|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-577 |
3.68e-141 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 421.88 E-value: 3.68e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 5 QLFKNLRPFVKPYRSLVVATLLLTLVGSFTSQVNALILQYTVDSInglveAGKGLKEGLKIISFISIVLMtkeILNAFIT 84
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDAL-----LAGGDLSALLLLLLLLLGLA---LLRALLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 85 FGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILM 164
Cdd:COG1132 79 YLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFF--DRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 165 FNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNN 244
Cdd:COG1132 157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 245 QMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFA 324
Cdd:COG1132 237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 325 ILKADDEKESSGNYIP-TKLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGK 403
Cdd:COG1132 317 LLDEPPEIPDPPGAVPlPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 404 ILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALL 479
Cdd:COG1132 397 ILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTvvgeRGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 480 LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT----------ViiishsisqiIDADYTYV 549
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTtiviahrlstI----------RNADRILV 546
|
570 580
....*....|....*....|....*...
gi 2534190046 550 MKQGEVVEHGIHEDVYKMNGTYKEIFDA 577
Cdd:COG1132 547 LDDGRIVEQGTHEELLARGGLYARLYRL 574
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
78-575 |
1.86e-123 |
|
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: 380.33 E-value: 1.86e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQdnQAGKLQTRIdRGIES----LTRLVQNFFIDILpl 153
Cdd:COG2274 207 LFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRF-RDVESirefLTGSLLTALLDLL-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 154 faNSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLsgRRRNLRGYREQ-KSQG-IISIINSITVIKSFNREDIEG 231
Cdd:COG2274 282 --FVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL--RRLSREESEASaKRQSlLVETLRGIETIKALGAESRFR 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 232 KKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDE 311
Cdd:COG2274 358 RRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQR 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 312 MNDAMIYSESFFAILKADDEKESSGNYIPT-KLKGKFEIQNVEFSYP-NGYKALKNINMTIQPNKITALVGLSGAGKSTV 389
Cdd:COG2274 438 FQDAKIALERLDDILDLPPEREEGRSKLSLpRLKGDIELENVSFRYPgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 390 INLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDL 469
Cdd:COG2274 518 LKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 470 PEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDAD 545
Cdd:COG2274 598 PMGYDTVvgegGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLAD 677
|
490 500 510
....*....|....*....|....*....|
gi 2534190046 546 YTYVMKQGEVVEHGIHEDVYKMNGTYKEIF 575
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
49-569 |
4.18e-101 |
|
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: 317.86 E-value: 4.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 49 INGLVEAGKGLKEGLKIISFISIVLmtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQdnQAGKL 128
Cdd:COG4988 44 LAGLIIGGAPLSALLPLLGLLLAVL----LLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGK--STGEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 129 QTRIDRGIESLtrlvQNFFIDILPLFANSIVA----LILMFNANFYVGLVGLC---IVPIYFIITQQQAKKLSgrRRNLR 201
Cdd:COG4988 118 ATLLTEGVEAL----DGYFARYLPQLFLAALVplliLVAVFPLDWLSGLILLVtapLIPLFMILVGKGAAKAS--RRQWR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 202 GYReQKSQGIISIINSITVIKSFNREDIEGKKqldLQKELTNNQ---MQTRKTSFffdgLKSFIEQF----GVVIIIILT 274
Cdd:COG4988 192 ALA-RLSGHFLDRLRGLTTLKLFGRAKAEAER---IAEASEDFRkrtMKVLRVAF----LSSAVLEFfaslSIALVAVYI 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 275 SYLVLDGQMTIGASMFHILL----FnnvsAPIRQL----HriyDEMNdAMIYSESFFAILKADDEKESSGNyIPTKLKGK 346
Cdd:COG4988 264 GFRLLGGSLTLFAALFVLLLapefF----LPLRDLgsfyH---ARAN-GIAAAEKIFALLDAPEPAAPAGT-APLPAAGP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEI--QNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIG 424
Cdd:COG4988 335 PSIelEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPlgegGRGLSGGQAQRLALARALLRDAPL 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 501 IFLDEPTASLDAiATEQ-IKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNG 569
Cdd:COG4988 495 LLLDEPTAHLDA-ETEAeILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-571 |
5.42e-89 |
|
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: 286.61 E-value: 5.42e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 6 LFKNLRPFVKPYRSLVVATLLLTLVGSFTSQVNALILQYTVDSINGLVEAGKGLKEGLKIISFIsivlmtkeILNAFITF 85
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLA--------VLRGICSF 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 86 GQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQDnqAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMF 165
Cdd:TIGR02203 73 VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQP--TGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 166 NANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQ 245
Cdd:TIGR02203 151 YYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 246 MQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAI 325
Cdd:TIGR02203 231 MKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 326 LKADDEKESSGNYIPtKLKGKFEIQNVEFSYP-NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKI 404
Cdd:TIGR02203 311 LDSPPEKDTGTRAIE-RARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 405 LLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNV-NATFEEIEDAAKRAYIHEQIMDLPEGYQ----SKALL 479
Cdd:TIGR02203 390 LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDtpigENGVL 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 480 LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:TIGR02203 470 LSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
|
570
....*....|..
gi 2534190046 560 IHEDVYKMNGTY 571
Cdd:TIGR02203 550 THNELLARNGLY 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
121-571 |
3.06e-82 |
|
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: 269.77 E-value: 3.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 121 QDNQAGKLQTRIDRG---IESLTRLVqnFFiDILP-LFANSIVALILMFNANFYVGLVGLCIVPIYFIITQqqakKLSGR 196
Cdd:COG5265 130 LERQTGGLSRDIERGtkgIEFLLRFL--LF-NILPtLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTV----VVTEW 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 197 RRNLRgyREQ-------KSQGIISIINSITViKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVI 269
Cdd:COG5265 203 RTKFR--REMneadseaNTRAVDSLLNYETV-KYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTA 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 270 IIILTSYLVLDGQMTIGAsmfhillFNNVSAPIRQLHR-------IYDEMNDAMIYSESFFAILKADDEKESSGNYIPTK 342
Cdd:COG5265 280 MMLMAAQGVVAGTMTVGD-------FVLVNAYLIQLYIplnflgfVYREIRQALADMERMFDLLDQPPEVADAPDAPPLV 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 343 LKG---KFEiqNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL 419
Cdd:COG5265 353 VGGgevRFE--NVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFL 495
Cdd:COG5265 431 RAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRvgerGLKLSGGEKQRVAIARTLL 510
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 496 KNPPIIFLDEPTASLDAiATEQ-IKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTY 571
Cdd:COG5265 511 KNPPILIFDEATSALDS-RTERaIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLY 586
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
10-574 |
1.31e-81 |
|
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: 267.34 E-value: 1.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 10 LRPFVKPYRSLVVATLLLTLVGSFTSQVNALILQYTVDsiNGLVEAGKGLkeglkIISFISIVLMTKEILnAFITFGQKY 89
Cdd:TIGR02204 9 LWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMID--HGFSKDSSGL-----LNRYFAFLLVVALVL-ALGTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 90 Y----GEKlrilVSQDLAQTIIEKILTYRMAFYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMF 165
Cdd:TIGR02204 81 LvtwlGER----VVADIRRAVFAHLISLSPSFFDK--NRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 166 NANFYVGLVGLCIVPiyFIItqqqAKKLSGRRRNLRGYREqkSQGIISIINS--------ITVIKSFNREDIEGKK---Q 234
Cdd:TIGR02204 155 ITSPKLTSLVLLAVP--LVL----LPILLFGRRVRKLSRE--SQDRIADAGSyagetlgaIRTVQAFGHEDAERSRfggA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 235 LDLQKELTNNQMQTRK--TSFFFdglksFIEQFGVVIIIILTSYLVLDGQM---TIGASMFHILLfnnVSAPIRQLHRIY 309
Cdd:TIGR02204 227 VEKAYEAARQRIRTRAllTAIVI-----VLVFGAIVGVLWVGAHDVIAGKMsagTLGQFVFYAVM---VAGSIGTLSEVW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 310 DEMNDAMIYSESFFAILKADDEKESSGN--YIPTKLKGKFEIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAG 385
Cdd:TIGR02204 299 GELQRAAGAAERLIELLQAEPDIKAPAHpkTLPVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 386 KSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQ 465
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 466 IMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQI 541
Cdd:TIGR02204 459 ISALPEGYDTylgeRGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538
|
570 580 590
....*....|....*....|....*....|...
gi 2534190046 542 IDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEI 574
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAKGGLYARL 571
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
348-575 |
1.56e-81 |
|
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: 256.00 E-value: 1.56e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPN-GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:cd03251 2 EFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTvigeRGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIF 575
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
348-573 |
3.16e-81 |
|
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: 255.16 E-value: 3.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGL 425
Cdd:cd03249 2 EFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKE 573
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
348-577 |
1.19e-79 |
|
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: 251.00 E-value: 1.19e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:cd03253 2 EFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:cd03253 82 QDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIvgerGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIFDA 577
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
90-573 |
5.36e-78 |
|
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: 257.39 E-value: 5.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 90 YGEKLrilVSQDLAQTIIEKIltyRMAFYTN--QDNQAGKLQTRidRGiESLTRLV------QNFFID-ILPLFANSIVA 160
Cdd:COG4987 73 YLERL---VSHDATLRLLADL---RVRLYRRlePLAPAGLARLR--SG-DLLNRLVadvdalDNLYLRvLLPLLVALLVI 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 161 LILMFNANFY----------VGLVGLCIVPIYFIITqqqAKKLSGRRRNLRG-YREQksqgIISIINSITVIKSFNREDI 229
Cdd:COG4987 144 LAAVAFLAFFspalalvlalGLLLAGLLLPLLAARL---GRRAGRRLAAARAaLRAR----LTDLLQGAAELAAYGALDR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 230 EGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMT---IGASMFHIL-LFNNVsAPIRQL 305
Cdd:COG4987 217 ALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSgplLALLVLAALaLFEAL-APLPAA 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 306 HRIYDEMNDAmiySESFFAILKADDEKESSGNYIPTKLKGKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGA 384
Cdd:COG4987 296 AQHLGRVRAA---ARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGS 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 385 GKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHE 464
Cdd:COG4987 373 GKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGD 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 465 QIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQ 540
Cdd:COG4987 453 WLAALPDGLDTwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAG 532
|
490 500 510
....*....|....*....|....*....|...
gi 2534190046 541 IIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKE 573
Cdd:COG4987 533 LERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
48-550 |
3.48e-75 |
|
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: 249.13 E-value: 3.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 48 SINGLVEAGKGLKEGLKIISFISIVLmtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILtyrmAFYTN--QDNQA 125
Cdd:TIGR02857 29 VVDGLISAGEPLAELLPALGALALVL----LLRALLGWLQERAAARAAAAVKSQLRERLLEAVA----ALGPRwlQGRPS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 126 GKLQTRIDRGIESLtrlvQNFFIDILP-LFANSIVALILM---FNANFYVGLVGLC---IVPIYFIITQQQAKKLSgrRR 198
Cdd:TIGR02857 101 GELATLALEGVEAL----DGYFARYLPqLVLAVIVPLAILaavFPQDWISGLILLLtapLIPIFMILIGWAAQAAA--RK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 199 NLRGYrEQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFffdgLKSFIEQF----GVVIIIILT 274
Cdd:TIGR02857 175 QWAAL-SRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAF----LSSAVLELfatlSVALVAVYI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 275 SYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYIPTKLKGKFEIQNVEF 354
Cdd:TIGR02857 250 GFRLLAGDLDLATGLFVLLLAPEFYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 355 SYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFN 434
Cdd:TIGR02857 330 AYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFA 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 435 GTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:TIGR02857 410 GTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2534190046 511 DAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVM 550
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-574 |
1.76e-72 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 243.39 E-value: 1.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 5 QLFKNLRPFVKPYRSlvvatllltlvGSFTSQVnALILQYTVDS-----INGLVEAGKGLKEG--LKIISFISIVLMtke 77
Cdd:PRK11176 11 QTFRRLWPTIAPFKA-----------GLIVAGV-ALILNAASDTfmlslLKPLLDDGFGKADRsvLKWMPLVVIGLM--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEklriLVSQDLAQTIIEKILTYRM----AFYTNQdnQAGKLQTRIDRGIESLTRLVQNFFIDILPL 153
Cdd:PRK11176 76 ILRGITSFISSYCIS----WVSGKVVMTMRRRLFGHMMgmpvSFFDKQ--STGTLLSRITYDSEQVASSSSGALITVVRE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 154 FANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLrgyreQKSQGIIS-----IINSITVIKSFNRED 228
Cdd:PRK11176 150 GASIIGLFIMMFYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNM-----QNTMGQVTtsaeqMLKGHKEVLIFGGQE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 229 IEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIG------ASMFHILlfnnvsAPI 302
Cdd:PRK11176 225 VETKRFDKVSNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGtitvvfSSMIALM------RPL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 303 RQLHRIYDEMNDAMIYSESFFAILKADDEKESsGNYIPTKLKGKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGL 381
Cdd:PRK11176 299 KSLTNVNAQFQRGMAACQTLFAILDLEQEKDE-GKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 382 SGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNA-TFEEIEDAAKRA 460
Cdd:PRK11176 378 SGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 461 YIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISH 536
Cdd:PRK11176 458 YAMDFINKMDNGLDTvigeNGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
570 580 590
....*....|....*....|....*....|....*...
gi 2534190046 537 SISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEI 574
Cdd:PRK11176 538 RLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
106-572 |
1.86e-71 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 243.48 E-value: 1.86e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 106 IIEKILTYRMAFYtnQDNQAGKLQTRIdrgiESLTRLVQNFFIDILPLFANSIV----ALILMFNANFYVGLVGLCIVPI 181
Cdd:TIGR00958 240 LFRSLLRQDLGFF--DENKTGELTSRL----SSDTQTMSRSLSLNVNVLLRNLVmllgLLGFMLWLSPRLTMVTLINLPL 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 182 YFIITqqqaKKLSGRRRNL-RGYRE---QKSQGIISIINSITVIKSFNREDIEGKKqldLQKELTNNQMQTRKTSFFFDG 257
Cdd:TIGR00958 314 VFLAE----KVFGKRYQLLsEELQEavaKANQVAEEALSGMRTVRSFAAEEGEASR---FKEALEETLQLNKRKALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 258 L---KSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKES 334
Cdd:TIGR00958 387 YlwtTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 335 SGNYIPTKLKGKFEIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE 412
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 413 EYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRI 488
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTevgeKGSQLSGGQKQRI 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAikKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMN 568
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....
gi 2534190046 569 GTYK 572
Cdd:TIGR00958 705 GCYK 708
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
345-569 |
8.62e-71 |
|
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: 227.49 E-value: 8.62e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIG 424
Cdd:cd03254 1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTvlgeNGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNG 569
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
108-559 |
9.51e-71 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 238.71 E-value: 9.51e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 108 EKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILplfaNSIVALILM----FNANFYVG--LVGLCIVpi 181
Cdd:PRK13657 97 ERIIQLPLAWH--SQRGSGRALHTLLRGTDALFGLWLEFMREHL----ATLVALVVLlplaLFMNWRLSlvLVVLGIV-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 182 YFIITQQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSF 261
Cdd:PRK13657 169 YTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPVLSWWALASVLNRA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 262 IEQFGVVIIIILTSYLVLDGQMTIG--------ASMFhILLFNNVSAPIRQLHriydeMNDAMIysESFFAILKA-DDEK 332
Cdd:PRK13657 249 ASTITMLAILVLGAALVQKGQLRVGevvafvgfATLL-IGRLDQVVAFINQVF-----MAAPKL--EEFFEVEDAvPDVR 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 333 ESSGNYIPTKLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE 412
Cdd:PRK13657 321 DPPGAIDLGRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 413 EYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKA----LLLSGGQQQRI 488
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVgergRQLSGGERQRL 480
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
134-531 |
2.90e-68 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 234.37 E-value: 2.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 134 RGIESltrlVQNFF--------IDiLPLFansIVALILMF---NANFYVGLVGLCIVPIYFIITQQQAKKLSGRrrnlrG 202
Cdd:TIGR03375 250 REFES----VRDFFtsatltalID-LPFA---LLFLLVIAiigGPLVWVPLVAIPLILLPGLLLQRPLSRLAEE-----S 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 203 YRE--QKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLD 280
Cdd:TIGR03375 317 MREsaQRNAVLVESLSGLETIKALNAEGRFQRRWEQTVAALARSGLKSRFLSNLATNFAQFIQQLVSVAIVVVGVYLISD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 281 GQMTIGASMFHILLFNNVSAPIRQLHRI---YDEMNDAMiysESFFAILKADDEKESSGNYI-PTKLKGKFEIQNVEFSY 356
Cdd:TIGR03375 397 GELTMGGLIACVMLSGRALAPLGQLAGLltrYQQAKTAL---QSLDELMQLPVERPEGTRFLhRPRLQGEIEFRNVSFAY 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 357 PN-GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNG 435
Cdd:TIGR03375 474 PGqETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYG 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQ----SKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:TIGR03375 554 TLRDNIALGAPYADDEEILRAAELAGVTEFVRRHPDGLDmqigERGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMD 633
|
410 420
....*....|....*....|
gi 2534190046 512 AIATEQIKNSLDAIKKDRTV 531
Cdd:TIGR03375 634 NRSEERFKDRLKRWLAGKTL 653
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
348-554 |
3.01e-63 |
|
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: 205.69 E-value: 3.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:cd03228 2 EFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNGTIEENIrygnvnatfeeiedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEP 506
Cdd:cd03228 82 PQDPFLFSGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534190046 507 TASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGE 554
Cdd:cd03228 124 TSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
260-571 |
2.23e-62 |
|
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: 218.46 E-value: 2.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 260 SFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYI 339
Cdd:TIGR01846 369 ELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILNSPTEPRSAGLAA 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 340 PTKLKGKFEIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQF 418
Cdd:TIGR01846 449 LPELRGAITFENIRFRYaPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAW 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 LRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMF 494
Cdd:TIGR01846 529 LRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTevgeKGANLSGGQRQRIAIARAL 608
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTY 571
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
336-555 |
6.51e-61 |
|
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: 201.55 E-value: 6.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 336 GNYIPTKLKGKFEIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEE 413
Cdd:cd03248 1 GSLAPDHLKGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 414 YDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIA 489
Cdd:cd03248 81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTevgeKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEV 555
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
348-576 |
1.25e-56 |
|
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: 190.78 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:cd03252 2 TFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:cd03252 82 LQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIFD 576
Cdd:cd03252 162 FDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
345-559 |
1.02e-55 |
|
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: 187.80 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSYPNG-YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNI 423
Cdd:cd03245 1 GRIEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGY----QSKALLLSGGQQQRIAIARMFLKNPP 499
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLdlqiGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
66-577 |
1.94e-54 |
|
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: 196.88 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 66 ISFISIVLMTKEILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQdnQAGKLQTRIDRG---IESLTRL 142
Cdd:TIGR01193 195 LGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTR--RTGEIVSRFTDAssiIDALAST 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 143 VQNFFIDILPLFansIVALILMFNaNFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIK 222
Cdd:TIGR01193 273 ILSLFLDMWILV---IVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 223 SFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPI 302
Cdd:TIGR01193 349 SLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPL 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 303 RQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYIPT-KLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGL 381
Cdd:TIGR01193 429 ENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGM 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 382 SGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNV-NATFEEIEDAAKRA 460
Cdd:TIGR01193 509 SGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIA 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 461 YIHEQIMDLPEGYQ----SKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIkKDRTVIIISH 536
Cdd:TIGR01193 589 EIKDDIENMPLGYQtelsEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAH 667
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2534190046 537 SISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIFDA 577
Cdd:TIGR01193 668 RLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
347-559 |
5.60e-49 |
|
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: 170.05 E-value: 5.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFY-----QPDSGKILLDGIDLEEYDTQF--L 419
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVleL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQKNHIFNGTIEENIRYG-------NVNATFEEIEDAAKRAYIHEQIMDlpegyQSKALLLSGGQQQRIAIAR 492
Cdd:cd03260 80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKD-----RLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
320-573 |
3.99e-46 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 171.57 E-value: 3.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 320 ESFFAILKADDEKESSG-NYIPTKLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKF-- 396
Cdd:PRK11174 322 ESLVTFLETPLAHPQQGeKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlp 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 397 YQpdsGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQS- 475
Cdd:PRK11174 402 YQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTp 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 476 ---KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQ 552
Cdd:PRK11174 479 igdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQD 558
|
250 260
....*....|....*....|.
gi 2534190046 553 GEVVEHGIHEDVYKMNGTYKE 573
Cdd:PRK11174 559 GQIVQQGDYAELSQAGGLFAT 579
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
347-566 |
5.97e-46 |
|
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: 161.73 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYiheQIMDLpEGYQSKA-LLLSGGQQQRIAIARMFLKNPPII 501
Cdd:COG1122 81 FQnpDDQLFAPTVEEDVAFGpeNLGLPREEIRERVEEAL---ELVGL-EHLADRPpHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDRT-----------VIIIshsisqiidADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKtviivthdldlVAEL---------ADRVIVLDDGRIVADGTPREVFS 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
276-567 |
4.82e-45 |
|
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: 168.00 E-value: 4.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 276 YLVLDGQMTIGAsMF--HILLfNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESsgnyiPTKL---KGKFEIQ 350
Cdd:COG4618 262 YLVIQGEITPGA-MIaaSILM-GRALAPIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPE-----RMPLprpKGRLSVE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 351 NVEFSYPNGYKA-LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQK 429
Cdd:COG4618 335 NLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQD 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 NHIFNGTIEENI-RYGNVNAtfEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:COG4618 415 VELFDGTIAENIaRFGDADP--EKVVAAAKLAGVHEMILRLPDGYDTRigegGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKD-RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKM 567
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-571 |
1.03e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 167.31 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 344 KGKFEIQNVEFSYPNG-YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDN 422
Cdd:PRK11160 336 QVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIhEQIMDLPEGYqsKALL------LSGGQQQRIAIARMFLK 496
Cdd:PRK11160 416 ISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGL--NAWLgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 497 NPPIIFLDEPTASLDAiATE-QIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTY 571
Cdd:PRK11160 493 DAPLLLLDEPTEGLDA-ETErQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRY 567
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
122-571 |
4.59e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 165.66 E-value: 4.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 122 DNQ-AGKLQTRIDRGieslTRLVQNFFIDILPLFANSI----VALILMFNANFYVGLVGLCIVP---IYFIITQQQAKKL 193
Cdd:PRK10790 117 DTQpVGQLISRVTND----TEVIRDLYVTVVATVLRSAaligAMLVAMFSLDWRMALVAIMIFPavlVVMVIYQRYSTPI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 194 SgrrRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFdgLKSFIEQFGVVIIIIL 273
Cdd:PRK10790 193 V---RRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHYMARMQTLRLDGFL--LRPLLSLFSALILCGL 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 274 TSYLVLDGQMTIGASMFH--ILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILkaDDEKESSGNYIPTKLKGKFEIQN 351
Cdd:PRK10790 268 LMLFGFSASGTIEVGVLYafISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELM--DGPRQQYGNDDRPLQSGRIDIDN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 352 VEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNH 431
Cdd:PRK10790 346 VSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPV 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IFNGTIEENIRYGNvNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:PRK10790 426 VLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTplgeQGNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 508 ASLDAiATEQ-IKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTY 571
Cdd:PRK10790 505 ANIDS-GTEQaIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
139-566 |
5.55e-44 |
|
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: 164.83 E-value: 5.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 139 LTRLVQNFFIDI--LPLFansiVALILMFNANFYVGLVGLCIVPIYF-----IITQQQAKK---LSGRRRNLRGYREQKS 208
Cdd:TIGR01842 115 LTGPGLFAFFDApwMPIY----LLVCFLLHPWIGILALGGAVVLVGLallnnRATKKPLKEateASIRANNLADSALRNA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 209 QgiisIINSITVIKSF-NREDIEGKKQLDLQKELTN-NQMQTRKTSFFFDGLKSFIEQFGvviiiiltSYLVLDGQMTIG 286
Cdd:TIGR01842 191 E----VIEAMGMMGNLtKRWGRFHSKYLSAQSAASDrAGMLSNLSKYFRIVLQSLVLGLG--------AYLAIDGEITPG 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 287 ASMFHILLFNNVSAPIRQLHRIYDEMNDAMI-YS--ESFFAILKADDEKESsgnyIPtKLKGKFEIQNVEFSYPNGYK-A 362
Cdd:TIGR01842 259 MMIAGSILVGRALAPIDGAIGGWKQFSGARQaYKrlNELLANYPSRDPAMP----LP-EPEGHLSVENVTIVPPGGKKpT 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENI- 441
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIa 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 442 RYGNvNATFEEIEDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQ 517
Cdd:TIGR01842 414 RFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTvigpGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2534190046 518 IKNSLDAIKKDR-TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:TIGR01842 493 LANAIKALKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
348-531 |
3.39e-43 |
|
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: 162.14 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:TIGR02868 336 ELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:TIGR02868 416 QDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVlgegGARLSGGERQRLALARALLADAPILLL 495
|
170 180
....*....|....*....|....*...
