647 5 IEVEDLHFRYKD-GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNV--HLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAM----DFISKMDNGldtvigengvlLSGGQRQRIAIARA 494
Cdd:PRK13647 84 VFQDPddQVFSSTVWDDVAFGpVNMGLDKDEVERRVEEALKAvrmwDFRDKPPYH-----------LSYGQKKRVAIAGV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIVVVEDGRIVERG 560
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-575 |
1.05e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.44 E-value: 1.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTY-PGRETPALRNIDLNIQEGKTVALVGRSGSGK-STIASLITRFYDIDNGQILLdghdlreytlaslRDQVALV 422
Cdd:PLN03130 618 KNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVI-------------RGTVAYV 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHLFNDTVANNIAYArtEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPIL 502
Cdd:PLN03130 685 PQVSWIFNATVRDNILFG--SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVY 762
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 503 ILDEATSALDTESERAI--QAALDELQkNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQL 575
Cdd:PLN03130 763 IFDDPLSALDAHVGRQVfdKCIKDELR-GKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
353-555 |
1.13e-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: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 353 GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDgHDLREYTLASL--RDQVAL-------VS 423
Cdd:COG4778 21 GKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLAQAspREILALrrrtigyVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QNVH--------------LFNDTVANNIAYARTEEY-SREQIEEAARMAYAMDFiskmdngldtvigengvllSGGQRQR 488
Cdd:COG4778 100 QFLRviprvsaldvvaepLLERGVDREEARARARELlARLNLPERLWDLPPATF-------------------SGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
342-561 |
2.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 2.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReYTLASL---RDQ 418
Cdd:PRK13639 2 LETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLlevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNV--HLFNDTVANNIAYAR-----TEEYSREQIEEAARMAYAMDFISKMDNGLdtvigengvllSGGQRQRIAI 491
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPlnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIE-QADEIVVVEDGRIVERGS 561
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGT 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-564 |
2.56e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRDQVAL 421
Cdd:COG3845 6 LELRGITKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 ----VSQNVHLFND-TVANNIAYARTEEYS--------REQIEEAARmAYAMDFiskmDngLDTVIGEngvlLSGGQRQR 488
Cdd:COG3845 81 gigmVHQHFMLVPNlTVAENIVLGLEPTKGgrldrkaaRARIRELSE-RYGLDV----D--PDAKVED----LSVGEQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 489 IAIARALLRNSPILILDEATSAL-DTESERAIqAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHAD 564
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVVGTVDTAE 227
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
340-574 |
2.82e-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: 102.63 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDnGQILLDGHDLREYTLASLRDQV 419
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIAyaRTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLD--PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRGVYAQ 574
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQ 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
343-566 |
3.12e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 102.08 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALV 422
Cdd:COG4604 3 EIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHlFND--TVANNIAYAR--------TEEySREQIEEAarMAYaMDFISKMDNGLDTvigengvlLSGGQRQRIAIA 492
Cdd:COG4604 81 RQENH-INSrlTVRELVAFGRfpyskgrlTAE-DREIIDEA--IAY-LDLEDLADRYLDE--------LSGGQRQRAFIA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAAL----DELqkNRTSLVIAHrlsTIEQA----DEIVVVEDGRIVERGSHAD 564
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLrrlaDEL--GKTVVIVLH---DINFAscyaDHIVAMKDGRVVAQGTPEE 222
|
..
gi 1336523670 565 LL 566
Cdd:COG4604 223 II 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
342-559 |
3.58e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.86 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR--ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReyTLASLRdqv 419
Cdd:COG4525 4 LTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFN-DTVANNIAYARteeysREQ-IEEAARMAYAMDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGL-----RLRgVPKAERRARAEELLALV--GLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQA----DEIVVVED--GRIVER 559
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITH---SVEEAlflaTRLVVMSPgpGRIVER 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
342-569 |
4.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.41 E-value: 4.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR---ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL----REYTLAS 414
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQ--NVHLFNDTVANNIAYARTE-EYSREQIEEAARMAYAMdfiskmdNGLD-TVIGENGVLLSGGQRQRIA 490
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfGVSEEDAKQKAREMIEL-------VGLPeELLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
..
gi 1336523670 568 HR 569
Cdd:PRK13634 236 DP 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
342-566 |
4.43e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 4.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK09536 4 IDVSDLSVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHL-FNDTVANNIAYARTEEYSR-EQIEEAARMAY--AMDFISkMDNGLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:PRK09536 82 VPQDTSLsFEFDVRQVVEMGRTPHRSRfDTWTETDRAAVerAMERTG-VAQFADRPVTS----LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 498 NSPILILDEATSALDTESE-RAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
97-574 |
4.94e-24 |
|
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: 107.30 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 97 VMTMRRRLFSHMMGM----PVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIG-LFV--MMFYYSWQLSL 169
Cdd:TIGR01271 953 LLTVSKRLHEQMLHSvlqaPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGaIFVvsVLQPYIFIAAI 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 170 ILIVLAPIVSMAIRVVSKRFRNI-SKNMQNTMGQVTTSaeqmLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSAS 248
Cdd:TIGR01271 1033 PVAVIFIMLRAYFLRTSQQLKQLeSEARSPIFSHLITS----LKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTL 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 249 SISDPVIQLIaslalaFVLY--AASFPSVMET-LTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDSE 325
Cdd:TIGR01271 1109 RWFQMRIDII------FVFFfiAVTFIAIGTNqDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLP 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 326 QEKDEGK-----------LVIER--------AKGNLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIA 386
Cdd:TIGR01271 1183 QEEPRPSggggkyqlstvLVIENphaqkcwpSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 387 SLITRFYDIDnGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNI-AYARteeYSREQIEEAARMAYAMDFISK 465
Cdd:TIGR01271 1263 SALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQ---WSDEEIWKVAEEVGLKSVIEQ 1338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 466 MDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQA 545
Cdd:TIGR01271 1339 FPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLEC 1418
|
490 500
....*....|....*....|....*....
gi 1336523670 546 DEIVVVEDGRIVERGSHADLLEHRGVYAQ 574
Cdd:TIGR01271 1419 QQFLVIEGSSVKQYDSIQKLLNETSLFKQ 1447
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
342-549 |
5.20e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.56 E-value: 5.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK10247 8 LQLQNVGYLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVANNIAYArteeYS-REQIEEAARMAYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSP 500
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFP----WQiRNQQPDPAIFLDDLERFALPDTILTKNIAE----LSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVI 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
358-561 |
5.42e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 100.97 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRdqVALVSQNVHLFND-TV 433
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitgLPPHEIARLG--IGRTFQIPRLFPElTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNI---AYARTEE------YSREQIEEAARMAYAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILIL 504
Cdd:cd03219 93 LENVmvaAQARTGSglllarARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 505 DEATSAL-DTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGS 561
Cdd:cd03219 168 DEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
353-561 |
1.33e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 102.47 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 353 GReTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLreyTLASLRD-QVALVSQNVHLFND 431
Cdd:PRK10851 13 GR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV---SRLHARDrKVGFVFQHYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 -TVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDngLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:PRK10851 89 mTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ--LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 511 LDTESERAIQAALDELQKNR--TSLVIAH-RLSTIEQADEIVVVEDGRIVERGS 561
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
341-563 |
1.36e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 99.70 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH------DLREYTLAS 414
Cdd:COG4161 2 SIQLKNINCFYGS--HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQNVHLF-NDTVANNIAYA--RTEEYSREQieeaARmAYAMDFISKMdnGLDTVIGENGVLLSGGQRQRIAI 491
Cdd:COG4161 80 LRQKVGMVFQQYNLWpHLTVMENLIEApcKVLGLSKEQ----AR-EKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHA 563
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
342-548 |
1.48e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 99.85 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID-----NGQILLDGHDL---REYTLa 413
Cdd:PRK14239 6 LQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 414 SLRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFISkmDNGLDTVIGengvlLSGGQRQ 487
Cdd:PRK14239 83 DLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEAVEKSLKGASIWDEVK--DRLHDSALG-----LSGGQQQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 488 RIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHrlsTIEQADEI 548
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
27-314 |
1.99e-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: 101.10 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFmlsllkPLLDDGFGKTDRSVLLWM-PLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLF 105
Cdd:cd18565 21 LIGVAIDAVFNGEASFL------PLVPASLGPADPRGQLWLlGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 106 SHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVV 185
Cdd:cd18565 95 DHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 186 SKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAF 265
Cdd:cd18565 175 QRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVA 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 266 VLYAASF------PSVMETLTAGTItVVFSSMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18565 255 TFVVGGYwvldgpPLFTGTLTVGTL-VTFLFYTQrLLWPLTRLGDLIDQYQRAMAS 309
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
342-561 |
2.02e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTY-PGR--ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT----LAS 414
Cdd:PRK13641 3 IKFENVDYIYsPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQ--NVHLFNDTVANNIAYAR-----TEEYSREQieeaarmayAMDFISKMdnGLDT-VIGENGVLLSGGQR 486
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPknfgfSEDEAKEK---------ALKWLKKV--GLSEdLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGS 561
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHAS 228
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
342-575 |
2.55e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRF--YDIDNGQILLDGHDLREYT-------- 411
Cdd:COG0396 1 LEIKNLHVSVEGKEI--LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSpderarag 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 412 --LA----------SLRDqvalvsqnvhlFNDTVANNIayaRTEEYSREQI-----EEAARMAYAMDFISKmdnGLDtvi 474
Cdd:COG0396 79 ifLAfqypveipgvSVSN-----------FLRTALNAR---RGEELSAREFlkllkEKMKELGLDEDFLDR---YVN--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 475 gengVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAH--RLSTIEQADEIVVV 551
Cdd:COG0396 139 ----EGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVL 214
|
250 260
....*....|....*....|....*.
gi 1336523670 552 EDGRIVERGSH--ADLLEHRGvYAQL 575
Cdd:COG0396 215 VDGRIVKSGGKelALELEEEG-YDWL 239
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
355-561 |
3.25e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 100.70 E-value: 3.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIAS-----LITRFYDIDNGQILLDGHDLREYTLAS-----------LRDQ 418
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIGDKKNNHELITNpyskkiknfkeLRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQ--NVHLFNDTVANNIAYARTEeYSREQIEEAARMAYamdFISKMdnGLD-TVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK13631 118 VSMVFQfpEYQLFKDTIEKDIMFGPVA-LGVKKSEAKKLAKF---YLNKM--GLDdSYLERSPFGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 496 LRNSPILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGS 561
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
358-571 |
3.45e-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: 98.96 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRdqVALVSQNVHLFND-TV 433
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitgLPPHRIARLG--IARTFQNPRLFPElTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNI--------------AYARTEEYSREQIEEAARMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:COG0411 97 LENVlvaaharlgrgllaALLRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:COG0411 172 KLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRADPRV 246
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
359-567 |
6.75e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 104.09 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDghdlreytlaslrDQVALVSQNVHLFNDTVANNIA 438
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 439 YARTEEYSReqIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTE-SER 517
Cdd:PTZ00243 743 FFDEEDAAR--LADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 518 AIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLE 567
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
342-568 |
1.13e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI-----LLDGH---DLREYTLA 413
Cdd:PRK11264 4 IEVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 414 SLRDQVALVSQNVHLF-NDTVANNIAYART--EEYSREQIEEAARMAYAMDFISKMDNGLDTvigengvLLSGGQRQRIA 490
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFpHRTVLENIIEGPVivKGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSfARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
374-568 |
1.35e-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: 99.11 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 374 LVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQVALVSQNVHLF-NDTVANNIAYA-RTEEYSREQIE 451
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRHINMVFQSYALFpHMTVEENVAFGlKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 452 ----EAARMAYAMDFISKMDNGLdtvigengvllSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ 527
Cdd:TIGR01187 79 prvlEALRLVQLEEFADRKPHQL-----------SGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1336523670 528 KNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:TIGR01187 148 EQLgiTFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
359-558 |
1.46e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 97.45 E-value: 1.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL----REYTLASLRDqVALVSQN-VHLFN--D 431
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRD-IQMVFQDsISAVNprK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 TVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSAL 511
Cdd:PRK10419 107 TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQ----LSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 512 DTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIVVVEDGRIVE 558
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
355-561 |
1.94e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.01 E-value: 1.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQnVHLFND--T 432
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ-HHLTPEgiT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIAYARTEEYS---REQIEEAARMAYAMDfiskmDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:PRK11231 93 VRELVAYGRSPWLSlwgRLSAEDNARVNQAME-----QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 510 ALDTESERAIQAALDELQKN-RTSLVIAHRLStieQA----DEIVVVEDGRIVERGS 561
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQgKTVVTVLHDLN---QAsrycDHLVVLANGHVMAQGT 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
361-566 |
2.09e-22 |
|
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: 99.02 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 361 NIDLNIQEGKTVALVGRSGSGKST----IASLITrfydIDNGQILLDGHDL----REYTLASLRDQVALVSQNVHLFND- 431
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTllraIAGLER----PDSGRIRLGGEVLqdsaRGIFLPPHRRRIGYVFQEARLFPHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 TVANNIAYAR---TEEYSREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:COG4148 93 SVRGNLLYGRkraPRAERRISFDEVVELL-----------GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 509 SALDTESERAIqaaLDELQKNRTSLVI-----AHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:COG4148 162 AALDLARKAEI---LPYLERLRDELDIpilyvSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
342-562 |
2.54e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 96.24 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH--DLR----EYTLASL 415
Cdd:PRK11124 3 IQLNGINCFYG--AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 416 RDQVALVSQNVHLF-NDTVANNIAYA--RTEEYSREQIeeaarMAYAMDFISKMDngLDTVIGENGVLLSGGQRQRIAIA 492
Cdd:PRK11124 81 RRNVGMVFQQYNLWpHLTVQQNLIEApcRVLGLSKDQA-----LARAEKLLERLR--LKPYADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSH 562
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
342-565 |
2.90e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR-EYTLASLRDQVA 420
Cdd:PRK11288 5 LSFDGIGKTFPG--VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIAYARTEEySREQIEEAARMAYAMDFISKMDNGLD--TVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:PRK11288 83 IIYQELHLVPEmTVAENLYLGQLPH-KGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 498 NSPILILDEATSALdteSERAIQ---AALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVErgSHADL 565
Cdd:PRK11288 158 NARVIAFDEPTSSL---SAREIEqlfRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-566 |
3.07e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID-----NGQILLDGHDLREYTLASLRDQVALVSQ----- 424
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQipnpi 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 -NVHLFnDTVA-----NNIAYARTEEYSReqIEEAARMAYAMDfisKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRN 498
Cdd:PRK14247 95 pNLSIF-ENVAlglklNRLVKSKKELQER--VRWALEKAQLWD---EVKDRLDAPAGK----LSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH------RLStieqaDEIVVVEDGRIVERGSHADLL 566
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVF 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
348-560 |
3.13e-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: 95.13 E-value: 3.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 348 TFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRdQVALVSQNVH 427