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:TIGR02868 496 DEPTEHLDAETADELLEDLLAALSGRTV 523
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
340-559 |
7.84e-42 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 151.73 E-value: 7.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 340 PTKLKGKFEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKST---VINLLDKFYqPD---SGKILLDGIDL-- 411
Cdd:COG1117 5 ASTLEPKIEVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLI-PGarvEGEILLDGEDIyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 412 EEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYG------NVNATFEEI-EDAAKRAYIHEQIMD-LpegyQSKALLLSGG 483
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEVKDrL----KKSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 484 QQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT-------------ViiishsisqiidADYTYVM 550
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTivivthnmqqaarV------------SDYTAFF 226
|
....*....
gi 2534190046 551 KQGEVVEHG 559
Cdd:COG1117 227 YLGELVEFG 235
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
346-565 |
3.79e-41 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 149.37 E-value: 3.79e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFY-----QPDSGKILLDGIDL--EEYDTQF 418
Cdd:TIGR00972 1 AIEIENLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNdlvpgVRIEGKVLFDGQDIydKKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 LRDNIGLVLQKNHIFNGTIEENIRYG------NVNATFEEI-EDAAKRAYIHEQIMDLPEGYqskALLLSGGQQQRIAIA 491
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFPMSIYDNIAYGprlhgiKDKKELDEIvEESLKKAALWDEVKDRLHDS---ALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKYTIVIVTHNMQQAARiSDRTAFFYDGELVEYGPTEQIF 231
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
363-508 |
4.12e-41 |
|
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: 145.87 E-value: 4.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNG-TIEENI 441
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 442 RYGnvnATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTA 508
Cdd:pfam00005 81 RLG---LLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
173-575 |
5.37e-41 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 156.80 E-value: 5.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 173 LVGLCIVPIYFIITQQQAKKLSGRRRNlrgyreqkSQGIISIIN--------SITVIKSFNREDIEGKKQLDLQKELTNN 244
Cdd:PRK10789 141 LLALLPMPVMAIMIKRYGDQLHERFKL--------AQAAFSSLNdrtqesltSIRMIKAFGLEDRQSALFAADAEDTGKK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 245 QMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIG-------------------ASMFHILlfNNVSAP---I 302
Cdd:PRK10789 213 NMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVVNGSLTLGqltsfvmylglmiwpmlalAWMFNIV--ERGSAAysrI 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 303 RQLhriydeMNDAMIysesffailkADDEKESsgnyIPTKlKGKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGL 381
Cdd:PRK10789 291 RAM------LAEAPV----------VKDGSEP----VPEG-RGELDVNIRQFTYPQTDHpALENVNFTLKPGQMLGICGP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 382 SGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKRAY 461
Cdd:PRK10789 350 TGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLAS 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 462 IHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHS 537
Cdd:PRK10789 430 VHDDILRLPQGYDTevgeRGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHR 509
|
410 420 430
....*....|....*....|....*....|....*...
gi 2534190046 538 ISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIF 575
Cdd:PRK10789 510 LSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMY 547
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
345-559 |
1.18e-40 |
|
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: 147.25 E-value: 1.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNI 423
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRYGNVnATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL----LSGGQQQRIAIARMFLKNPP 499
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEggenLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
348-554 |
2.67e-40 |
|
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: 145.69 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLpEGYQSKALL-LSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENLGLPE-EEIEERVEEALELVGL-EGLRDRSPFtLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIKKDRT--VIIISHSISQIIDADYTYVMKQGE 554
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKtiIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
348-559 |
5.32e-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: 146.16 E-value: 5.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFlRDNIGLVL 427
Cdd:COG4555 3 EVENLSKKYGKV-PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG-TIEENIRYgnvNATFEEI--EDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:COG4555 81 DERGLYDRlTVRENIRY---FAELYGLfdEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKK-DRTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQG 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
348-555 |
7.22e-40 |
|
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: 144.94 E-value: 7.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYD----TQFLR 420
Cdd:cd03255 2 ELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQKNHIFNG-TIEENIRYGnvnATFEEIEDAAKRAYIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:cd03255 82 RHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEEllERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEV 555
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
348-529 |
1.96e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKSTVINL---LDKfyqPDSGKILLDGIDLEEYD----TQ 417
Cdd:COG1136 6 ELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 FLRDNIGLVLQKNHIFNG-TIEENI----RYGNVNAtfeeiEDAAKRAyihEQIMD---LPEGYQSKALLLSGGQQQRIA 489
Cdd:COG1136 83 LRRRHIGFVFQFFNLLPElTALENValplLLAGVSR-----KERRERA---RELLErvgLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR 529
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNREL 194
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
348-531 |
3.91e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.58 E-value: 3.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLVL 427
Cdd:COG1131 2 EVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG-TIEENIRYgnvNATFEEIEDAAKRAYIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:COG1131 80 QEPALYPDlTVRENLRF---FARLYGLPRKEARERIDEllELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180
....*....|....*....|....*...
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKD-RTV 531
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEgKTV 184
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
66-573 |
5.65e-38 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 150.95 E-value: 5.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 66 ISFISIVLMTKEILnafitfgQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQDNQAGKLQTRIDRGIESL-TRLVQ 144
Cdd:PTZ00265 872 ILVIAIAMFISETL-------KNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLkTGLVN 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 145 NFFIdilplFANSIVALILMFNANFY-VGLVGLCIVPIYFIITQ--------QQAKKLSGRRRNLRG-----------YR 204
Cdd:PTZ00265 945 NIVI-----FTHFIVLFLVSMVMSFYfCPIVAAVLTGTYFIFMRvfairarlTANKDVEKKEINQPGtvfaynsddeiFK 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 205 EQKSQGIISIINSITVIkSFNRED-----IEgkKQLDLQkeltnNQMQTRKTSF------FFDGLKSFIEQFGVviiiIL 273
Cdd:PTZ00265 1020 DPSFLIQEAFYNMNTVI-IYGLEDyfcnlIE--KAIDYS-----NKGQKRKTLVnsmlwgFSQSAQLFINSFAY----WF 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 274 TSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKAD---DEKESSGNYIPTK--LKGKFE 348
Cdd:PTZ00265 1088 GSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKsniDVRDNGGIRIKNKndIKGKIE 1167
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSY---PNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQ--------------------------- 398
Cdd:PTZ00265 1168 IMDVNFRYisrPN-VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgde 1246
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 399 ---------------------------PDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGNVNATFE 451
Cdd:PTZ00265 1247 eqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATRE 1326
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 452 EIEDAAKRAYIHEQIMDLPEGYQSK----ALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK 527
Cdd:PTZ00265 1327 DVKRACKFAAIDEFIESLPNKYDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1406
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 528 --DRTVIIISHSISQIIDADYTYVM----KQGEVVE-HGIHEDVYKM-NGTYKE 573
Cdd:PTZ00265 1407 kaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVqDGVYKK 1460
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
348-566 |
7.83e-37 |
|
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 downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 138.35 E-value: 7.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSY----PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL---EEYDTQFLR 420
Cdd:TIGR04521 2 KLKNVSYIYqpgtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakKKKKLKDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYiheQIMDLPEGYQSKA-LLLSGGQQQRIAIARMFL 495
Cdd:TIGR04521 82 KKVGLVFQfpEHQLFEETVYKDIAFGpkNLGLSEEEAEERVKEAL---ELVGLDEEYLERSpFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 496 KNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR---TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKgltVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-565 |
1.35e-36 |
|
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: 143.12 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYP----NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD-- 421
Cdd:COG1123 262 EVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRElr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 -NIGLVLQK-NHIFN--GTIEENIRYGNVNATFEEIEDAAKRAyihEQIMD---LPEGYQSK-ALLLSGGQQQRIAIARM 493
Cdd:COG1123 342 rRVQMVFQDpYSSLNprMTVGDIIAEPLRLHGLLSRAERRERV---AELLErvgLPPDLADRyPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 494 FLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR------------TVIIIshsisqiidADYTYVMKQGEVVEHGIH 561
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELgltylfishdlaVVRYI---------ADRVAVMYDGRIVEDGPT 489
|
....
gi 2534190046 562 EDVY 565
Cdd:COG1123 490 EEVF 493
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
348-564 |
2.10e-36 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 136.28 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:cd03295 2 EFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIryGNVnATFEEIEDAAKRAYIHE--QIMDLPEG-----YQSKallLSGGQQQRIAIARMFLKNPP 499
Cdd:cd03295 82 QQIGLFpHMTVEENI--ALV-PKLLKWPKEKIRERADEllALVGLDPAefadrYPHE---LSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKD--RT-VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElgKTiVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
347-559 |
4.85e-36 |
|
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: 133.21 E-value: 4.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYP-NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQfLRDNIGL 425
Cdd:cd03247 1 LSINNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNGTIEENIrygnvnatfeeiedaakrayiheqimdlpeGYQskallLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------------------GRR-----FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 506 PTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
347-518 |
8.77e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.40 E-value: 8.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNGTIEENI----RYGNVNATFEEIEDAAKRAYIHEQIMDLPegyqskALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:COG4619 80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKP------VERLSGGERQRLALIRALLLQPDVLL 153
|
170
....*....|....*.
gi 2534190046 503 LDEPTASLDAIATEQI 518
Cdd:COG4619 154 LDEPTSALDPENTRRV 169
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
347-526 |
2.81e-35 |
|
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: 130.80 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKA-LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGL 425
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNGTIEENIrygnvnatfeeiedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:cd03246 81 LPQDDELFSGSIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180
....*....|....*....|.
gi 2534190046 506 PTASLDaIATEQIKNslDAIK 526
Cdd:cd03246 123 PNSHLD-VEGERALN--QAIA 140
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
347-531 |
2.92e-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: 133.08 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD---NI 423
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQK-NHIFNGTIEENI---RYGNVNA--------TFEEIEDAakrAYIHEQImDLPEGYQSKALLLSGGQQQRIAIA 491
Cdd:cd03256 81 GMIFQQfNLIERLSVLENVlsgRLGRRSTwrslfglfPKEEKQRA---LAALERV-GLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKNSL--DAIKKDRTV 531
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLkrINREEGITV 198
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
348-559 |
4.39e-35 |
|
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: 131.49 E-value: 4.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVL 427
Cdd:cd03259 2 ELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYGNVNATF--EEIEDAAKRAyihEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:cd03259 79 QDYALFpHLTVAENIAFGLKLRGVpkAEIRARVREL---LELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKDR---TVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELgitTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
348-559 |
3.24e-34 |
|
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: 129.55 E-value: 3.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGY---KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD--- 421
Cdd:cd03257 3 EVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQK-----NHIFngTIEENIRYGNVNATFEEIEDAAKRAYIHEQI-MDLPEGY-QSKALLLSGGQQQRIAIARMF 494
Cdd:cd03257 83 EIQMVFQDpmsslNPRM--TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPEEVlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR------------TVIIIshsisqiidADYTYVMKQGEVVEHG 559
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELgltllfithdlgVVAKI---------ADRVAVMYAGKIVEEG 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
348-531 |
3.53e-34 |
|
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: 126.98 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QknhifngtieenirygnvnatfeeiedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180
....*....|....*....|....*
gi 2534190046 508 ASLDAIATEQIKNSLDAI-KKDRTV 531
Cdd:cd00267 109 SGLDPASRERLLELLRELaEEGRTV 133
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
347-518 |
3.54e-34 |
|
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: 127.69 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL--EEYDTQFLRDNIG 424
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdLEDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNG-TIEENIRYGnvnatfeeiedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:cd03229 80 MVFQDFALFPHlTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170
....*....|....*
gi 2534190046 504 DEPTASLDAIATEQI 518
Cdd:cd03229 125 DEPTSALDPITRREV 139
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
348-527 |
3.55e-34 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 130.11 E-value: 3.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRDNIG 424
Cdd:TIGR02315 3 EVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDitkLRGKKLRKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQK-NHIFNGTIEENIRYGNVNAT---------FEEiEDAAKRAYIHEQImDLPEGYQSKALLLSGGQQQRIAIARMF 494
Cdd:TIGR02315 83 MIFQHyNLIERLTVLENVLHGRLGYKptwrsllgrFSE-EDKERALSALERV-GLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190
....*....|....*....|....*....|...
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK 527
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINK 193
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
347-527 |
3.68e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.18 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD---NI 423
Cdd:COG3638 3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNG-TIEENI------RYGNVNATF-----EEIEdaakRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIA 491
Cdd:COG3638 83 GMIFQQFNLVPRlSVLTNVlagrlgRTSTWRSLLglfppEDRE----RALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIknsLDAIKK 527
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQV---MDLLRR 191
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
31-316 |
4.74e-34 |
|
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: 131.13 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 31 GSFTSQVNALILQYTVDSInglveAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKI 110
Cdd:cd07346 11 ATALGLALPLLTKLLIDDV-----IPAGDLSLLLWIALLLLLLA---LLRALLSYLRRYLAARLGQRVVFDLRRDLFRHL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 111 LTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQA 190
Cdd:cd07346 83 QRLSLSFF--DRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 191 KKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVII 270
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2534190046 271 IILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAM 316
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQAL 286
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
348-531 |
6.29e-34 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 127.13 E-value: 6.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRdNIGLVL 427
Cdd:cd03230 2 EVRNLSKRYGKK-TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG-TIEENIRYgnvnatfeeiedaakrayiheqimdlpegyqskalllSGGQQQRIAIARMFLKNPPIIFLDEP 506
Cdd:cd03230 80 EEPSLYENlTVRENLKL-------------------------------------SGGMKQRLALAQALLHDPELLILDEP 122
|
170 180
....*....|....*....|....*.
gi 2534190046 507 TASLDAIATEQIKNSLDAIKKD-RTV 531
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEgKTI 148
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
348-531 |
2.15e-33 |
|
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: 127.24 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeYDTQFLRDNIGLV 426
Cdd:cd03263 2 QIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR-TDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIR-YGNVNATFEEIEDAAKRAYIHEqiMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:cd03263 81 PQFDALFDElTVREHLRfYARLKGLPKSEIKEEVELLLRV--LGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180
....*....|....*....|....*..
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSI 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
348-565 |
2.77e-33 |
|
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: 133.49 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKST----VINLLDKFYQPdSGKILLDGIDLEEYDTQFLRDN 422
Cdd:COG1123 6 EVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYiheQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNP 498
Cdd:COG1123 85 IGMVFQdpMTQLNPVTVGDQIAEAleNLGLSRAEARARVLELL---EAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 499 PIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
348-527 |
3.18e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.71 E-value: 3.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRDNIG 424
Cdd:COG2884 3 RFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNH-IFNGTIEENIRY-----GnvnatfeeiedaAKRAYIHEQIMDLPE--GYQSKALL----LSGGQQQRIAIAR 492
Cdd:COG2884 83 VVFQDFRlLPDRTVYENVALplrvtG------------KSRKEIRRRVREVLDlvGLSDKAKAlpheLSGGEQQRVAIAR 150
|
170 180 190
....*....|....*....|....*....|....*
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK 527
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINR 185
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
348-527 |
4.01e-33 |
|
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: 125.98 E-value: 4.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYD---TQFLRDNIG 424
Cdd:cd03292 2 EFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNH-IFNGTIEENIRYGnVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:cd03292 82 VVFQDFRlLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180
....*....|....*....|....
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIKK 527
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINK 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
356-576 |
5.57e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 126.81 E-value: 5.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 356 YPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKF--YQPD---SGKILLDGIDL--EEYDTQFLRDNIGLVLQ 428
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 429 KNHIFNGTIEENIRYG-------NVNATFEEIEDAAKRAYIHEQIMDLpegYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK14239 94 QPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKDR---LHDSALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVYkMNGTYKEIFD 576
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMF-MNPKHKETED 245
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
347-564 |
1.05e-32 |
|
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: 126.31 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:COG1120 2 LEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHI-FNGTIEENIRYG---------NVNAT-FEEIEDAAKRayiheqiMDLpEGYQSKALL-LSGGQQQRIAIARMF 494
Cdd:COG1120 81 PQEPPApFGLTVRELVALGryphlglfgRPSAEdREAVEEALER-------TGL-EHLADRPVDeLSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 495 LKNPPIIFLDEPTASLDaiateqIKNSLD--------AIKKDRTViiishs-isqiidADYTYVMKQGEVVEHGIHEDV 564
Cdd:COG1120 153 AQEPPLLLLDEPTSHLD------LAHQLEvlellrrlARERGRTVvmvlhdlnlaaryADRLVLLKDGRIVAQGPPEEV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
348-522 |
2.78e-32 |
|
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: 124.12 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydtqfLRDNIG 424
Cdd:cd03293 2 EVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFN-GTIEENIRYG--NVNATFEEIEDAAKR------------AYIHEqimdlpegyqskallLSGGQQQRIA 489
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVALGleLQGVPKAEARERAEEllelvglsgfenAYPHQ---------------LSGGMRQRVA 141
|
170 180 190
....*....|....*....|....*....|...
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAIATEQIKNSL 522
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEEL 174
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
348-528 |
4.79e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 125.97 E-value: 4.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTV---INLLdkfYQPDSGKILLDGIDLEEYDTQFLRDNIG 424
Cdd:COG1125 3 EFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTlrmINRL---IEPTSGRILIDGEDIRDLDPVELRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIF-NGTIEENIrygnvnATFEEI-----EDAAKRAyihEQIMDL----PEGY------QskallLSGGQQQRI 488
Cdd:COG1125 80 YVIQQIGLFpHMTVAENI------ATVPRLlgwdkERIRARV---DELLELvgldPEEYrdryphE-----LSGGQQQRV 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD 528
Cdd:COG1125 146 GVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRE 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
348-559 |
5.99e-32 |
|
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: 121.77 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNgtieenirygnvnatfeeIEDAAKRAYIHeqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:cd03214 80 QALELLG------------------LAHLADRPFNE----------------LSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 508 ASLDaiateqIKNSLD--------AIKKDRTViiishsISQIID-------ADYTYVMKQGEVVEHG 559
Cdd:cd03214 126 SHLD------IAHQIEllellrrlARERGKTV------VMVLHDlnlaaryADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
348-513 |
6.35e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.05 E-value: 6.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYP---NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydtqfLRDNIG 424
Cdd:COG1116 9 ELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFN-GTIEENIRYG--NVNATFEEIEDAAKR------------AYIHEqimdlpegyqskallLSGGQQQRIA 489
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALGleLRGVPKAERRERAREllelvglagfedAYPHQ---------------LSGGMRQRVA 148
|
170 180
....*....|....*....|....
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAI 513
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDAL 172
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
348-518 |
7.83e-32 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 122.36 E-value: 7.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEY---DTQFLRDNIG 424
Cdd:TIGR02673 3 EFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLrgrQLPLLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIF-NGTIEENIrygnvnaTFEEIEDAAKRAYIHEQI------MDLPEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:TIGR02673 83 VVFQDFRLLpDRTVYENV-------ALPLEVRGKKEREIQRRVgaalrqVGLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180
....*....|....*....|.
gi 2534190046 498 PPIIFLDEPTASLDAIATEQI 518
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERI 176
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
347-595 |
2.54e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.79 E-value: 2.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGL 425
Cdd:PRK13632 8 IKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQK--NHIFNGTIEENIRYG--NVNATFEE----IEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKN 497
Cdd:PRK13632 88 IFQNpdNQFIGATVEDDIAFGleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-------LSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKmngtYKEIF 575
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILN----NKEIL 236
|
250 260
....*....|....*....|....*...
gi 2534190046 576 DAMA--------KSLNIEKIAKTFDDEE 595
Cdd:PRK13632 237 EKAKidspfiykLSKKLKGIDPTYNEEE 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
347-526 |
4.01e-31 |
|
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: 120.33 E-value: 4.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTV---INLLDKfyqPDSGKILLDGIDLEEYDTQF--LRD 421
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLTDDKKNIneLRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:cd03262 77 KVGMVFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180
....*....|....*....|....*.
gi 2534190046 501 IFLDEPTASLDAiatEQIKNSLDAIK 526
Cdd:cd03262 157 MLFDEPTSALDP---ELVGEVLDVMK 179
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
348-564 |
8.27e-31 |
|
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: 120.30 E-value: 8.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRDNIG 424
Cdd:cd03261 2 ELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNG-TIEENIRYG---NVNATFEEIEDAAkrayihEQIMD---LPEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:cd03261 81 MLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIV------LEKLEavgLRGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKN---SLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDlirSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
348-575 |
9.56e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 9.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeEYDTQFL---RDNIG 424
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQK--NHIFNGTIEENIRYGNVNATF--EEIEDAAKRAyIHEQIMdlpEGYQSKA-LLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK13639 82 IVFQNpdDQLFAPTVEEDVAFGPLNLGLskEEVEKRVKEA-LKAVGM---EGFENKPpHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSL-DAIKKDRTVIIISHSISQI-IDADYTYVMKQGEVVehgihedvykMNGTYKEIF 575
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKII----------KEGTPKEVF 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-559 |
1.08e-30 |
|
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: 120.29 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK---ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIG 424
Cdd:COG1124 3 EVRNLSVSYGQGGRrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQK-------NHIFNGTIEENIRYGNVNATFEEIEDAAKRayiheqiMDLPEGY------QskallLSGGQQQRIAIA 491
Cdd:COG1124 83 MVFQDpyaslhpRHTVDRILAEPLRIHGLPDREERIAELLEQ-------VGLPPSFldryphQ-----LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT------------VIIIshsisqiidADYTYVMKQGEVVEHG 559
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGltylfvshdlavVAHL---------CDRVAVMQNGRIVEEL 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
348-531 |
1.82e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.42 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydtqfLRDNIGLVL 427
Cdd:COG1121 8 ELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI---FNGTIEENI---RYGNVNATF-------EEIEDAAKR----AYIHEQIMDLpegyqskalllSGGQQQRIAI 490
Cdd:COG1121 82 QRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERvgleDLADRPIGEL-----------SGGQQQRVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK-DRTV 531
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTI 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
348-564 |
4.27e-30 |
|
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: 117.92 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLV 426
Cdd:cd03224 2 EVENLNAGYG-KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIRYGNVNATFEEIEDAAKRAYihEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:cd03224 81 PEGRRIFPElTVEENLLLGAYARRRAKRKARLERVY--ELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 506 PTASLDAIATEQIKNSLDAIKKDRT--------VIIISHSisqiidADYTYVMKQGEVVEHGIHEDV 564
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVtillveqnARFALEI------ADRAYVLERGRVVLEGTAAEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
348-574 |
4.63e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 4.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSY----PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL--EEYDTQFLRD 421
Cdd:PRK13637 4 KIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYiheQIMDLP-EGYQSKALL-LSGGQQQRIAIARMFL 495
Cdd:PRK13637 84 KVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAM---NIVGLDyEDYKDKSPFeLSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 496 KNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR---TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYK 572
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmtIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLE 240
|
..
gi 2534190046 573 EI 574
Cdd:PRK13637 241 SI 242
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
348-559 |
9.07e-30 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 117.40 E-value: 9.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTV---INLLDKfyqPDSGKILLDGIDLEEYDTQF--LRDN 422
Cdd:COG1126 3 EIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLTDSKKDInkLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIF-NGTIEENIRYGNV---NATFEEIEDAAKR------------AYIHEqimdlpegyqskallLSGGQQQ 486
Cdd:COG1126 79 VGMVFQQFNLFpHLTVLENVTLAPIkvkKMSKAEAEERAMEllervgladkadAYPAQ---------------LSGGQQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 487 RIAIAR---MflkNPPIIFLDEPTASLDAiatEQIKNSLDAIK---KD--------------RTViiishsisqiidADY 546
Cdd:COG1126 144 RVAIARalaM---EPKVMLFDEPTSALDP---ELVGEVLDVMRdlaKEgmtmvvvthemgfaREV------------ADR 205
|
250
....*....|...
gi 2534190046 547 TYVMKQGEVVEHG 559
Cdd:COG1126 206 VVFMDGGRIVEEG 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
348-559 |
1.23e-29 |
|
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: 117.00 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRDNIG 424
Cdd:COG1127 7 EVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDitgLSEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNG-TIEENI-----RYGNVNAtfEEIEDAAkRAYIHEqiMDLPEgyqSKALL---LSGGQQQRIAIARMFL 495
Cdd:COG1127 86 MLFQGGALFDSlTVFENVafplrEHTDLSE--AEIRELV-LEKLEL--VGLPG---AADKMpseLSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 496 KNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---------------RTViiishsisqiidADYTYVMKQGEVVEHG 559
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDElgltsvvvthdldsaFAI------------ADRVAVLADGKIIAEG 224
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
346-565 |
1.47e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.32 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQ--PD---SGKILLDGIDLEEYDTQFLR 420
Cdd:PRK14247 3 KIEIRDLKVSFGQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQ-KNHIFNGTIEENIRYG--------NVNATFEEIEDAAKRAYIHEQI---MDLPEGYqskallLSGGQQQRI 488
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKAQLWDEVkdrLDAPAGK------LSGGQQQRL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT-VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTiVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
348-565 |
2.06e-29 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 119.43 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydtqfL---RDNIG 424
Cdd:COG3842 7 ELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-----LppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIF-NGTIEENIRYG----NVNAtfEEIEDAAKRA------------YIHEqimdlpegyqskallLSGGQQQR 487
Cdd:COG3842 81 MVFQDYALFpHLTVAENVAFGlrmrGVPK--AEIRARVAELlelvglegladrYPHQ---------------LSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 488 IAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK--------------------DRTViiishsisqiidadyt 547
Cdd:COG3842 144 VALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRelgitfiyvthdqeealalaDRIA---------------- 207
|
250
....*....|....*...
gi 2534190046 548 yVMKQGEVVEHGIHEDVY 565
Cdd:COG3842 208 -VMNDGRIEQVGTPEEIY 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
348-511 |
2.66e-29 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 116.01 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgykALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeydtqfLRDNIG--- 424
Cdd:COG3840 3 RLDDLTYRYGD---FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-------TALPPAerp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 --LVLQKNHIFNG-TIEENIRYG-----NVNAT-FEEIEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFL 495
Cdd:COG3840 73 vsMLFQENNLFPHlTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLPGQ-------LSGGQRQRVALARCLV 145
|
170
....*....|....*.
gi 2534190046 496 KNPPIIFLDEPTASLD 511
Cdd:COG3840 146 RKRPILLLDEPFSALD 161
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
348-565 |
2.69e-29 |
|
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: 116.14 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK---ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRD 421
Cdd:cd03258 3 ELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQKNHIFNG-TIEENIRYGnvnatfEEIEDAAKrAYIHEQIMDLPE--GYQSKALL----LSGGQQQRIAIARMF 494
Cdd:cd03258 83 RIGMIFQHFNLLSSrTVFENVALP------LEIAGVPK-AEIEERVLELLElvGLEDKADAypaqLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
348-531 |
6.31e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 113.89 E-value: 6.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDtqfLRDNIGLVL 427
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 Q--KNHIFNGTIEENIRYGNvnatfeeiEDAAKRAYIHEQIMDLPEGYQSK---ALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:cd03226 78 QdvDYQLFTDSVREELLLGL--------KELDAGNEQAETVLKDLDLYALKerhPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180
....*....|....*....|....*....
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKA 178
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
349-527 |
1.01e-28 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 113.48 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQ----FLRDNIG 424
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskFRREKLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQK-NHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQiMDLpEGYQSKALL-LSGGQQQRIAIARMFLKNPPIIF 502
Cdd:TIGR03608 80 YLFQNfALIENETVEENLDLGLKYKKLSKKEKREKKKEALEK-VGL-NLKLKQKIYeLSGGEQQRVALARAILKPPPLIL 157
|
170 180
....*....|....*....|....*
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKK 527
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELND 182
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
348-559 |
1.08e-28 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 113.44 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIqPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLVL 427
Cdd:cd03264 2 QLENLTKRYGKK-RALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYgnvNATFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:cd03264 79 QEFGVYpNFTVREFLDY---IAWLKGIPSKEVKARVDEVLelVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKDRTViiiSHSISQIIDADYTY----VMKQGEVVEHG 559
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDRIV---ILSTHIVEDVESLCnqvaVLNKGKLVFEG 211
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
356-526 |
3.71e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 111.36 E-value: 3.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 356 YPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeYDTQFL---RDNIGLVLQ--KN 430
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLD-YSRKGLlerRQRVGLVFQdpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 431 HIFNGTIEENIRYGNVNATFEEIEdaaKRAYIHE--QIMDLpEGYQSKAL-LLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAE---VERRVREalTAVGA-SGLRERPThCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170
....*....|....*....
gi 2534190046 508 ASLDAIATEQIKNSLDAIK 526
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLR 174
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
348-559 |
4.63e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.18 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKST---VINLLDKfyqPDSGKILLDGIDLEEYDTQFLRD 421
Cdd:COG1135 3 ELENLSKTFPTKggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 ---NIGLVLQknHiFN----GTIEENIRY-----GnvnatfeeiedaAKRAYIHEQIMDLPE--GYQSKALL----LSGG 483
Cdd:COG1135 80 arrKIGMIFQ--H-FNllssRTVAENVALpleiaG------------VPKAEIRKRVAELLElvGLSDKADAypsqLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 484 QQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---------------RTViiishsisqiidADYTY 548
Cdd:COG1135 145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRElgltivlithemdvvRRI------------CDRVA 212
|
250
....*....|.
gi 2534190046 549 VMKQGEVVEHG 559
Cdd:COG1135 213 VLENGRIVEQG 223
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
363-566 |
4.65e-28 |
|
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: 112.43 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVLQKNHIF-NGTIEENI 441
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 442 RYGNVNATFEEIEdaakrayIHEQIMDLPEGYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIAT 515
Cdd:cd03299 93 AYGLKKRKVDKKE-------IERKVLEIAEMLGIDHLLnrkpetLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 516 EQIKNSLDAIKKDRTVIIISH---SISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVthdFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
345-559 |
5.60e-28 |
|
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: 111.35 E-value: 5.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNI 423
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRygnvnaTFEEIEDaakrayihEQIMD---LPEGyqskALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLD------PFDEYSD--------EEIYGalrVSEG----GLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
348-512 |
2.63e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.24 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDtqflRdNIG 424
Cdd:COG3839 5 ELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvtdLPPKD----R-NIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQkN-----HIfngTIEENIRYG----NVNAtfEEIEDAAKRAyihEQIMDLpEGY-QSKALLLSGGQQQRIAIARMF 494
Cdd:COG3839 79 MVFQ-SyalypHM---TVYENIAFPlklrKVPK--AEIDRRVREA---AELLGL-EDLlDRKPKQLSGGQRQRVALGRAL 148
|
170
....*....|....*...
gi 2534190046 495 LKNPPIIFLDEPTASLDA 512
Cdd:COG3839 149 VREPKVFLLDEPLSNLDA 166
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
348-531 |
2.84e-27 |
|
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: 109.55 E-value: 2.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydtqfLRDNIGLVL 427
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI---FNGTIEENI---RYGNVN-------ATFEEIEDAAKR----AYIHEQIMdlpegyqskalLLSGGQQQRIAI 490
Cdd:cd03235 75 QRRSIdrdFPISVRDVVlmgLYGHKGlfrrlskADKAKVDEALERvglsELADRQIG-----------ELSGGQQQRVLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD-RTV 531
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTI 185
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
347-512 |
3.18e-27 |
|
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: 109.11 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpnGYKAL-KNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFlRDNIGL 425
Cdd:COG4133 3 LEAENLSCRR--GERLLfSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNG-TIEENIRY----GNVNATFEEIEDAAKRAYIhEQIMDLPEGYqskallLSGGQQQRIAIARMFLKNPPI 500
Cdd:COG4133 80 LGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGL-AGLADLPVRQ------LSAGQKRRVALARLLLSPAPL 152
|
170
....*....|..
gi 2534190046 501 IFLDEPTASLDA 512
Cdd:COG4133 153 WLLDEPFTALDA 164
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
348-565 |
4.63e-27 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 109.74 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVL 427
Cdd:cd03296 4 EVRNVSKRFGD-FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYG-NVNATFEEIEDAAKRAYIHE-----QIMDLPEGYQSKallLSGGQQQRIAIARMFLKNPPI 500
Cdd:cd03296 81 QHYALFrHMTVFDNVAFGlRVKPRSERPPEAEIRAKVHEllklvQLDWLADRYPAQ---LSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
348-564 |
5.53e-27 |
|
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: 109.45 E-value: 5.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeydTQFLRDNI---G 424
Cdd:cd03219 2 EVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI----TGLPPHEIarlG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LV--LQKNHIFNG-TIEENIRYGNVNATFEEI-------EDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIAR 492
Cdd:cd03219 77 IGrtFQIPRLFPElTVLENVMVAAQARTGSGLllararrEEREARERAEELLerVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIK-KDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDV 564
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELReRGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
348-565 |
5.97e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.71 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--IDLEEYDTQFLRDNIGL 425
Cdd:PRK13636 7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQK--NHIFNGTIEENIRYGNVNATFEE------IEDAAKRAYIhEQIMDLPEGYqskallLSGGQQQRIAIARMFLKN 497
Cdd:PRK13636 87 VFQDpdNQLFSASVYQDVSFGAVNLKLPEdevrkrVDNALKRTGI-EHLKDKPTHC------LSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDA---DYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlycDNVFVMKEGRVILQGNPKEVF 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
348-559 |
1.13e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.83 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK13647 6 EVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 Q--KNHIFNGTIEENIRYGNVNA--TFEEIEDAAKRAYiheQIMDLpEGYQSKA-LLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK13647 86 QdpDDQVFSSTVWDDVAFGPVNMglDKDEVERRVEEAL---KAVRM-WDFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKKD-RTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEG 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
348-512 |
2.01e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.62 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeyDTQF-LRD-NIGL 425
Cdd:COG1118 4 EVRNISKRFGS-FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL---FTNLpPRErRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIF-NGTIEENIRYG-NVNATFEeiedAAKRAYIHEQI--MDLpEGY------QskallLSGGQQQRIAIARMFL 495
Cdd:COG1118 80 VFQHYALFpHMTVAENIAFGlRVRPPSK----AEIRARVEELLelVQL-EGLadrypsQ-----LSGGQRQRVALARALA 149
|
170
....*....|....*..
gi 2534190046 496 KNPPIIFLDEPTASLDA 512
Cdd:COG1118 150 VEPEVLLLDEPFGALDA 166
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
348-574 |
4.86e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 4.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:PRK13635 7 RVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQK--NHIFNGTIEENIRYGNVN------ATFEEIEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKNP 498
Cdd:PRK13635 87 FQNpdNQFVGATVQDDVAFGLENigvpreEMVERVDQALRQVGMEDFLNREPHR-------LSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 499 PIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEI 574
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHMLQEI 237
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
348-567 |
6.74e-26 |
|
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: 106.17 E-value: 6.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVL 427
Cdd:cd03300 2 ELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYGnvnATFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:cd03300 79 QNYALFpHLTVFENIAFG---LRLKKLPKAEIKERVAEALdlVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKM 567
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
346-531 |
1.20e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 106.40 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVI-------NLLDKFYQpdSGKILLDGIDL--EEYDT 416
Cdd:PRK14243 10 VLRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFRV--EGKVTFHGKNLyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 417 QFLRDNIGLVLQKNHIFNGTIEENIRYG-NVNA----TFEEIEDAAKRAYIHEQIMDlpeGYQSKALLLSGGQQQRIAIA 491
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGaRINGykgdMDELVERSLRQAALWDEVKD---KLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
348-566 |
1.33e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSY----PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE----EYDTQFL 419
Cdd:PRK13634 4 TFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKALL-LSGGQQQRIAIARMFLK 496
Cdd:PRK13634 84 RKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 497 NPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR---TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKgltTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFA 235
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
348-518 |
3.35e-25 |
|
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: 104.44 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKA---LKNINMTIQPNKITALVGLSGAGKSTVINL---LDkfyQPDSGKILLDGIDLEEYD----TQ 417
Cdd:COG4181 10 ELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLlagLD---RPTSGTVRLAGQDLFALDedarAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 FLRDNIGLVLQKNH-IFNGTIEENIRygnVNATFEEIEDAAKRAyiheqimdlpegyqsKALL---------------LS 481
Cdd:COG4181 87 LRARHVGFVFQSFQlLPTLTALENVM---LPLELAGRRDARARA---------------RALLervglghrldhypaqLS 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534190046 482 GGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:COG4181 149 GGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
348-559 |
5.61e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 103.52 E-value: 5.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLV 426
Cdd:COG0410 5 EVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIRYGNVNATfeeieDAAKRAYIHEQIMDL-P---EGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:COG0410 84 PEGRRIFPSlTVEENLLLGAYARR-----DRAEVRADLERVYELfPrlkERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDRT--------------ViiishsisqiidADYTYVMKQGEVVEHG 559
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVtillveqnarfaleI------------ADRAYVLERGRIVLEG 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
348-575 |
9.39e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.40 E-value: 9.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-----ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID-LEEYDTQFLRD 421
Cdd:PRK13633 6 KCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtSDEENLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQK--NHIFNGTIEENIRYG--NVNATFEEI----EDAAKRAYIHEQIMDLPEgyqskalLLSGGQQQRIAIARM 493
Cdd:PRK13633 86 KAGMVFQNpdNQIVATIVEEDVAFGpeNLGIPPEEIrervDESLKKVGMYEYRRHAPH-------LLSGGQKQRVAIAGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 494 FLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEVVehgihedvykMNGTY 571
Cdd:PRK13633 159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVV----------MEGTP 228
|
....
gi 2534190046 572 KEIF 575
Cdd:PRK13633 229 KEIF 232
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
31-302 |
9.98e-25 |
|
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: 103.88 E-value: 9.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 31 GSFTSQVNALILQYTVDSINGlveAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKI 110
Cdd:pfam00664 11 SGAISPAFPLVLGRILDVLLP---DGDPETQALNVYSLALLLLG---LAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 111 LTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQA 190
Cdd:pfam00664 85 LRQPMSFF--DTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 191 KKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVII 270
Cdd:pfam00664 163 KILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALA 242
|
250 260 270
....*....|....*....|....*....|..
gi 2534190046 271 IILTSYLVLDGQMTIGASMFHILLFNNVSAPI 302
Cdd:pfam00664 243 LWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
348-518 |
1.01e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKST---VINLLDkfyQPDSGKILLDG------IDLEEYDTQF 418
Cdd:COG4161 4 QLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLE---TPDSGQLNIAGhqfdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 LRDNIGLVLQKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:COG4161 80 LRQKVGMVFQQYNLWpHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180
....*....|....*....|.
gi 2534190046 498 PPIIFLDEPTASLDAIATEQI 518
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQV 180
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
347-517 |
1.30e-24 |
|
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: 100.20 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeydtqflrdniglv 426
Cdd:cd03216 1 LELRGITKRFGGV-KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 lqknhiFNGTIEenirygnvnatfeeiedaAKRAYIhEQImdlpegYQskallLSGGQQQRIAIARMFLKNPPIIFLDEP 506
Cdd:cd03216 66 ------FASPRD------------------ARRAGI-AMV------YQ-----LSVGERQMVEIARALARNARLLILDEP 109
|
170
....*....|.
gi 2534190046 507 TASLDAIATEQ 517
Cdd:cd03216 110 TAALTPAEVER 120
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
348-565 |
1.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 103.73 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK13652 5 ETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QK--NHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:PRK13652 85 QNpdDQIFSPTVEQDIAFGPINLGLDE-ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 506 PTASLDAIATEQIKNSLDAIKKD--RTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIF 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
368-513 |
2.25e-24 |
|
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: 101.42 E-value: 2.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 368 MTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVLQKNHIF-NGTIEENIRYG-- 444
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLGls 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 445 -NVNATFEE---IEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:cd03298 97 pGLKLTAEDrqaIEVALARVGLAGLEKRLPGE-------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
347-517 |
3.01e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.26 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidlEEYD----TQFLRDN 422
Cdd:COG1129 5 LEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG---EPVRfrspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNG-TIEENI-------RYGNVN--ATFEEIEDAAKRayiheqiMDLPEGYQSKALLLSGGQQQRIAIAR 492
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIflgreprRGGLIDwrAMRRRARELLAR-------LGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180
....*....|....*....|....*
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQ 517
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVER 178
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
348-565 |
4.51e-24 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 103.96 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQfLRDnIGLVL 427
Cdd:TIGR03265 6 SIDNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-KRD-YGIVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQImDLP---EGYQSKallLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:TIGR03265 83 QSYALFpNLTVADNIAYGLKNRGMGRAEVAERVAELLDLV-GLPgseRKYPGQ---LSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:TIGR03265 159 DEPLSALDARVREHLRTEIRQLQRRlgvTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIY 223
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
349-565 |
4.81e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.99 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLVL 427
Cdd:PRK13644 4 LENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 Q--KNHIFNGTIEENIRYGNVNATFE--EIEDAAKRAYIHEQImdlpEGYQSKA-LLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK13644 84 QnpETQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGL----EKYRHRSpKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAI-KKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
378-565 |
4.96e-24 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 103.34 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 378 LVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLVLQKNHIF-NGTIEENIRYGnvnatfeEIEDA 456
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFG-------LKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 457 AKRAYIHEQIMD------LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD-- 528
Cdd:TIGR01187 72 VPRAEIKPRVLEalrlvqLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlg 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534190046 529 -RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:TIGR01187 152 iTFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIY 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
361-529 |
1.22e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 99.36 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLVLQKNHIFNG-TIEE 439
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRYgnvnatFEEIEdAAKRAYIHEQIMDLPEGYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:cd03266 98 NLEY------FAGLY-GLKGDELTARLEELADRLGMEELLdrrvggFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170
....*....|....*.
gi 2534190046 514 ATEQIknsLDAIKKDR 529
Cdd:cd03266 171 ATRAL---REFIRQLR 183
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
348-511 |
1.48e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYdTQFLRDnIGLVL 427
Cdd:PRK11607 21 EIRNLTKSF-DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-PPYQRP-INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYGNVNATFEEIEDAAKrayIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:PRK11607 98 QSYALFpHMTVEQNIAFGLKQDKLPKAEIASR---VNEmlGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
....*..
gi 2534190046 505 EPTASLD 511
Cdd:PRK11607 175 EPMGALD 181
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
348-566 |
1.79e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 100.59 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGY----KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL----EEYDTQFL 419
Cdd:PRK13649 4 NLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKALL-LSGGQQQRIAIARMFLK 496
Cdd:PRK13649 84 RKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILAM 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 497 NPPIIFLDEPTASLDAIATEQIKNSLDAIKKD--RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgmTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
348-527 |
1.96e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.80 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK---ALKNINMTIQPNKITALVGLSGAGKST---VINLLDKfyqPDSGKILLDGIDLEEYDTQFL-- 419
Cdd:PRK11153 3 ELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 -RDNIGLVLQknHiFN----GTIEENIrygnvnATFEEIeDAAKRAYIHEQIMDLPE--GYQSKALL----LSGGQQQRI 488
Cdd:PRK11153 80 aRRQIGMIFQ--H-FNllssRTVFDNV------ALPLEL-AGTPKAEIKARVTELLElvGLSDKADRypaqLSGGQKQRV 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIknsLDAIKK 527
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSI---LELLKD 185
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
348-574 |
3.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 3.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS---GKILLDGIDLEEYDTQFLRDNI 423
Cdd:PRK13640 7 EFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQK--NHIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQImDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK13640 87 GIVFQNpdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADV-GMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEI 574
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEMLKEI 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
349-559 |
4.08e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.70 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSY----PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEE-----YDTQFL 419
Cdd:PRK13645 9 LDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQ--KNHIFNGTIEENIRYGNVNATfEEIEDAAKRAYIHEQIMDLPEGYQSKA-LLLSGGQQQRIAIARMFLK 496
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDYVKRSpFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 497 NPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykkRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
348-559 |
4.32e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.55 E-value: 4.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--IDLE----EYDTQFLRD 421
Cdd:PRK11124 4 QLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSktpsDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:PRK11124 83 NVGMVFQQYNLWpHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 501 IFLDEPTASLDAIATEQIknsLDAIKKDR-----TVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:PRK11124 163 LLFDEPTAALDPEITAQI---VSIIRELAetgitQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
346-526 |
9.54e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 103.57 E-value: 9.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILL-DGIDLEEYDTQFLRDN 422
Cdd:PTZ00265 382 KIQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNGTIEENIRYG----------------NVNATFE----------------------------------- 451
Cdd:PTZ00265 462 IGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliemrkny 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 452 ------EIEDAAKRAYIHEQIMDLPEGYQ----SKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNS 521
Cdd:PTZ00265 542 qtikdsEVVDVSKKVLIHDFVSALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
|
....*
gi 2534190046 522 LDAIK 526
Cdd:PTZ00265 622 INNLK 626
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
348-522 |
1.11e-22 |
|
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: 96.55 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYkALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGI---DLEEYDTqflrdNIG 424
Cdd:cd03301 2 ELENVTKRFGNVT-ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKDR-----DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIF-NGTIEENIRYGNVNATF--EEIEDAAKRAyihEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGLKLRKVpkDEIDERVREV---AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180
....*....|....*....|.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSL 522
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAEL 173
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
363-559 |
1.42e-22 |
|
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: 95.70 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLD--KFYQPDSGKILLDGIDLEEydtQFLRDNIGLVLQKNHIF-NGTIEE 439
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHpTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRYgnvnatfeeiedAAK-RAyiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:cd03213 102 TLMF------------AAKlRG-------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2534190046 519 KNSLDAIKKD-RTVIIIS--HSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03213 151 MSLLRRLADTgRTIICSIhqPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
348-576 |
1.62e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:COG4604 3 EIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI-FNGTIEENI---RY----GNVNAtfeeiEDaakRAYIHEQI--MDLpEGYQSKAL-LLSGGQQQRIAIARMFLK 496
Cdd:COG4604 82 QENHInSRLTVRELVafgRFpyskGRLTA-----ED---REIIDEAIayLDL-EDLADRYLdELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 497 NPPIIFLDEPTASLDaiateqIKNSLD--------AIKKDRTViiishsISQIID-------ADYTYVMKQGEVVEHGIH 561
Cdd:COG4604 153 DTDYVLLDEPLNNLD------MKHSVQmmkllrrlADELGKTV------VIVLHDinfascyADHIVAMKDGRVVAQGTP 220
|
250
....*....|....*.
gi 2534190046 562 EDVykMNG-TYKEIFD 576
Cdd:COG4604 221 EEI--ITPeVLSDIYD 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
359-529 |
1.67e-22 |
|
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: 97.03 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 359 GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTqFLRDNIGLV--LQKNHIFNG- 435
Cdd:COG0411 16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIArtFQNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENI--------RYGNVNATFEEIEDAAKRAYIHEQIMDLPE--GYQSK----ALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:COG0411 95 TVLENVlvaaharlGRGLLAALLRLPRARREEREARERAEELLErvGLADRadepAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180
....*....|....*....|....*...
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDR 529
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRDER 202
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
348-518 |
1.69e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYK---ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRdniG 424
Cdd:COG4525 5 TVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNG-TIEENIRYGnvnATFEEIEDAAKRAYIHE--QIMDLpEGYQSKALL-LSGGQQQRIAIARMFLKNPPI 500
Cdd:COG4525 80 VVFQKDALLPWlNVLDNVAFG---LRLRGVPKAERRARAEEllALVGL-ADFARRRIWqLSGGMRQRVGIARALAADPRF 155
|
170
....*....|....*...
gi 2534190046 501 IFLDEPTASLDAIATEQI 518
Cdd:COG4525 156 LLMDEPFGALDALTREQM 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
346-566 |
1.92e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEF--SYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL----EEYDTQFL 419
Cdd:PRK13643 3 KFEKVNYTYqpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKA-LLLSGGQQQRIAIARMFLK 496
Cdd:PRK13643 83 RKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEFWEKSpFELSGGQMRRVAIAGILAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 497 NPPIIFLDEPTASLDAIATEQIKNSLDAIKKD-RTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
347-565 |
2.30e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 96.07 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGL 425
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNG-TIEENIRygnvnATFEEIEDAakRAYIHEQIMDLPEGYQ------SKALLLSGGQQQRIAIARMFLKNP 498
Cdd:cd03218 80 LPQEASIFRKlTVEENIL-----AVLEIRGLS--KKEREEKLEELLEEFHithlrkSKASSLSGGERRRVEIARALATNP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 499 PIIFLDEPTASLDAIATEQIKNsLDAIKKDR-------------TVIIishsisqiidADYTYVMKQGEVVEHGIHEDVY 565
Cdd:cd03218 153 KFLLLDEPFAGVDPIAVQDIQK-IIKILKDRgigvlitdhnvreTLSI----------TDRAYIIYEGKVLAEGTPEEIA 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
361-528 |
2.65e-22 |
|
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: 95.44 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQ---PNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeYDTQ---FL---RDNIGLVLQKNH 431
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRkkiNLppqQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IF-NGTIEENIRYGnvnatFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTA 508
Cdd:cd03297 86 LFpHLNVRENLAFG-----LKRKRNREDRISVDELLdlLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180
....*....|....*....|
gi 2534190046 509 SLDAIATEQIKNSLDAIKKD 528
Cdd:cd03297 161 ALDRALRLQLLPELKQIKKN 180
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
346-566 |
3.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYPNG----YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL----EEYDTQ 417
Cdd:PRK13646 2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 FLRDNIGLVLQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAkrayiHEQIMDLpeGY-----QSKALLLSGGQQQRI 488
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HRLLMDL--GFsrdvmSQSPFQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 489 AIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT---VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENktiILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
.
gi 2534190046 566 K 566
Cdd:PRK13646 235 K 235
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
37-308 |
3.56e-22 |
|
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: 97.12 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 37 VNALILQYTVDSInglveAGKGLKEGLKIISFIsIVLMTkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMA 116
Cdd:cd18542 17 LIPLLIRRIIDSV-----IGGGLRELLWLLALL-ILGVA--LLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLsgr 196
Cdd:cd18542 89 FHDK--ARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 197 RRNLRGYREQksqgiISIINS--------ITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVV 268
Cdd:cd18542 164 RPAFEEIREQ-----EGELNTvlqenltgVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIV 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2534190046 269 IIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRI 308
Cdd:cd18542 239 LVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRL 278
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
347-525 |
4.04e-22 |
|
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: 95.92 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSG---KIL---LDGIDLEEydtqfLR 420
Cdd:COG1119 4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWE-----LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLV---LQKNHIFNGTIEENI---RYGNVnATFEEIEDA-AKRAyihEQIMDL--PEGYQSKALL-LSGGQQQRIAI 490
Cdd:COG1119 78 KRIGLVspaLQLRFPRDETVLDVVlsgFFDSI-GLYREPTDEqRERA---RELLELlgLAHLADRPFGtLSQGEQRRVLI 153
|
170 180 190
....*....|....*....|....*....|....*
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAI 525
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKL 188
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
367-511 |
4.18e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 95.42 E-value: 4.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 367 NMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDleEYDTQFLRDNIGLVLQKNHIFNG-TIEENIRYG- 444
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 445 ----NVNAT-FEEIEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10771 97 npglKLNAAqREKLHAIARQMGIEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
347-554 |
4.32e-22 |
|
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: 94.46 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGY----KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdN 422
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNGTIEENIRYGnvnATFEE------IEDAAKRAYIheQIMdlPEGYQS----KALLLSGGQQQRIAIAR 492
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG---KPFDEeryekvIKACALEPDL--EIL--PDGDLTeigeKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNS--LDAIKKDRTVIIISHSISQIIDADYTYVMKQGE 554
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
346-518 |
5.57e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 94.56 E-value: 5.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEiqNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYDTQFLRDN 422
Cdd:PRK10908 3 RFE--HVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIF-NGTIEENIRYGNV--NATFEEIEDAAKRAYIHEQIMDLPEGYqskALLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK10908 81 IGMIFQDHHLLmDRTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNF---PIQLSGGEQQRVGIARAVVNKPA 157
|
170
....*....|....*....
gi 2534190046 500 IIFLDEPTASLDAIATEQI 518
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGI 176
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
362-564 |
5.66e-22 |
|
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: 95.79 E-value: 5.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL----RDNIGLVLQKNHIF-NGT 436
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 437 IEENIRYG----NVNAtfEEIEDAAKRAYiheQIMDLpEGY-QSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:cd03294 119 VLENVAFGlevqGVPR--AEREERAAEAL---ELVGL-EGWeHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 512 AIATEQIKNSLDAIKKDR---TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:cd03294 193 PLIRREMQDELLRLQAELqktIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
363-511 |
6.13e-22 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 95.16 E-value: 6.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE--EYDTQFLRDNIGLVLQKNHIF-NGTIEE 439
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFpHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRYGNVNATfeeiedAAKRAYIHEQIMDL---------PEGYQSKallLSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:PRK09493 97 NVMFGPLRVR------GASKEEAEKQARELlakvglaerAHHYPSE---LSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
.
gi 2534190046 511 D 511
Cdd:PRK09493 168 D 168
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
348-556 |
6.30e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL----R 420
Cdd:PRK10535 6 ELKDIRRSYPSGeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQKNHIFNG-TIEENIRygnVNATFEEIEDAAKRAYIHEQIMDLPEG----YQSKALllSGGQQQRIAIARMFL 495
Cdd:PRK10535 86 EHFGFIFQRYHLLSHlTAAQNVE---VPAVYAGLERKQRLLRAQELLQRLGLEdrveYQPSQL--SGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 496 KNPPIIFLDEPTASLDAIATEQIKNSLDAIK-KDRTVIIISHSISQIIDADYTYVMKQGEVV 556
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
83-570 |
6.59e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.82 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 83 ITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYtnQDNQAGKLQTR-------IDRGIESLTRLVQNFFIDILPLFA 155
Cdd:PLN03232 966 VTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFF--HTNPTGRVINRfskdigdIDRNVANLMNMFMNQLWQLLSTFA 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 156 N----------SIVALILMFNANFyvglvglcivpIYFIITQQQAKKL-SGRRRNLRGYREQKSQGIisiiNSITVIKSF 224
Cdd:PLN03232 1044 LigtvstislwAIMPLLILFYAAY-----------LYYQSTSREVRRLdSVTRSPIYAQFGEALNGL----SSIRAYKAY 1108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 225 NREDIEGKKQLDlqkeltNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVL-----DGQMTIGASMFHILLFNN-- 297
Cdd:PLN03232 1109 DRMAKINGKSMD------NNIRFTLANTSSNRWLTIRLETLGGVMIWLTATFAVLrngnaENQAGFASTMGLLLSYTLni 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 298 ---VSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYIPTKLKGKFEIQNVEFSY-PNGYKALKNINMTIQPN 373
Cdd:PLN03232 1183 ttlLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGSIKFEDVHLRYrPGLPPVLHGLSFFVSPS 1262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 374 KITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRygnvnaTFEEI 453
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNID------PFSEH 1336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 454 EDAA-----KRAYIHEQIMDLPEGYQSKALL----LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDA 524
Cdd:PLN03232 1337 NDADlwealERAHIKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE 1416
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2534190046 525 IKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGT 570
Cdd:PLN03232 1417 EFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTS 1462
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
348-566 |
7.58e-22 |
|
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: 96.66 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQN--VEFSYPNGY-KALKNINMTIQPNKITALVGLSGAGKST----VINLLDKFYQpDSGKILLDGIDLEEYDTQFLR 420
Cdd:COG0444 3 EVRNlkVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTlaraILGLLPPPGI-TSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 D----NIGLVLQ------------KNHIfngtiEENIRYGN----------VNATFEE--IEDAAKRA--YIHEqimdlp 470
Cdd:COG0444 82 KirgrEIQMIFQdpmtslnpvmtvGDQI-----AEPLRIHGglskaearerAIELLERvgLPDPERRLdrYPHE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 471 egyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR------------TVIIIshsi 538
Cdd:COG0444 151 ---------LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglailfithdlgVVAEI---- 217
|
250 260
....*....|....*....|....*...
gi 2534190046 539 sqiidADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:COG0444 218 -----ADRVAVMYAGRIVEEGPVEELFE 240
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
343-557 |
9.58e-22 |
|
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: 94.98 E-value: 9.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 343 LKGKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTV----INLLDKFyqpdSGKILLDGIDLEEYDTQ 417
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIF----DGKIVIDGIDISKLPLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 FLRDNIGLVLQKNHIFNGTIEENIRyGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQskALLLSGG------QQQRIAIA 491
Cdd:cd03288 92 TLRSRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLD--AVVTEGGenfsvgQRQLFCLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDaIATEQI--KNSLDAIKkDRTVIIISHSISQIIDADYTYVMKQGEVVE 557
Cdd:cd03288 169 RAFVRKSSILIMDEATASID-MATENIlqKVVMTAFA-DRTVVTIAHRVSTILDADLVLVLSRGILVE 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
363-531 |
1.16e-21 |
|
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: 94.07 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEY--DTQFLRDNIGLVLQKnhifngTIEEN 440
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpDRMVVFQNYSLLPWL------TVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 441 IrYGNVNATFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:TIGR01184 75 I-ALAVDRVLPDLSKSERRAIVEEHIalVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170
....*....|...