Cdd:cd03266 10 RFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-RLGFVSDSTG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 428 LFND-TVANNIAY-ARTEEYSREQIEEAARmayamDFISKMDNG--LDTVIGEngvlLSGGQRQRIAIARALLRNSPILI 503
Cdd:cd03266 89 LYDRlTARENLEYfAGLYGLKGDELTARLE-----ELADRLGMEelLDRRVGG----FSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 504 LDEATSALDTESERAIQAALDELQK-NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
342-556 |
6.46e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.51 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQiLLDGhdlrEYTLASLRDQVAL 421
Cdd:PRK11247 13 LLLNAVSKRYGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAG----TAPLAEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFN-DTVANNIAYARTEEYsREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSP 500
Cdd:PRK11247 86 MFQDARLLPwKKVIDNVGLGLKGQW-RDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 501 ILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLS-TIEQADEIVVVEDGRI 556
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
342-579 |
7.83e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 95.54 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTY----PGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD-LREYTLASLR 416
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DQVALVSQNVHlfNDTVAN----NIAYA------RTEEYsREQIEEAARMAYAMDFISKMDNgldtvigengvLLSGGQR 486
Cdd:PRK13633 85 NKAGMVFQNPD--NQIVATiveeDVAFGpenlgiPPEEI-RERVDESLKKVGMYEYRRHAPH-----------LLSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRIVERGShad 564
Cdd:PRK13633 151 QRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT--- 227
|
250
....*....|....*
gi 1336523670 565 lleHRGVYAQLHKMQ 579
Cdd:PRK13633 228 ---PKEIFKEVEMMK 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
351-549 |
9.46e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.07 E-value: 9.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 351 YPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlreytlaslrdQVALVSQNVHL-- 428
Cdd:NF040873 2 YGGR--PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 429 -FNDTVANNIA---YARTEEYSREQIEEAARMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILIL 504
Cdd:NF040873 69 sLPLTVRDLVAmgrWARRGLWRRLTRDDRAAVDDALERV-----GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1336523670 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEhARGATVVVVTHDLELVRRADPCV 189
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
331-558 |
9.47e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 9.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 331 GKLVIErakgnleFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLdGHDLRey 410
Cdd:COG0488 312 GKKVLE-------LEGLSKSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 tlaslrdqVALVSQNVHLF--NDTVANNIAyarteEYSREQIEEAARmAY--AMDFISKMdngLDTVIGEngvlLSGGQR 486
Cdd:COG0488 380 --------IGYFDQHQEELdpDKTVLDELR-----DGAPGGTEQEVR-GYlgRFLFSGDD---AFKPVGV----LSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 487 QRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEIVVVEDGRIVE 558
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
342-566 |
1.03e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK13548 3 LEARNLSVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHL-FNDTVANNIA---YARTEEYSREQIEEAARMAYAmdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK13548 81 LPQHSSLsFPFTVEEVVAmgrAPHGLSRAEDDALVAAALAQV---------DLAHLAGRDYPQLSGGEQQRVQLARVLAQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 498 NS------PILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLS-TIEQADEIVVVEDGRIVERGSHAD 564
Cdd:PRK13548 152 LWepdgppRWLLLDEPTSALDL----AHQHHVLRLARQLAHerglavIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 1336523670 565 LL 566
Cdd:PRK13548 228 VL 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
342-557 |
1.14e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.03 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETP--ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREY---TLASLR 416
Cdd:PRK10535 5 LELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 -DQVALVSQNVHLFND-TVANNI----AYArteeysreQIEEAARMAYAMDFISKMdnGLDTVIGENGVLLSGGQRQRIA 490
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHlTAAQNVevpaVYA--------GLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIVVVEDGRIV 557
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
358-568 |
1.46e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.03 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRD----QVALVSQNVHLF-NDT 432
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIAYArteeYSREQIEEAARMAYAMDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALD 512
Cdd:PRK10070 123 VLDNTAFG----MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 513 TESERAIQAALDELQ--KNRTSLVIAHRL-STIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
344-515 |
1.61e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 344 FKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI----------------LLDGHDL 407
Cdd:COG0488 1 LENLSKSFGGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsipkglrigylpqeppLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 408 REYTLASLRDQVALVSQNVHL---FNDTVANNIAYARTEE-------YSREQieEAARMAYAMDFiskMDNGLDTVIGEn 477
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELeakLAEPDEDLERLAELQEefealggWEAEA--RAEEILSGLGF---PEEDLDRPVSE- 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 1336523670 478 gvlLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:COG0488 153 ---LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
342-568 |
1.90e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQVAL 421
Cdd:PRK11607 20 LEIRNLTKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAY-------ARTEEYSReqIEEAARMAYAMDFISKMDNGldtvigengvlLSGGQRQRIAIAR 493
Cdd:PRK11607 96 MFQSYALFpHMTVEQNIAFglkqdklPKAEIASR--VNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 494 ALLRNSPILILDEATSALDTE-SERAIQAALDELQK-NRTSLVIAH-RLSTIEQADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
358-561 |
2.27e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.08 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDN-----GQILLDGHDL--REYTLASLRDQVALVSQNVHLFN 430
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 DTVANNIAY-ARTEEYS---REQIEEAARMAYAMDFISKMdngldtvIGENGVLLSGGQRQRIAIARALLRNSPILILDE 506
Cdd:PRK14243 105 KSIYDNIAYgARINGYKgdmDELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGS 561
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
342-569 |
2.29e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 92.97 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpGReTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLAslRDQ 418
Cdd:TIGR03410 1 LEVSNLNVYY-GQ-SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDitkLPPHERA--RAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNI--AYARTEEYSREQIEEAarmaYAMDFIskmdngLDTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:TIGR03410 77 IAYVPQGREIFPRlTVEENLltGLAALPRRSRKIPDEI----YELFPV------LKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 496 LRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEHR 569
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDEDK 223
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-568 |
2.48e-21 |
|
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: 92.20 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRF--YDIDNGQILLDGHDLREYTlaslrdqv 419
Cdd:cd03217 1 LEIKDLHVSVGGKEI--LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 alvsqnvhlfndtvanniayarteeysreqIEEAARMAYAMDFIS-------KMDNGLDTVigenGVLLSGGQRQRIAIA 492
Cdd:cd03217 71 ------------------------------PEERARLGIFLAFQYppeipgvKNADFLRYV----NEGFSGGEKKRNEIL 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 493 RALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIVVVEDGRIVERGShADLLEH 568
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLrEEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
362-581 |
2.54e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.56 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 362 IDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLRE----YTLASLRDQVALVSQNVHLFND-TVANN 436
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 437 IAYARTE---EYSREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:TIGR02142 96 LRYGMKRarpSERRISFERVIELL-----------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 514 ESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEhRGVYAQLHKMQFG 581
Cdd:TIGR02142 165 PRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWA-SPDLPWLAREDQG 234
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
70-316 |
2.87e-21 |
|
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: 94.41 E-value: 2.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 70 VVIGLML-----LRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALI 144
Cdd:cd18554 46 TIIGIMFfifliLRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 145 TVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQA 224
Cdd:cd18554 126 NIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEK 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 225 VETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLKSLTNV 304
Cdd:cd18554 206 HEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNS 285
|
250
....*....|..
gi 1336523670 305 NAQFQRGMAACQ 316
Cdd:cd18554 286 FTTLTQSFASMD 297
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
356-569 |
3.59e-21 |
|
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: 93.77 E-value: 3.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlreytlaslrdQVALVSQNVHLFNDTVAN 435
Cdd:cd03291 50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 436 NIAYART-EEYSREQIEEAARMAYAMDFISKMDNgldTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTE 514
Cdd:cd03291 117 NIIFGVSyDEYRYKSVVKACQLEEDITKFPEKDN---TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 515 SERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHR 569
Cdd:cd03291 194 TEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
342-555 |
5.11e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 96.54 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFY---DIDnGQILLDGHDLREYTLA-SLRD 417
Cdd:PRK13549 6 LEMKNITKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQASNIRdTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 QVALVSQNVHLFND-TVANNIayarteeYSREQIEEAARMAYAMDFIS--------KMDNGLDTVIGEngvlLSGGQRQR 488
Cdd:PRK13549 83 GIAIIHQELALVKElSVLENI-------FLGNEITPGGIMDYDAMYLRaqkllaqlKLDINPATPVGN----LGLGQQQL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 489 IAIARALLRNSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
340-561 |
6.03e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 340 GNLEFKDVTFTYpGRETP----ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL-----REY 410
Cdd:PRK13645 5 KDIILDNVSYTY-AKKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 TLASLRDQVALVSQ--NVHLFNDTVANNIAYARTEEYSREQiEEAARMAYAMDFISKMDNgldtVIGENGVLLSGGQRQR 488
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQ-EAYKKVPELLKLVQLPED----YVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTIEQ-ADEIVVVEDGRIVERGS 561
Cdd:PRK13645 159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvTHNMDQVLRiADEVIVMHEGKVISIGS 234
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
342-568 |
6.89e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 92.59 E-value: 6.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR-------ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLrEYTLAS 414
Cdd:COG4167 5 LEVRNLSKTFKYRtglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL-EYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQ-VALVSQNVhlfNDTVANNIAYAR------------TEEYSREQIEEAARM----AYAMDFISKMdngldtvigen 477
Cdd:COG4167 84 YRCKhIRMIFQDP---NTSLNPRLNIGQileeplrlntdlTAEEREERIFATLRLvgllPEHANFYPHM----------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 478 gvlLSGGQRQRIAIARALLRNSPILILDEATSALDTeSERA-IQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVED 553
Cdd:COG4167 150 ---LSSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqIINLMLELQEKLgiSYIYVSQHLGIVKHiSDKVLVMHQ 225
|
250
....*....|....*
gi 1336523670 554 GRIVERGSHADLLEH 568
Cdd:COG4167 226 GEVVEYGKTAEVFAN 240
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
349-568 |
1.13e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 93.23 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 349 FTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRD---------QV 419
Cdd:PRK15079 27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqmifQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLfndTVANNIAYA-RT--EEYSREQIEEAARmayAMdfisKMDNGL-DTVIGENGVLLSGGQRQRIAIARAL 495
Cdd:PRK15079 107 PLASLNPRM---TIGEIIAEPlRTyhPKLSRQEVKDRVK---AM----MLKVGLlPNLINRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 496 LRNSPILILDEATSALDTeserAIQAA----LDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK15079 177 ILEPKLIICDEPVSALDV----SIQAQvvnlLQQLQREmGLSLIfIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
356-565 |
1.27e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 96.52 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlreytlaslrdQVALVSQNVHLFNDTVAN 435
Cdd:TIGR01271 439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 436 NIAYART-EEYSREQIEEAARMAyamDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTE 514
Cdd:TIGR01271 506 NIIFGLSyDEYRYTSVIKACQLE---EDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 515 SERAI-QAALDELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADL 565
Cdd:TIGR01271 583 TEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
342-566 |
1.56e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 91.69 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGR-ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVA 420
Cdd:PRK13642 5 LEVENLVFKYEKEsDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNV--HLFNDTVANNIAYA-RTEEYSREQ----IEEAARMAYAMDFISKmdngldtvigeNGVLLSGGQRQRIAIAR 493
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGmENQGIPREEmikrVDEALLAVNMLDFKTR-----------EPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 494 ALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
357-565 |
1.61e-20 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 91.30 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKS-TIASL-------ITRFydidNGQILLDGhdlREYTLASLRDQ-VALVSQNVH 427
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAlgilpagVRQT----AGRVLLDG---KPVAPCALRGRkIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 428 LFNDTVANNIAYARTEEYSREQIEEAARMAYAMDFIskmdnGLD---TVIGENGVLLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK10418 90 SAFNPLHTMHTHARETCLALGKPADDATLTAALEAV-----GLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 505 DEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADL 565
Cdd:PRK10418 165 DEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
341-556 |
2.03e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 92.98 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVTFTYPGReTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASlRDqVA 420
Cdd:PRK11650 3 GLKLQAVRKSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLF-NDTVANNIAY----ARTEEYSREQ-IEEAARmayamdfISKMDNGLDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:PRK11650 80 MVFQNYALYpHMSVRENMAYglkiRGMPKAEIEErVAEAAR-------ILELEPLLDRKPRE----LSGGQRQRVAMGRA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIVVVEDGRI 556
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
342-557 |
3.75e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLASLRDQ 418
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANN------IAYARTEEYSReqieeaaRMAYAMDFISKMDNGLDTVIGengvlLSGGQRQRIAI 491
Cdd:PRK10908 81 IGMIFQDHHLLMDrTVYDNvaipliIAGASGDDIRR-------RVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTIEQAD-EIVVVEDGRIV 557
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLISRRSyRMLTLSDGHLH 216
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
345-567 |
3.90e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.23 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQ 424
Cdd:PRK10575 15 RNVSFRVPGRTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 NVHLFND-TVANNIAYARTEEY---------SREQIEEAARMAYAMDFISKMdngLDTvigengvlLSGGQRQRIAIARA 494
Cdd:PRK10575 93 QLPAAEGmTVRELVAIGRYPWHgalgrfgaaDREKVEEAISLVGLKPLAHRL---VDS--------LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAhRLSTIEQA----DEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELMR 237
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
51-314 |
4.49e-20 |
|
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: 90.97 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 51 LLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITy 130
Cdd:cd18570 28 LIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 131 DSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQM 210
Cdd:cd18570 107 DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIES 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 211 LKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFpSVME-TLTAGTItVVFS 289
Cdd:cd18570 187 LKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSY-LVIKgQLSLGQL-IAFN 264
|
250 260
....*....|....*....|....*.
gi 1336523670 290 SMIA-LMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18570 265 ALLGyFLGPIENLINLQPKIQEAKVA 290
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-567 |
4.96e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.05 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpGRETPAlRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIA---YARTEEYSREQIEEAARMAYAMdfiskMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:PRK10253 86 LAQNATTPGDiTVQELVArgrYPHQPLFTRWRKEDEEAVTKAM-----QATGITHLADQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGS-----HADLLE 567
Cdd:PRK10253 161 ETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQGApkeivTAELIE 238
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
341-560 |
5.51e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 92.01 E-value: 5.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytLASLRDQVA 420
Cdd:PRK11000 3 SVTLRNVTKAYG--DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND--VPPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLF-NDTVANNIAY-------ARTEEYSR-EQIEEAARMAYAMDFISKMdngldtvigengvlLSGGQRQRIAI 491
Cdd:PRK11000 79 MVFQSYALYpHLSVAENMSFglklagaKKEEINQRvNQVAEVLQLAHLLDRKPKA--------------LSGGQRQRVAI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAH-RLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
342-514 |
6.67e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID---NGQILLDGHDLReyTLASLRDQ 418
Cdd:COG4136 2 LSLENLTITLGGR--PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT--ALPAEQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLF-NDTVANNIAYARTEEYSREQIEEAARMAYAmdfiskmDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
Cdd:COG4136 78 IGILFQDDLLFpHLSVGENLAFALPPTIGRAQRRARVEQALE-------EAGLAGFADRDPATLSGGQRARVALLRALLA 150
|
170
....*....|....*..
gi 1336523670 498 NSPILILDEATSALDTE 514
Cdd:COG4136 151 EPRALLLDEPFSKLDAA 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
347-566 |
1.55e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 347 VTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRF-------YDidNGQILLDGHDL---REYTLASLR 416
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppvvYP--SGDIRFHGESLlhaSEQTLRGVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 -DQVALVSQN--VHLfndTVANNIAYARTEEYS--REQIEEAARmayamdfiSKMDNGLDTVIGENGV--------LLSG 483
Cdd:PRK15134 91 gNKIAMIFQEpmVSL---NPLHTLEKQLYEVLSlhRGMRREAAR--------GEILNCLDRVGIRQAAkrltdyphQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQN 239
|
....*.