gi 2534190046 519 KNSLDAIKKDRTV 531
Cdd:TIGR01184 154 QEELMQIWEEHRV 166
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
348-566 |
1.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.82 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLV 426
Cdd:PRK13648 9 VFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQ--KNHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYihEQImDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK13648 89 FQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEAL--KQV-DMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIK--KDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
367-531 |
2.17e-21 |
|
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: 92.62 E-value: 2.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 367 NMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEydTQFLRDNIGLVLQKNHIFNG-TIEENIRYG- 444
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG--LAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 445 ----NVNATFEE-IEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQ-- 517
Cdd:TIGR01277 96 hpglKLNAEQQEkVVDAAQQVGIADYLDRLPEQ-------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEml 168
|
170
....*....|....*.
gi 2534190046 518 --IKNSLDaiKKDRTV 531
Cdd:TIGR01277 169 alVKQLCS--ERQRTL 182
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
346-566 |
2.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEiqNVEFSYPNGY----KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--IDLEEYDTQF- 418
Cdd:PRK13641 4 KFE--NVDYIYSPGTpmekKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhITPETGNKNLk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 -LRDNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKALL-LSGGQQQRIAIARMF 494
Cdd:PRK13641 82 kLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQI-KNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
358-559 |
3.03e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTV---INLLDkfyQPDSGKILLDGIdleEYDT-----------QFLRDNI 423
Cdd:PRK11264 14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLE---QPEAGTIRVGDI---TIDTarslsqqkgliRQLRQHV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK11264 88 GFVFQNFNLFpHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 503 LDEPTASLDAIATEQIKNSLDAIKKD-RTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQG 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
357-559 |
3.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.92 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 357 PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILL------DGIDLEEY----------DTQFLR 420
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigDKKNNHELitnpyskkikNFKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEIEdAAKRAYIHEQIMDLPEGYQSKALL-LSGGQQQRIAIARMFLKN 497
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 498 PPIIFLDEPTASLD-AIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:PRK13631 195 PEILIFDEPTAGLDpKGEHEMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
348-511 |
3.15e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK13548 4 EARNLSVRL-GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI-FNGTIEENIRYGNVNATFEEIEDAAkrayIHEQIMDLPE--GYQSKALL-LSGGQQQRIAIARMFL------KN 497
Cdd:PRK13548 83 QHSSLsFPFTVEEVVAMGRAPHGLSRAEDDA----LVAAALAQVDlaHLAGRDYPqLSGGEQQRVQLARVLAqlwepdGP 158
|
170
....*....|....
gi 2534190046 498 PPIIFLDEPTASLD 511
Cdd:PRK13548 159 PRWLLLDEPTSALD 172
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
324-565 |
3.45e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 324 AILKADDekessgnyiptkLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGK 403
Cdd:PRK11308 4 PLLQAID------------LKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 404 ILLDGIDLEEYDTQ---FLRDNIGLVLQKNhifngtieenirYGNVN------ATFEE---IE---DAAKRAYIHEQIMD 468
Cdd:PRK11308 72 LYYQGQDLLKADPEaqkLLRQKIQIVFQNP------------YGSLNprkkvgQILEEpllINtslSAAERREKALAMMA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 469 L----PEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKN-----------SLDAIKKDRTVII 533
Cdd:PRK11308 140 KvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNlmmdlqqelglSYVFISHDLSVVE 219
|
250 260 270
....*....|....*....|....*....|..
gi 2534190046 534 IShsisqiidADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK11308 220 HI--------ADEVMVMYLGRCVEKGTKEQIF 243
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
341-520 |
3.46e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.56 E-value: 3.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 341 TKLKGKFEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS-----GKILLDGIDLEEYD 415
Cdd:PRK14258 2 SKLIPAIKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 416 TQF--LRDNIGLVLQKNHIFNGTIEENIRYGNVNATFE---EIEDAAKRAYIHEQIMD-LPEGYQSKALLLSGGQQQRIA 489
Cdd:PRK14258 81 VNLnrLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRpklEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190
....*....|....*....|....*....|.
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAIATEQIKN 520
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVES 191
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
40-320 |
5.73e-21 |
|
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: 93.61 E-value: 5.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDsiNGLVEAGKGLkEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYT 119
Cdd:cd18544 20 LLIKRAID--DYIVPGQGDL-QGLLLLALLYLGLL---LLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 120 NqdNQAGKLQTRIDRGIESL----TRLVQNFFIDILPLfansIVALILMFNANFYVGLVGLCIVPIYFIITqqqakkLSG 195
Cdd:cd18544 94 R--TPVGRLVTRVTNDTEALnelfTSGLVTLIGDLLLL----IGILIAMFLLNWRLALISLLVLPLLLLAT------YLF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 196 RRRNLRGYREQKSQgiISIINS--------ITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGV 267
Cdd:cd18544 162 RKKSRKAYREVREK--LSRLNAflqesisgMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLAL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 268 VIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSE 320
Cdd:cd18544 240 ALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAE 292
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
358-559 |
6.58e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. 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. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 93.61 E-value: 6.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID-LEEYDTqfLRDNIGLVLQKNHIFNG- 435
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvVREPRK--VRRSIGIVPQYASVDEDl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIRygnVNATFEEIEDAAKRAYIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:TIGR01188 82 TGRENLE---MMGRLYGLPKDEAEERAEEllELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534190046 514 ATEQIKNSLDAIKKDRTVIIISHSISQIID--ADYTYVMKQGEVVEHG 559
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADklCDRIAIIDHGRIIAEG 206
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
348-564 |
8.23e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 91.43 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLV 426
Cdd:TIGR03410 2 EVSNLNVYY-GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPhERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIRYGnvnatFEEIEDAAKRayIHEQIMDL-P---EGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:TIGR03410 81 PQGREIFPRlTVEENLLTG-----LAALPRRSRK--IPDEIYELfPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDV 564
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
78-580 |
1.03e-20 |
|
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: 97.32 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANS 157
Cdd:TIGR00957 1016 ILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFF--ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNV 1093
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 158 IVALILMFNANFYVGLVGLCIVPIYFII------TQQQAKKL-SGRRRNLRGYREQKSQGIisiinsiTVIKSFNR-EDI 229
Cdd:TIGR00957 1094 IGALIVILLATPIAAVIIPPLGLLYFFVqrfyvaSSRQLKRLeSVSRSPVYSHFNETLLGV-------SVIRAFEEqERF 1166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 230 EGKKQLDL---QKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLvldGQMTIGASMFHILlfnNVSAPIRQLH 306
Cdd:TIGR00957 1167 IHQSDLKVdenQKAYYPSIVANRWLAVRLECVGNCIVLFAALFAVISRHSL---SAGLVGLSVSYSL---QVTFYLNWLV 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 307 RIYDEMNDAMIYSESffaiLK--ADDEKES----SGNYIPTKL--KGKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITA 377
Cdd:TIGR00957 1241 RMSSEMETNIVAVER----LKeySETEKEApwqiQETAPPSGWppRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVG 1316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 378 LVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENI----RYGNvnatfEEI 453
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSD-----EEV 1391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 454 EDAAKRAYIHEQIMDLPEGYQSKALL----LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR 529
Cdd:TIGR00957 1392 WWALELAHLKTFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDC 1471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 530 TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGtykeIFDAMAK 580
Cdd:TIGR00957 1472 TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRG----IFYSMAK 1518
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
348-555 |
1.89e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.72 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG--YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGL 425
Cdd:PRK13650 6 EVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQK--NHIFNGTIEENIRYG--NVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKallLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK13650 86 VFQNpdNQFVGATVEDDVAFGleNKGIPHEEMKERVNEALELVGMQDFKEREPAR---LSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEV 555
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
32-316 |
2.64e-20 |
|
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: 91.33 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 32 SFTSQVNALILQYTVDSINGlveagKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKIL 111
Cdd:cd18552 12 AATTAALAWLLKPLLDDIFV-----EKDLEALLLVPLAIIGLF---LLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 112 TYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAK 191
Cdd:cd18552 84 RLPLSFF--DRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 192 KLsgRRRNLRGyreQKSQGIIS-----IINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFG 266
Cdd:cd18552 162 RL--RKISRRS---QESMGDLTsvlqeTLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2534190046 267 VVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAM 316
Cdd:cd18552 237 IALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
361-556 |
2.87e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLVLQKNHIFNG-TIE 438
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRYGNVNATFEEIEDAAKRAYihEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:PRK11614 99 ENLAMGGFFAERDQFQERIKWVY--ELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534190046 519 KNSLDAIKKD-RTVIIISHSISQIID-ADYTYVMKQGEVV 556
Cdd:PRK11614 177 FDTIEQLREQgMTIFLVEQNANQALKlADRGYVLENGHVV 216
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
37-317 |
3.06e-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: 91.35 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 37 VNALILQYTVDSInglveAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMA 116
Cdd:cd18570 20 AGSFFFQILIDDI-----IPSGDINLLNIISIGLILLY---LFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYTNQdnQAGKLQTR---IDRGIESLTRLVQNFFIDILPLfansIVALILMFNANFYVGLVGLCIVPIYFIITqqqakkL 193
Cdd:cd18570 92 FFETR--KTGEIISRfndANKIREAISSTTISLFLDLLMV----IISGIILFFYNWKLFLITLLIIPLYILII------L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 194 SGRRRNLRGYREQKSQG------IISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGV 267
Cdd:cd18570 160 LFNKPFKKKNREVMESNaelnsyLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2534190046 268 VIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMI 317
Cdd:cd18570 240 LLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKV 289
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
365-512 |
3.18e-20 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 92.47 E-value: 3.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 365 NINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeYDTQ---FL---RDNIGLVLQKNHIFNG-TI 437
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSArgiFLpphRRRIGYVFQEARLFPHlSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 438 EENIRYGNVNAtfeeieDAAKRAYIHEQIMDLPE-GyqskALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:COG4148 95 RGNLLYGRKRA------PRAERRISFDEVVELLGiG----HLLdrrpatLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
..
gi 2534190046 511 DA 512
Cdd:COG4148 165 DL 166
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
347-527 |
4.05e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.32 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQflRDNIGLV 426
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIF-NGTIEENIRYG----NVNAtfEEIEDAAKRAYiheQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK09452 92 FQSYALFpHMTVFENVAFGlrmqKTPA--AEITPRVMEAL---RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180
....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKK 527
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQR 192
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
349-530 |
4.28e-20 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 89.01 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPNGY---KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYD----TQFLRD 421
Cdd:NF038007 4 MQNAEKCYITKTiktKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSysqkIILRRE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQK-NHIFNGTIEENI----RYGNVNATfEEIEDAAkrayiheQIMDL---PEGYQSKALLLSGGQQQRIAIARM 493
Cdd:NF038007 84 LIGYIFQSfNLIPHLSIFDNValplKYRGVAKK-ERIERVN-------QVLNLfgiDNRRNHKPMQLSGGQQQRVAIARA 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534190046 494 FLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT 530
Cdd:NF038007 156 MVSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGT 192
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
354-565 |
7.16e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 89.72 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 354 FSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQP-DS-----GKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK14246 17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYGNVNATFEE-------IEDAAKRAYIHEQIMDLpegYQSKALLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK14246 97 QQPNPFpHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEVYDR---LNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
348-566 |
1.13e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.75 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYkALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPD-----SGKILLDGIDL--EEYDTQFLR 420
Cdd:PRK14267 6 ETVNLRVYYGSNH-VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQKNHIF-NGTIEENI----RYGNVNATFEEIED----AAKRAYIHEQIMDLPEGYQSKallLSGGQQQRIAIA 491
Cdd:PRK14267 85 REVGMVFQYPNPFpHLTIYDNVaigvKLNGLVKSKKELDErvewALKKAALWDEVKDRLNDYPSN---LSGGQRQRLVIA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT-VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTiVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
31-320 |
1.16e-19 |
|
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: 89.83 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 31 GSFTSQVNALILQYTVDSInglveAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKL--RILVsqDLAQTIIE 108
Cdd:cd18545 12 STAASLAGPYLIKIAIDEY-----IPNGDLSGLLIIALLFLALN---LVNWVASRLRIYLMAKVgqRILY--DLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 109 KILTYRMAFYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITqq 188
Cdd:cd18545 82 HLQKLSFSFFDS--RPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVV-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 189 qakkLSGRRRNLRGYREQKSQgiISIINS--------ITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKS 260
Cdd:cd18545 158 ----FLLRRRARKAWQRVRKK--ISNLNAylhesisgIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVE 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 261 FIEQFGVVIIIILTSYLVLDGQMTIG---ASMFHILLFNNvsaPIRQLHRIYDEMNDAMIYSE 320
Cdd:cd18545 232 LISALGTALVYWYGGKLVLGGAITVGvlvAFIGYVGRFWQ---PIRNLSNFYNQLQSAMASAE 291
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
362-529 |
1.17e-19 |
|
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: 88.16 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRdNIGLVL-QKNH-IFNGTIEE 439
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVFgQKTQlWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRygnVNATFEEIEDAAKRAYIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQ 517
Cdd:cd03267 115 SFY---LLAAIYDLPPARFKKRLDElsELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170
....*....|..
gi 2534190046 518 IKNSLDAIKKDR 529
Cdd:cd03267 192 IRNFLKEYNRER 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
346-531 |
1.30e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.76 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSY----PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKI---------LLDGIDLE 412
Cdd:PRK13651 2 QIKVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 413 EYDTQF---------------LRDNIGLVLQ--KNHIFNGTIEENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGY-Q 474
Cdd:PRK13651 82 KVLEKLviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYlQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 475 SKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAI-KKDRTV 531
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTI 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
365-512 |
1.45e-19 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 90.55 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 365 NINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQfLRDnIGLVLQKNHIF-NGTIEENIRY 443
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-QRD-ICMVFQSYALFpHMSLGENVGY 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 444 G----NVNAtfEEIEDAAKRAYiheQIMDLpEGYQSKAL-LLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:PRK11432 102 GlkmlGVPK--EERKQRVKEAL---ELVDL-AGFEDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
348-511 |
1.49e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 88.63 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:COG4559 3 EAENLSVRL-GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI-FNGTIEENIRYGNVNATFEEIEDAAkrayIHEQIMDLP-----EG--YQSkallLSGGQQQRIAIARMF--LKN 497
Cdd:COG4559 82 QHSSLaFPFTVEEVVALGRAPHGSSAAQDRQ----IVREALALVglahlAGrsYQT----LSGGEQQRVQLARVLaqLWE 153
|
170
....*....|....*....
gi 2534190046 498 PP-----IIFLDEPTASLD 511
Cdd:COG4559 154 PVdggprWLFLDEPTSALD 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
362-512 |
1.51e-19 |
|
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: 87.87 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLD----GIDLEE---------------YDTQFLRdn 422
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQaspreilalrrrtigYVSQFLR-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 iglVLQKNhifnGTIE---ENIRYGNVNAtfEEIEDAAKRAYIHeqiMDLPEG-YQSKALLLSGGQQQRIAIARMFLKNP 498
Cdd:COG4778 104 ---VIPRV----SALDvvaEPLLERGVDR--EEARARARELLAR---LNLPERlWDLPPATFSGGEQQRVNIARGFIADP 171
|
170
....*....|....
gi 2534190046 499 PIIFLDEPTASLDA 512
Cdd:COG4778 172 PLLLLDEPTASLDA 185
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
359-564 |
1.86e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 88.12 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 359 GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRdNIGLVLQKNHI--FNG- 435
Cdd:PRK11300 17 GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-RMGVVRTFQHVrlFREm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENI-----RYGNVN--------ATFEEIE-DAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK11300 96 TVIENLlvaqhQQLKTGlfsgllktPAFRRAEsEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISH---SISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIehdMKLVMGISDRIYVVNQGTPLANGTPEEI 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
347-599 |
2.33e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.61 E-value: 2.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYP--NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIG 424
Cdd:PRK13642 5 LEVENLVFKYEkeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQK--NHIFNGTIEENIRYGNVNATF--EEIEDAAKRAYIHEQIMDLPEGYQSKallLSGGQQQRIAIARMFLKNPPI 500
Cdd:PRK13642 85 MVFQNpdNQFVGATVEDDVAFGMENQGIprEEMIKRVDEALLAVNMLDFKTREPAR---LSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIKKDR--TVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIFDAM 578
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDMVEIGLDV 241
|
250 260
....*....|....*....|.
gi 2534190046 579 AKSLNIEKIAKTFDDEEEENY 599
Cdd:PRK13642 242 PFSSNLMKDLRKNGFDLPEKY 262
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
366-518 |
2.93e-19 |
|
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: 89.40 E-value: 2.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 366 INMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEE----YDTQFLRDNIGLVLQKNHIF-NGTIEEN 440
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 441 IRYGNVNAtfeeieDAAKRAYIHEQIMDLpegYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:TIGR02142 96 LRYGMKRA------RPSERRISFERVIEL---LGIGHLLgrlpgrLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
....
gi 2534190046 515 TEQI 518
Cdd:TIGR02142 167 KYEI 170
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
348-553 |
3.28e-19 |
|
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: 86.62 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL----RDNI 423
Cdd:cd03290 2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRYGNV--NATFEEIEDAAKrayIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKN 497
Cdd:cd03290 82 AYAAQKPWLLNATVEENITFGSPfnKQRYKAVTDACS---LQPDIDLLPFGDQTeigeRGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNS--LDAIKKD-RTVIIISHSISQIIDADYTYVMKQG 553
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
365-511 |
5.98e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.78 E-value: 5.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 365 NINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLeeYDTQ---FL---RDNIGLVLQKNHIF-NGTI 437
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVL--FDAEkgiCLppeKRRIGYVFQDARLFpHYKV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 438 EENIRYG---NVNATFEE------IEDAAKRayiheqimdLPegyqskaLLLSGGQQQRIAIARMFLKNPPIIFLDEPTA 508
Cdd:PRK11144 94 RGNLRYGmakSMVAQFDKivallgIEPLLDR---------YP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
...
gi 2534190046 509 SLD 511
Cdd:PRK11144 158 SLD 160
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
348-531 |
8.41e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.59 E-value: 8.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidlEEYDTQFLRD----NI 423
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG---QEMRFASTTAalaaGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIF-NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL--LSGGQQQRIAIARMFLKNPPI 500
Cdd:PRK11288 82 AIIYQELHLVpEMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLkyLSIGQRQMVEIAKALARNARV 161
|
170 180 190
....*....|....*....|....*....|.
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRV 192
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
348-528 |
1.59e-18 |
|
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: 84.73 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLVL 427
Cdd:cd03265 2 EVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG-TIEENIRygnVNATFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:cd03265 80 QDLSVDDElTGWENLY---IHARLYGVPGAERRERIDELLdfVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180
....*....|....*....|....
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKKD 528
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEE 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
361-565 |
1.96e-18 |
|
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: 88.59 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKST----VINLLdkfyqPDSGKILLDGIDLEEYDT---QFLRDNIGLVLQKNhif 433
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSRralRPLRRRMQVVFQDP--- 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 434 NG------TIEENI---------------RYGNVNATFEEI---EDAAKRaYIHEqimdlpegyqskallLSGGQQQRIA 489
Cdd:COG4172 372 FGslsprmTVGQIIaeglrvhgpglsaaeRRARVAEALEEVgldPAARHR-YPHE---------------FSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 490 IAR-MFLKnPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---------------RTViiishsisqiidADYTYVMKQG 553
Cdd:COG4172 436 IARaLILE-PKLLVLDEPTSALDVSVQAQILDLLRDLQREhglaylfishdlavvRAL------------AHRVMVMKDG 502
|
250
....*....|..
gi 2534190046 554 EVVEHGIHEDVY 565
Cdd:COG4172 503 KVVEQGPTEQVF 514
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
348-522 |
1.96e-18 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE----EYDTQFLRDni 423
Cdd:PRK11248 3 QISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaERGVVFQNE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNhifngtIEENIRYGnvnATFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK11248 80 GLLPWRN------VQDNVAFG---LQLAGVEKMQRLEIAHQMLkkVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180
....*....|....*....|.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSL 522
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLL 171
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
348-520 |
2.39e-18 |
|
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: 83.81 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeyDTQFLRDNIGlVL 427
Cdd:cd03268 2 KTNDLTKTYGKK-RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG-AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG--TIEENIRYgnvNATFEEIEDAakrayIHEQIMD---LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:cd03268 78 IEAPGFYPnlTARENLRL---LARLLGIRKK-----RIDEVLDvvgLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170
....*....|....*...
gi 2534190046 503 LDEPTASLDAIATEQIKN 520
Cdd:cd03268 150 LDEPTNGLDPDGIKELRE 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
348-585 |
5.96e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 5.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLD--KFYQPDSGKIL-------------------- 405
Cdd:TIGR03269 2 EVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 406 -------------LDGIDLEEYDTQFLRDNIGLVLQKNHIFNG--TIEENIrygnVNATFE---EIEDAAKRAYIHEQIM 467
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNV----LEALEEigyEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 468 DLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLD--AIKKDRTVIIISHSISQIID-A 544
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDlS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2534190046 545 DYTYVMKQGEVVEHGIHEDVYKMngtYKEIFDAMAKSLNIE 585
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAV---FMEGVSEVEKECEVE 274
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
348-564 |
7.86e-18 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 83.34 E-value: 7.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID--------LEEYDTQFL 419
Cdd:TIGR02323 5 QVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 -RDNIGLVLQknHIFNG---------TIEENI------RYGNVNAT----FEEIEDAAKRayiheqIMDLPEGYqskall 479
Cdd:TIGR02323 84 mRTEWGFVHQ--NPRDGlrmrvsagaNIGERLmaigarHYGNIRATaqdwLEEVEIDPTR------IDDLPRAF------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 480 lSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVV 556
Cdd:TIGR02323 150 -SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlglAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
....*...
gi 2534190046 557 EHGIHEDV 564
Cdd:TIGR02323 229 ESGLTDQV 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
362-559 |
7.88e-18 |
|
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: 86.66 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKS----TVINLLDKFYQPDSGKILLDGIDL---EEYDTQFLRDN-IGLVLQK---- 429
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRGNrIAMIFQEpmts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 -NHIFngTIEENI-----RYGNVNAT---------FEE--IEDAAKR--AYIHEqimdlpegyqskallLSGGQQQRIAI 490
Cdd:COG4172 105 lNPLH--TIGKQIaevlrLHRGLSGAaararalelLERvgIPDPERRldAYPHQ---------------LSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 491 ArMFLKNPPIIFL-DEPTASLDAIATEQIKNSLDAIKKDR-------T-----VIIIshsisqiidADYTYVMKQGEVVE 557
Cdd:COG4172 168 A-MALANEPDLLIaDEPTTALDVTVQAQILDLLKDLQRELgmallliThdlgvVRRF---------ADRVAVMRQGEIVE 237
|
..
gi 2534190046 558 HG 559
Cdd:COG4172 238 QG 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-581 |
8.01e-18 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 87.87 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSY-PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNI 423
Cdd:PLN03130 1236 GSIKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRygnvnaTFEEIEDA-----AKRAYIHEQIMDLPEGYQSKALL----LSGGQQQRIAIARMF 494
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD------PFNEHNDAdlwesLERAHLKDVIRRNSLGLDAEVSEagenFSVGQRQLLSLARAL 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTykeI 574
Cdd:PLN03130 1390 LRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGS---A 1466
|
....*..
gi 2534190046 575 FDAMAKS 581
Cdd:PLN03130 1467 FSKMVQS 1473
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
348-510 |
8.62e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.62 E-value: 8.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDN-IGLV 426
Cdd:COG3845 7 ELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQknHiF----NGTIEENIRYGNVNATF---------EEIEDAAKR--------AYIHEqimdlpegyqskallLSGGQQ 485
Cdd:COG3845 86 HQ--H-FmlvpNLTVAENIVLGLEPTKGgrldrkaarARIRELSERygldvdpdAKVED---------------LSVGEQ 147
|
170 180
....*....|....*....|....*
gi 2534190046 486 QRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVL 172
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
349-516 |
9.01e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.66 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPnGYKALKNINMTIQP-NKItALVGLSGAGKSTVINLLDKFYQPDSGKILLDG---I-----DLEEYDTQFL 419
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPgDRI-GLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrIgylpqEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNI--------GLVLQKNHI---FNGTIEENIRYGNVNATFEEIE--DAAKRAyihEQIMD---LPEGYQSKAL-LLSG 482
Cdd:COG0488 79 LDTVldgdaelrALEAELEELeakLAEPDEDLERLAELQEEFEALGgwEAEARA---EEILSglgFPEEDLDRPVsELSG 155
|
170 180 190
....*....|....*....|....*....|....
gi 2534190046 483 GQQQRIAIARMFLKNPPIIFLDEPTASLDAIATE 516
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIE 189
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
361-518 |
1.15e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 80.94 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLVL---QKNHIF-NG 435
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPedrKREGLVlDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIrygnvnatfeeiedaakrayiheqimdlpegyqSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIAT 515
Cdd:cd03215 94 SVAENI---------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
...
gi 2534190046 516 EQI 518
Cdd:cd03215 141 AEI 143
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
63-305 |
1.33e-17 |
|
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: 83.65 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 63 LKIISFISIVLMTKEILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNqdNQAGKLQTRIDRGIESLTRL 142
Cdd:cd18549 38 LRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDN--NKTGQLMSRITNDLFDISEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 143 V----QNFFIDILPLfansIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSgrrrnlRGYREQKSQgiISIINS- 217
Cdd:cd18549 116 AhhgpEDLFISIITI----IGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMK------KAFRRVREK--IGEINAq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 218 -------ITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKT-SFFFDGLKSFIeQFGVVIIIILTSYLVLDGQMTIGASM 289
Cdd:cd18549 184 ledslsgIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAmAYFFSGMNFFT-NLLNLVVLVAGGYFIIKGEITLGDLV 262
|
250
....*....|....*.
gi 2534190046 290 FHILLFNNVSAPIRQL 305
Cdd:cd18549 263 AFLLYVNVFIKPIRRL 278
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
31-316 |
1.69e-17 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 83.33 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 31 GSFTSQVNALILQYTVDSIngLVEAGKGLKEGLKIISFISIVLMTkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKI 110
Cdd:cd18563 11 GTALGLVPPYLTKILIDDV--LIQLGPGGNTSLLLLLVLGLAGAY--VLSALLGILRGRLLARLGERITADLRRDLYEHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 111 LTYRMAFYtnQDNQAGKLQTRIDRGIESLtrlvQNFFIDILPLFANSIVALI----LMFNANFYVGLVGLCIVPIYFIIT 186
Cdd:cd18563 87 QRLSLSFF--DKRQTGSLMSRVTSDTDRL----QDFLSDGLPDFLTNILMIIgigvVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 187 QQQAKKLsgRRRNLRGYREQ-KSQGIIS-IINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQ 264
Cdd:cd18563 161 YFFWKKI--RRLFHRQWRRWsRLNSVLNdTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTS 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 265 FGVVIIIILTSYLVLDGQMTIG--------ASMFHillfnnvsAPIRQLHRIYDEMNDAM 316
Cdd:cd18563 239 LGTLIVWYFGGRQVLSGTMTLGtlvaflsyLGMFY--------GPLQWLSRLNNWITRAL 290
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
363-518 |
2.67e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 80.99 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPD---SGKILLDGIDLEEYDTQflRDNIGLVLQKNHIF-NGTIE 438
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFpHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRYgnvnATFEEIEDAAKRAYIH---EQImDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIAT 515
Cdd:COG4136 95 ENLAF----ALPPTIGRAQRRARVEqalEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
...
gi 2534190046 516 EQI 518
Cdd:COG4136 170 AQF 172
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
363-520 |
3.39e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 3.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--IDLEEYDTQ--------FLRDNIglvlqknhi 432
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEAchylghrnAMKPAL--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 433 fngTIEENIRY-GNVNATFE-EIEDAAKRAYIHEqIMDLPEGYqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:PRK13539 89 ---TVAENLEFwAAFLGGEElDIAAALEAVGLAP-LAHLPFGY------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170
....*....|
gi 2534190046 511 DAIATEQIKN 520
Cdd:PRK13539 159 DAAAVALFAE 168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
363-518 |
4.17e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.02 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQF---LRDN-IGLVLQKNHIF-NGTI 437
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQFHHLLpDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 438 EENIRY----GNVNAtfeeiEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:PRK11629 105 LENVAMplliGKKKP-----AEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
....*
gi 2534190046 514 ATEQI 518
Cdd:PRK11629 180 NADSI 184
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
343-511 |
5.28e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 82.47 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 343 LKGKFEIQNVEFSYPNGY-KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD 421
Cdd:COG4608 13 LKKHFPVRGGLFGRTVGVvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 ---NIGLVLQKNhifngtieenirYGNVNA--TFEEI-----------EDAAKRAYIHEqIMDL----PEGYQSKALLLS 481
Cdd:COG4608 93 lrrRMQMVFQDP------------YASLNPrmTVGDIiaeplrihglaSKAERRERVAE-LLELvglrPEHADRYPHEFS 159
|
170 180 190
....*....|....*....|....*....|
gi 2534190046 482 GGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
348-520 |
5.57e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.46 E-value: 5.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVinlldkFY------QPDSGKILLDGIDLeeydTQF--- 418
Cdd:COG1137 5 EAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDI----THLpmh 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 --LRDNIGLVLQKNHIFNG-TIEENIRygnvnATFEEIE-DAAKRAYIHEQIMD---LPEGYQSKALLLSGGQQQRIAIA 491
Cdd:COG1137 74 krARLGIGYLPQEASIFRKlTVEDNIL-----AVLELRKlSKKEREERLEELLEefgITHLRKSKAYSLSGGERRRVEIA 148
|
170 180
....*....|....*....|....*....
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAIATEQIKN 520
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQK 177
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
362-564 |
6.01e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 6.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRD----NIGLVLQKNHIF-NGT 436
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 437 IEENIRYGNVNATF--EEIEDAAKRAYIHEQIMDLPEGYQSKallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:PRK10070 123 VLDNTAFGMELAGInaEERREKALDALRQVGLENYAHSYPDE---LSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 515 TEQIKNSLDAI--KKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK10070 200 RTEMQDELVKLqaKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEI 252
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
345-531 |
6.15e-17 |
|
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: 81.44 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSYPNGYKA-LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDsGKILLDGIDLEEYDTQFLRDNI 423
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAvLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIR-YGNVNAtfEEIEDAAKRAYIHEQIMDLPEGYQSKAL----LLSGGQQQRIAIARMFLKNP 498
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVdggcVLSHGHKQLMCLARSVLSKA 157
|
170 180 190
....*....|....*....|....*....|...
gi 2534190046 499 PIIFLDEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTV 190
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
348-564 |
6.37e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 6.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK11231 4 RTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNG-TIEENIRYGNV--NATFEEI--EDAAK--RAYIHEQIMDLPEgyqSKALLLSGGQQQRIAIARMFLKNPPI 500
Cdd:PRK11231 83 QHHLTPEGiTVRELVAYGRSpwLSLWGRLsaEDNARvnQAMEQTRINHLAD---RRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 501 IFLDEPTASLDaiateqIKNSLDAIK-------KDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK11231 160 VLLDEPTTYLD------INHQVELMRlmrelntQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPEEV 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
363-565 |
7.14e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 7.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--IDLEEYDTQFLRDNIGLVLQ--KNHIFNGTIE 438
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATVFQdpEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRYGNVNATFEEiEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:PRK13638 97 SDIAFSLRNLGVPE-AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2534190046 519 KNSLDAI--KKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK13638 176 IAIIRRIvaQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
363-511 |
7.35e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 7.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHI-FNGTIEENI 441
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVV 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 442 RYGNVNAT--FEEIEDAAKRAYihEQIMDLPEGYQSKA---LLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK09536 99 EMGRTPHRsrFDTWTETDRAAV--ERAMERTGVAQFADrpvTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-511 |
9.12e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.52 E-value: 9.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGY----KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGID---LEEYD-TQFl 419
Cdd:COG1101 3 ELKNLSKTFNPGTvnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtkLPEYKrAKY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 rdnIGLVLQ---KNHIFNGTIEENI--------RYGNVNATfeeieDAAKRAYIHEQI----MDLPEGYQSKALLLSGGQ 484
Cdd:COG1101 82 ---IGRVFQdpmMGTAPSMTIEENLalayrrgkRRGLRRGL-----TKKRRELFRELLatlgLGLENRLDTKVGLLSGGQ 153
|
170 180
....*....|....*....|....*..
gi 2534190046 485 QQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-565 |
9.75e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.22 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYP---------NGYK-ALKNINMTIQPNKITALVGLSGAGKST----VINLLdkfyqPDSGKILLDGIDLEE 413
Cdd:PRK15134 277 DVEQLQVAFPirkgilkrtVDHNvVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 414 YD-TQFL--RDNIGLVLQK-NHIFN------GTIEENIRYGNVNATFEEIEDAAKRAyIHEQIMDlPEGYQSKALLLSGG 483
Cdd:PRK15134 352 LNrRQLLpvRHRIQVVFQDpNSSLNprlnvlQIIEEGLRVHQPTLSAAQREQQVIAV-MEEVGLD-PETRHRYPAEFSGG 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 484 QQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIiishsisqiidadYTY--------------- 548
Cdd:PRK15134 430 QRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLA-------------YLFishdlhvvralchqv 496
|
250
....*....|....*...
gi 2534190046 549 -VMKQGEVVEHGIHEDVY 565
Cdd:PRK15134 497 iVLRQGEVVEQGDCERVF 514
|
|
| ABC_6TM_HMT1 |
cd18583 |
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ... |
99-320 |
1.16e-16 |
|
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.
Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 80.65 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 99 SQDLAQTIIEKILTYRMAFYTNQDnqAGKLQTRIDRGiESLTRLVQNFFIDILPLFANSIVALI---LMFNAnfYVGLVg 175
Cdd:cd18583 69 YRALSTAAFNHVMNLSMDFHDSKK--SGEVLKAIEQG-SSINDLLEQILFQIVPMIIDLVIAIVylyYLFDP--YMGLI- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 176 LCIVPIYFI-----ITQQQAKKlsgRRRNLRGYREQKSQGIISIINSITViKSFNREDIEgkkqLDLQKELTNNQMQTRK 250
Cdd:cd18583 143 VAVVMVLYVwstikLTSWRTKL---RRDMIDADREERSILTESLLNWETV-KYFNREPYE----KERYREAVKNYQKAER 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 251 TSFFFD----GLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAMIYSE 320
Cdd:cd18583 215 KYLFSLnllnAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAE 288
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
247-517 |
1.44e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.93 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 247 QTRKTSFFfdglKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSA----PIRQ----------LHRIYdem 312
Cdd:COG4178 264 RQRNLTFF----TTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGalswFVDNyqslaewratVDRLA--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 313 ndamiyseSFFAILKADDEKESSGNYIPTKLKGKFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKST---V 389
Cdd:COG4178 337 --------GFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTllrA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 390 INLLDKFYqpdSGKILL-DGIDLeeydtqflrdnigLVL-QKNHIFNGTIEENIRYGNVNATF--EEIEDAAKRAYIHEQ 465
Cdd:COG4178 409 IAGLWPYG---SGRIARpAGARV-------------LFLpQRPYLPLGTLREALLYPATAEAFsdAELREALEAVGLGHL 472
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 466 IMDLPEGyQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAiATEQ 517
Cdd:COG4178 473 AERLDEE-ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE-ENEA 522
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
348-531 |
1.47e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDtqflRDNIGLV- 426
Cdd:COG4152 3 ELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 ----LQKNHifngTIEENIRYgnvnatFEEI-----EDAAKRA-YIHEQiMDLPEGYQSKALLLSGGQQQRIAIARMFLK 496
Cdd:COG4152 78 eergLYPKM----KVGEQLVY------LARLkglskAEAKRRAdEWLER-LGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534190046 497 NPPIIFLDEPTASLDAIATEQIKNSL-DAIKKDRTV 531
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTV 182
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
348-559 |
1.82e-16 |
|
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: 78.48 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDtqflRDNIGLVL 427
Cdd:cd03269 2 EVENVTKRFGR-VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIF-NGTIEENIRYgnvnatFEEIEDaAKRAYIHEQIMDLPE-----GYQSKAL-LLSGGQQQRIAIARMFLKNPPI 500
Cdd:cd03269 77 EERGLYpKMKVIDQLVY------LAQLKG-LKKEEARRRIDEWLErlelsEYANKRVeELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 501 IFLDEPTASLDAIATEQIKNSLDAIK-KDRTVIIISHSISQIID-ADYTYVMKQGEVVEHG 559
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
348-512 |
2.17e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.90 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTqflRD-NIGLV 426
Cdd:PRK10851 4 EIANIKKSFGRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIF-NGTIEENIRYGnvnATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL------LSGGQQQRIAIARMFLKNPP 499
Cdd:PRK10851 80 FQHYALFrHMTVFDNIAFG---LTVLPRRERPNAAAIKAKVTQLLEMVQLAHLAdrypaqLSGGQKQRVALARALAVEPQ 156
|
170
....*....|...
gi 2534190046 500 IIFLDEPTASLDA 512
Cdd:PRK10851 157 ILLLDEPFGALDA 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
348-564 |
2.27e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDN-IGLV 426
Cdd:PRK09700 7 SMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIRYGN--------VNATfeEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:PRK09700 86 YQELSVIDElTVLENLYIGRhltkkvcgVNII--DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT--VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTaiVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
140-317 |
2.33e-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: 79.91 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 140 TRLVQNFFI-DILPLFANS---IVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLsgrRRNLRGY--REQKSQG-II 212
Cdd:cd18568 108 NQKIRRFLTrSALTTILDLlmvFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKL---KRNSREIfqANAEQQSfLV 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 213 SIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHI 292
Cdd:cd18568 185 EALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFN 264
|
170 180
....*....|....*....|....*
gi 2534190046 293 LLFNNVSAPIRQLHRIYDEMNDAMI 317
Cdd:cd18568 265 MLFGSVINPLLALVGLWDELQETRI 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-531 |
3.65e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.75 E-value: 3.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 357 PNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLVLQKNHIFNG- 435
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIR-YGNVNATFEEIEDAAKRAYIHEqiMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:TIGR01257 1019 TVAEHILfYAQLKGRSWEEAQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170
....*....|....*..
gi 2534190046 515 TEQIKNSLDAIKKDRTV 531
Cdd:TIGR01257 1097 RRSIWDLLLKYRSGRTI 1113
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
94-310 |
3.86e-16 |
|
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: 79.12 E-value: 3.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 94 LRILVSQDLAQTII--------EKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRL----VQNFFIDILPLfansIVAL 161
Cdd:cd18778 59 LRIYLNHVAEQKVVadlrsdlyDKLQRLSLRYF--DDRQTGDLMSRVINDVANVERLiadgIPQGITNVLTL----VGVA 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 162 ILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRnlrgyREQKSQGIISI-----INSITVIKSFNREDIEGKKQLD 236
Cdd:cd18778 133 IILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYR-----KVREALGELNAllqdnLSGIREIQAFGREEEEAKRFEA 207
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 237 LQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIG---ASMFHILLFNNvsaPIRQLHRIYD 310
Cdd:cd18778 208 LSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGdlvAFLLYLGLFYE---PITSLHGLNE 281
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
158-580 |
4.46e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 82.33 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 158 IVALILMFN----ANFYVGLVGLCIVPIYFIITQQQakklsgRRRNLRG-YREQKSQGIIS-IINSITVIKSFNRE-DIE 230
Cdd:PLN03232 429 IVSMVLLYQqlgvASLFGSLILFLLIPLQTLIVRKM------RKLTKEGlQWTDKRVGIINeILASMDTVKCYAWEkSFE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 231 GKKQldlqkELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILT--SYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRI 308
Cdd:PLN03232 503 SRIQ-----GIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLVSfgVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 309 YDEMNDAMIYSESFFAILKADdEKESSGNyiPTKLKG--KFEIQNVEFSYPNGYK--ALKNINMTIQPNKITALVGLSGA 384
Cdd:PLN03232 578 LSQVVNANVSLQRIEELLLSE-ERILAQN--PPLQPGapAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGE 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 385 GKSTVINlldkfyqpdsgkILLDGIDLEEYDTQFLRDNIGLVLQKNHIFNGTIEENIRYGnvnATFE-EIEDAAKRAYIH 463
Cdd:PLN03232 655 GKTSLIS------------AMLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFG---SDFEsERYWRAIDVTAL 719
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 464 EQIMDLPEGYQ-----SKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSldAIK---KDRTVIIIS 535
Cdd:PLN03232 720 QHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS--CMKdelKGKTRVLVT 797
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2534190046 536 HSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIFDAMAK 580
Cdd:PLN03232 798 NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGK 842
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
361-531 |
4.54e-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: 77.70 E-value: 4.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPD---SGKILLDGidlEEYDTQFLRDNIGLVLQKNHIFNG-T 436
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG---QPRKPDQFQKCVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 437 IEENIRYGNVNATFEEIEDAAKRAyiheqiMDLPEGYQSKALL---------LSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:cd03234 98 VRETLTYTAILRLPRKSSDAIRKK------RVEDVLLRDLALTriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*
gi 2534190046 508 ASLDA-IATEQIKNSLDAIKKDRTV 531
Cdd:cd03234 172 SGLDSfTALNLVSTLSQLARRNRIV 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
365-524 |
4.71e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 365 NINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDniglVLQKNHIfNG-----TIEE 439
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD----LLYLGHQ-PGiktelTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRY-----GNVNAtfEEIEDAAKRAYIHEQiMDLPEGYqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:PRK13538 94 NLRFyqrlhGPGDD--EALWEALAQVGLAGF-EDVPVRQ------LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170
....*....|
gi 2534190046 515 TEQIKNSLDA 524
Cdd:PRK13538 165 VARLEALLAQ 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
361-529 |
5.33e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 79.36 E-value: 5.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRdNIGLVL-QKNH-IFNGTIE 438
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVFgQRSQlWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRygnVNATFEEIEDAAKRAYIHE--QIMDLpegyqsKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:COG4586 115 DSFR---LLKAIYRIPDAEYKKRLDElvELLDL------GELLdtpvrqLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170
....*....|....*....
gi 2534190046 511 DAIATEQIKNSLDAIKKDR 529
Cdd:COG4586 186 DVVSKEAIREFLKEYNRER 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
363-511 |
5.71e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 77.92 E-value: 5.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTV---INLLDkfyQPDSGKILLDGidlEEYDT----------------QFLRDNI 423
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFlrcINLLE---TPDSGEIRVGG---EEIRLkpdrdgelvpadrrqlQRIRTRL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKnhiFN----GTIEENIRYGNVN----ATFEEIEDAakRAYIHE-QIMDLPEGYQSKallLSGGQQQRIAIARMF 494
Cdd:COG4598 98 GMVFQS---FNlwshMTVLENVIEAPVHvlgrPKAEAIERA--EALLAKvGLADKRDAYPAH---LSGGQQQRAAIARAL 169
|
170
....*....|....*..
gi 2534190046 495 LKNPPIIFLDEPTASLD 511
Cdd:COG4598 170 AMEPEVMLFDEPTSALD 186
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
66-287 |
7.17e-16 |
|
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: 78.37 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 66 ISFISIVLMTKEILNAFITFGQKYY----GEKlrilVSQDLAQTIIEKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTR 141
Cdd:cd18557 35 LNELALILLAIYLLQSVFTFVRYYLfniaGER----IVARLRRDLFSSLLRQEIAFF--DKHKTGELTSRLSSDTSVLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 142 LVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLsgrRRNLRGYREQK---SQGIISIINSI 218
Cdd:cd18557 109 AVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALakaGQVAEESLSNI 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 219 TVIKSFNREDIEGKK-QLDLQKELTNNQMQTRKTSFFFdGLKSFIEQFGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18557 186 RTVRSFSAEEKEIRRySEALDRSYRLARKKALANALFQ-GITSLLIYLSLLLVLWYGGYLVLSGQLTVGE 254
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
359-564 |
8.31e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 8.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 359 GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKI--------LLDGIDLEEYDTQFL-RDNIGLVLQk 429
Cdd:PRK11701 18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRRLlRTEWGFVHQ- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 nHIFNG-----TIEENI----------RYGNVNAT----FEEIEDAAKRayiheqIMDLPEGYqskalllSGGQQQRIAI 490
Cdd:PRK11701 97 -HPRDGlrmqvSAGGNIgerlmavgarHYGDIRATagdwLERVEIDAAR------IDDLPTTF-------SGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQIknsLDAIKK--------------DRTVIIIShsisqiidADYTYVMKQGEVV 556
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARL---LDLLRGlvrelglavvivthDLAVARLL--------AHRLLVMKQGRVV 231
|
....*...
gi 2534190046 557 EHGIHEDV 564
Cdd:PRK11701 232 ESGLTDQV 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
340-511 |
1.41e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 340 PTKLKGkfeiQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL 419
Cdd:PRK10253 5 VARLRG----EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 RDNIGLVLQkNHIFNG--TIEENIRYGNV--NATF----EEIEDAAKRAYIHEQIMDLPEgyQSkALLLSGGQQQRIAIA 491
Cdd:PRK10253 80 ARRIGLLAQ-NATTPGdiTVQELVARGRYphQPLFtrwrKEDEEAVTKAMQATGITHLAD--QS-VDTLSGGQRQRAWIA 155
|
170 180
....*....|....*....|
gi 2534190046 492 RMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLD 175
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-531 |
1.46e-15 |
|
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: 80.72 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSYPNGYKA-LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDsGKILLDGIDLEEYDTQFLRDNI 423
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGRAvLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENI----RYGNvnatfEEIEDAAKRAYIHEQIMDLPE---------GYqskalLLSGGQQQRIAI 490
Cdd:TIGR01271 1295 GVIPQKVFIFSGTFRKNLdpyeQWSD-----EEIWKVAEEVGLKSVIEQFPDkldfvlvdgGY-----VLSNGHKQLMCL 1364
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTV 531
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTV 1405
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-527 |
3.63e-15 |
|
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: 76.00 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQ----FLRDnIGLVLQKNH-IFNG-- 435
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrraFRRD-VQLVFQDSPsAVNPrm 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIRYGNVNatFEEIEDAAKRAYIHE--QIMDL-PEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:TIGR02769 106 TVRQIIGEPLRH--LTSLDESEQKARIAEllDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170
....*....|....*
gi 2534190046 513 IATEQIKNSLDAIKK 527
Cdd:TIGR02769 184 VLQAVILELLRKLQQ 198
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
326-523 |
4.60e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 326 LKADDEKESSGN---YIPTKLK-GK--FEIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQP 399
Cdd:COG0488 289 LEREEPPRRDKTveiRFPPPERlGKkvLELEGLSKSYG-DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 400 DSGKILLdGIDLEeydtqflrdnIGLVLQKNHIFNG--TIEENIRYGNVNATFEEIedaakRAYIheQIMDLPEGYQSKA 477
Cdd:COG0488 368 DSGTVKL-GETVK----------IGYFDQHQEELDPdkTVLDELRDGAPGGTEQEV-----RGYL--GRFLFSGDDAFKP 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534190046 478 L-LLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDaIAT-EQIKNSLD 523
Cdd:COG0488 430 VgVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD-IETlEALEEALD 476
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
69-305 |
5.11e-15 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 76.01 E-value: 5.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 69 ISIVLMTkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQdnQAGKLQTRI--DrgieslTRLVQNF 146
Cdd:cd18564 58 AALVGIA--LLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR--RTGDLLSRLtgD------VGAIQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 147 FID-ILPLFANsIVALILMFNANFYV----GLVGLCIVPIYFIITQQQAKKLSGRRRnlrgyREQKSQGIIS-----IIN 216
Cdd:cd18564 128 LVSgVLPLLTN-LLTLVGMLGVMFWLdwqlALIALAVAPLLLLAARRFSRRIKEASR-----EQRRREGALAsvaqeSLS 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 217 SITVIKSFNREDIEGKKqldLQKEltNNQ-----MQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGAsmfh 291
Cdd:cd18564 202 AIRVVQAFGREEHEERR---FARE--NRKslragLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGD---- 272
|
250
....*....|....*...
gi 2534190046 292 ILLF----NNVSAPIRQL 305
Cdd:cd18564 273 LLVFlaylKNLYKPVRDL 290
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
348-512 |
6.22e-15 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 76.42 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG---IDLEEYDtqflRDnIG 424
Cdd:PRK11650 5 KLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELEPAD----RD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQkN-----HIfngTIEENIRYGNVNATF--EEIE----DAAKrayiheqIMDLPEGYQSKALLLSGGQQQRIAIARM 493
Cdd:PRK11650 80 MVFQ-NyalypHM---SVRENMAYGLKIRGMpkAEIEervaEAAR-------ILELEPLLDRKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*....
gi 2534190046 494 FLKNPPIIFLDEPTASLDA 512
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA 167
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
363-528 |
7.17e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL----EEYDTQFLRDNIGLVLQK-------NH 431
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRAKHVGFVFQSfmliptlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-------LSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170
....*....|....*..
gi 2534190046 512 AIATEQIKNSLDAIKKD 528
Cdd:PRK10584 179 RQTGDKIADLLFSLNRE 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
345-564 |
8.55e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.83 E-value: 8.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEfsypngykALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE----EYDTQFLR 420
Cdd:PRK15112 19 GWFRRQTVE--------AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdySYRSQRIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 -------------DNIGLVLQKNHIFNGTIEENIRYGNVNATFEeiedaakrayiheQIMDLPEGYQSKALLLSGGQQQR 487
Cdd:PRK15112 91 mifqdpstslnprQRISQILDFPLRLNTDLEPEQREKQIIETLR-------------QVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 488 IAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSI---SQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQhlgMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
358-524 |
9.18e-15 |
|
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: 73.16 E-value: 9.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL----EEYDTQFL----RDNIGLVLqk 429
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqrDEPHENILylghLPGLKPEL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 nhifngTIEENIRYgnvnatFEEIEDAAKRAyIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:TIGR01189 89 ------SALENLHF------WAAIHGGAQRT-IEDALaaVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170
....*....|....*..
gi 2534190046 508 ASLDAIATEQIKNSLDA 524
Cdd:TIGR01189 156 TALDKAGVALLAGLLRA 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
348-516 |
1.21e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYD-TQFLRDNIGLV 426
Cdd:PRK15439 13 CARSISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIF-NGTIEENIRYG--NVNATFEEIEDAAKRAYIHeqiMDLpegyQSKALLLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:PRK15439 92 PQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDL----DSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170
....*....|...
gi 2534190046 504 DEPTASLDAIATE 516
Cdd:PRK15439 165 DEPTASLTPAETE 177
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
378-518 |
1.33e-14 |
|
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: 72.91 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 378 LVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDniglVLQKNHIfNG-----TIEENIRYGNVNATFEE 452
Cdd:cd03231 31 VTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG----LLYLGHA-PGikttlSVLENLRFWHADHSDEQ 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 453 IEDAAKRAYIhEQIMDLPEGYqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:cd03231 106 VEEALARVGL-NGFEDRPVAQ------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
348-522 |
1.72e-14 |
|
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: 70.94 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflRDNIGLVL 427
Cdd:cd03221 2 ELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QknhifngtieenirygnvnatfeeiedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:cd03221 70 Q---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170
....*....|....*
gi 2534190046 508 ASLDAIATEQIKNSL 522
Cdd:cd03221 99 NHLDLESIEALEEAL 113
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
359-565 |
2.38e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 359 GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQP-----DSGKILLDGIDLEEY-DTQFLRDNIGLVLQKNHI 432
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 433 FNGTIEENIRYGnVNA----TFEEIEDAAKRAYIHEQIMD-LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:PRK14271 113 FPMSIMDNVLAG-VRAhklvPRKEFRGVAQARLTEVGLWDaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 508 ASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLF 250
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
363-527 |
2.78e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 73.18 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQ----FLRDnIGLVLQK-------NH 431
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkaFRRD-IQMVFQDsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IFNGTIEENIRYgnvnatFEEIEDAAKRAYIHE--QIMDLPEGYQSK-ALLLSGGQQQRIAIARMFLKNPPIIFLDEPTA 508
Cdd:PRK10419 107 TVREIIREPLRH------LLSLDKAERLARASEmlRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
|
170
....*....|....*....
gi 2534190046 509 SLDAIATEQIknsLDAIKK 527
Cdd:PRK10419 181 NLDLVLQAGV---IRLLKK 196
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
37-312 |
3.07e-14 |
|
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: 73.40 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 37 VNALILQYTVDSIngLVEAGKGLkegLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMA 116
Cdd:cd18782 20 ANPLLFQVIIDKV--LVQQDLAT---LYVIGVVMLVAA---LLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYtnQDNQAGKLQTRIDRgieslTRLVQNFFID-ILPLFAN---SIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKK 192
Cdd:cd18782 92 FF--DKRPVGELSTRISE-----LDTIRGFLTGtALTTLLDvlfSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 193 LsgrRRNLRGYREQ--KSQG-IISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVI 269
Cdd:cd18782 165 L---RRQIRRRAEAsaKTQSyLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2534190046 270 IIILTSYLVLDGQMTIGASM-FHILLfNNVSAPIRQLHRIYDEM 312
Cdd:cd18782 242 VLWVGAYLVLRGELTLGQLIaFRILS-GYVTGPILRLSTLWQQF 284
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-528 |
4.47e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG--ID-LEEYDTQFLRDNIGLVLQK-------NH 431
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDtLSPGKLQALRRDIQFIFQDpyasldpRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IFNGTIEENIRygnVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10261 419 TVGDSIMEPLR---VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170
....*....|....*..