gi 1336523670 561 SHADLL 566
Cdd:PRK15134 240 RAATLF 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-566 |
1.55e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH------DLREYTLASLRDQVALVSQNVHLF-ND 431
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFpHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 TVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTvIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSAL 511
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 512 DTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
358-555 |
1.63e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.51 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD---LREYTLAslRDQVALVSQNVHLFND-TV 433
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPGHQIA--RMGVVRTFQHVRLFREmTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIAYA--------------RTEEYSREQIEEAARMAYAMDFIskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgllKTPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIVVVEDGR 555
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGT 231
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
342-560 |
2.71e-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: 86.57 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReytlASLRDQVAL 421
Cdd:cd03269 1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIAY-ARTEEYSREQIEEAARmayamDFISKMD--NGLDTVIGEngvlLSGGQRQRIAIARALLR 497
Cdd:cd03269 75 LPEERGLYPKmKVIDQLVYlAQLKGLKKEEARRRID-----EWLERLElsEYANKRVEE----LSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNRTSLVI-AHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03269 146 DPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILsTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
44-289 |
4.57e-19 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 87.90 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 44 MLSLLKPL-----LDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDK 118
Cdd:cd18567 16 LFALASPLylqlvIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 119 QSTGTLLSRItyDS-EQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLIlIVLAPIVSMAIRVVS-KRFRNIsknm 196
Cdd:cd18567 96 RHLGDIVSRF--GSlDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALI-VLAAVALYALLRLALyPPLRRA---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 197 qnTMGQVTTSAEQ------MLKGHKEVLMFGGQAVETKRF-----DKVSNKMRLQGMKMvSASSISdpviQLIASLALAF 265
Cdd:cd18567 169 --TEEQIVASAKEqshfleTIRGIQTIKLFGREAEREARWlnllvDAINADIRLQRLQI-LFSAAN----GLLFGLENIL 241
|
250 260
....*....|....*....|....*
gi 1336523670 266 VLYAASFpSVME-TLTAGTITVVFS 289
Cdd:cd18567 242 VIYLGAL-LVLDgEFTVGMLFAFLA 265
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
314-561 |
7.14e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.15 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 314 ACQTLFA---------ILDSEQEKDEGKLViERAKGNLEFKDVTFTYPGR---------ETPALRNIDLNIQEGKTVALV 375
Cdd:PRK15134 240 RAATLFSapthpytqkLLNSEPSGDPVPLP-EPASPLLDVEQLQVAFPIRkgilkrtvdHNVVVKNISFTLRPGETLGLV 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 376 GRSGSGKSTIASLITRFYDiDNGQILLDGHDLREYT---LASLRDQVALVSQ------NVHLfndTVANNIAYARTEEY- 445
Cdd:PRK15134 319 GESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQdpnsslNPRL---NVLQIIEEGLRVHQp 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 446 --SREQIEEaaRMAYAMdfiskMDNGLDTVI-----GEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESERA 518
Cdd:PRK15134 395 tlSAAQREQ--QVIAVM-----EEVGLDPETrhrypAE----FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQ 463
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1336523670 519 IQAALDELQ-KNRTS-LVIAHRLSTIEQ-ADEIVVVEDGRIVERGS 561
Cdd:PRK15134 464 ILALLKSLQqKHQLAyLFISHDLHVVRAlCHQVIVLRQGEVVEQGD 509
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
342-565 |
7.47e-19 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 85.50 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTlASLRDQVAL 421
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNDTVA--NNIAYARTEEYSREQIEEaaRMAYAMDFISKMDNGlDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:cd03265 78 VFQDLSVDDELTGweNLYIHARLYGVPGAERRE--RIDELLDFVGLLEAA-DRLVKT----YSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADL 565
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
356-556 |
1.27e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL---ASLRDQ-VALVSQNVHLFND 431
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakAELRNQkLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 -TVANNIAYAR-TEEYSREQIEEAAR-MAYAMdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:PRK11629 102 fTALENVAMPLlIGKKKPAEINSRALeMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 509 SALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:PRK11629 174 GNLDARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
342-555 |
1.40e-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: 82.50 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLdGHDLReytlaslrdqVAL 421
Cdd:cd03221 1 IELENLSKTYGGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQnvhlfndtvanniayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARALLRNSPI 501
Cdd:cd03221 68 FEQ--------------------------------------------------------LSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQknRTSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
342-565 |
1.40e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAsLRDQVA- 420
Cdd:PRK15439 12 LCARSISKQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 -LVSQNVHLF-NDTVANNIAY--ARTEEYSREQIEEAARMAYAMDfiskmdngLDTVIGengvLLSGGQRQRIAIARALL 496
Cdd:PRK15439 89 yLVPQEPLLFpNLSVKENILFglPKRQASMQKMKQLLAALGCQLD--------LDSSAG----SLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHADL 565
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVfISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
342-576 |
1.63e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.01 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK13652 4 IETRDLCYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNV--HLFNDTVANNIAYART-----EEYSREQIEEAARMAYAMDFISKMDNGLdtvigengvllSGGQRQRIAIARA 494
Cdd:PRK13652 83 VFQNPddQIFSPTVEQDIAFGPInlgldEETVAHRVSSALHMLGLEELRDRVPHHL-----------SGGEKKRVAIAGV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVI--AHRLSTI-EQADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:PRK13652 152 IAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIfsTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
....*
gi 1336523670 572 YAQLH 576
Cdd:PRK13652 232 LARVH 236
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
342-565 |
2.66e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.55 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReytlASLRDQVA- 420
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 ------LVSQNvhlfndTVANNIAY-ARTEEYSREQIEEAAR--------MAYAMDFISKmdngldtvigengvlLSGGQ 485
Cdd:COG4152 76 lpeergLYPKM------KVGEQLVYlARLKGLSKAEAKRRADewlerlglGDRANKKVEE---------------LSKGN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSlVI--AHRLSTIEQ-ADEIVVVEDGRIVERGSH 562
Cdd:COG4152 135 QQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTT-VIfsSHQMELVEElCDRIVIINKGRKVLSGSV 213
|
...
gi 1336523670 563 ADL 565
Cdd:COG4152 214 DEI 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
354-571 |
2.68e-18 |
|
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: 84.13 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL-ASLRDQVALVSQNVHLFND- 431
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 TVANNI-AYARTEEYSREQIEEaaRMAYAMDfiskmDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:cd03218 91 TVEENIlAVLEIRGLSKKEREE--KLEELLE-----EFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 511 LDTESERAIQAALDELQKNRTSLVIA-HRLS-TIEQADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELV 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
358-556 |
5.12e-18 |
|
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: 82.09 E-value: 5.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRDQVALvsqnvhlfndtvanNI 437
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIRA--------------GI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 438 AYArTEEYSREQIeeaarmayamdfISKMDngldtvIGEN---GVLLSGGQRQRIAIARALLRNSPILILDEATSALDTE 514
Cdd:cd03215 78 AYV-PEDRKREGL------------VLDLS------VAENialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1336523670 515 SERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:cd03215 139 AKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEGRI 182
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
80-292 |
6.93e-18 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 84.64 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 80 VTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVM 159
Cdd:cd18558 74 ITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFII 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 160 MFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRL 239
Cdd:cd18558 154 GFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKR 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 240 QGMKMVSASSISDPVIQLI--ASLALAFvLYAASFPSVMETLTAGTITVVFSSMI 292
Cdd:cd18558 234 NGIKKAITFNISMGAAFLLiyASYALAF-WYGTYLVTQQEYSIGEVLTVFFSVLI 287
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
359-557 |
7.38e-18 |
|
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: 82.90 E-value: 7.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLrdqvaLVSQNVHLFN-DTVANNI 437
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 438 AYA-------RTEEYSREQIEEAARMAyamdfisKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:TIGR01184 76 ALAvdrvlpdLSKSERRAIVEEHIALV-------GLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1336523670 511 LDTESERAIQAALDEL-QKNR-TSLVIAHRLstieqaDEIVVVEDgRIV 557
Cdd:TIGR01184 145 LDALTRGNLQEELMQIwEEHRvTVLMVTHDV------DEALLLSD-RVV 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
342-567 |
9.00e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.01 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRE---TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI----LLDGHDLREYTLAS 414
Cdd:PRK13643 2 IKFEKVNYTYQPNSpfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQ--NVHLFNDTVANNIAYA-RTEEYSREQIEEAARMAYAMDFISKmdngldTVIGENGVLLSGGQRQRIAI 491
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGpQNFGIPKEKAEKIAAEKLEMVGLAD------EFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-570 |
9.96e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.88 E-value: 9.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI-LLDGHDLREYTLAslRDQVA 420
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLA--RARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANN-IAYARTEEYSREQIEEAarMAYAMDFiSKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRN 498
Cdd:PRK13536 118 VVPQFDNLDLEfTVRENlLVFGRYFGMSTREIEAV--IPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 499 SPILILDEATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGR-IVERGSHADLLEHRG 570
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRkIAEGRPHALIDEHIG 265
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
342-561 |
1.04e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH--DLREYTLASLRDQV 419
Cdd:PRK13636 6 LKVEELNYNYSD-GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNV--HLFNDTVANNIAY-ARTEEYSREQIEEAARMAYAMDFISKMDNgldtvigENGVLLSGGQRQRIAIARALL 496
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSFgAVNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIE-QADEIVVVEDGRIVERGS 561
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGN 225
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
342-538 |
1.80e-17 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 79.89 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI-LLDGHDL-----REY-TLAS 414
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGEDLlflpqRPYlPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQNVhlfndtvanniayarteeysreqieeaarmayamdfiskmdngldtvigengvlLSGGQRQRIAIARA 494
Cdd:cd03223 80 LREQLIYPWDDV------------------------------------------------------LSGGEQQRLAFARL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELqknRTSLV-IAHR 538
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVIsVGHR 147
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
342-558 |
1.84e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVAL 421
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFNdtvanniayaRTEEYSREQIEEAARMAYaMDFIsKMDNGLDTvigENGVL----LSGGQRQRIAIARALLR 497
Cdd:PRK10522 402 VFTDFHLFD----------QLLGPEGKPANPALVEKW-LERL-KMAHKLEL---EDGRIsnlkLSKGQKKRLALLLALAE 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 498 NSPILILDEATSALDTESERAI-QAALDELQ-KNRTSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:PRK10522 467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
354-567 |
1.86e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH---DLREYTLASLRDQVALVSQNVHLFN 430
Cdd:PRK10261 335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 D---TVANNIAYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEA 507
Cdd:PRK10261 415 DprqTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHE----FSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 508 TSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
342-569 |
4.20e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.28 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRD-QVA 420
Cdd:PRK10762 5 LQLKGIDKAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSsQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVS---QNVHLF-NDTVANNIAYAR--TEEYSR----EQIEEAARMAYAMdfisKMDNGLDTVIGEngvlLSGGQRQRIA 490
Cdd:PRK10762 80 GIGiihQELNLIpQLTIAENIFLGRefVNRFGRidwkKMYAEADKLLARL----NLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSAL-DTESErAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIVVVEDGRIVERGSHADLLE 567
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETE-SLFRVIRELKSQGRGIVyISHRLKEIfEICDDVTVFRDGQFIAEREVADLTE 230
|
..
gi 1336523670 568 HR 569
Cdd:PRK10762 231 DS 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
358-561 |
5.52e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.21 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTI----ASLITRfYDIDNGQILLDGHDL-REYTLA----SLRDQVALVSQNVHL 428
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLlrhlSGLITG-DKSAGSHIELLGRTVqREGRLArdirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 429 FND-TVANNI--------AYART--EEYSREQIEEAARMAYAMDFISKMDNGLDTvigengvlLSGGQRQRIAIARALLR 497
Cdd:PRK09984 98 VNRlSVLENVligalgstPFWRTcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEQADEIVVVEDGRIVERGS 561
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-561 |
6.57e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.07 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLrEYTLASLRDQVALVSQNVHLFND-TVAN 435
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 436 NIA-YARTEEYSRE--QIEEAARMAyamdfiskmDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALD 512
Cdd:TIGR01257 1023 HILfYAQLKGRSWEeaQLEMEAMLE---------DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 513 TESERAIQAALDELQKNRTSLVIAHRLSTIE-QADEIVVVEDGRIVERGS 561
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
342-561 |
6.91e-17 |
|
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: 83.70 E-value: 6.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLI--TRFYDIDNGQIL------------------ 401
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 402 ---------------LDGHDLREYTLASLRDQVALVSQNVHLF--NDTVANNIAYARTE-EYSREqieEAARMAYAMDFI 463
Cdd:TIGR03269 79 gepcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEiGYEGK---EAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 464 SKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST 541
Cdd:TIGR03269 156 VQLSHRITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231
|
250 260
....*....|....*....|.
gi 1336523670 542 IEQ-ADEIVVVEDGRIVERGS 561
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGT 252
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-558 |
6.98e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 83.69 E-value: 6.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID--NGQILLDGhDLREYtlASLRD-- 417
Cdd:NF040905 2 LEMRGITKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDG-EVCRF--KDIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 ---------QVALVSQnvhLfndTVANNIaYARTEEYSREQIEEAARMAYAMDFISKMdnGL----DTVIGENGVllsgG 484
Cdd:NF040905 77 algiviihqELALIPY---L---SIAENI-FLGNERAKRGVIDWNETNRRARELLAKV--GLdespDTLVTDIGV----G 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEQ-ADEIVVVEDGRIVE 558
Cdd:NF040905 144 KQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
352-568 |
7.58e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 7.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 352 PGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlreyTLASLrdqVAL---------V 422
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgagfhpeltG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHLfndtvanniaYARTEEYSREQIEEaaRMAYAMDFiSKMDNGLDTVIGengvLLSGGQRQRIAIARALLRNSPIL 502
Cdd:COG1134 106 RENIYL----------NGRLLGLSRKEIDE--KFDEIVEF-AELGDFIDQPVK----TYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 503 ILDEATSALDTE-SERAiQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:COG1134 169 LVDEVLAVGDAAfQKKC-LARIRELRESGRTVIFVsHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
342-568 |
9.86e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 81.69 E-value: 9.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKD--VTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIA----SLITRFYDID-----NGQILLDghdLREY 410
Cdd:PRK09473 13 LDVKDlrVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfalmGLLAANGRIGgsatfNGREILN---LPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 TLASLR-DQVALVsqnvhlFNDTVANNIAYARTEE-----------YSR-EQIEEAARMAYAMdfisKMDNGLDTvIGEN 477
Cdd:PRK09473 90 ELNKLRaEQISMI------FQDPMTSLNPYMRVGEqlmevlmlhkgMSKaEAFEESVRMLDAV----KMPEARKR-MKMY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 478 GVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEQ-ADEIVVVEDG 554
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAG 238
|
250
....*....|....