gi 2534190046 512 AIATEQIKNSLDAIKKD 528
Cdd:PRK10261 496 VSIRGQIINLLLDLQRD 512
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
347-511 |
5.00e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQ-FLRDNIGL 425
Cdd:PRK10575 12 FALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNGTIEENI------------RYGnvnatfeeiedAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIA 491
Cdd:PRK10575 91 PQQLPAAEGMTVRELVaigrypwhgalgRFG-----------AADREKVEEAIslVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180
....*....|....*....|
gi 2534190046 492 RMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALD 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
358-559 |
6.30e-14 |
|
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: 70.63 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKF--YQPDSGKILLDGIDLEEYDTQ-FLRDNIGLVLQKNHIFN 434
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARLGIFLAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 435 G-TIEENIRYgnVNATFeeiedaakrayiheqimdlpegyqskalllSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:cd03217 91 GvKNADFLRY--VNEGF------------------------------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2534190046 514 ATEQIKNSLDAIKKDRT---VIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:cd03217 139 ALRLVAEVINKLREEGKsvlIITHYQRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
351-510 |
6.63e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.38 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 351 NVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE--------EYDTQFLRDN 422
Cdd:PRK10982 3 NISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFN----------GTIEENIRYGNVNATFEEiedaakrayiheqiMDLPEGYQSKALLLSGGQQQRIAIAR 492
Cdd:PRK10982 82 LNLVLQRSVMDNmwlgryptkgMFVDQDKMYRDTKAIFDE--------------LDIDIDPRAKVATLSVSQMQMIEIAK 147
|
170
....*....|....*...
gi 2534190046 493 MFLKNPPIIFLDEPTASL 510
Cdd:PRK10982 148 AFSYNAKIVIMDEPTSSL 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
348-559 |
7.79e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 71.64 E-value: 7.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSyPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLL--DKFYQPDSGKILLDGIDLEEYDT-QFLRDNIG 424
Cdd:COG0396 2 EIKNLHVS-VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPdERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQ--------KNHIFNGTIEENIRYGNVNATF--EEIEDAAKRayiheqiMDLPEGYQSKALL--LSGGQQQRIAIAR 492
Cdd:COG0396 81 LAFQypveipgvSVSNFLRTALNARRGEELSAREflKLLKEKMKE-------LGLDEDFLDRYVNegFSGGEKKRNEILQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIK-KDRTVIII--SHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:COG0396 154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIIthYQRILDYIKPDFVHVLVDGRIVKSG 223
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
350-564 |
9.33e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 71.08 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 350 QNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDT-QFLRDNIGLVLQ 428
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 429 KNHIFngtiEENIRYGNVNATFEEIED--AAKRAYIHEQIMD---LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:PRK10895 86 EASIF----RRLSVYDNLMAVLQIRDDlsAEQREDRANELMEefhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 504 DEPTASLDAIATEQIKNSLDAIkKDRTVIIISHSISQIIDADY---TYVMKQGEVVEHGIHEDV 564
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVcerAYIVSQGHLIAHGTPTEI 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
348-511 |
9.69e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 9.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSyPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVL 427
Cdd:PRK10247 9 QLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHIFNGTIEENIRYgnvnaTFEEIEDAAKRAYIHEQIM--DLPEGYQSKAL-LLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:PRK10247 88 QTPTLFGDTVYDNLIF-----PWQIRNQQPDPAIFLDDLErfALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLD 162
|
....*..
gi 2534190046 505 EPTASLD 511
Cdd:PRK10247 163 EITSALD 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
214-573 |
1.03e-13 |
|
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: 74.60 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 214 IINSITVIKSFNREDIEGKKQLDLQKEltnnQMQTRKTSFFFDGLKSFI---EQFgVVIIIILTSYLVLDGQMTIGA--S 288
Cdd:TIGR00957 502 ILNGIKVLKLYAWELAFLDKVEGIRQE----ELKVLKKSAYLHAVGTFTwvcTPF-LVALITFAVYVTVDENNILDAekA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 289 MFHILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYIPTKLKGKFEI--QNVEFSYPNGYK-ALKN 365
Cdd:TIGR00957 577 FVSLALFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNSItvHNATFTWARDLPpTLNG 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 366 INMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdNIGLVLQKNHIFNGTIEENIRYG- 444
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGk 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 445 --NVNATFEEIEDAAKRAyiheQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:TIGR00957 724 alNEKYYQQVLEACALLP----DLEILPSGDRTeigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 519 KNSL---DAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKE 573
Cdd:TIGR00957 800 FEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAE 857
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
360-511 |
1.10e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 360 YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDL-------------EEYDTQFLRDNIGLV 426
Cdd:PRK10619 18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIFNG-TIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSK-ALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:PRK10619 98 FQHFNLWSHmTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
....*..
gi 2534190046 505 EPTASLD 511
Cdd:PRK10619 178 EPTSALD 184
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
31-309 |
1.46e-13 |
|
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: 71.36 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 31 GSFTSQVNALILQYTVDSINGlveagKGLKEGLKIISFISIVLMtkeILNAFITFGQKYY----GEKlrilVSQDLAQTI 106
Cdd:cd18576 8 SSAIGLVFPLLAGQLIDAALG-----GGDTASLNQIALLLLGLF---LLQAVFSFFRIYLfarvGER----VVADLRKDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 107 IEKILTYRMAFYtnQDNQAGKLQTRIDRGIEsltrLVQNFFIDILPLFANSIV----ALILMFNANFYVGLVGLCIVPIY 182
Cdd:cd18576 76 YRHLQRLPLSFF--HERRVGELTSRLSNDVT----QIQDTLTTTLAEFLRQILtligGVVLLFFISWKLTLLMLATVPVV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 183 FIITqqqakKLSGRR-RNL-RGYREQ--KSQGIIS-IINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDG 257
Cdd:cd18576 150 VLVA-----VLFGRRiRKLsKKVQDElaEANTIVEeTLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSS 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 258 LKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIY 309
Cdd:cd18576 225 FIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLY 276
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
347-520 |
1.66e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYqPD---SGKILLDGIDLEEY---DTQflR 420
Cdd:PRK13549 6 LEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASnirDTE--R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DNIGLVLQK-NHIFNGTIEENIRYGNvnatfeEIEdaakrayiHEQIMDLPEGYQ-SKALL---------------LSGG 483
Cdd:PRK13549 82 AGIAIIHQElALVKELSVLENIFLGN------EIT--------PGGIMDYDAMYLrAQKLLaqlkldinpatpvgnLGLG 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534190046 484 QQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKN 520
Cdd:PRK13549 148 QQQLVEIAKALNKQARLLILDEPTASLTESETAVLLD 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
349-511 |
2.05e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKIlldgidleEYDTQfLRdnIGLVLQ 428
Cdd:PRK09544 7 LENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGK-LR--IGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 429 KNHI---FNGTIEENIRYgNVNATFEEIEDAAKR---AYIHEQIMDlpegyqskalLLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK09544 75 KLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRvqaGHLIDAPMQ----------KLSGGETQRVLLARALLNRPQLLV 143
|
....*....
gi 2534190046 503 LDEPTASLD 511
Cdd:PRK09544 144 LDEPTQGVD 152
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
348-518 |
3.03e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidlEEYDTQFLRDN----I 423
Cdd:PRK10762 6 QLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQK-NHIFNGTIEENI--------RYGNVN--ATFEEIEDAAKRayiheqimdLPEGYQSKALL--LSGGQQQRIAI 490
Cdd:PRK10762 82 GIIHQElNLIPQLTIAENIflgrefvnRFGRIDwkKMYAEADKLLAR---------LNLRFSSDKLVgeLSIGEQQMVEI 152
|
170 180
....*....|....*....|....*...
gi 2534190046 491 ARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESL 180
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
358-528 |
3.05e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.04 E-value: 3.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS---GKILLDGIDLEEY-----DTQFLRDNIGLVLQK 429
Cdd:PRK09984 15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTGYIFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 NHIFNG-TIEENIRYGNVNAT---------FEEIEDaaKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK09984 95 FNLVNRlSVLENVLIGALGSTpfwrtcfswFTREQK--QRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAK 172
|
170 180
....*....|....*....|....*....
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKD 528
Cdd:PRK09984 173 VILADEPIASLDPESARIVMDTLRDINQN 201
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
40-309 |
3.60e-13 |
|
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: 70.33 E-value: 3.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDSingLVEAGKGLKEGlkiiSFISIVLMtkeilnAFITFGQKYYGEKLRIL---VSQ----DLAQTIIEKILT 112
Cdd:cd18560 17 LFLGRAVNA---LTLAKVKDLES----AVTLILLY------ALLRFSSKLLKELRSLLyrrVQQnayrELSLKTFAHLHS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 113 YRMAFYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVA-LILMFNANFYVGLVGLCIVPIYFIITqqqaK 191
Cdd:cd18560 84 LSLDWHLS--KKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVsVVFAFHFGAWLALIVFLSVLLYGVFT----I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 192 KLSGRRRNLR---GYREQKSQGII--SIINSITViKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFG 266
Cdd:cd18560 158 KVTEWRTKFRraaNKKDNEAHDIAvdSLLNFETV-KYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2534190046 267 VVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIY 309
Cdd:cd18560 237 LTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIY 279
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
347-512 |
4.26e-13 |
|
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: 71.89 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILL-DGIdleeydtqflrdNIGL 425
Cdd:TIGR03719 5 YTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI------------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHI-FNGTIEENI------------RYGNVNATFEEIED-----AAKRAYIHEQI---------------MD---L 469
Cdd:TIGR03719 73 LPQEPQLdPTKTVRENVeegvaeikdaldRFNEISAKYAEPDAdfdklAAEQAELQEIIdaadawdldsqleiaMDalrC 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2534190046 470 PEGyQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:TIGR03719 153 PPW-DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
358-531 |
4.88e-13 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 68.03 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflRDNIGLVLQKNHI---FN 434
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 435 GTIEENIRYGnvnaTFEEIE-----DAAKRAYIHEQIMDLP-EGYQSKAL-LLSGGQQQRIAIARMFLKNPPIIFLDEPT 507
Cdd:NF040873 72 LTVRDLVAMG----RWARRGlwrrlTRDDRAAVDDALERVGlADLAGRQLgELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180
....*....|....*....|....*
gi 2534190046 508 ASLDAIATEQIKNSLDAIKKD-RTV 531
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARgATV 172
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
363-518 |
6.34e-13 |
|
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: 67.65 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLD--KFYQPDSGKILLDGIDLEEYdtqFLRdNIGLVLQKN-HIFNGTIEE 439
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKN---FQR-STGYVEQQDvHSPNLTVRE 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 440 NIRYgnvnatfeeieDAAKRAyiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:cd03232 99 ALRF-----------SALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
348-559 |
6.34e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.41 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFL---RDNIG 424
Cdd:PRK11831 9 DMRGVSFTRGN-RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNG-TIEENIRYGNVNATfeeiedAAKRAYIHEQIMDLPE--GYQSKALL----LSGGQQQRIAIARMFLKN 497
Cdd:PRK11831 88 MLFQSGALFTDmNVFDNVAYPLREHT------QLPAPLLHSTVMMKLEavGLRGAAKLmpseLSGGMARRAALARAIALE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHG 559
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSAlgvTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
115-310 |
8.99e-13 |
|
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: 69.05 E-value: 8.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 115 MAFYTNqdNQAGKLQTRIDRGIESLTRLVQ----NFFIDILPLfansIVALILMFNANFYVGLVGLCIVPIYFIITqqqa 190
Cdd:cd18546 87 LDFHER--ETSGRIMTRMTSDIDALSELLQtglvQLVVSLLTL----VGIAVVLLVLDPRLALVALAALPPLALAT---- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 191 kkLSGRRRNLRGYREQKSQgiISIINS--------ITVIKSFNRED--IEGKKQLDLQKELTNNQMQtRKTSFFFDGLKs 260
Cdd:cd18546 157 --RWFRRRSSRAYRRARER--IAAVNAdlqetlagIRVVQAFRRERrnAERFAELSDDYRDARLRAQ-RLVAIYFPGVE- 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534190046 261 FIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIYD 310
Cdd:cd18546 231 LLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFD 280
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
346-511 |
9.19e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 9.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGL 425
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKNHIFNGTIEENIRYGN---VNATFEEIEDAAKRAYIHEQIMDLPegyqskallLSGGQQQRIAIARMFLKNPPIIF 502
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKPANpalVEKWLERLKMAHKLELEDGRISNLK---------LSKGQKKRLALLLALAEERDILL 472
|
....*....
gi 2534190046 503 LDEPTASLD 511
Cdd:PRK10522 473 LDEWAADQD 481
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
265-512 |
9.67e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 9.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 265 FGVVIIIILTSYLvlDGQMTIGAsmfhILLFNNVSAPIRQLHRIYDEMNDAMIYSESFFAILKADDEKESSGNYIPTKLK 344
Cdd:TIGR00956 681 FFFFVYILLTEFN--KGAKQKGE----ILVFRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKE 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GK---FEIQNVefSYPNGYKA-----LKNINMTIQPNKITALVGLSGAGKSTvinLLDKFYQPDSGKILLDGIDL---EE 413
Cdd:TIGR00956 755 SGediFHWRNL--TYEVKIKKekrviLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLvngRP 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 414 YDTQFLRdNIGLVLQKN-HIFNGTIEENIRYGNVNATFEEIEDAAKRAYIhEQIMDLPEGYQSK-ALL------LSGGQQ 485
Cdd:TIGR00956 830 LDSSFQR-SIGYVQQQDlHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYV-EEVIKLLEMESYAdAVVgvpgegLNVEQR 907
|
250 260
....*....|....*....|....*...
gi 2534190046 486 QRIAIARMFLKNPP-IIFLDEPTASLDA 512
Cdd:TIGR00956 908 KRLTIGVELVAKPKlLLFLDEPTSGLDS 935
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
347-511 |
1.28e-12 |
|
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: 66.02 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKIlldgIDLEEYDTQFLRdniglv 426
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----GMPEGEDLLFLP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 lQKNHIFNGTIEENIRYgnvnaTFEEIedaakrayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEP 506
Cdd:cd03223 71 -QRPYLPLGTLREQLIY-----PWDDV--------------------------LSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
....*
gi 2534190046 507 TASLD 511
Cdd:cd03223 119 TSALD 123
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
349-513 |
1.33e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEY--DTQFL----R-- 420
Cdd:PRK11247 15 LNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAreDTRLMfqdaRll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 ------DNIGLVLQknhifngtieeniryGNVNATFEEIEDA---AKRAyiheqiMDLPEGyqskallLSGGQQQRIAIA 491
Cdd:PRK11247 94 pwkkviDNVGLGLK---------------GQWRDAALQALAAvglADRA------NEWPAA-------LSGGQKQRVALA 145
|
170 180
....*....|....*....|..
gi 2534190046 492 RMFLKNPPIIFLDEPTASLDAI 513
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDAL 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
347-524 |
1.66e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDN---- 422
Cdd:COG3845 258 LEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 -------IGLVLqknhifNGTIEENI-----------RYGNVNatFEEIEDAAKRayiheqIMD----LPEGYQSKALLL 480
Cdd:COG3845 338 ipedrlgRGLVP------DMSVAENLilgryrrppfsRGGFLD--RKAIRAFAEE------LIEefdvRTPGPDTPARSL 403
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2534190046 481 SGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDA 524
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE 447
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
349-565 |
2.05e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeydtQFLRDN-IGLVL 427
Cdd:PRK15056 9 VNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QKNHI---FNGTIEENI---RYGNVNatFEEIEDAAKRAYIHEQI--MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK15056 85 QSEEVdwsFPVLVEDVVmmgRYGHMG--WLRRAKKRDRQIVTAALarVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKD-RTVIIISHSISQIID-ADYTyVMKQGEVVEHGIHEDVY 565
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEfCDYT-VMVKGTVLASGPTETTF 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
361-522 |
2.08e-12 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 69.83 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILL-----------DGIDLEEYDTQFlrdnIGLVLQK 429
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkPGPDGRGRAKRY----IGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 NHIF-NGTIEENIrygnVNATFEEIED--AAKRAYIHEQIMDLPEGYQSKAL-----LLSGGQQQRIAIARMFLKNPPII 501
Cdd:TIGR03269 374 YDLYpHRTVLDNL----TEAIGLELPDelARMKAVITLKMVGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEPRIV 449
|
170 180
....*....|....*....|.
gi 2534190046 502 FLDEPTASLDAIATEQIKNSL 522
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSI 470
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
98-317 |
2.62e-12 |
|
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: 67.91 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 98 VSQD----LAQTIIEKILTYRMAFYTNQdnQAGKLQTRIDRGIESLTRLVQNFFIDILPLFAN-SIVALILMFNANFYVG 172
Cdd:cd18582 65 VSQRavrrLALRVFRHLHSLSLRFHLSR--KTGALSRAIERGTRGIEFLLRFLLFNILPTILElLLVCGILWYLYGWSYA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 173 LVGLCIVPIYFIITQqqakKLSGRRRNLRGYR---EQKSQGII--SIINSITViKSFNREDIEGKKQLDLQKELTNNQMQ 247
Cdd:cd18582 143 LITLVTVALYVAFTI----KVTEWRTKFRREMneaDNEANAKAvdSLLNYETV-KYFNNEEYEAERYDKALAKYEKAAVK 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 248 TRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGA-SMFHILLFnNVSAPIRQLHRIYDEMNDAMI 317
Cdd:cd18582 218 SQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDfVLVNTYLL-QLYQPLNFLGFVYREIRQSLI 287
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
364-512 |
2.70e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 68.52 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 364 KNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeyDTQFLRDNIGLVLQKNHIF-NGTIEENIR 442
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYpHLSVAENMS 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 443 YGNVNAtfeeiedAAKRAYIHEQIMDLPEGYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:PRK11000 98 FGLKLA-------GAKKEEINQRVNQVAEVLQLAHLLdrkpkaLSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
40-305 |
3.43e-12 |
|
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: 67.43 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDSI-NGLVEAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYygekLRILVSQDLAQTI----IEKILTYR 114
Cdd:cd18547 20 YLLGKAIDLIiEGLGGGGGVDFSGLLRILLLLLGLY---LLSALFSYLQNR----LMARVSQRTVYDLrkdlFEKLQRLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 115 MAFYTNqdNQAGKLQTRI--DrgIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITqqqaKK 192
Cdd:cd18547 93 LSYFDT--HSHGDIMSRVtnD--VDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVT----KF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 193 LSGRRRNLrgYREQ-KSQGIIS-----IINSITVIKSFNREDiEGKKQLDlqkELTNNQMQTRKTSFFFDGL----KSFI 262
Cdd:cd18547 165 IAKRSQKY--FRKQqKALGELNgyieeMISGQKVVKAFNREE-EAIEEFD---EINEELYKASFKAQFYSGLlmpiMNFI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2534190046 263 EQFGVVIIIILTSYLVLDGQMTIGA-SMFhILLFNNVSAPIRQL 305
Cdd:cd18547 239 NNLGYVLVAVVGGLLVINGALTVGViQAF-LQYSRQFSQPINQI 281
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
347-527 |
3.44e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNgYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLV 426
Cdd:PRK13540 2 LDVIELDFDYHD-QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHIF-NGTIEENIRYG-NVNATFEEIEDAAkRAYIHEQIMDLPEGyqskalLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:PRK13540 80 GHRSGINpYLTLRENCLYDiHFSPGAVGITELC-RLFSLEHLIDYPCG------LLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170 180
....*....|....*....|...
gi 2534190046 505 EPTASLDAIATEQIKNSLDAIKK 527
Cdd:PRK13540 153 EPLVALDELSLLTIITKIQEHRA 175
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
40-305 |
4.08e-12 |
|
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: 67.44 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDSI---NGLVEAGKglKEGLKIISFISIVLMTkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMA 116
Cdd:cd18554 20 LILKYIVDDViqgSSLTLDEK--VYKLFTIIGIMFFIFL--ILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQ---QQAKKL 193
Cdd:cd18554 96 YYAN--NRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKyffGRLRKL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 194 SGRRRN----LRGYREQKSQGiisiinsITVIKSFNREDIEgKKQLD--LQKELTNNQMQTRKTSFFFDGLKSFIEqFGV 267
Cdd:cd18554 174 TKERSQalaeVQGFLHERIQG-------MSVIKSFALEKHE-QKQFDkrNGHFLTRALKHTRWNAKTFSAVNTITD-LAP 244
|
250 260 270
....*....|....*....|....*....|....*...
gi 2534190046 268 VIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQL 305
Cdd:cd18554 245 LLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRL 282
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
78-305 |
4.29e-12 |
|
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: 67.07 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNqdNQAGKLQTRI--DrgieslTRLVQNFFIDILPLFA 155
Cdd:cd18551 47 LLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDR--RRSGDLVSRVtnD------TTLLRELITSGLPQLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 156 NSIV----ALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRrrnlrGYREQKSQGIIS-----IINSITVIKSFNR 226
Cdd:cd18551 119 TGVLtvvgAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKA-----SKRAQDALGELSaalerALSAIRTVKASNA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 227 EDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQL 305
Cdd:cd18551 194 EERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQL 272
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
363-512 |
4.83e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLdKFYQPD----SGKILLDGIDLeeyDTQFLRDNIGLVLQKNhIFNG--T 436
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDD-LFIPtlT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 437 IEENIrygNVNATFEEIEDAA---KRAYIHEQIMDLpeGYQSKALL----------LSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:TIGR00955 116 VREHL---MFQAHLRMPRRVTkkeKRERVDEVLQAL--GLRKCANTrigvpgrvkgLSGGERKRLAFASELLTDPPLLFC 190
|
....*....
gi 2534190046 504 DEPTASLDA 512
Cdd:TIGR00955 191 DEPTSGLDS 199
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
363-521 |
9.13e-12 |
|
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: 66.03 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdNIGLVLQKNHIFNGTIEENIR 442
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 443 YGnvnATFEEI--EDAAKRAYIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATE 516
Cdd:cd03291 120 FG---VSYDEYryKSVVKACQLEEDITKFPEKDNTvlgeGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
....*
gi 2534190046 517 QIKNS 521
Cdd:cd03291 197 EIFES 201
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
32-294 |
9.82e-12 |
|
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: 65.99 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 32 SFTSQVNALIL----QYTVDSINGlveagkglKEGLKIISFISIVLMTKEILNAFITFGQKYYGEKLRILVSQDLAQTII 107
Cdd:cd18555 11 SLLLQLLTLLIpiltQYVIDNVIV--------PGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 108 EKILTYRMAFYTNqdNQAGKLQTRID-----RGIesLTRLVQNFFIDILPLfansIVALILMFNANFYVGLVGLCIVPIY 182
Cdd:cd18555 83 EHLLKLPYSFFEN--RSSGDLLFRANsnvyiRQI--LSNQVISLIIDLLLL----VIYLIYMLYYSPLLTLIVLLLGLLI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 183 FIITQQQAKKLsgRRRNLRGYREQ-KSQGIIS-IINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKS 260
Cdd:cd18555 155 VLLLLLTRKKI--KKLNQEEIVAQtKVQSYLTeTLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISS 232
|
250 260 270
....*....|....*....|....*....|....*
gi 2534190046 261 FIEQFGVVIIIILTSYLVLDGQMTIGASM-FHILL 294
Cdd:cd18555 233 SIQFIAPLLILWIGAYLVINGELTLGELIaFSSLA 267
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-507 |
1.04e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKSTVINLLdkF--YQPDSGKILLDGidlEEYDTQFLRDNI--------------G 424
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIRSPRDAIragiayvpedrkgeG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKnhifngTIEENI---------RYGNVNATfEEIEDAAKraYIHEqiMDL-PEGYQSKALLLSGGQQQRIAIARMF 494
Cdd:COG1129 341 LVLDL------SIRENItlasldrlsRGGLLDRR-RERALAEE--YIKR--LRIkTPSPEQPVGNLSGGNQQKVVLAKWL 409
|
170
....*....|...
gi 2534190046 495 LKNPPIIFLDEPT 507
Cdd:COG1129 410 ATDPKVLILDEPT 422
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
158-598 |
1.17e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 68.23 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 158 IVALILMFN----ANFYVGLVGLCIVPIY-FIITQQQakKLSgrRRNLRgyREQKSQGIIS-IINSITVIKSFNRED-IE 230
Cdd:PLN03130 429 IIAMVLLYQqlgvASLIGSLMLVLMFPIQtFIISKMQ--KLT--KEGLQ--RTDKRIGLMNeVLAAMDTVKCYAWENsFQ 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 231 GKKQLDLQKELTnnqmQTRKTSFFfDGLKSFIEQFGVVIIIILT--SYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRI 308
Cdd:PLN03130 503 SKVQTVRDDELS----WFRKAQLL-SAFNSFILNSIPVLVTVVSfgVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNL 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 309 YDEMNDAMIYSESFFAILKADDEKESSGNYIPTKLKGkFEIQNVEFSY--PNGYKALKNINMTIQPNKITALVGLSGAGK 386
Cdd:PLN03130 578 ITQAVNANVSLKRLEELLLAEERVLLPNPPLEPGLPA-ISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGK 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 387 STVINLLDKFYQPDSGKILLdgidleeydtqfLRDNIGLVLQKNHIFNGTIEENIRYGnvnATFE--EIEDAAKRAYIHE 464
Cdd:PLN03130 657 TSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFG---SPFDpeRYERAIDVTALQH 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 465 QIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSldAIK---KDRTVIIISHS 537
Cdd:PLN03130 722 DLDLLPGGDLTeigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDK--CIKdelRGKTRVLVTNQ 799
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 538 ISQIIDADYTYVMKQGEVVEHGIHEDVYKMNGTYKEIfdaMAKSLNIEKIAKTFDDEEEEN 598
Cdd:PLN03130 800 LHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL---MENAGKMEEYVEENGEEEDDQ 857
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
78-316 |
1.30e-11 |
|
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: 65.58 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFytnQDN-QAGKLqtrIDRGIESLtRLVQNFFIDILPLFAN 156
Cdd:cd18543 50 VAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAF---HDRwQSGQL---LSRATSDL-SLVQRFLAFGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 157 S---IVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRnlrgyREQKSQGIISI-----INSITVIKSFNRED 228
Cdd:cd18543 123 LltlVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASR-----RAQDQAGDLATvveesVTGIRVVKAFGRER 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 229 IEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRI 308
Cdd:cd18543 198 RELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWL 277
|
....*...
gi 2534190046 309 YDEMNDAM 316
Cdd:cd18543 278 LAMAQRAR 285
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
362-566 |
1.54e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.19 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKS-TVINLLDKFYQP----DSGKILL-----DGIDLEEYDTQFLRD----NIGLVL 427
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLrrrsrQVIELSEQSAAQMRHvrgaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 428 QK-----NHIF--NGTIEENIRYgNVNATFEEIEDAAKRayiheqIMDLPEGYQSKALL------LSGGQQQRIAIARMF 494
Cdd:PRK10261 111 QEpmtslNPVFtvGEQIAESIRL-HQGASREEAMVEAKR------MLDQVRIPEAQTILsryphqLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT--VIIISHSISQIID-ADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQIFH 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
364-565 |
1.72e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 64.72 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 364 KNINMTIQPNKITALVGLSGAGKS----TVINLLDKFYQPDSGKILLDGIDLEEYDtqfLRD-NIGLVLQK-NHIFNG-- 435
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCA---LRGrKIATIMQNpRSAFNPlh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEENIRYgNVNATFEEIEDAAKRAYIHEQIMDLPEGY-QSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:PRK10418 97 TMHTHARE-TCLALGKPADDATLTAALEAVGLENAARVlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 515 TEQIKNSLDAIKKDRTViiisHSISQIID-------ADYTYVMKQGEVVEHGIHEDVY 565
Cdd:PRK10418 176 QARILDLLESIVQKRAL----GMLLVTHDmgvvarlADDVAVMSHGRIVEQGDVETLF 229
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
40-286 |
3.34e-11 |
|
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: 64.35 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDSINglveAGKGLKEGLKIISFIsIVLMTkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYt 119
Cdd:cd18541 20 RIIGRAIDALT----AGTLTASQLLRYALL-ILLLA--LLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFY- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 120 nQDNQAGKLQTRIDRGIESLTRLVQ---NFFIDILPLFansIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGR 196
Cdd:cd18541 92 -QKNRTGDLMARATNDLNAVRMALGpgiLYLVDALFLG---VLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 197 rrnlrgYRE-QKSQGIIS-----IINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVII 270
Cdd:cd18541 168 ------FRKvQEAFSDLSdrvqeSFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIV 241
|
250
....*....|....*.