gi 1336523670 555 RIVERGSHADLLEH 568
Cdd:PRK09473 239 RTMEYGNARDVFYQ 252
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
342-568 |
1.08e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.00 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASlRDQVAL 421
Cdd:PRK13537 8 IDFRNVEKRYG--DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNI-AYARTEEYSREQIEeaARMAYAMDFiSKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNS 499
Cdd:PRK13537 85 VPQFDNLDPDfTVRENLlVFGRYFGLSAAAAR--ALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
357-573 |
1.34e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhdlREYTLASLRDQ----VALVSQNVH---LF 429
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG---KPVRIRSPRDAiragIAYVPEDRKgegLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 430 -NDTVANNIAYARTEEYSREQ-IEEAARMAYAMDFISKMD---NGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILIL 504
Cdd:COG1129 343 lDLSIRENITLASLDRLSRGGlLDRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 505 DEATSALDTESERAIQAALDELQKNRTSLVIAhrlST-----IEQADEIVVVEDGRIVERGSHADLLEHRGVYA 573
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI---SSelpelLGLSDRILVMREGRIVGELDREEATEEAIMAA 489
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
355-566 |
1.61e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 79.63 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR-------------EYTLASLRDQVAL 421
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLFND-TVANNIAYARTEEYSREQIEEAARmayAMDFISKMdnGLD-TVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK10619 97 VFQHFNLWSHmTVLENVMEAPIQVLGLSKQEARER---AVKYLAKV--GIDeRAQGKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 500 PILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK10619 172 EVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
60-309 |
1.75e-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: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 60 DRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSS 139
Cdd:cd18568 37 NISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVGDIITRF-QENQKIRRFL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 140 SSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVlm 219
Cdd:cd18568 116 TRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATI-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 220 fGGQAVETKRFDKVSNKM------RLQGMKMVSASSIsdpVIQLIASLALAFVL-YAASFpsVM-ETLTAGTItVVFSSM 291
Cdd:cd18568 194 -KALAAERPIRWRWENKFakalntRFRGQKLSIVLQL---ISSLINHLGTIAVLwYGAYL--VIsGQLTIGQL-VAFNML 266
|
250
....*....|....*....
gi 1336523670 292 IA-LMRPLKSLTNVNAQFQ 309
Cdd:cd18568 267 FGsVINPLLALVGLWDELQ 285
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-557 |
1.87e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.85 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVT--FTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLIT---RFYDIDNGQILLDGHDLREYTLasl 415
Cdd:cd03234 3 VLPWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPDQF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 416 RDQVALVSQ-NVHLFNDTVANNIAYA---RTEEYSREQIEEAarmayaMDFISKMDNGLDTVIGENGVL-LSGGQRQRIA 490
Cdd:cd03234 80 QKCVAYVRQdDILLPGLTVRETLTYTailRLPRKSSDAIRKK------RVEDVLLRDLALTRIGGNLVKgISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAH--RLSTIEQADEIVVVEDGRIV 557
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
351-559 |
1.96e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 79.36 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 351 YPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHdlreyTLASLRDQVALVSQNVHLFN 430
Cdd:PRK11248 11 YGGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-----PVEGPGAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 -DTVANNIAYA-RTEEYSREQIEEAARmayamdfisKMDNGLDTVIGENGVL--LSGGQRQRIAIARALLRNSPILILDE 506
Cdd:PRK11248 84 wRNVQDNVAFGlQLAGVEKMQRLEIAH---------QMLKKVGLEGAEKRYIwqLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 507 ATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEQ----ADEIVVVE--DGRIVER 559
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwqETGKQVLLITH---DIEEavfmATELVLLSpgPGRVVER 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
354-560 |
2.00e-16 |
|
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: 78.73 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlreytlaslrdqVALVSQNVHLFND-T 432
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV------------SSLLGLGGGFNPElT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIA-YARTEEYSREQIEEaaRMAYAMDFiSKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSAL 511
Cdd:cd03220 101 GRENIYlNGRLLGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 512 DTESERAIQAALDELQKNRTSLVIA-HRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
45-309 |
2.27e-16 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 79.86 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 45 LSLLKPLL-----DDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQ 119
Cdd:cd18555 17 LTLLIPILtqyviDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 120 STGTLLSRITyDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLApIVSMAIRVVSKRfRNISKNMQNT 199
Cdd:cd18555 97 SSGDLLFRAN-SNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLLLLTRK-KIKKLNQEEI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 200 MGQVTTSAEQ--MLKGHKEVLMFGgqaVETKRFDKVSN-----------KMRLQGmKMVSASSIsdpvIQLIASLalaFV 266
Cdd:cd18555 174 VAQTKVQSYLteTLYGIETIKSLG---SEKNIYKKWENlfkkqlkafkkKERLSN-ILNSISSS----IQFIAPL---LI 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1336523670 267 LYAASFPSVMETLTAGTItVVFSSM-IALMRPLKSLTNVNAQFQ 309
Cdd:cd18555 243 LWIGAYLVINGELTLGEL-IAFSSLaGSFLTPIVSLINSYNQFI 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
358-566 |
3.39e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 79.06 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLrEYTLASLRdqvalvSQNVHL-FNDtvann 436
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYR------SQRIRMiFQD----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 437 iayARTEEYSREQIEEAarmayaMDFISKMDNGLDTVIGENGV-------------------LLSGGQRQRIAIARALLR 497
Cdd:PRK15112 96 ---PSTSLNPRQRISQI------LDFPLRLNTDLEPEQREKQIietlrqvgllpdhasyyphMLAPGQKQRLGLARALIL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 498 NSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
346-561 |
3.83e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.83 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 346 DVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTlaslRDQVALVSQN 425
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRS----RQVIELSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 426 VHLFNDTVANNIAYARTEEYSR--------EQIEEAARM------AYAMDFISKMdngLDTV-IGENGVL-------LSG 483
Cdd:PRK10261 95 AAQMRHVRGADMAMIFQEPMTSlnpvftvgEQIAESIRLhqgasrEEAMVEAKRM---LDQVrIPEAQTIlsryphqLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV--IAHRLSTI-EQADEIVVVEDGRIVERG 560
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVifITHDMGVVaEIADRVLVMYQGEAVETG 251
|
.
gi 1336523670 561 S 561
Cdd:PRK10261 252 S 252
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
342-544 |
6.90e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.77 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDN-----GQILLDGHDL--REYTLAS 414
Cdd:PRK14258 8 IKVNNLSFYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 415 LRDQVALVSQNVHLFNDTVANNIAYA------RTEEYSREQIEEAARMAYAMDFISKMdngldtvIGENGVLLSGGQRQR 488
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKDADLWDEIKHK-------IHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTESERAIQAALD--ELQKNRTSLVIAHRLSTIEQ 544
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSR 216
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
359-561 |
7.16e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 81.69 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKST----IASLITRFYDIDNGQILLDGHDLREYtLASLRDQVALVSQN-VHLFNDTV 433
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETdVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIAYA--------RTEEYSREqiEEAARMA-YAMDfISKMDNGLDTVIGEN---GVllSGGQRQRIAIARALLRNSPI 501
Cdd:TIGR00956 156 GETLDFAarcktpqnRPDGVSRE--EYAKHIAdVYMA-TYGLSHTRNTKVGNDfvrGV--SGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 502 LILDEATSALDT----ESERAIQAALDELqkNRTSLVIAHRLS--TIEQADEIVVVEDGRIVERGS 561
Cdd:TIGR00956 231 QCWDNATRGLDSatalEFIRALKTSANIL--DTTPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
355-570 |
7.77e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 77.37 E-value: 7.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRF--YDIDNGQILLDGHDLREYTlASLRDQVALVSQNVHLFNDT 432
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLE-PEERAHLGIFLAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIAYARTeEYSREQIEEAARMAYAMDFISKMDNGLDtVIGENGVLL--------SGGQRQRIAIARALLRNSPILIL 504
Cdd:CHL00131 98 GVSNADFLRL-AYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 505 DEATSALDTESERAIQAALDELQKNRTSLV-IAH--RLSTIEQADEIVVVEDGRIVERGSH--ADLLEHRG 570
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAelAKELEKKG 246
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
354-560 |
1.21e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.60 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTV 433
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFGQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIAYARTEEYSREQIEEAARMAYAMDFIsKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 514 ESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERG 560
Cdd:cd03267 187 VAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
342-557 |
1.42e-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: 79.48 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID--NGQILLDGHDLREytlASLRDQ- 418
Cdd:TIGR02633 2 LEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKA---SNIRDTe 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 ---VALVSQNVHLFND-TVANNIAYARteeysrEQIEEAARMAYA---------MDFISKMDNGLDTVIGENGvllsGGQ 485
Cdd:TIGR02633 77 ragIVIIHQELTLVPElSVAENIFLGN------EITLPGGRMAYNamylraknlLRELQLDADNVTRPVGDYG----GGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1336523670 486 RQRIAIARALLRNSPILILDEATSALdTESERAIQAAL--DELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
66-309 |
1.45e-15 |
|
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: 77.52 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 66 WMPLVVIGL---MLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYdSEQVASSSSSA 142
Cdd:cd18569 40 WLRPLLLGMaltALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQS-NDRVANLLSGQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 143 LITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQ---VTTSAEQMLKGHK---- 215
Cdd:cd18569 119 LATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKltgTTMSGLQMIETLKasga 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 216 EVLMF----GGQAvetkrfdKVSNkmrlQGMKMVSASSISDPVIQLIASLALAFVLYAASFpSVME-TLTAGTItVVFSS 290
Cdd:cd18569 199 ESDFFsrwaGYQA-------KVLN----AQQELGRTNQLLGALPTLLSALTNAAILGLGGL-LVMDgALTIGML-VAFQS 265
|
250 260
....*....|....*....|
gi 1336523670 291 -MIALMRPLKSLTNVNAQFQ 309
Cdd:cd18569 266 lMASFLAPVNSLVGLGGTLQ 285
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
342-571 |
1.63e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPgrETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLAS-LRDQVA 420
Cdd:PRK11614 6 LSFDKVSAHYG--KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIA----YARTEEYSReqieeaaRMAYAMDFISKMdngLDTVIGENGVlLSGGQRQRIAIARAL 495
Cdd:PRK11614 84 IVPEGRRVFSRmTVEENLAmggfFAERDQFQE-------RIKWVYELFPRL---HERRIQRAGT-MSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 496 LRNSPILILDEATSALdteSERAIQAALDELQKNRTS-----LVIAHRLSTIEQADEIVVVEDGRIVERGSHADLLEHRG 570
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREQgmtifLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 1336523670 571 V 571
Cdd:PRK11614 230 V 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
342-567 |
2.57e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 77.05 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpGRETP----ALRNIDLNIQEGKTVALVGRSGSGKST------------IASLITRFYDI-DNGQILLDG 404
Cdd:PRK13651 3 IKVKNIVKIF-NKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTfiehlnalllpdTGTIEWIFKDEkNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 405 HDLREYTLA-----------SLRDQVALVSQ--NVHLFNDTVANNIAY-ARTEEYSREQIEEAARmayamDFISKMdnGL 470
Cdd:PRK13651 82 KVLEKLVIQktrfkkikkikEIRRRVGVVFQfaEYQLFEQTIEKDIIFgPVSMGVSKEEAKKRAA-----KYIELV--GL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 471 D-TVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL-STIEQADE 547
Cdd:PRK13651 155 DeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLdNVLEWTKR 234
|
250 260
....*....|....*....|
gi 1336523670 548 IVVVEDGRIVERGSHADLLE 567
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDILS 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
342-557 |
5.78e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTyPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQ-VA 420
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVH---LFND-TVANNIA--YARTEEYSR-EQIEEAARMAYAMDFISKMD---NGLDTVIGengvLLSGGQRQRIA 490
Cdd:COG3845 337 YIPEDRLgrgLVPDmSVAENLIlgRYRRPPFSRgGFLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVI 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 491 IARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTI-EQADEIVVVEDGRIV 557
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAvLLISEDLDEIlALSDRIAVMYEGRIV 481
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
359-561 |
7.64e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 77.78 E-value: 7.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKST----IASLITRFYDIdNGQILLDGH--DLREYTLASlrdqvALVSQNVHLFNDT 432
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTlmnaLAFRSPKGVKG-SGSVLLNGMpiDAKEMRAIS-----AYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIAYARTEEYSREQIEEAARMAYAMDFISKMdnGL----DTVIGENGVL--LSGGQRQRIAIARALLRNSPILILDE 506
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRVTKKEKRERVDEVLQAL--GLrkcaNTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 507 ATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEQADEIVVVEDGRIVERGS 561
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
342-565 |
1.50e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLA-SLRDQVA 420
Cdd:PRK09700 6 ISMAGIGKSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNVHLFND-TVANNIAYAR--TEEYSREQIEEAARM---AYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARA 494
Cdd:PRK09700 84 IIYQELSVIDElTVLENLYIGRhlTKKVCGVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 495 LLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIVERGSHADL 565
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-568 |
1.90e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDID-----NGQILLDGHDL--REYTLASLRDQVALVSQNVHLF-N 430
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFpH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 431 DTVANNIA-------YARTEEYSREQIEEAARMAYAMDfisKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILI 503
Cdd:PRK14267 100 LTIYDNVAigvklngLVKSKKELDERVEWALKKAALWD---EVKDRLNDYPSN----LSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEH 568
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
30-232 |
3.04e-14 |
|
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: 73.50 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 30 AAVALVFNAASDTFMLSLLKPLLDD-----GFGKTDRSVLLwMPLVVIGLMLLRGVTSYISSYCISwvsgKVVMTMRRRL 104
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGiviekSQDKFSRAIII-MGLLAIASSVAAGIRGGLFTLAMA----RLNIRIRNLL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 105 FSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRV 184
Cdd:cd18784 76 FRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1336523670 185 VSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDK 232
Cdd:cd18784 156 YGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSE 203
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
354-557 |
3.51e-14 |
|
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: 71.52 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKST----IASLITRFYDIdNGQILLDGHDLREyTLASLRDQVALVSQN-VHL 428
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKE-FAEKYPGEIIYVSEEdVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 429 FNDTVanniayarteeysREQIEEAARMayamdfiskmdNGLDTVIGengvlLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:cd03233 96 PTLTV-------------RETLDFALRC-----------KGNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 509 SALDTESeraiqaALDELQKNRTslvIAH--RLSTI-----------EQADEIVVVEDGRIV 557
Cdd:cd03233 147 RGLDSST------ALEILKCIRT---MADvlKTTTFvslyqasdeiyDLFDKVLVLYEGRQI 199
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
351-571 |
6.22e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.85 E-value: 6.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 351 YPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL-ASLRDQVALVSQNVHLF 429
Cdd:PRK10895 13 YKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 430 ND-TVANNIAYART--EEYSREQIEEAARMAYAMDFISKMDNGLdtvigenGVLLSGGQRQRIAIARALLRNSPILILDE 506
Cdd:PRK10895 91 RRlSVYDNLMAVLQirDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 507 ATSALDTESERAIQAALDELQKNRTSLVIA-HRL-STIEQADEIVVVEDGRIVERGSHADLLEHRGV 571
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
346-560 |
7.82e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 346 DVTFTYPGRETpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLrdqVALVSQN 425
Cdd:PRK15056 11 DVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 426 VH-------LFNDTVA----NNIAYAR-TEEYSREQIEEAARMAYAMDFISKMdngldtvIGEngvlLSGGQRQRIAIAR 493
Cdd:PRK15056 87 EEvdwsfpvLVEDVVMmgryGHMGWLRrAKKRDRQIVTAALARVDMVEFRHRQ-------IGE----LSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 494 ALLRNSPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEIVVVEDGRIVERG 560
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
342-536 |
1.27e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDlreYTLASLRDQVAL 421
Cdd:PRK13539 3 LEGEDLACVRGGRV--LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VS-QNVHLFNDTVANNIAY-ARTEEYSREQIEEAArmaYAMdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK13539 78 LGhRNAMKPALTVAENLEFwAAFLGGEELDIAAAL---EAV--------GLAPLAHLPFGYLSAGQKRRVALARLLVSNR 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1336523670 500 PILILDEATSALDTESERAIqAALDELQKNRTSLVIA 536
Cdd:PRK13539 147 PIWILDEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
47-314 |
1.56e-13 |
|
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: 71.16 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 47 LLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLS 126
Cdd:cd18561 18 LLARALARIFAGGPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 127 RITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTS 206
Cdd:cd18561 98 TVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 207 AEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITV 286
Cdd:cd18561 178 FLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLL 257
|
250 260
....*....|....*....|....*...