gi 2534190046 271 IILTSYLVLDGQMTIG 286
Cdd:cd18541 242 LWYGGRLVIRGTITLG 257
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
348-505 |
3.80e-11 |
|
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: 65.59 E-value: 3.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPN-----GYkALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDN 422
Cdd:COG4615 329 ELRGVTYRYPGedgdeGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNGTIEENirygnvnatfEEIEDAAKRAYIHEqiMDLPE--GYQSKALL---LSGGQQQRIAIARMFLKN 497
Cdd:COG4615 408 FSAVFSDFHLFDRLLGLD----------GEADPARARELLER--LELDHkvSVEDGRFSttdLSQGQRKRLALLVALLED 475
|
....*...
gi 2534190046 498 PPIIFLDE 505
Cdd:COG4615 476 RPILVFDE 483
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
358-522 |
4.61e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 358 NGYKALKNINMTIQPNKITALVGLSGAGKSTVI----NLLDKFYQPdSGKILLDGIDLEEYDTQFLRDNIGLVLQKNHIF 433
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSV-EGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 434 NGTIEENIrygnvnatfeeieDAAKRAYIHEQImdlpEGyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:cd03233 97 TLTVRETL-------------DFALRCKGNEFV----RG-------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
....*....
gi 2534190046 514 ATEQIKNSL 522
Cdd:cd03233 153 TALEILKCI 161
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
354-522 |
5.27e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 354 FSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKIL--------------LDGIDLeeydtqfl 419
Cdd:PLN03073 516 FGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrmavfsqhhVDGLDL-------- 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 rdNIGLVLQKNHIFNGTIEENIR--YGNVNATfeeiedaakrAYIHEQIMdlpegyqskaLLLSGGQQQRIAIARMFLKN 497
Cdd:PLN03073 588 --SSNPLLYMMRCFPGVPEQKLRahLGSFGVT----------GNLALQPM----------YTLSGGQKSRVAFAKITFKK 645
|
170 180
....*....|....*....|....*
gi 2534190046 498 PPIIFLDEPTASLDAIATEQIKNSL 522
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALIQGL 670
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
348-525 |
5.38e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpnGYKALKN-INMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEyDTQFLRDNIGLV 426
Cdd:PRK13536 43 DLAGVSKSY--GDKAVVNgLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHI-FNGTIEENI----RYGNVNAtfEEIEDAAKRAYiheQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK13536 120 PQFDNLdLEFTVRENLlvfgRYFGMST--REIEAVIPSLL---EFARLESKADARVSDLSGGMKRRLTLARALINDPQLL 194
|
170 180
....*....|....*....|....
gi 2534190046 502 FLDEPTASLDAIATEQIKNSLDAI 525
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSL 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
363-518 |
5.44e-11 |
|
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: 66.09 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdNIGLVLQKNHIFNGTIEENIR 442
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 443 YGnvnATFEEIE--DAAKRAYIHEQIMDLPEgyQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIA 514
Cdd:TIGR01271 509 FG---LSYDEYRytSVIKACQLEEDIALFPE--KDKTVLgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
....
gi 2534190046 515 TEQI 518
Cdd:TIGR01271 584 EKEI 587
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
345-511 |
5.64e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GK--FEIQNVEFSYPnGYKALKNINMTIQP-NKItALVGLSGAGKSTVINLLDKFYQPDSGKILLdGIDLE-EYDTQFLR 420
Cdd:PRK11147 316 GKivFEMENVNYQID-GKQLVKDFSAQVQRgDKI-ALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEvAYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 421 DnigLVLQKnhifngTIEENIRYGNvnatfEEIEDAAKRAYIHEQIMDL---PEGYQSKALLLSGGQQQRIAIARMFLKN 497
Cdd:PRK11147 393 E---LDPEK------TVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPVKALSGGERNRLLLARLFLKP 458
|
170
....*....|....
gi 2534190046 498 PPIIFLDEPTASLD 511
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
363-511 |
1.11e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYqPDSGKILLDGIDLEEYDTQFLRDNIG-LVLQKNHIFNGTIEENI 441
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAyLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 442 R-YGNVNATFEEIEDAakrayiheqIMDLPEGYQSKALL------LSGGQQQRIAIARMFLK-----NPP--IIFLDEPT 507
Cdd:COG4138 91 AlHQPAGASSEAVEQL---------LAQLAEALGLEDKLsrpltqLSGGEWQRVRLAAVLLQvwptiNPEgqLLLLDEPM 161
|
....
gi 2534190046 508 ASLD 511
Cdd:COG4138 162 NSLD 165
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
369-519 |
1.11e-10 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 62.04 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 369 TIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEeYDTQFLRDNiglvlqknhiFNGTIEENIrygnvna 448
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKAD----------YEGTVRDLL------- 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 449 tFEEIEDAAKRAYIHEQIMD---LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA----IATEQIK 519
Cdd:cd03237 83 -SSITKDFYTHPYFKTEIAKplqIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIR 159
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
359-526 |
1.12e-10 |
|
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: 64.08 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 359 GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS--GKILLDGidlEEYDTQFLRDN----IGLVLQK-NH 431
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSG---SPLKASNIRDTeragIVIIHQElTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 IFNGTIEENIRYGNvnatfeEIEDAAKRayiheqiMDLPEGY-QSKALL----------------LSGGQQQRIAIARMF 494
Cdd:TIGR02633 90 VPELSVAENIFLGN------EITLPGGR-------MAYNAMYlRAKNLLrelqldadnvtrpvgdYGGGQQQLVEIAKAL 156
|
170 180 190
....*....|....*....|....*....|..
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIknsLDAIK 526
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEIL---LDIIR 185
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
78-286 |
1.51e-10 |
|
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: 62.50 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYY----GEKlrilVSQDLAQTIIEKILTYRMAFYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPL 153
Cdd:cd18550 50 VASALLGVVQTYLsariGQG----VMYDLRVQLYAHLQRMSLAFFTR--TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSN 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 154 FANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKklsgRRRNLRGYREQKSQGIISIINS------ITVIKSFNRE 227
Cdd:cd18550 124 VVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGR----RRRKLTREQQEKLAELNSIMQEtlsvsgALLVKLFGRE 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 228 DIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIG 286
Cdd:cd18550 200 DDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIG 258
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
347-512 |
2.20e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNGYKALKNINMTIQPN-KItALVGLSGAGKSTVINL---LDKFYQPDSgkILLDGIdleeydtqflrdN 422
Cdd:PRK11819 7 YTMNRVSKVVPPKKQILKDISLSFFPGaKI-GVLGLNGAGKSTLLRImagVDKEFEGEA--RPAPGI------------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQKNHIFNG-TIEENI------------RYGNVNATFEEIED-----AAKRAYIHEQI---------------MD- 468
Cdd:PRK11819 72 VGYLPQEPQLDPEkTVRENVeegvaevkaaldRFNEIYAAYAEPDAdfdalAAEQGELQEIIdaadawdldsqleiaMDa 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534190046 469 --LPEGyQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:PRK11819 152 lrCPPW-DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
348-514 |
2.27e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 62.13 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpnGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYdTQFLRDNIGLV 426
Cdd:PRK13537 9 DFRNVEKRY--GDKlVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-ARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 427 LQKNHI---FngTIEENIRygnVNATFEEIEDAAKRAYIHE--QIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPII 501
Cdd:PRK13537 86 PQFDNLdpdF--TVRENLL---VFGRYFGLSAAAARALVPPllEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170
....*....|...
gi 2534190046 502 FLDEPTASLDAIA 514
Cdd:PRK13537 161 VLDEPTTGLDPQA 173
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
59-290 |
2.41e-10 |
|
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: 62.08 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 59 LKEGLKIISFISIVLMtkeILNAFITFGQKYY----GEKLrilvSQDLAQTIIEKILTYRMAFYTNQDNQAGKLQTRIDR 134
Cdd:cd18578 47 LRSEANFWALMFLVLA---IVAGIAYFLQGYLfgiaGERL----TRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLST 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 135 GIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLRGYREQKSQGIISI 214
Cdd:cd18578 120 DASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEA 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 215 INSITVIKSFNRED-IEGKKQLDLQKELTNNQMQTRKTSFFFdGLKSFIEQFGVVIIIILTSYLVLDGQMTIgASMF 290
Cdd:cd18578 200 VSNIRTVASLTLEDyFLEKYEEALEEPLKKGLRRALISGLGF-GLSQSLTFFAYALAFWYGGRLVANGEYTF-EQFF 274
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
338-511 |
2.60e-10 |
|
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: 63.03 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 338 YIPT--KLKGK-FEIQNVEFSYpnGYKAL-KNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILL-DGIDLE 412
Cdd:TIGR03719 311 YIPPgpRLGDKvIEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 413 EYDtQFlRDniGLVLQKN---HIFNGTieENIRYGNVnatfeeieDAAKRAYI-------HEQimdlpegyQSKALLLSG 482
Cdd:TIGR03719 389 YVD-QS-RD--ALDPNKTvweEISGGL--DIIKLGKR--------EIPSRAYVgrfnfkgSDQ--------QKKVGQLSG 446
|
170 180
....*....|....*....|....*....
gi 2534190046 483 GQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
363-518 |
5.17e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.87 E-value: 5.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDgidleeydtqflrDNIGLVLQKNHIFNGTIEENIR 442
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 443 YgnvnatFEEiEDAAKRA------YIHEQIMDLPEGYQS----KALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:PTZ00243 743 F------FDE-EDAARLAdavrvsQLEADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
....*.
gi 2534190046 513 IATEQI 518
Cdd:PTZ00243 816 HVGERV 821
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
348-510 |
5.67e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPnGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS--GKILLDGidlEEydTQF--LRD-- 421
Cdd:NF040905 3 EMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDG---EV--CRFkdIRDse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 422 NIGLVLQknH-----IFNGTIEENIRYGNV---------NATFEEIEDAAKRAYIHE----QIMDLpegyqskalllsG- 482
Cdd:NF040905 77 ALGIVII--HqelalIPYLSIAENIFLGNErakrgvidwNETNRRARELLAKVGLDEspdtLVTDI------------Gv 142
|
170 180
....*....|....*....|....*...
gi 2534190046 483 GQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
348-558 |
6.51e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.64 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNG---YKALKNINMTIQPNKITALVGLSGAGKS-TVINLLDKFYQPD----SGKILLDGIDLEEYDTQFL 419
Cdd:PRK15134 7 AIENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 420 R----DNIGLVLQKNHI-FN--GTIEENI-------RYGNVNATFEEIEDAAKRAYIHE---QIMDLPegYQskallLSG 482
Cdd:PRK15134 87 RgvrgNKIAMIFQEPMVsLNplHTLEKQLyevlslhRGMRREAARGEILNCLDRVGIRQaakRLTDYP--HQ-----LSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 483 GQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHS---ISQIIDADYTYVMKQGEVVEH 558
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFIThnlSIVRKLADRVAVMQNGRCVEQ 238
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
157-286 |
7.09e-10 |
|
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: 60.55 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 157 SIVALILMFNANFYVGLVGLCIVPIYFIItqqqakklsgRRRNLRGYREQKSQGIIS----------IINSITVIKSFNR 226
Cdd:cd18567 129 AILTLVMMFLYSPKLALIVLAAVALYALL----------RLALYPPLRRATEEQIVAsakeqshfleTIRGIQTIKLFGR 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 227 EDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIG 286
Cdd:cd18567 199 EAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVG 258
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
347-559 |
1.35e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.88 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKF--YQPDSGKILLDGIDLEEYDTQfLRDNIG 424
Cdd:CHL00131 8 LEIKNLHASV-NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQknhiFNGTIEENiryGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQ--SKALLL----------------SGGQQQ 486
Cdd:CHL00131 86 IFLA----FQYPIEIP---GVSNADFLRLAYNSKRKFQGLPELDPLEFLEiiNEKLKLvgmdpsflsrnvnegfSGGEKK 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 487 RIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID---ADYTYVMKQGEVVEHG 559
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDyikPDYVHVMQNGKIIKTG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-582 |
1.61e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.33 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 345 GKFEIQNVEFSYPNGYK-ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNI 423
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQKNHIFNGTIEENIRyGNVNATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL----LSGGQQQRIAIARMFLK-NP 498
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEggsnYSVGQRQLMCMARALLKkGS 1465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 499 PIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYkMNgtYKEIFDAM 578
Cdd:PTZ00243 1466 GFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV-MN--RQSIFHSM 1542
|
....
gi 2534190046 579 AKSL 582
Cdd:PTZ00243 1543 VEAL 1546
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
132-287 |
2.00e-09 |
|
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: 58.95 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 132 IDR-GIESL-TRL------VQNFFIDILPLFANS----IVALILMFNANFYVGLVGLCIVPIYFII------------TQ 187
Cdd:cd18548 90 IDKfGTSSLiTRLtndvtqVQNFVMMLLRMLVRApimlIGAIIMAFRINPKLALILLVAIPILALVvflimkkaiplfKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 188 QQAK--KLSGR-RRNLRGYReqksqgiisiinsitVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQ 264
Cdd:cd18548 170 VQKKldRLNRVvRENLTGIR---------------VIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMN 234
|
170 180
....*....|....*....|...
gi 2534190046 265 FGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18548 235 LAIVAILWFGGHLINAGSLQVGD 257
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
360-512 |
2.47e-09 |
|
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: 57.93 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 360 YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdNIGLVLQKNHIFNG--TI 437
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------RVSSLLGLGGGFNPelTG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 438 EENIRYgnvNATFEEIEDAAKRAYIHEQIM--DLPEGYQSKALLLSGGQQQRI--AIARMFlkNPPIIFLDEPTASLDA 512
Cdd:cd03220 102 RENIYL---NGRLLGLSRKEIDEKIDEIIEfsELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDA 175
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
364-555 |
2.92e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.68 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 364 KNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQfLRDNIGLVL-----QKNHIFngtIE 438
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVYlpedrQSSGLY---LD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRYGNVNATFEE----IEDAAKRAYI---HEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK15439 356 APLAWNVCALTHNRrgfwIKPARENAVLeryRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534190046 512 AIATEQIKNSLDAIKKDRTVIIISHSISQIID--ADYTYVMKQGEV 555
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEqmADRVLVMHQGEI 481
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
94-309 |
3.39e-09 |
|
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: 58.45 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 94 LRILVSQDLAQTIIEKILTYRMAF-------YTnQDNQAGKLQTRIDRGIESLtrlvQNFFIDILPLFANSIVALIL--- 163
Cdd:cd18561 55 LRERVAHRAAQRVKQHLRRRLFAKllklgpgYL-EGERTGELQTTVVDGVEAL----EAYYGRYLPQLLVALLGPLLili 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 164 -MFNANFYVGLVGLCIVPIYFI---ITQQQAKKLSgrRRNLRGYrEQKSQGIISIINSITVIKSFNREDIEGKKQLDLQK 239
Cdd:cd18561 130 yLFFLDPLVALILLVFALLIPLspaLWDRLAKDTG--RRHWAAY-GRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAE 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 240 ELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQLHRIY 309
Cdd:cd18561 207 DLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYW 276
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
371-511 |
4.95e-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: 57.38 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 371 QPNKITALVGLSGAGKSTVINLLD--------KFYQPDSGKILLD---GIDLEEYDTQFLRDNIGLVLQKNHI------F 433
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVdlipkaV 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 434 NGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:cd03236 104 KGKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQ----------LSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
363-531 |
6.19e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 6.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLL--DKFYQPDSGKILLDGIDLEEyDTqFLRdnIGLVLQKNHIFNG--TIE 438
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQ-ET-FAR--ISGYCEQNDIHSPqvTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 439 ENIRYGNVNATFEEIEDAAKRAYIhEQIMDLPEGYQSKALL--------LSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:PLN03140 972 ESLIYSAFLRLPKEVSKEEKMMFV-DEVMELVELDNLKDAIvglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*
gi 2534190046 511 D----AIATEQIKNSLDAikkDRTV 531
Cdd:PLN03140 1051 DaraaAIVMRTVRNTVDT---GRTV 1072
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
355-559 |
1.20e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 56.24 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 355 SYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGidleeydtqflrdNIGLVLQKNHIFN 434
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-------------RVSALLELGAGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 435 G--TIEENIR-----YG----NVNATFEEIEDAAKrayIHEQImDLPEGYqskallLSGGQQQRIAIARMFLKNPPIIFL 503
Cdd:COG1134 101 PelTGRENIYlngrlLGlsrkEIDEKFDEIVEFAE---LGDFI-DQPVKT------YSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 504 DEPTA---------SLDAIatEQIKN----------SLDAIKK--DRTViiishsisqiidadytyVMKQGEVVEHG 559
Cdd:COG1134 171 DEVLAvgdaafqkkCLARI--RELREsgrtvifvshSMGAVRRlcDRAI-----------------WLEKGRLVMDG 228
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
40-312 |
1.40e-08 |
|
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: 56.33 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 40 LILQYTVDSInglveAGKGLKEGLKIISFISIVLMtkeILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYt 119
Cdd:cd18540 23 LLTKYAIDHF-----ITPGTLDGLTGFILLYLGLI---LIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 120 NQdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITqqqakkLSGRRRN 199
Cdd:cd18540 94 DK-TPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVS------IYFQKKI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 200 LRGY---REQKSQgIISIIN-SIT---VIKSFNREDiegkKQLDLQKELTNNqMqtRKTSF-------FFDGLKSFIEQF 265
Cdd:cd18540 167 LKAYrkvRKINSR-ITGAFNeGITgakTTKTLVREE----KNLREFKELTEE-M--RRASVraarlsaLFLPIVLFLGSI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2534190046 266 GVVIIIILTSYLVLDGQMTIG---ASMFHILLFNNvsaPIRQLHRIYDEM 312
Cdd:cd18540 239 ATALVLWYGGILVLAGAITIGtlvAFISYATQFFE---PIQQLARVLAEL 285
|
|
| ABC_6TM_NHLM_bacteriocin |
cd18569 |
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ... |
78-305 |
1.41e-08 |
|
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: 56.33 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLRILVSQDLAQTIIEKILTYRMAFYTNQdnQAGKLQTRIdrgiESLTRLVQNFFIDILPLFANS 157
Cdd:cd18569 53 LLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQR--YAGDIASRV----QSNDRVANLLSGQLATTVLNL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 158 IVA---LILMFNANFYVGLVGLCIVPIYFIITqqqakKLSGRRR---NLRGYREQ-KSQGI-ISIINSITVIKSFNREDI 229
Cdd:cd18569 127 VMAvfyALLMLQYDVPLTLIGIAIALLNLLVL-----RLVSRKRvdlNRRLLQDSgKLTGTtMSGLQMIETLKASGAESD 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534190046 230 EGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASM-FHILLfNNVSAPIRQL 305
Cdd:cd18569 202 FFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVaFQSLM-ASFLAPVNSL 277
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
343-566 |
1.71e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 56.64 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 343 LKGKFEIQNVE---FSYPNGYKALKNINMTIQPNKITALVGLSGAGKST----VINLLdkfyQPDSGKILLDGIDLEEYD 415
Cdd:PRK15079 14 LKVHFDIKDGKqwfWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTfaraIIGLV----KATDGEVAWLGKDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 416 TQFLRD---NIGLVLQK-------NHIFNGTIEENIRYGNVNATFEEIEDAAK-------------RAYIHEqimdlpeg 472
Cdd:PRK15079 90 DDEWRAvrsDIQMIFQDplaslnpRMTIGEIIAEPLRTYHPKLSRQEVKDRVKammlkvgllpnliNRYPHE-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 473 yqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKK-----------DRTVIIIShsisqi 541
Cdd:PRK15079 162 -------FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemglslifiahDLAVVKHI------ 228
|
250 260
....*....|....*....|....*
gi 2534190046 542 idADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK15079 229 --SDRVLVMYLGHAVELGTYDEVYH 251
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
349-518 |
1.84e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.45 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQN--VEFSYPNGY-KALKNINMTIQPNKITALVGLSGAGKSTV----INLLDKFYQPDSGKILLDGIDL----EEYDTQ 417
Cdd:COG4170 6 IRNltIEIDTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIakaiCGITKDNWHVTADRFRWNGIDLlklsPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 FLRDNIGLVLQK--------NHIFNgTIEENIRYGNVNATFEEIEDAAKRAYI----------HEQIMDlpegyqSKALL 479
Cdd:COG4170 86 IIGREIAMIFQEpsscldpsAKIGD-QLIEAIPSWTFKGKWWQRFKWRKKRAIellhrvgikdHKDIMN------SYPHE 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534190046 480 LSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQI 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
363-511 |
2.63e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFY--QPDSGKILLDGIDLEEydtqflrdniglvlqknhifNGTIEEN 440
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLIDA 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 441 I-RYGNVNATFEEIEDAakrayiheqimdlpeGYQSKALL------LSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:COG2401 106 IgRKGDFKDAVELLNAV---------------GLSDAVLWlrrfkeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
108-316 |
2.86e-08 |
|
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: 55.65 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 108 EKILTYRMAFYTNQdnQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQ 187
Cdd:cd18565 95 DHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTY 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 188 QQAKKLSGRRRNLRgyreqKSQGIISI-----INSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFI 262
Cdd:cd18565 173 WFQRRIEPRYRAVR-----EAVGDLNArlennLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLV 247
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 263 EQFGVVIIIILTSYLVLDG------QMTIGASMFHILLFNNVSAPIRQLHRIYDEMNDAM 316
Cdd:cd18565 248 AGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAM 307
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
347-518 |
3.63e-08 |
|
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: 55.99 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPNG--YKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPD-SGKILLDGIDLEEYD-TQFLRDN 422
Cdd:TIGR02633 258 LEARNLTCWDVINphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQ--KNH--IFNGTIEENIRYGNVN--ATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL---LSGGQQQRIAIARM 493
Cdd:TIGR02633 338 IAMVPEdrKRHgiVPILGVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPigrLSGGNQQKAVLAKM 417
|
170 180
....*....|....*....|....*
gi 2534190046 494 FLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEI 442
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
46-286 |
4.45e-08 |
|
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: 54.83 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 46 VDSINGLVEAGKGLKEGLKIISFISIVLMTkeiLNAFITFGQKYYgekLRIL---VSQDLAQTIIEKILTYRMAFYtnQD 122
Cdd:cd18573 23 IDVASKESGDIEIFGLSLKTFALALLGVFV---VGAAANFGRVYL---LRIAgerIVARLRKRLFKSILRQDAAFF--DK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 123 NQAGKLQTRI--DRGI--ESLTrlvQNFfIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITqqqakKLSGRR- 197
Cdd:cd18573 95 NKTGELVSRLssDTSVvgKSLT---QNL-SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA-----VFYGRYv 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 198 RNLrGYREQKSQGIISI-----INSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIII 272
Cdd:cd18573 166 RKL-SKQVQDALADATKvaeerLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
|
250
....*....|....
gi 2534190046 273 LTSYLVLDGQMTIG 286
Cdd:cd18573 245 YGGSLVASGELTVG 258
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
355-511 |
5.79e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 355 SYPNGYKALKNINMTIQP-----NKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDgIDLEeYDTQFLRDNiglvlqk 429
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-YKPQYIKPD------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 nhiFNGTIEENIRygnvnatfeEIEDAAKRAYIHEQIMD---LPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEP 506
Cdd:PRK13409 413 ---YDGTVEDLLR---------SITDDLGSSYYKSEIIKplqLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
....*
gi 2534190046 507 TASLD 511
Cdd:PRK13409 481 SAHLD 485
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
363-531 |
1.13e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS--GKILLDGIDLEEydtQFLRdNIGLVLQKNHIF-NGTIEE 439
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 440 NIRYGNV----NATFEEIEDAAKRAYIHEQIMDLPEGY---QSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDA 512
Cdd:PLN03211 160 TLVFCSLlrlpKSLTKQEKILVAESVISELGLTKCENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|
gi 2534190046 513 IATEQIKNSLDAI-KKDRTV 531
Cdd:PLN03211 240 TAAYRLVLTLGSLaQKGKTI 259
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
354-511 |
2.08e-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: 54.02 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 354 FSYPNGYKALKNINMTIQP-----NKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDgIDLEeYDTQFLRDNiglvlq 428
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGgeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS-YKPQYISPD------ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 429 knhiFNGTIEENIRygnvNATFEEIEDAakraYIHEQI---MDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:COG1245 414 ----YDGTVEEFLR----SANTDDFGSS----YYKTEIikpLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
....*.
gi 2534190046 506 PTASLD 511
Cdd:COG1245 482 PSAHLD 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
347-518 |
2.11e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEfSYPNgyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLE---EYDTqfLRDNI 423
Cdd:PRK09700 266 FEVRNVT-SRDR--KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsPLDA--VKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 424 GLVLQ---KNHIF-NGTIEENI---------RYGNVNATFEEIEDAaKRAYIHEQIMDLP-EGYQSKALLLSGGQQQRIA 489
Cdd:PRK09700 341 AYITEsrrDNGFFpNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQ-RTAENQRELLALKcHSVNQNITELSGGNQQKVL 419
|
170 180
....*....|....*....|....*....
gi 2534190046 490 IARMFLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEI 448
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
363-511 |
3.61e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 53.03 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGiDL-----------EEYDTQFlrD-------NIG 424
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLivarlqqdpprNVEGTVY--DfvaegieEQA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQKNHIFNGTIEENIRYGNVN--ATFEEIEDAAKRAYIHEQIMDLPE--GYQSKALL--LSGGQQQRIAIARMFLKNP 498
Cdd:PRK11147 96 EYLKRYHDISHLVETDPSEKNLNelAKLQEQLDHHNLWQLENRINEVLAqlGLDPDAALssLSGGWLRKAALGRALVSNP 175
|
170
....*....|...
gi 2534190046 499 PIIFLDEPTASLD 511
Cdd:PRK11147 176 DVLLLDEPTNHLD 188
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
349-511 |
4.66e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 349 IQNVEFSYPNgyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLR---DNIGL 425
Cdd:PRK13541 4 LHQLQFNIEQ--KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTyigHNLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 426 VLQKnhifngTIEENIRYgnvnatFEEIEDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDE 505
Cdd:PRK13541 82 KLEM------TVFENLKF------WSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
....*.