gi 1336523670 287 VFSSMIALMRPLKSLTNVNAQFQRGMAA 314
Cdd:cd18561 258 ILFLSREFFRPLRDLGAYWHAGYQGISA 285
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-566 |
1.75e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 346 DVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDI-----DNGQILLDGHDLREY-TLASLRDQV 419
Cdd:PRK14271 26 NLTLGFAGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQNVHLFNDTVANNIaYARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK14271 104 GMLFQRPNPFPMSIMDNV-LAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
366-580 |
1.89e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 70.35 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 366 IQEGKTVALVGRSGSGKST----IASLITrfydiDNGQILLDGHDLREYTLASLRDQVALVSQNVH-LFNDTV----ANN 436
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTllarMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRAYLSQQQTpPFAMPVfqylTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 437 IAYARTEEYSREQIEEAARMAYAMDFISKMDNGldtvigengvlLSGGQRQRIAIARALLRNSP-------ILILDEATS 509
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQ-----------LSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 510 ALDTeserAIQAALDEL-----QKNRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHADLLEHRGVyAQLHKMQF 580
Cdd:PRK03695 163 SLDV----AQQAALDRLlselcQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL-AQVFGVNF 234
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
342-506 |
2.00e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL---AslRDQ 418
Cdd:COG1137 4 LEAENLVKSYGKR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkrA--RLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 VALVSQNVHLFND-TVANNI-AYARTEEYSREQIEEaaRMAYAMDfiskmDNGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:COG1137 80 IGYLPQEASIFRKlTVEDNIlAVLELRKLSKKEREE--RLEELLE-----EFGITHLRKSKAYSLSGGERRRVEIARALA 152
|
170
....*....|
gi 1336523670 497 RNSPILILDE 506
Cdd:COG1137 153 TNPKFILLDE 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
324-567 |
2.43e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.53 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 324 SEQEKDEgklVIERAKGNLEFKDVTFTYPGRE---TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQI 400
Cdd:TIGR03269 265 SEVEKEC---EVEVGEPIIKVRNVSKRYISVDrgvVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 401 -------LLDGHDLREYTLASLRDQVALVSQNVHLF-NDTVANNIayarTEEYSREQIEEAARMAYAMDFIS------KM 466
Cdd:TIGR03269 342 nvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELPDELARMKAVITLKMvgfdeeKA 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 467 DNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESERA----IQAALDELqkNRTSLVIAHRLSTI 542
Cdd:TIGR03269 418 EEILDKYPDE----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDvthsILKAREEM--EQTFIIVSHDMDFV 491
|
250 260
....*....|....*....|....*.
gi 1336523670 543 -EQADEIVVVEDGRIVERGSHADLLE 567
Cdd:TIGR03269 492 lDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
342-571 |
3.54e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGH--DLREYTLASLRDQV 419
Cdd:PRK13638 2 LATSDLWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 420 ALVSQN--VHLFNDTVANNIAYA------RTEEYSReQIEEAARMAYAMDFISKMDNgldtvigengvLLSGGQRQRIAI 491
Cdd:PRK13638 80 ATVFQDpeQQIFYTDIDSDIAFSlrnlgvPEAEITR-RVDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVERG------SHA 563
Cdd:PRK13638 148 AGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACT 227
|
....*...
gi 1336523670 564 DLLEHRGV 571
Cdd:PRK13638 228 EAMEQAGL 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
341-565 |
4.59e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 341 NLEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKS----TIASLITRFYDIDNGQILLDGHDLREYTLASLR 416
Cdd:PRK11022 5 NVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 DqvaLVSQNVHL-FNDTVAN-NIAYarTEEYsreQIEEA----------ARMAYAMDFISKM-----DNGLDTVIGEngv 479
Cdd:PRK11022 85 N---LVGAEVAMiFQDPMTSlNPCY--TVGF---QIMEAikvhqggnkkTRRQRAIDLLNQVgipdpASRLDVYPHQ--- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 480 lLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTI-EQADEIVVVEDGRI 556
Cdd:PRK11022 154 -LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
....*....
gi 1336523670 557 VERGSHADL 565
Cdd:PRK11022 233 VETGKAHDI 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
359-566 |
4.63e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.86 E-value: 4.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTI---------ASLITRFYDIdNGQILLDGHDLREY---TLASLRDQVALVSQNV 426
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLlkalagdltGGGAPRGARV-TGDVTLNGEPLAAIdapRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 427 HLFNdtvANNIA------YAR----TEEYSREQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALL 496
Cdd:PRK13547 96 FAFS---AREIVllgrypHARragaLTHRDGEIAWQALALA-----------GATALVGRDVTTLSGGELARVQFARVLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 497 RNSP---------ILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLS-TIEQADEIVVVEDGRIVERGSHAD 564
Cdd:PRK13547 162 QLWPphdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPAD 241
|
..
gi 1336523670 565 LL 566
Cdd:PRK13547 242 VL 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
354-576 |
5.33e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.12 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 354 RETPALRNIDLNIQEGKTVALVGRSGSGKST----IASLITRfydiDNGQILLDGHD--LREYTLASlrdQVALV----S 423
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILVP----TSGEVRVLGYVpfKRRKEFAR---RIGVVfgqrS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QnvhLFND-TVANNIAYAR------TEEYsREQIEEAARMayaMDfiskMDNGLDTVIGEngvlLSGGQRQRIAIARALL 496
Cdd:COG4586 106 Q---LWWDlPAIDSFRLLKaiyripDAEY-KKRLDELVEL---LD----LGELLDTPVRQ----LSLGQRMRCELAAALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGSHADLLEHRGVYA 573
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250
|
...
gi 1336523670 574 QLH 576
Cdd:COG4586 251 TIV 253
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
355-525 |
1.06e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 67.00 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTlASLRDQVALVSQNVHLFND-TV 433
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR-DEPHENILYLGHLPGLKPElSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIA-YARTEEYSREQIEEAarmayamdfISKMD-NGLDTVIGENgvlLSGGQRQRIAIARALLRNSPILILDEATSAL 511
Cdd:TIGR01189 91 LENLHfWAAIHGGAQRTIEDA---------LAAVGlTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|....
gi 1336523670 512 DTESERAIQAALDE 525
Cdd:TIGR01189 159 DKAGVALLAGLLRA 172
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
367-551 |
1.84e-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: 69.81 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 367 QEGKTVALVGRSGSGKSTIAS-----LITRFYDIDNG----QIL--LDGHDLREYtLASLRDQ---VALVSQNVHL---- 428
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrFRGTELQDY-FKKLANGeikVAHKPQYVDLipkv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 429 FNDTVanniayarteeysREQIEEAARMAYAMDFISK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDE 506
Cdd:COG1245 176 FKGTV-------------RELLEKVDERGKLDELAEKlgLENILDRDISE----LSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 507 ATSALD----TESERAIQaalDELQKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:COG1245 239 PSSYLDiyqrLNVARLIR---ELAEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
369-559 |
5.28e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 63.93 E-value: 5.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 369 GKTVALVGRSGSGKSTIASLITRFYDIDNGQ-ILLDGHDLREYTLASLRDqvalvsqnvhlfndtvanniayarteeysr 447
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 448 eqieeaarmayamdfiskmdngldTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALD--- 524
Cdd:smart00382 52 ------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*...
gi 1336523670 525 ---ELQKNRTSLVIAHRLSTIEQADEIVVVEDGRIVER 559
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLL 145
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-546 |
7.59e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.59 E-value: 7.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREyTLASLRDQVAL 421
Cdd:PRK13540 2 LDVIELDFDY--HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVHLF-NDTVANNIAYARTEEYSREQIEEAARmayamdfISKMDNGLDTVIGengvLLSGGQRQRIAIARALLRNSP 500
Cdd:PRK13540 79 VGHRSGINpYLTLRENCLYDIHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1336523670 501 ILILDEATSALDtesERAIQAALDELQKNRTS----LVIAHRLSTIEQAD 546
Cdd:PRK13540 148 LWLLDEPLVALD---ELSLLTIITKIQEHRAKggavLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
72-238 |
9.61e-12 |
|
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: 65.82 E-value: 9.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 72 IGLMLLRGVTSYISSYC----ISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVV 147
Cdd:cd18590 39 IGLMCLFSLGSSLSAGLrgglFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 148 REGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVET 227
Cdd:cd18590 119 RSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEA 198
|
170
....*....|.
gi 1336523670 228 KRFDKVSNKMR 238
Cdd:cd18590 199 CRYSEALERTY 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
359-558 |
1.75e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR---EYTLASLRDQ-VALVSQNVHLFNDTVA 434
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdEEARAKLRAKhVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 435 -NNI---AYAR--TEEYSREQieeaarmayAMDFISKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:PRK10584 106 lENVelpALLRgeSSRQSRNG---------AKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 509 SALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQADEIVVVEDGRIVE 558
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREHgtTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
72-314 |
2.41e-11 |
|
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: 64.87 E-value: 2.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 72 IGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGA 151
Cdd:cd18574 49 LGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 152 SIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFD 231
Cdd:cd18574 129 QTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 232 KVSNKMRlqgmKMVSASSISDPVIQLIASLALA----FVLYAASFPSVMETLTAGTITvvfSSMIALMRPLKSLTNVNA- 306
Cdd:cd18574 209 EEVEKAA----KLNEKLGLGIGIFQGLSNLALNgivlGVLYYGGSLVSRGELTAGDLM---SFLVATQTIQRSLAQLSVl 281
|
250
....*....|
gi 1336523670 307 --QFQRGMAA 314
Cdd:cd18574 282 fgQYVKGKSA 291
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
373-561 |
4.57e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 64.51 E-value: 4.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 373 ALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDL----REYTLASLRDQVALVSQNVHLF-NDTVANNIAYARTEEySR 447
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRYGMAKS-MV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 448 EQIEEAARMAyamdfiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQ 527
Cdd:PRK11144 107 AQFDKIVALL-----------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1336523670 528 K--NRTSLVIAHRLSTIEQ-ADEIVVVEDGRIVERGS 561
Cdd:PRK11144 176 ReiNIPILYVSHSLDEILRlADRVVVLEQGKVKAFGP 212
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
356-557 |
4.83e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 356 TPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGhDLreyTLASL-RDQVALVSQNVHlfnDTVA 434
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DL---IVARLqQDPPRNVEGTVY---DFVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 435 NNIA--------YART-----EEYSREQIEEAARMAYAMDFiskmDNG--LDTVIGENGVL-----------LSGGQRQR 488
Cdd:PRK11147 89 EGIEeqaeylkrYHDIshlveTDPSEKNLNELAKLQEQLDH----HNLwqLENRINEVLAQlgldpdaalssLSGGWLRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 489 IAIARALLRNSPILILDEATSALDTEserAIQaALDELQKN-RTSLV-IAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIE---TIE-WLEGFLKTfQGSIIfISHDRSFIRNmATRIVDLDRGKLV 232
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
72-279 |
6.14e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 63.64 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 72 IGLMLLRGVTSYISS------YCISwvSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALIT 145
Cdd:cd18589 39 ITVMSLLTIASAVSEfvcdliYNIT--MSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 146 VVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAV 225
Cdd:cd18589 117 LMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEG 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 226 ETKRF-DKVSNKMRLQGMKMVS------ASSISDPVI---------QLIASLAL------AFVLYAASFPSVMETL 279
Cdd:cd18589 197 EAQRYrQRLQKTYRLNKKEAAAyavsmwTSSFSGLALkvgilyyggQLVTAGTVssgdlvTFVLYELQFTSAVEVL 272
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
355-570 |
1.19e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 62.12 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTI-ASLITRF-YDIDNGQILLDGHDLREYT---------LASLRDQVALVS 423
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREdYEVTGGTVEFKGKDLLELSpedragegiFMAFQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QNVHLFNDTVANNIayartEEYsREQiEEAARMAYAmDFISK----MDNGLDTVIGENGVLLSGGQRQRIAIARALLRNS 499
Cdd:PRK09580 93 VSNQFFLQTALNAV-----RSY-RGQ-EPLDRFDFQ-DLMEEkialLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIA---HRLSTIEQADEIVVVEDGRIVERGSH--ADLLEHRG 570
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDFtlVKQLEEQG 240
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-190 |
1.25e-10 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 62.53 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 69 LVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRItYDSEQVASSSSSALITVVR 148
Cdd:cd18783 46 IGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTKHM-QQIERIRQFLTGQLFGTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1336523670 149 EGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFR 190
Cdd:cd18783 125 DATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFR 166
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
345-557 |
1.26e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTYPGreTPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR-EYTLASLRDQVALVS 423
Cdd:PRK10982 2 SNISKSFPG--VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QNVHLFND-TVANNIAYARteeYSREQI-EEAARMAYAMDFISKmDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPI 501
Cdd:PRK10982 80 QELNLVLQrSVMDNMWLGR---YPTKGMfVDQDKMYRDTKAIFD-ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 502 LILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTIEQ-ADEIVVVEDGRIV 557
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWI 213
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-554 |
1.85e-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: 61.66 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 365 NIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLR---EYTLAslrDQVALVSQNVHLFNDTVANNiAYAR 441
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpQYIKA---DYEGTVRDLLSSITKDFYTH-PYFK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 442 TEEYSREQIEeaarmayamdfiSKMDNGLDTvigengvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESE----R 517
Cdd:cd03237 97 TEIAKPLQIE------------QILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRlmasK 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1336523670 518 AIQAALDELQKnrTSLVIAHRLSTIEQADEIVVVEDG 554
Cdd:cd03237 157 VIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
359-549 |
2.03e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 61.48 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTI------ASLITRFYdidNGQILLDGHDlREYTLASLrDQVALVSQNvhLFNDT 432
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLindtlyPALARRLH---LKKEQPGNHD-RIEGLEHI-DKVIVIDQS--PIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIA-YA--------------RTEEYSRE-----------------QIEEAARMAYAMDFISK-----MDNGLDTV-I 474
Cdd:cd03271 84 PRSNPAtYTgvfdeirelfcevcKGKRYNREtlevrykgksiadvldmTVEEALEFFENIPKIARklqtlCDVGLGYIkL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 475 GENGVLLSGGQRQRIAIARALLRNSP---ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:cd03271 164 GQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLvDKGNTVVVIEHNLDVIKCADWII 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-551 |
2.75e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 366 IQEGKTVALVGRSGSGKSTIASlitrfydIDNGQIL---------------LD---GHDLREYtLASLRDQ---VALVSQ 424
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-------ILSGELIpnlgdyeeepswdevLKrfrGTELQNY-FKKLYNGeikVVHKPQ 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 425 NVHL----FNDTVanniayarteeysREQIEEAARMAYAMDFISK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRN 498
Cdd:PRK13409 168 YVDLipkvFKGKV-------------RELLKKVDERGKLDEVVERlgLENILDRDISE----LSGGELQRVAIAAALLRD 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 499 SPILILDEATSALD----TESERAIQaaldELQKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:PRK13409 231 ADFYFFDEPTSYLDirqrLNVARLIR----ELAEGKYVLVVEHDLAVLDYlADNVHIA 284
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
323-554 |
2.88e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.59 E-value: 2.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 323 DSEQEKDEGKlviERAKGNLEFKDVTFTYP--GRETPALRNIDLNIQEGKTVALVGRSGSGKST----IASLITRFYdID 396
Cdd:TIGR00956 744 DVNDEKDMEK---ESGEDIFHWRNLTYEVKikKEKRVILNNVDGWVKPGTLTALMGASGAGKTTllnvLAERVTTGV-IT 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 397 NGQILLDGHDLREytlaSLRDQVALVSQN-VHLFNDTVanniayarteeysREQIEEAARM--------AYAMDFISK-- 465
Cdd:TIGR00956 820 GGDRLVNGRPLDS----SFQRSIGYVQQQdLHLPTSTV-------------RESLRFSAYLrqpksvskSEKMEYVEEvi 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 466 ----MDNGLDTVIGENGVLLSGGQRQRIAIARALLRNSPILI-LDEATSALDTESERAIQAALDELQKN-RTSLVIAHRL 539
Cdd:TIGR00956 883 klleMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQP 962
|
250
....*....|....*..
gi 1336523670 540 STI--EQADEIVVVEDG 554
Cdd:TIGR00956 963 SAIlfEEFDRLLLLQKG 979
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
362-523 |
5.96e-10 |
|
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: 59.04 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 362 IDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQNVHLFNDTVANNIAYAR 441
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 442 tEEYSREQIEEAarmayamdfiskmdngLDTViGENGV------LLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:cd03231 99 -ADHSDEQVEEA----------------LARV-GLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....*...
gi 1336523670 516 ERAIQAAL 523
Cdd:cd03231 161 VARFAEAM 168
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
27-197 |
1.26e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 59.44 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 27 LIVAAVALVFNAASDTFMLSLLKPLLDDGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVsmaiRVVS 186
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVY----YLLQ 156
|
170
....*....|.
gi 1336523670 187 KRFRNISKNMQ 197
Cdd:cd18580 157 RYYLRTSRQLR 167
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
72-182 |
1.40e-09 |
|
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: 59.43 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 72 IGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSALITVVREGA 151
Cdd:cd18588 49 LVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVGDTVARVR-ELESIRQFLTGSALTLVLDLV 127
|
90 100 110
....*....|....*....|....*....|.
gi 1336523670 152 SIIGLFVMMFYYSWQLSliLIVLAPIVSMAI 182
Cdd:cd18588 128 FSVVFLAVMFYYSPTLT--LIVLASLPLYAL 156
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
342-560 |
2.31e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGREtpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDqval 421
Cdd:PRK11701 7 LSVRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 vSQNVHLFndtvanniayaRTE-EYSREQIEEAARMA------------------Y------AMDFISKMDNGLDTvIGE 476
Cdd:PRK11701 81 -AERRRLL-----------RTEwGFVHQHPRDGLRMQvsaggnigerlmavgarhYgdiratAGDWLERVEIDAAR-IDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 477 NGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTeserAIQAALDELQKNRTS------LVIAHRLSTIEQ-ADEIV 549
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVRelglavVIVTHDLAVARLlAHRLL 223
|
250
....*....|.
gi 1336523670 550 VVEDGRIVERG 560
Cdd:PRK11701 224 VMKQGRVVESG 234
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
350-538 |
2.36e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 350 TYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVSQnvhlF 429
Cdd:COG2401 37 ELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD----F 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 430 NDTVAnniayarteeysreqIEEAARMAYAMDFISKMDNgldtvigengvlLSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:COG2401 113 KDAVE---------------LLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|.
gi 1336523670 510 ALDTESERAIQAALDEL-QKNRTSLVIA-HR 538
Cdd:COG2401 166 HLDRQTAKRVARNLQKLaRRAGITLVVAtHH 196
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
355-568 |
2.44e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 59.15 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETP-----ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDiDNGQI-----LLDGHDLreytLA-SLRDQVALVS 423
Cdd:COG4170 14 DTPqgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVtadrfRWNGIDL----LKlSPRERRKIIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 424 QNVHL-FNDTvannIAYARTEEYSREQIEEA---------------ARMAYAMDFISKmdngldtvIG---ENGVL---- 480
Cdd:COG4170 89 REIAMiFQEP----SSCLDPSAKIGDQLIEAipswtfkgkwwqrfkWRKKRAIELLHR--------VGikdHKDIMnsyp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 --LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEQ-ADEIVVVEDGR 555
Cdd:COG4170 157 heLTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgtSILLISHDLESISQwADTITVLYCGQ 236
|
250
....*....|...
gi 1336523670 556 IVERGSHADLLEH 568
Cdd:COG4170 237 TVESGPTEQILKS 249
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
355-575 |
2.49e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 355 ETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITrfydidNGQILLDGH---DLREYTLASLRDQVALVSQ-----NV 426
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA------GELPLLSGErqsQFSHITRLSFEQLQKLVSDewqrnNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 427 HLF----NDTvanniayART-EEYSREQIEEAAR-MAYAMDFiskmdnGLDTVIGENGVLLSGGQRQRIAIARALLRNSP 500
Cdd:PRK10938 89 DMLspgeDDT-------GRTtAEIIQDEVKDPARcEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 501 ILILDEATSALDTESERAIQAALDELQKNRTSLV-IAHRLSTI-EQADEIVVVEDGRIVERGSHADLLEhRGVYAQL 575
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ-QALVAQL 231
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
367-551 |
3.26e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.76 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 367 QEGKTVALVGRSGSGKSTIASLIT--------RFYDIDNGQILLD---GHDLREYTLASLRDQVALV--SQNVHLFNDTV 433
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIvkPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIAYARTEEYSREQIEEaarmayamdFISKMDngLDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDT 513
Cdd:cd03236 104 KGKVGELLKKKDERGKLDE---------LVDQLE--LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1336523670 514 ESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVV 551
Cdd:cd03236 173 KQRLNAARLIRELaEDDNYVLVVEHDLAVLDYlSDYIHCL 212
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
69-191 |
5.72e-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: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 69 LVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSALITVVR 148
Cdd:cd18782 46 VVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLL 124
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1336523670 149 EGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRN 191
Cdd:cd18782 125 DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
71-318 |
6.49e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 57.23 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 71 VIGLMLLRGVTSYISSYC-ISWVsgKVVMTMRRRL----FSHMMGMPVSFFDKQSTGTLLS---RITYDSEQVASSSSSA 142
Cdd:cd18560 41 ILLYALLRFSSKLLKELRsLLYR--RVQQNAYRELslktFAHLHSLSLDWHLSKKTGEVVRimdRGTESANTLLSYLVFY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 143 LITVVREGASIIGLFvmMFYYSWQLSLILIV---LAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAeqmLKGHKEVLM 219
Cdd:cd18560 119 LVPTLLELIVVSVVF--AFHFGAWLALIVFLsvlLYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDS---LLNFETVKY 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 220 FGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSSMIALMRPLK 299
Cdd:cd18560 194 FTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLN 273
|
250
....*....|....*....
gi 1336523670 300 SLTNVNAQFQRGMAACQTL 318
Cdd:cd18560 274 FLGTIYRMIIQSLTDMENL 292
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
357-556 |
6.61e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 6.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHdlreyTLASLRDQVALVSQNVHLFND----- 431
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH-----EVVTRSPQDGLANGIVYISEDrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 -----TVANNIAYARTEEYSRE--QIEEAARMAYAMDFIsKMDN----GLDTVIGengvLLSGGQRQRIAIARALLRNSP 500
Cdd:PRK10762 341 lvlgmSVKENMSLTALRYFSRAggSLKHADEQQAVSDFI-RLFNiktpSMEQAIG----LLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 501 ILILDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEQADEIVVVEDGRI 556
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSiiLVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
369-555 |
6.85e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.74 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 369 GKTVALVGRSGSGKSTIASLITRFYDIDN--GQILLDGHDLREYTLAslrdQVALVSQNVHLF-NDTVANNIAYAR---- 441
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILK----RTGFVTQDDILYpHLTVRETLVFCSllrl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 442 TEEYSREQIEEAARMAYAMDFISKMDNgldTVIGENGVL-LSGGQRQRIAIARALLRNSPILILDEATSALD-TESERAI 519
Cdd:PLN03211 170 PKSLTKQEKILVAESVISELGLTKCEN---TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDaTAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 1336523670 520 QAALDELQKNRTSLVIAHRLST--IEQADEIVVVEDGR 555
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
360-525 |
9.19e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.58 E-value: 9.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 360 RNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlasLRDQVAlvsQNV----HL--FND-- 431
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-----QRDEYH---QDLlylgHQpgIKTel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 432 TVANNIA-YAR-TEEYSREQIEEA-ARMayamdfiskmdnGL----DTVIGEngvlLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK13538 90 TALENLRfYQRlHGPGDDEALWEAlAQV------------GLagfeDVPVRQ----LSAGQQRRVALARLWLTRAPLWIL 153
|
170 180
....*....|....*....|.
gi 1336523670 505 DEATSALDTESERAIQAALDE 525
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQ 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
342-554 |
1.20e-08 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.94 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTY--PGRETPALRNIDLNIQEGKTVALVGRSGSGKST---------IASLITrfydidnGQILLDGHDLREy 410
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVIT-------GEILINGRPLDK- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 tlaSLRDQVALVSQN-VHLFNDTVanniayarteeysREQIEEAARMayamdfiskmdNGldtvigengvlLSGGQRQRI 489
Cdd:cd03232 76 ---NFQRSTGYVEQQdVHSPNLTV-------------REALRFSALL-----------RG-----------LSVEQRKRL 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336523670 490 AIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS--TIEQADEIVVVEDG 554
Cdd:cd03232 118 TIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
358-549 |
1.85e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.25 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLItrFYDiDNGQILLDGHDLREYTLASLRDQVALVsqnvhlfndtVANNI 437
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYA-SGKARLISFLPKFSRNKLIFIDQLQFL----------IDVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 438 AYARteeysreqieeaarmayamdfiskmdngldtvIGENGVLLSGGQRQRIAIARALLRNSP--ILILDEATSALDTES 515
Cdd:cd03238 77 GYLT--------------------------------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*
gi 1336523670 516 ERAIQAALDEL-QKNRTSLVIAHRLSTIEQADEIV 549
Cdd:cd03238 125 INQLLEVIKGLiDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
353-549 |
3.09e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.13 E-value: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 353 GRETPALRNIDLNIQEGKTVALVGRSGSGKSTIA---SLITrfydidngqiLLDGHDLREYTLASLRDQVALVSqnvhlf 429
Cdd:cd03227 5 GRFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILdaiGLAL----------GGAQSATRRRSGVKAGCIVAAVS------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 430 ndtvanniayarteeysreqieeaarmayaMDFISkmdngldTVIGengvlLSGGQRQRIAIARAL----LRNSPILILD 505
Cdd:cd03227 69 ------------------------------AELIF-------TRLQ-----LSGGEKELSALALILalasLKPRPLYILD 106
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1336523670 506 EATSALDTESERAIQAALDE-LQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:cd03227 107 EIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLI 151
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
479-552 |
3.19e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 3.19e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 479 VLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseEGKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
342-543 |
3.83e-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: 56.56 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLreytLASLRDqval 421
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISD---- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNV-----------------HLFndtvanniAYARTEEYSREQIEEAARMAyamdfISKMdnGLDTVIGENGVLLSGG 484
Cdd:TIGR01257 2010 VHQNMgycpqfdaiddlltgreHLY--------LYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGG 2074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLSTIE 543
Cdd:TIGR01257 2075 NKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECE 2134
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
342-566 |
4.26e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.19 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRETP--ALRNIDLNIQEGKTVALVGRSGSGKSTIASLIT--------------RFYDIDNGQIlldgh 405
Cdd:PRK15093 4 LDIRNLTIEFKTSDGWvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDIDLLRL----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 406 dlreytlaSLRDQVALVSQNVHLF----------NDTVANNIA------------YARTEEYSREQIEEAARMAyamdfI 463
Cdd:PRK15093 79 --------SPRERRKLVGHNVSMIfqepqscldpSERVGRQLMqnipgwtykgrwWQRFGWRKRRAIELLHRVG-----I 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 464 SKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLST 541
Cdd:PRK15093 146 KDHKDAMRSFPYE----LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQM 221
|
250 260
....*....|....*....|....*.
gi 1336523670 542 IEQ-ADEIVVVEDGRIVERGSHADLL 566
Cdd:PRK15093 222 LSQwADKINVLYCGQTVETAPSKELV 247
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
70-191 |
6.07e-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: 54.51 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 70 VVIGLMLLRGVTSYIssycISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITyDSEQVASSSSSALITVVRE 149
Cdd:cd18566 51 AILLESLLRLLRSYI----LAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLN-SLEQIREFLTGQALLALLD 125
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1336523670 150 GASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRN 191
Cdd:cd18566 126 LPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRR 167
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
346-570 |
6.24e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 6.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 346 DVTFTYpgRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREytlASLRDQV----AL 421
Cdd:NF033858 6 GVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVcpriAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQ----NvhLFND-TVANNIAY-ARTEEYSREqiEEAARMAYAMDfiskmDNGL----DTVIGEngvlLSGGQRQRIAI 491
Cdd:NF033858 81 MPQglgkN--LYPTlSVFENLDFfGRLFGQDAA--ERRRRIDELLR-----ATGLapfaDRPAGK----LSGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIahrLST--IEQA---DEIVVVEDGRIVERGSHADL 565
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGMsVL---VATayMEEAerfDWLVAMDAGRVLATGTPAEL 224
|
....*
gi 1336523670 566 LEHRG 570
Cdd:NF033858 225 LARTG 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
352-515 |
6.42e-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: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 352 PGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTI----ASLITRFydidNGQIL---------------LD-GHDLREYT 411
Cdd:TIGR03719 16 PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKDF----NGEARpqpgikvgylpqepqLDpTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 412 LASLRDQVALVSQnvhlFNDTVAnniAYARTEEYSREQIEEAARM------AYAMDFISKMDNGLDTV---IGENGV-LL 481
Cdd:TIGR03719 90 EEGVAEIKDALDR----FNEISA---KYAEPDADFDKLAAEQAELqeiidaADAWDLDSQLEIAMDALrcpPWDADVtKL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1336523670 482 SGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
345-515 |
7.42e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 345 KDVTFTYPGrETPALRNIDLNIQEGKTVALVGRSGSGKSTI----ASLITRFydidNGQILL----------------DG 404
Cdd:PRK11819 10 NRVSKVVPP-KKQILKDISLSFFPGAKIGVLGLNGAGKSTLlrimAGVDKEF----EGEARPapgikvgylpqepqldPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 405 HDLREYTLASLRDQVALVSQnvhlFNDTvanNIAYARTEEYSREQIEEAARM------AYAMDFISKMD---NGL----- 470
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDR----FNEI---YAAYAEPDADFDALAAEQGELqeiidaADAWDLDSQLEiamDALrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1336523670 471 DTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:PRK11819 158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
343-558 |
7.92e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.18 E-value: 7.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTftypGRETPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT-LASLRDQVAL 421
Cdd:PRK09700 267 EVRNVT----SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 VSQNVH---LF-NDTVANNIAYART-------------EEYSREQIEEAARMAYAMDFISKMDNgldtvIGEngvlLSGG 484
Cdd:PRK09700 343 ITESRRdngFFpNFSIAQNMAISRSlkdggykgamglfHEVDEQRTAENQRELLALKCHSVNQN-----ITE----LSGG 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTI-EQADEIVVVEDGRIVE 558
Cdd:PRK09700 414 NQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIiTVCDRIAVFCEGRLTQ 489
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
366-552 |
9.06e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 366 IQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDghdLR-----EYTLASLRDQV-ALVSQNVHLFNDTvanniaY 439
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKisykpQYIKPDYDGTVeDLLRSITDDLGSS------Y 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 440 ARTEEYSREQIEEAarmayamdfiskMDNGLDTvigengvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESE--- 516
Cdd:PRK13409 433 YKSEIIKPLQLERL------------LDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlav 492
|
170 180 190
....*....|....*....|....*....|....*...
gi 1336523670 517 -RAIQAALDElqKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:PRK13409 493 aKAIRRIAEE--REATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
450-549 |
1.04e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.02 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 450 IEEAARMAYAMDFISK-----MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRNS---PILILDEATSALDTESeraIQ 520
Cdd:TIGR00630 793 VEEAYEFFEAVPSISRklqtlCDVGLGYIrLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDD---IK 869
|
90 100 110
....*....|....*....|....*....|...
gi 1336523670 521 AALDELQ----KNRTSLVIAHRLSTIEQADEIV 549
Cdd:TIGR00630 870 KLLEVLQrlvdKGNTVVVIEHNLDVIKTADYII 902
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
366-552 |
1.26e-07 |
|
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: 54.41 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 366 IQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDghdlreytlasLRdqVALVSQNV-HLFNDTVANNIAYARTEE 444
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LK--ISYKPQYIsPDYDGTVEEFLRSANTDD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 445 Y--SREQIEEAARMAyamdfISK-MDNGLDTvigengvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESE----R 517
Cdd:COG1245 430 FgsSYYKTEIIKPLG-----LEKlLDKNVKD--------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRlavaK 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 1336523670 518 AIQAALDElqKNRTSLVIAHRLSTIEQ-ADEIVVVE 552
Cdd:COG1245 497 AIRRFAEN--RGKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
331-537 |
1.36e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 331 GKLVierakgnLEFKDVTFTYPGRETpaLRNIDLNIQEGKTVALVGRSGSGKSTIASLITrfydidnGQILLDGHDLREY 410
Cdd:PRK11147 316 GKIV-------FEMENVNYQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKLML-------GQLQADSGRIHCG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 TlaslRDQVALVSQNVHLFN--DTVANNIAYARTEeysreqIEEAAR----MAYAMDFISKMDNGLDTVIGengvlLSGG 484
Cdd:PRK11147 380 T----KLEVAYFDQHRAELDpeKTVMDNLAEGKQE------VMVNGRprhvLGYLQDFLFHPKRAMTPVKA-----LSGG 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 485 QRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH 537
Cdd:PRK11147 445 ERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
342-556 |
3.19e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGreTPAL-RNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILldghdlreytlASLRDQVA 420
Cdd:PLN03073 509 ISFSDASFGYPG--GPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 421 LVSQNvHLFN-DTVANNIAY-ARTEEYSREQieeaarmayamdfisKMDNGLDTvIGENGVL-------LSGGQRQRIAI 491
Cdd:PLN03073 576 VFSQH-HVDGlDLSSNPLLYmMRCFPGVPEQ---------------KLRAHLGS-FGVTGNLalqpmytLSGGQKSRVAF 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 492 ARALLRNSPILILDEATSALDTESERAIQAALDELQKNrtSLVIAHRLSTIE-QADEIVVVEDGRI 556
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISgSVDELWVVSEGKV 702
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
66-309 |
3.27e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 52.16 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 66 WMPLVVIGLMLL---RGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSeQVASSSSSA 142
Cdd:cd18779 40 LLGVLGLGLAALvltQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNA-TIRELLTSQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 143 LITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFG- 221
Cdd:cd18779 119 TLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGa 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 222 -GQAVE--TKRFDKVSNKMRLQGmkmvSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTitvvfssMIAL---- 294
Cdd:cd18779 199 eDRALDrwSNLFVDQLNASLRRG----RLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGT-------MLALnala 267
|
250
....*....|....*...
gi 1336523670 295 ---MRPLKSLTNVNAQFQ 309
Cdd:cd18779 268 gafLAPLASLVGTAQQLQ 285
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
361-568 |
4.75e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 52.52 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 361 NIDLNIQEGKTVALVGRSGSGKS-TIASLITRFYDIDNGQILLDGHDLREYTLA-SLRDQVALVSQNVH----LFNDTVA 434
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAqAIRAGIAMVPEDRKrhgiVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 435 NNIAYARTEEYS-REQIEEAARMAYAMDFISKMD---NGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSA 510
Cdd:TIGR02633 358 KNITLSVLKSFCfKMRIDAAAELQIIGSAIQRLKvktASPFLPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 511 LDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EQADEIVVVEDGRIvergsHADLLEH 568
Cdd:TIGR02633 434 VDVGAKYEIYKLINQLAQEGVAIiVVSSELAEVlGLSDRVLVIGEGKL-----KGDFVNH 488
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
360-556 |
4.76e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.75 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 360 RNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTL-----------------------ASLR 416
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyldAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 417 -DQVALVSQNVHLFNDTVANNiayARTEEYSR------EQIEEAARMayamdfiskmdngldtvigengvlLSGGQRQRI 489
Cdd:PRK15439 360 wNVCALTHNRRGFWIKPAREN---AVLERYRRalnikfNHAEQAART------------------------LSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 490 AIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEQ-ADEIVVVEDGRI 556
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
346-569 |
6.90e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 346 DVTFTYPGRETPALRN-IDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLReytLASLRD------- 417
Cdd:PRK11288 255 EVRLRLDGLKGPGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDairagim 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 418 ------------QVALVSQNVhlfndtvanNIAYARTEEYSREQIEEAARMAYAMDFISKMD---NGLDTVIGengvLLS 482
Cdd:PRK11288 332 lcpedrkaegiiPVHSVADNI---------NISARRHHLRAGCLINNRWEAENADRFIRSLNiktPSREQLIM----NLS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 483 GGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGRIVERG 560
Cdd:PRK11288 399 GGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGEL 478
|
....*....
gi 1336523670 561 SHADLLEHR 569
Cdd:PRK11288 479 AREQATERQ 487
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
359-560 |
7.15e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 50.33 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIAslitrFYDI-DNGQilldghdlREYtLASL------------RDQVALV--- 422
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA-----FDTIyAEGQ--------RRY-VESLsayarqflgqmdKPDVDSIegl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 423 SQNVHLFNDTVANNiayARTEEYSREQIEEAARMAYAMDFISK-----MDNGLDTV-IGENGVLLSGGQRQRIAIARALL 496
Cdd:cd03270 77 SPAIAIDQKTTSRN---PRSTVGTVTEIYDYLRLLFARVGIRErlgflVDVGLGYLtLSRSAPTLSGGEAQRIRLATQIG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 497 RN--SPILILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEQADEIVVV------EDGRIVERG 560
Cdd:cd03270 154 SGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
153-294 |
1.10e-06 |
|
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: 50.56 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 153 IIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSKRF-RNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFD 231
Cdd:cd18585 123 ILATILFLAFFSPALALILLAGLLLAGVVIPLLFYRLgKKIGQQLVQLRAELRTELVDGLQGMAELLIFGALERQRQQLE 202
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 232 KVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASfPSVmetlTAGTITVVFSSMIAL 294
Cdd:cd18585 203 QLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGA-PLV----QNGALDGALLAMLVF 260
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
331-541 |
1.43e-06 |
|
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: 51.09 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 331 GKLVIErakgnleFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLdGHDLrey 410
Cdd:TIGR03719 319 GDKVIE-------AENLTKAFGDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 411 tlaslrdQVALVSQnvhlFNDTVANNiayaRT--EEYS--REQIE----EAARMAYAMDFISKmdnGLDT--VIGEngvl 480
Cdd:TIGR03719 386 -------KLAYVDQ----SRDALDPN----KTvwEEISggLDIIKlgkrEIPSRAYVGRFNFK---GSDQqkKVGQ---- 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336523670 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH------RLST 541
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG--CAVVISHdrwfldRIAT 508
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
363-540 |
1.54e-06 |
|
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: 51.29 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 363 DLNIQ--EGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHD------LREY-TLASLRDQValvsqnvhLFNDTV 433
Cdd:TIGR00954 470 SLSFEvpSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGklfyvpQRPYmTLGTLRDQI--------IYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 anniayartEEYSREQIEEAARMAY----AMDFISKMDNGLDTVIGENGVLlSGGQRQRIAIARALLRNSPILILDEATS 509
Cdd:TIGR00954 542 ---------EDMKRRGLSDKDLEQIldnvQLTHILEREGGWSAVQDWMDVL-SGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|.
gi 1336523670 510 ALDTESERAIQAALDElqKNRTSLVIAHRLS 540
Cdd:TIGR00954 612 AVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
359-539 |
1.61e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDgHDLReytlaslrdqVALVSQNVHLfNDTVANNIA 438
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR----------IGYVPQKLYL-DTTLPLTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 439 -YARTEEYSREQ-IEEAARMAYAMDFISK-MDNgldtvigengvlLSGGQRQRIAIARALLRNSPILILDEATSALDTES 515
Cdd:PRK09544 88 rFLRLRPGTKKEdILPALKRVQAGHLIDApMQK------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*.
gi 1336523670 516 ERAIQAALDELQK--NRTSLVIAHRL 539
Cdd:PRK09544 156 QVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-554 |
2.12e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIASLI----TRFYdIDnGQILLDGHDLREYTLASLRdqvALVSQN-VHLFNDTV 433
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGY-IE-GDIRISGFPKKQETFARIS---GYCEQNdIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 434 ANNIAYAR----TEEYSREqiEEAARMAYAMDFIsKMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRNSPILILDEAT 508
Cdd:PLN03140 971 RESLIYSAflrlPKEVSKE--EKMMFVDEVMELV-ELDNLKDAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 509 SALDTESE----RAIQAALDelqKNRTSLVIAHRLS--TIEQADEIVVVEDG 554
Cdd:PLN03140 1048 SGLDARAAaivmRTVRNTVD---TGRTVVCTIHQPSidIFEAFDELLLMKRG 1096
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
28-266 |
3.58e-06 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 48.94 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 28 IVAAVALVFNAAsdtfmlsLLKPLLDDGFGKTDRSVLLWMPLVV-IGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFS 106
Cdd:cd18584 6 LLAALLIIAQAW-------LLARIIAGVFLEGAGLAALLPLLLLlLAALLLRALLAWAQERLAARAAARVKAELRRRLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 107 HMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVRegASII--GLFVMMFYYSWQLSLILIVLAPI--VSMAI 182
Cdd:cd18584 79 RLLALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVL--AAIVplLILVAVFPLDWVSALILLVTAPLipLFMIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 183 rvVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMK-----MVSASsisdpVIQL 257
Cdd:cd18584 157 --IGKAAQAASRRQWAALSRLSGHFLDRLRGLPTLKLFGRARAQAARIARASEDYRRRTMKvlrvaFLSSA-----VLEF 229
|
....*....
gi 1336523670 258 IASLALAFV 266
Cdd:cd18584 230 FATLSIALV 238
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
481-552 |
4.48e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.60 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 LSGGQRQ------RIAIARALLRNSPILILDEATSALDTES-ERAIQAALDEL--QKNRTSLVIAHRLSTIEQADEIVVV 551
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENiEESLAEIIEERksQKNFQLIVITHDEELVDAADHIYRV 195
|
.
gi 1336523670 552 E 552
Cdd:cd03240 196 E 196
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
44-200 |
5.75e-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: 48.21 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 44 MLSLLKPLL-----DDGFGKTDRSVLLwmpLVVIG-LMLLRGVTS--YISSYCISWVSGKVVMTMRRRLFSHMMGMPVSF 115
Cdd:cd18571 16 LLQLIFPFLtqsivDKGINNKDLNFIY---LILIAqLVLFLGSTSieFIRSWILLHISSRINISIISDFLIKLMRLPISF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 116 FDKQSTGTLLSRItYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLApIVS-------MAIRVV--S 186
Cdd:cd18571 93 FDTKMTGDILQRI-NDHSRIESFLTSSSLSILFSLLNLIVFSIVLAYYNLTIFLIFLIGS-VLYilwillfLKKRKKldY 170
|
170
....*....|....
gi 1336523670 187 KRFRNISKNMQNTM 200
Cdd:cd18571 171 KRFDLSSENQSKLI 184
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
480-549 |
1.65e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 480 LLSGGQRQRIAIA--RALLRN--SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKYkpAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKLV 1150
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
54-193 |
2.62e-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: 46.37 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 54 DGFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVsgkvvmtMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSE 133
Cdd:cd18605 38 NDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARR-------LHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVY 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 134 QVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIvsmaIRVVSKRFRNIS 193
Cdd:cd18605 111 TIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLPLAFI----YYRIQRYYRATS 166
|
|
| ABC_6TM_AarD_CydDC_like |
cd18781 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ... |
32-187 |
2.62e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350054 [Multi-domain] Cd Length: 290 Bit Score: 46.38 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 32 VALVFNAASDTFMLSLLKPLLddgFGKTDRSVLLWMPLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGM 111
Cdd:cd18781 7 ISLLANIAFVFSIANLLQKLL---EGKLTTASLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRL 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1336523670 112 PVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIGLFVMMFYYSWQLSLILIVLAPIVSMAIRVVSK 187
Cdd:cd18781 84 GPSYQEKVSTAEVVQLSVEGVEQLEIYFGRYLPQFFYSMLAPLTLFVVLAPINWKAALVLLICVPLIPISIIAVQK 159
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
26-188 |
3.03e-05 |
|
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350006 [Multi-domain] Cd Length: 289 Bit Score: 46.08 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 26 GLIVAAVALVfnaasdtfMLSLLKPLLddgFGKTDRSVLLW-MPLVVIGLMLLRGVTSYISSYCISWVSGKvvMTMRRRL 104
Cdd:cd18562 3 GLALANVALA--------GVQFAEPVL---FGRVVDALSSGgDAFPLLALWAALGLFSILAGVLVALLADR--LAHRRRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 105 ------FSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSsssaLITVVREG-ASIIGLFVMM---FYYSWQLSLILIVL 174
Cdd:cd18562 70 avmasyFEHVITLPLSFHSQRGSGRLLRIMLRGTDALFGL----WLGFFREHlAALVSLIVLLpvaLWMNWRLALLLVVL 145
|
170
....*....|....
gi 1336523670 175 APIVSMAIRVVSKR 188
Cdd:cd18562 146 AAVYAALNRLVMRR 159
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
398-556 |
3.30e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 398 GQILLDGHDLREYTLA-SLRDQVALVSQN------VHLFNdtVANNIAYARTEEYS-REQIEEAARMAYAMDFISKMD-- 467
Cdd:PRK13549 318 GEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgiVPVMG--VGKNITLAALDRFTgGSRIDDAAELKTILESIQRLKvk 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 468 -NGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSL-VIAHRLSTI-EQ 544
Cdd:PRK13549 396 tASPELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIiVISSELPEVlGL 471
|
170
....*....|..
gi 1336523670 545 ADEIVVVEDGRI 556
Cdd:PRK13549 472 SDRVLVMHEGKL 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
343-546 |
4.00e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 343 EFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRfydiDNGQilldGH--DLREY--------TL 412
Cdd:PRK10938 262 VLNNGVVSYNDR--PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQ----GYsnDLTLFgrrrgsgeTI 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 413 ASLRDQVALVSQNVHL---FNDTVANNIAYARTEEYSREQIEEAARMAYAMDFISKMdnGLDTVIGENGVL-LSGGQrQR 488
Cdd:PRK10938 332 WDIKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDIL--GIDKRTADAPFHsLSWGQ-QR 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336523670 489 IA-IARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLV------------IAHRLSTIEQAD 546
Cdd:PRK10938 409 LAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGD 480
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
480-546 |
6.06e-05 |
|
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: 44.38 E-value: 6.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1336523670 480 LLSGGQRQRIAIAR--ALLR--NSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEQAD 546
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvrPSPFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAAD 183
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
369-537 |
6.21e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 369 GKTVALVGRSGSGKSTIASLITrFYDID----NGQIL-----LDGHDLR--EYTLASLRDQVALVSQNVHLF-------- 429
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkNCQILhveqeVVGDDTTalQCVLNTDIERTQLLEEEAQLVaqqrelef 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 430 -----------NDTVANNIAYARTEE-YSR-EQIEEAARMAYAMDFISKMDNGLDTVIGENGVLlSGGQRQRIAIARALL 496
Cdd:PLN03073 282 etetgkgkganKDGVDKDAVSQRLEEiYKRlELIDAYTAEARAASILAGLSFTPEMQVKATKTF-SGGWRMRIALARALF 360
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1336523670 497 RNSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHAVLWLETYL--LKWPKTFIVVSH 399
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
72-178 |
1.05e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 44.39 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 72 IGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGA 151
Cdd:cd18606 42 AGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLS 121
|
90 100
....*....|....*....|....*..
gi 1336523670 152 SIIGLFVMMFYYswqLSLILIVLAPIV 178
Cdd:cd18606 122 SIIGTFILIIIY---LPWFAIALPPLL 145
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
359-567 |
1.09e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 359 LRNIDLNIQEGKTVALVGRSGSGKSTIasLITRFYDID-----NGQILLDGHDLREYTLaslRDQVALVSQN-VHLFNDT 432
Cdd:PLN03140 181 LKDASGIIKPSRMTLLLGPPSSGKTTL--LLALAGKLDpslkvSGEITYNGYRLNEFVP---RKTSAYISQNdVHVGVMT 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 433 VANNIAY-ARTEE--YSREQIEEAARM-----------------AYAM---------DFISK---MDNGLDTVIGENGVL 480
Cdd:PLN03140 256 VKETLDFsARCQGvgTRYDLLSELARRekdagifpeaevdlfmkATAMegvksslitDYTLKilgLDICKDTIVGDEMIR 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 481 -LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS----TIEQADEIVVVEDGR 555
Cdd:PLN03140 336 gISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLFDDIILLSEGQ 415
|
250
....*....|..
gi 1336523670 556 IVERGSHADLLE 567
Cdd:PLN03140 416 IVYQGPRDHILE 427
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
357-558 |
1.49e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 357 PALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYT-LASLRDQVALVSQ---------NV 426
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEerrstgiyaYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 427 HL-FNDTVANNIAY-ARTEEYSREQIEEAARmaYAMDFISKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRNSPILIL 504
Cdd:PRK10982 342 DIgFNSLISNIRNYkNKVGLLDNSRMKSDTQ--WVIDSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1336523670 505 DEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGR---IVE 558
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELaKKDKGIIIISSEMpELLGITDRILVMSNGLvagIVD 474
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
481-525 |
1.51e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1336523670 481 LSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDE 525
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE 490
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
26-194 |
1.59e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 44.09 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 26 GLIVAAVALVF---NAASDTFMLSLLKPLLDDGFGKTDRSVL--------------LWM-PLVVIGLMLLRGVTSYISSY 87
Cdd:cd18599 1 GYVVFLFVLLLfilSVGSTVFSDWWLSYWLKQGSGNTTNNVDnstvdsgnisdnpdLNFyQLVYGGSILVILLLSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 88 CISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSALITVVREGASIIG-LFVMMFYYSWq 166
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFsLIIIAIVFPW- 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 1336523670 167 lslILIVLAP--IVSMAIRVVS-------KRFRNISK 194
Cdd:cd18599 160 ---FLIALIPlaIIFVFLSKIFrrairelKRLENISR 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
342-557 |
1.72e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPG-RETPALRNIDLNIQEGKTVALVGRSGSGKSTIA-SLITRFYDID-NGQILLDGhdlREYTLASLRDQ 418
Cdd:NF040905 258 FEVKNWTVYHPLhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRNiSGTVFKDG---KEVDVSTVSDA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 419 V----ALVSQN-----VHLfNDTVANNIAYARTEEYSREQ-IEEAARMAYAMDFISKMD---NGLDTVIGEngvlLSGGQ 485
Cdd:NF040905 335 IdaglAYVTEDrkgygLNL-IDDIKRNITLANLGKVSRRGvIDENEEIKVAEEYRKKMNiktPSVFQKVGN----LSGGN 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336523670 486 RQRIAIARALLRNSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRL-STIEQADEIVVVEDGRIV 557
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELpELLGMCDRIYVMNEGRIT 483
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
69-301 |
1.85e-04 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 43.64 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 69 LVVIGLMLLRGVTSYISSYCISWVSGKVVMTMR----------------RRLFSHMMGMPVSFFDKQSTGTLLSRITYDS 132
Cdd:cd18582 26 LSAPASALLAVPLLLLLAYGLARILSSLFNELRdalfarvsqravrrlaLRVFRHLHSLSLRFHLSRKTGALSRAIERGT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 133 EQVASSSSSALITVVREGASIIGLFVMMFY-YSWQLSLILIV-LAPIVSMAIRVVSKRfRNISKNMQNTMGQVTTSAEQM 210
Cdd:cd18582 106 RGIEFLLRFLLFNILPTILELLLVCGILWYlYGWSYALITLVtVALYVAFTIKVTEWR-TKFRREMNEADNEANAKAVDS 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 211 LKGHKEVLMFGGQAVETKRFDKVSNKMRLQGMKMVSASSISDPVIQLIASLALAFVLYAASFPSVMETLTAGTITVVFSS 290
Cdd:cd18582 185 LLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTY 264
|
250
....*....|.
gi 1336523670 291 MIALMRPLKSL 301
Cdd:cd18582 265 LLQLYQPLNFL 275
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
358-543 |
2.55e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.73 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 358 ALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLDGHDLREYTLASLRDQVALVsQNVHLfndtvaNNI 437
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI-ENIEL------KGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 438 AYARTEEYSREQIEEAARMAYAMDFISKmdnGLDTvigengvlLSGGQRQRIAIARALLRNSPILILDEATSALDTESER 517
Cdd:PRK13545 112 MMGLTKEKIKEIIPEIIEFADIGKFIYQ---PVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|....*..
gi 1336523670 518 AIQAALDELQKN-RTSLVIAHRLSTIE 543
Cdd:PRK13545 181 KCLDKMNEFKEQgKTIFFISHSLSQVK 207
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
450-549 |
3.43e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.52 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 450 IEEAArmayamDF---ISK--------MDNGLDTV-IGENGVLLSGGQRQRIAIARALLRNS---PILILDEATSALDTE 514
Cdd:PRK00349 794 VEEAL------EFfeaIPKiarklqtlVDVGLGYIkLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFE 867
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1336523670 515 SeraIQAALDELQK-----NrTSLVIAHRLSTIEQADEIV 549
Cdd:PRK00349 868 D---IRKLLEVLHRlvdkgN-TVVVIEHNLDVIKTADWII 903
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
470-565 |
3.97e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 470 LDTVIGENGVLLSGGQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEQ-ADE 547
Cdd:NF000106 134 LTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQlAHE 213
|
90
....*....|....*...
gi 1336523670 548 IVVVEDGRIVERGSHADL 565
Cdd:NF000106 214 LTVIDRGRVIADGKVDEL 231
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
342-571 |
4.97e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 342 LEFKDVTFTYPGRetPALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILLdghdlreytlaslrdqval 421
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------------------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 422 vSQNVhlfndtvanNIAYarteeYSREQIEEAARMAYAMDFIS--KMDNGLDTVIgeNGVL----------------LSG 483
Cdd:PRK15064 379 -SENA---------NIGY-----YAQDHAYDFENDLTLFDWMSqwRQEGDDEQAV--RGTLgrllfsqddikksvkvLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 484 GQRQRIAIARALLRNSPILILDEATSALDTESERAIQAALDELQKnrTSLVIAH-R--LSTIeqADEIVVVEDGRIVE-R 559
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHdRefVSSL--ATRIIEITPDGVVDfS 517
|
250
....*....|..
gi 1336523670 560 GSHADLLEHRGV 571
Cdd:PRK15064 518 GTYEEYLRSQGI 529
|
|
| ABC_6TM_PglK_like |
cd18553 |
Six-transmembrane helical domain of the ABC transporter PglK and similar proteins; This group ... |
69-236 |
7.77e-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: 41.76 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 69 LVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSSaLITVVR 148
Cdd:cd18553 58 IILIGFYIFRSLYNIFYTYLLNRFSFGRYHSIAYRLFKNYLKLNYQDFTNKNSSDLSKSIINEASNLSQVIQS-FLFILS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 149 EGASIIGLFVMMFYYSWQLSLIL-IVLAPIVSMAIRVVSKRFRN---ISKNMQNTMGQVTTSAeqmLKGHKEVLMFGGQA 224
Cdd:cd18553 137 EIFVILFIYSLLLYVNWKITLVLtLFLGLNVFFITKIVSKKIKKqgkKREESQKKFYKILSET---FGNFKIIKLKSNEK 213
|
170
....*....|..
gi 1336523670 225 VETKRFDKVSNK 236
Cdd:cd18553 214 EILKNFSQASLK 225
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
480-557 |
9.70e-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: 42.35 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 480 LLSGGQRQRIAIARA----LLRNSPILILDEATSALD-TESERAIQaALDELQKNRTSLVIAHRLSTIEQADEIVVV--- 551
Cdd:TIGR02168 1089 LLSGGEKALTALALLfaifKVKPAPFCILDEVDAPLDdANVERFAN-LLKEFSKNTQFIVITHNKGTMEVADQLYGVtmq 1167
|
....*...
gi 1336523670 552 EDG--RIV 557
Cdd:TIGR02168 1168 EKGvsKIV 1175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
326-512 |
1.25e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 326 QEKDEGKLVIErAKG-NLEFKDvtFTypgretpALRNIDLNIQEGKTVALVGRSGSGKSTIASLITRFYDIDNGQILL-- 402
Cdd:NF033858 258 PADDDDEPAIE-ARGlTMRFGD--FT-------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfg 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 403 ---DGHDLreytlaSLRDQVALVSQNVHLFND-TVANNIA-YARTEEYSREQIeeAARMAYAMD-FiskmdnGLDTVIGE 476
Cdd:NF033858 328 qpvDAGDI------ATRRRVGYMSQAFSLYGElTVRQNLElHARLFHLPAAEI--AARVAEMLErF------DLADVADA 393
|
170 180 190
....*....|....*....|....*....|....*.
gi 1336523670 477 NGVLLSGGQRQRIAIARALLRNSPILILDEATSALD 512
Cdd:NF033858 394 LPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
362-537 |
1.66e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 362 IDLniqEGKTVALVGRSGSGKSTIASLIT-------RFYDIDNGQILLDG-----------HDLREYTL----------- 412
Cdd:COG0419 19 IDF---DDGLNLIVGPNGAGKSTILEAIRyalygkaRSRSKLRSDLINVGseeasvelefeHGGKRYRIerrqgefaefl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 413 -ASLRDQVALVSQnvhLFNDTVANNIA--YARTEEYSREQIEEAARMAYAMDFISKMDNGLDTVigengVLLSGGQRQRI 489
Cdd:COG0419 96 eAKPSERKEALKR---LLGLEIYEELKerLKELEEALESALEELAELQKLKQEILAQLSGLDPI-----ETLSGGERLRL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1336523670 490 AIARALLrnspiLILDeaTSALDTESERAIQAALDELQknrtslVIAH 537
Cdd:COG0419 168 ALADLLS-----LILD--FGSLDEERLERLLDALEELA------IITH 202
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
481-549 |
2.11e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 2.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336523670 481 LSGGQRQRIAIARALLRNSP---ILILDEATSALDTESERA-IQAALDELQKNRTSLVIAHRLSTIEQADEIV 549
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKAlIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
60-175 |
5.89e-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: 38.99 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 60 DRSVLLWMpLVVIGLMLLRGVTSYISSYCISWVSGKVVMTMRRRLFSHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSS 139
Cdd:cd18604 39 EVSVLYYL-GIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110
....*....|....*....|....*....|....*.
gi 1336523670 140 SSALITVVREGASIIGLFVMMFYYSWQLSLILIVLA 175
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA 153
|
|
| CysC |
COG0529 |
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ... |
364-409 |
6.21e-03 |
|
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 440295 [Multi-domain] Cd Length: 189 Bit Score: 38.15 E-value: 6.21e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1336523670 364 LNIQEGKTVALVGRSGSGKSTIASLI-TRFYDIDNGQILLDGHDLRE 409
Cdd:COG0529 11 LKGQKGFVVWFTGLSGSGKSTLANALeRRLFERGRHVYLLDGDNVRH 57
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
475-552 |
6.33e-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: 38.06 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336523670 475 GENGVLLSGGQRQRIAIARAL----LRNSPILILDEATSALDTESERAIQAALDELQKNRTS-LVIAHRLSTIEQADEIV 549
Cdd:cd03239 89 GKVEQILSGGEKSLSALALIFalqeIKPSPFYVLDEIDAALDPTNRRRVSDMIKEMAKHTSQfIVITLKKEMFENADKLI 168
|
...
gi 1336523670 550 VVE 552
Cdd:cd03239 169 GVL 171
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
366-386 |
9.07e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 38.76 E-value: 9.07e-03
|
| |