gi 2534190046 506 PTASLD 511
Cdd:PRK13541 150 VETNLS 155
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
347-518 |
4.93e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYPN--GYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDS-GKILLDGIDLE-EYDTQFLRDN 422
Cdd:PRK13549 260 LEVRNLTAWDPVnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 423 IGLVLQ--KNH--IFNGTIEENIRYGNVN--ATFEEIEDAAKRAYIHEQIMDLPEGYQSKALL---LSGGQQQRIAIARM 493
Cdd:PRK13549 340 IAMVPEdrKRDgiVPVMGVGKNITLAALDrfTGGSRIDDAAELKTILESIQRLKVKTASPELAiarLSGGNQQKAVLAKC 419
|
170 180
....*....|....*....|....*
gi 2534190046 494 FLKNPPIIFLDEPTASLDAIATEQI 518
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEI 444
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
363-528 |
6.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.31 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQ-FLRDNI----------GLVLQKnh 431
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIvyisedrkrdGLVLGM-- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 ifngTIEEN-----IRY-----GNVNATFE--EIEDAAKRAYIHEQIMDLPEGyqskalLLSGGQQQRIAIARMFLKNPP 499
Cdd:PRK10762 346 ----SVKENmsltaLRYfsragGSLKHADEqqAVSDFIRLFNIKTPSMEQAIG------LLSGGNQQKVAIARGLMTRPK 415
|
170 180
....*....|....*....|....*....
gi 2534190046 500 IIFLDEPTASLDAIATEQIKNSLDAIKKD 528
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAE 444
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
307-511 |
7.18e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.04 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 307 RI--YDEMNdamiySESFFailKADDEKESsgnYIPT--KLKGK-FEIQNVEFSYpnGYKAL-KNINMTIQPNKITALVG 380
Cdd:PRK11819 291 RLarYEELL-----SEEYQ---KRNETNEI---FIPPgpRLGDKvIEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 381 LSGAGKSTVINLLDKFYQPDSGKILL-DGIDLEEYDtQFlRDNIGLvlqknhifNGTIEENIRYGNvnatfEEIE----D 455
Cdd:PRK11819 358 PNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYVD-QS-RDALDP--------NKTVWEEISGGL-----DIIKvgnrE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 456 AAKRAYI-------HEQimdlpegyQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK11819 423 IPSRAYVgrfnfkgGDQ--------QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
115-305 |
9.06e-07 |
|
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: 50.96 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 115 MAFYTNqdNQAGKLQTRIdRGIESltrlVQNFF--------IDILplFanSIVALILMFNANFYVGLVGLCIVPIYFIIT 186
Cdd:cd18588 90 LSYFES--RQVGDTVARV-RELES----IRQFLtgsaltlvLDLV--F--SVVFLAVMFYYSPTLTLIVLASLPLYALLS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 187 QQQAKKLsgRRR-NLRGYREQKSQG-IISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQ 264
Cdd:cd18588 159 LLVTPIL--RRRlEEKFQRGAENQSfLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQK 236
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534190046 265 FGVVIIIILTSYLVLDGQMTIGA----SMfhilLFNNVSAPIRQL 305
Cdd:cd18588 237 LTTLAILWFGAYLVMDGELTIGQliafNM----LAGQVSQPVLRL 277
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
348-559 |
1.27e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 50.17 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLL--DKFYQPDSGKILLDGIDLEEYDTQ-FLRDNIG 424
Cdd:PRK09580 3 SIKDLHVSV-EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEdRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLQ--------KNHIFNGTIEENIRYGNVNATFEEIEDAAkraYIHEQI--MDLPEGYQSKALLL--SGGQQQRIAIAR 492
Cdd:PRK09580 82 MAFQypveipgvSNQFFLQTALNAVRSYRGQEPLDRFDFQD---LMEEKIalLKMPEDLLTRSVNVgfSGGEKKRNDILQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 493 MFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIID---ADYTYVMKQGEVVEHG 559
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDyikPDYVHVLYQGRIVKSG 228
|
|
| ABC_6TM_NdvA_beta-glucan_exporter_like |
cd18562 |
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ... |
108-286 |
1.82e-06 |
|
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: 49.93 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 108 EKILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPlfanSIVALILMFNANFYVG------LVGLCIVpi 181
Cdd:cd18562 77 EHVITLPLSFH--SQRGSGRLLRIMLRGTDALFGLWLGFFREHLA----ALVSLIVLLPVALWMNwrlallLVVLAAV-- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 182 YFIITQQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQ-----------TRK 250
Cdd:cd18562 149 YAALNRLVMRRTKAGQAAVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITRRLLAAQYPvlnwwalasvlTRA 228
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534190046 251 TSfffdglksfieQFGVVIIIILTSYLVLDGQMTIG 286
Cdd:cd18562 229 AS-----------TLTMVAIFALGAWLVQRGELTVG 253
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
351-565 |
3.13e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 351 NVEFSYPNG-YKALKNINMTIQPNKITALVGLSGAGKS----TVINLLDKfyqpdSGKI----LLDG---IDLEEYDTQF 418
Cdd:PRK09473 19 RVTFSTPDGdVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGreiLNLPEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 419 LRDN------------------IG------LVLQKNHIFNGTIEENIRYgnVNATfeEIEDAAKR--AYIHEqimdlpeg 472
Cdd:PRK09473 94 LRAEqismifqdpmtslnpymrVGeqlmevLMLHKGMSKAEAFEESVRM--LDAV--KMPEARKRmkMYPHE-------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 473 yqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVIIISHSISQIIDA---DYTYV 549
Cdd:PRK09473 162 -------FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAgicDKVLV 234
|
250
....*....|....*.
gi 2534190046 550 MKQGEVVEHGIHEDVY 565
Cdd:PRK09473 235 MYAGRTMEYGNARDVF 250
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
37-305 |
3.36e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 49.02 E-value: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 37 VNALILQYTVDSINGlvEAGKGLKEGLKIISFISIVLMTKEILNAFITFGQKYYGEKLRILvsqdLAQTIIEKILtyRMA 116
Cdd:cd18579 15 AQPLLLGLLISYLSS--YPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSA----LSSLIYRKAL--RLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYTNQDNQAGKLQT-------RIDRGIESLtrlvqnFFIDILPLFAnsIVALILMFNanfYVG---LVGLCIVPIYFIIT 186
Cdd:cd18579 87 SSARQETSTGEIVNlmsvdvqRIEDFFLFL------HYLWSAPLQI--IVALYLLYR---LLGwaaLAGLGVLLLLIPLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 187 QQQAKKLSGRRRNLRGYREQKSQGIISIINSITVIKSFNREdiegKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFG 266
Cdd:cd18579 156 AFLAKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAWE----KPFLKRIEELRKKELKALRKFGYLRALNSFLFFST 231
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2534190046 267 VVIIIILT--SYLVLDGQMTIgASMFHIL-LFNNVSAPIRQL 305
Cdd:cd18579 232 PVLVSLATfaTYVLLGNPLTA-AKVFTALsLFNLLRFPLLML 272
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
42-287 |
4.40e-06 |
|
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: 48.63 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 42 LQYTVDsiNGLVEAGKG-LKEGLKIISFISIVLmtkeilnAFITFGQKYY----GEKlrilVSQDLAQTIIEKILTYRMA 116
Cdd:cd18575 19 LRLLID--QGFAAGNTAlLNRAFLLLLAVALVL-------ALASALRFYLvswlGER----VVADLRKAVFAHLLRLSPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 117 FYtnQDNQAGKLQTRI--DrgieslTRLVQNFFIDILPLFANSIV----ALILMFNANFYVGLVGLCIVPIYFIITqqqa 190
Cdd:cd18575 86 FF--ETTRTGEVLSRLttD------TTLIQTVVGSSLSIALRNLLlligGLVMLFITSPKLTLLVLLVIPLVVLPI---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 191 kKLSGRR-RNLRgyRE-QKSQGIIS-----IINSITVIKSFNREDIEGKK-QLDLQKELTNNQMQTRKTSFFFdGLKSFI 262
Cdd:cd18575 154 -ILFGRRvRRLS--RAsQDRLADLSafaeeTLSAIKTVQAFTREDAERQRfATAVEAAFAAALRRIRARALLT-ALVIFL 229
|
250 260
....*....|....*....|....*
gi 2534190046 263 EQFGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18575 230 VFGAIVFVLWLGAHDVLAGRMSAGE 254
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
372-529 |
4.61e-06 |
|
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: 46.60 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 372 PNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLVLQKnhifngtieenirygnvnatfe 451
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534190046 452 eiedaakrayiheqimdlpegyqskaLLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDR 529
Cdd:smart00382 59 --------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLL 110
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
346-510 |
5.60e-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: 49.36 E-value: 5.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEiqNVEFSYPNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKF--------YQPDSGKILLdgIDLEEYDTQ 417
Cdd:TIGR00954 453 KFE--NIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY--VPQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 418 -FLRDNIglvlqknhIFNGTIEENIRYGNVNATFEEIEDAAKRAYIHEQIMDLpEGYQSKALLLSGGQQQRIAIARMFLK 496
Cdd:TIGR00954 529 gTLRDQI--------IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGW-SAVQDWMDVLSGGEKQRIAMARLFYH 599
|
170
....*....|....
gi 2534190046 497 NPPIIFLDEPTASL 510
Cdd:TIGR00954 600 KPQFAILDECTSAV 613
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
369-525 |
7.09e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.62 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 369 TIQPNKITALVGLSGAGKSTVI----NLLdkfyqPDSGKILLDGIDLEEYDTQFL-RDNIGLVLQKNHIFNGTIEENI-R 442
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLarmaGLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVFQYLtL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 443 YGNVNATFEEIEDAakrayIHE-----QIMD-LPEGYQSkallLSGGQQQRIAIARMFLK-----NP--PIIFLDEPTAS 509
Cdd:PRK03695 93 HQPDKTRTEAVASA-----LNEvaealGLDDkLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170
....*....|....*.
gi 2534190046 510 LDaIATEqikNSLDAI 525
Cdd:PRK03695 164 LD-VAQQ---AALDRL 175
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
362-525 |
9.29e-06 |
|
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: 46.55 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINllDKFYQpdSGKILLDGiDLEEYDTQFLrdniglvlqknhIFNGTIEeni 441
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA--SGKARLIS-FLPKFSRNKL------------IFIDQLQ--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 442 rygnvnatfeeiedaakrayiheQIMDLPEGYQS---KALLLSGGQQQRIAIAR-MFLKNPPIIF-LDEPTASLDAIATE 516
Cdd:cd03238 70 -----------------------FLIDVGLGYLTlgqKLSTLSGGELQRVKLASeLFSEPPGTLFiLDEPSTGLHQQDIN 126
|
....*....
gi 2534190046 517 QIKNSLDAI 525
Cdd:cd03238 127 QLLEVIKGL 135
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
363-511 |
9.77e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 9.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKI-LLDGIDL---EEYDTQFLRDNIGLVLQKNHIFNGTIE 438
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLgyfAQHQLEFLRADESPLQHLARLAPQELE 407
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 439 ENIR--YGNVNATFEEIEDAAKRayiheqimdlpegyqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK10636 408 QKLRdyLGGFGFQGDKVTEETRR--------------------FSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABC_6TM_LapB_like |
cd18587 |
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ... |
102-287 |
1.10e-05 |
|
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.
Pssm-ID: 350031 Cd Length: 293 Bit Score: 47.43 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 102 LAQTIIEKILTYRMAfytNQDNQAGKLQTRIdRGIESltrlVQNFF--------IDiLPlFAnsIVALILMFNANFYVGL 173
Cdd:cd18587 77 LSSRLFERVLGLRLE---ARPASVGSFANNL-REFES----VRDFFtsatltalID-LP-FV--LLFLAVIALIGGPLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 174 VGLCIVPI---YFIITQQQAKKLSgrrrnLRGYRE--QKSQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQT 248
Cdd:cd18587 145 VPLVAIPLvllYGLLLQKPLRRLV-----EESMREsaQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKS 219
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534190046 249 RKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18587 220 RLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGG 258
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
363-564 |
1.29e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVINLL-DKFYQPD-------SGKILLDGIDLEEYD-TQFLRDNIGLVLQKNHIF 433
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDaPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 434 NGTIEENI---RYGNVN---ATFEEIEDAAKRAYiheqimdlpEGYQSKALL------LSGGQQQRIAIARMFLK----- 496
Cdd:PRK13547 97 AFSAREIVllgRYPHARragALTHRDGEIAWQAL---------ALAGATALVgrdvttLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 497 ----NPPIIFLDEPTASLDAIATEQIKNSLDAIKKD---RTVIIISHSISQIIDADYTYVMKQGEVVEHGIHEDV 564
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
370-511 |
1.74e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.38 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 370 IQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYD----TQFLRDNIGL-----VLQKNHIFNGTIEEN 440
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrsrfMAYLGHLPGLkadlsTLENLHFLCGLHGRR 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534190046 441 IRYGNVNATfeeiedaakrayiheQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLD 511
Cdd:PRK13543 114 AKQMPGSAL---------------AIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
78-286 |
1.94e-05 |
|
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: 46.70 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 78 ILNAFITFGQKYYGEKLrilvSQDLAQTIIEKILTYRMAFYTnqDNQAGKLQTRIDRGIEsltrLVQNFFIDILPLF--- 154
Cdd:cd18577 62 VLSYIQTACWTITGERQ----ARRIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTN----LIQDGIGEKLGLLiqs 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 155 -ANSIVALILMFNANFYVGLVGLCIVPIYFI---ITQQQAKKLSGRRRNLrgyrEQKSQGIIS-IINSITVIKSFNREDI 229
Cdd:cd18577 132 lSTFIAGFIIAFIYSWKLTLVLLATLPLIAIvggIMGKLLSKYTKKEQEA----YAKAGSIAEeALSSIRTVKAFGGEEK 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 230 EGKKqldLQKELTNNQMQTRKTSFFFdGLksfieQFGVVIIIILTSY---------LVLDGQMTIG 286
Cdd:cd18577 208 EIKR---YSKALEKARKAGIKKGLVS-GL-----GLGLLFFIIFAMYalafwygsrLVRDGEISPG 264
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
360-566 |
2.14e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 360 YKALKNINMTIQPNKITALVGLSGAGKS----TVINLLDKFYQPDSGKILLDGIDLEEYDTQFLRDNIGLvlQKNHIFNG 435
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGA--EVAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 436 TIEenirygNVNATFE---EIEDAAK------RAYIHEQIMDL--------PEG----YQSKallLSGGQQQRIAIARMF 494
Cdd:PRK11022 98 PMT------SLNPCYTvgfQIMEAIKvhqggnKKTRRQRAIDLlnqvgipdPASrldvYPHQ---LSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 495 LKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRT---VIIISHSISQIIDADYTYVMKQGEVVEHGIHEDVYK 566
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmalVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
|
|
| ABC_6TM_peptidase_like |
cd18571 |
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and ... |
126-289 |
3.07e-05 |
|
Six-transmembrane helical domain (6-TMD) of an uncharacterized peptidase ABC transporter and similar proteins; This group includes the 6-TMD of an uncharacterized peptidase-containing ABC transporter of T1SS (type 1 secretion systems), similar to heterocyst differentiation protein HetC. HetC is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350015 [Multi-domain] Cd Length: 294 Bit Score: 46.28 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 126 GKLQTRID--RGIES-LTRLVQNFFIDILPLFANSIValilMFNANFYVGLVGLCIVPIYFIIT---QQQAKKLSGRRRN 199
Cdd:cd18571 99 GDILQRINdhSRIESfLTSSSLSILFSLLNLIVFSIV----LAYYNLTIFLIFLIGSVLYILWIllfLKKRKKLDYKRFD 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 200 LRGYREQKsqgIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVL 279
Cdd:cd18571 175 LSSENQSK---LIELINGMQEIKLNNSERQKRWEWERIQAKLFKINIKSLKLDQYQQIGALFINQLKNILITFLAAKLVI 251
|
170
....*....|
gi 2534190046 280 DGQMTIGASM 289
Cdd:cd18571 252 DGEITLGMML 261
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
473-527 |
3.14e-05 |
|
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: 44.87 E-value: 3.14e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2534190046 473 YQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDaiaTEQIKNSLDAIKK 527
Cdd:cd03222 65 YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD---IEQRLNAARAIRR 116
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
100-287 |
4.93e-05 |
|
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: 45.65 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 100 QDLAQTIIEKILTYRMAFYTNqdNQAGKLQTRIdRGIESLtrlvQNFF--------IDiLPLfanSIVALILMFNANFYV 171
Cdd:cd18566 75 HRLSNAAFEHLLSLPLSFFER--EPSGAHLERL-NSLEQI----REFLtgqallalLD-LPF---VLIFLGLIWYLGGKL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 172 GLVGLCIVPIYFIITQQQAKKLsgrRRNLRGYREQKSQG---IISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQT 248
Cdd:cd18566 144 VLVPLVLLGLFVLVAILLGPIL---RRALKERSRADERRqnfLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKV 220
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534190046 249 RKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18566 221 AKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
375-529 |
5.45e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 375 ITALVGLSGAGKSTVInlldkfyqpdsgkillDGIDLEEYDTQFLRDNIGLVLQKnhifngTIEENIRYGNVNATFEEIE 454
Cdd:cd03240 24 LTLIVGQNGAGKTTII----------------EALKYALTGELPPNSKGGAHDPK------LIREGEVRAQVKLAFENAN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 455 D---AAKRAY-IHEQIMDLPEGyQSKALL------LSGGQQQ------RIAIARMFLKNPPIIFLDEPTASLDAiatEQI 518
Cdd:cd03240 82 GkkyTITRSLaILENVIFCHQG-ESNWPLldmrgrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDE---ENI 157
|
170
....*....|.
gi 2534190046 519 KNSLDAIKKDR 529
Cdd:cd03240 158 EESLAEIIEER 168
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
369-511 |
8.09e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 369 TIQPNKITALVGLSGAGKSTVINLLD--------KFYQPDSGKILLD---GIDLEEYDTQfLRDNIGLVLQKNH------ 431
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKrfrGTELQNYFKK-LYNGEIKVVHKPQyvdlip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 432 -IFNGTIEENIRYGNVNATFEEIedaAKRAYIhEQIMDLPEGYqskallLSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:PRK13409 174 kVFKGKVRELLKKVDERGKLDEV---VERLGL-ENILDRDISE------LSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
.
gi 2534190046 511 D 511
Cdd:PRK13409 244 D 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
348-523 |
1.74e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 348 EIQNVEFSYPNGyKALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKI----------------------- 404
Cdd:PRK15064 321 EVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydfendl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 405 -LLDGIDL---EEYDTQFLRDNIGLVLqknhiFNGtieenirygnvnatfeeiEDAAKrayiheqimdlpegyqsKALLL 480
Cdd:PRK15064 400 tLFDWMSQwrqEGDDEQAVRGTLGRLL-----FSQ------------------DDIKK-----------------SVKVL 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2534190046 481 SGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLD 523
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
369-511 |
1.74e-04 |
|
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: 44.39 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 369 TIQPNKITALVGLSGAGKSTVINLLdkfyqpdSGKILldgIDLEEYDTQFLRDNI-----GLVLQkNHiFNGTIEENIR- 442
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKIL-------SGELK---PNLGDYDEEPSWDEVlkrfrGTELQ-DY-FKKLANGEIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 443 -----Y---------GNVNATFEEIEDAAKRAYIHEQiMDLpegyqsKALL------LSGGQQQRIAIARMFLKNPPIIF 502
Cdd:COG1245 163 ahkpqYvdlipkvfkGTVRELLEKVDERGKLDELAEK-LGL------ENILdrdiseLSGGELQRVAIAAALLRDADFYF 235
|
....*....
gi 2534190046 503 LDEPTASLD 511
Cdd:COG1245 236 FDEPSSYLD 244
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
109-284 |
2.96e-04 |
|
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: 43.24 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 109 KILTY-RMAFYTN---------QDNQAGKLQTRIDRGIESLtrlvQNFFIDIL-PLFANSIVALILMFNANFY------V 171
Cdd:cd18585 65 RLLSNlRVWFYRKleplaparlQKYRSGDLLNRIVADIDTL----DNLYLRVLsPPVVALLVILATILFLAFFspalalI 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 172 GLVGL----CIVPIYFiitQQQAKKLSGRRRNLRG-YREQksqgIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQM 246
Cdd:cd18585 141 LLAGLllagVVIPLLF---YRLGKKIGQQLVQLRAeLRTE----LVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQR 213
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534190046 247 QTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMT 284
Cdd:cd18585 214 RLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
366-520 |
3.28e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 366 INMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDGIDLEEYDTqflRDNI--GLVL-----QKNHIFNG-TI 437
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIraGIMLcpedrKAEGIIPVhSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 438 EENI---------RYGNVnatfeeIEDAAKRAYIHEQIMDL----PEGYQsKALLLSGGQQQRIAIARMFLKNPPIIFLD 504
Cdd:PRK11288 349 ADNInisarrhhlRAGCL------INNRWEAENADRFIRSLniktPSREQ-LIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170
....*....|....*.
gi 2534190046 505 EPTASLDAIATEQIKN 520
Cdd:PRK11288 422 EPTRGIDVGAKHEIYN 437
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
362-531 |
3.90e-04 |
|
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: 43.85 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 362 ALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSG-------KILLDGIDLEE---YDTQFlrDNIG-LVLQKN 430
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagkSILTNISDVHQnmgYCPQF--DAIDdLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 431 HIFngtieENIRYGNVNAtfEEIEDAAKRAYiheQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASL 510
Cdd:TIGR01257 2032 HLY-----LYARLRGVPA--EEIEKVANWSI---QSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGM 2101
|
170 180
....*....|....*....|..
gi 2534190046 511 DAIATEQIKNSL-DAIKKDRTV 531
Cdd:TIGR01257 2102 DPQARRMLWNTIvSIIREGRAV 2123
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
154-287 |
4.57e-04 |
|
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: 42.62 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 154 FANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLsgrrRNLRgYREQKSQGIIS-----IINSITVIKSFNRED 228
Cdd:cd18780 127 LVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYV----RKLS-KKFQDALAAAStvaeeSISNIRTVRSFAKET 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534190046 229 IEgkkqldlQKELTNNQMQT----RKTSF---FFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18780 202 KE-------VSRYSEKINESyllgKKLARasgGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL 260
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
472-529 |
5.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534190046 472 GYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKN-SLDAIKKDR 529
Cdd:PRK10982 384 GHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQlIAELAKKDK 442
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
347-513 |
7.30e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 347 FEIQNVEFSYpNGYKALKNINMTIQPNKITALVGLSGAGKSTVINLLD----KFYQPD---------SGKILLDgidlee 413
Cdd:PRK10938 261 IVLNNGVVSY-NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGYSNDltlfgrrrgSGETIWD------ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 414 ydtqfLRDNIGLVLQKNHI---FNGTIEENIRYGNVNA--TFEEIEDAAK--------RAYIHEQIMDLPegYQSkallL 480
Cdd:PRK10938 334 -----IKKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSigIYQAVSDRQQklaqqwldILGIDKRTADAP--FHS----L 402
|
170 180 190
....*....|....*....|....*....|...
gi 2534190046 481 SGGQQQRIAIARMFLKNPPIIFLDEPTASLDAI 513
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDPL 435
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
102-305 |
7.78e-04 |
|
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: 41.73 E-value: 7.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 102 LAQTIIEKILTYRMAFYtnQDNQAG----KLQtRIDRGIESLTRLVQNFFIDILPLfansIVALILMFnanFY------- 170
Cdd:cd18783 77 LALRTFDRLLSLPIDFF--ERTPAGvltkHMQ-QIERIRQFLTGQLFGTLLDATSL----LVFLPVLF---FYsptlalv 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 171 ----VGLVGLCI---VPIYfiitqqqakklsgRRRNLRGYREQKSQG--IISIINSITVIKSFNREDIEGKKQLDLQKEL 241
Cdd:cd18783 147 vlafSALIALIIlafLPPF-------------RRRLQALYRAEGERQafLVETVHGIRTVKSLALEPRQRREWDERVARA 213
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534190046 242 TNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSAPIRQL 305
Cdd:cd18783 214 IRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQL 277
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
49-316 |
8.06e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. 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: 350000 Cd Length: 298 Bit Score: 41.86 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 49 INGLVEAGKGLKEGLKI--ISFISIVLMTKeILNAFITFGQKYygekLRILVSQDLAQTIIEKILTYRMAFYtnQDNQAG 126
Cdd:cd18556 29 TDLLTSSSSDSYNYIVVlaALYVITISATK-LLGFLSLYLQSS----LRVELIISISSSYFRYLYEQPKTFF--VKENSG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 127 KLQTRIDRGIESLTRLVQNFFIDIL-PLFANSIVALILMFNANFYVGLVGLCIVPIYFIITQQQAKKLSGRRRNLRGyRE 205
Cdd:cd18556 102 DITQRLNQASNDLYTLVRNLSTNILpPLLQLIIAIVVILSSGDYFVAALFLLYAVLFVINNTIFTKKIVSLRNDLMD-AG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 206 QKSQGII--SIINsITVIKSFNREDI---EGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIeQFGVVIIIILtsYLVLD 280
Cdd:cd18556 181 RKSYSLLtdSVKN-IVAAKQNNAFDFlfkRYEATLTNDRNSQKRYWKLTFKMLILNSLLNVI-LFGLSFFYSL--YGVVN 256
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2534190046 281 GQMTIG-----ASmfHILLFnnvSAPIRQLHRIYDEMNDAM 316
Cdd:cd18556 257 GQVSIGhfvliTS--YILLL---STPIESLGNMLSELRQSV 292
|
|
| ABC_6TM_ABCB6 |
cd18581 |
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ... |
94-286 |
8.92e-04 |
|
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, 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: 350025 [Multi-domain] Cd Length: 300 Bit Score: 41.46 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 94 LRILVSQDLAQTIIEKILTY----RMAFYTNqdNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNA-N 168
Cdd:cd18581 69 LWIPVQQFTTREISVKLFAHlhslSLRWHLS--RKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAfN 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 169 FYVGLVGLCIVPIY----FIITQQQAKKlsgRRRNLRGYREQKSQGIISIINSITViKSFNREDIEGKKqldLQKELTNN 244
Cdd:cd18581 147 PWFGLIVFVTMALYliltIIITEWRTKF---RREMNKLDNEKRAKAVDSLLNFETV-KYYNAERFEVER---YRRAIDDY 219
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534190046 245 QMQTRKTSFFFDGL---KSFIEQFGVVIIIILTSYLVLDGQMTIG 286
Cdd:cd18581 220 QVAEWKSNASLNLLntaQNLIITIGLLAGSLLCAYFVVEGKLTVG 264
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
363-526 |
1.01e-03 |
|
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: 41.09 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVInlLDKFYQpDSGKILLDGidLEEYDTQFLR-------DNI-GL-----VLQK 429
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLA--FDTIYA-EGQRRYVES--LSAYARQFLGqmdkpdvDSIeGLspaiaIDQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 430 nhifngTIEENIRygNVNATFEEIEDAAK----RAYIHEQI---MDLPEGYQS---KALLLSGGQQQRIAIARMFLKN-P 498
Cdd:cd03270 86 ------TTSRNPR--STVGTVTEIYDYLRllfaRVGIRERLgflVDVGLGYLTlsrSAPTLSGGEAQRIRLATQIGSGlT 157
|
170 180
....*....|....*....|....*....
gi 2534190046 499 PIIF-LDEPTASLDAIATEQIKNSLDAIK 526
Cdd:cd03270 158 GVLYvLDEPSIGLHPRDNDRLIETLKRLR 186
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
110-287 |
1.10e-03 |
|
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: 41.37 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 110 ILTYRMAFYtnQDNQAGKLQTRIDRGIESLTRLVQNFFIDILPLFANSIVALILMFNANFYVGLVGLCIVPIYFIITqqq 189
Cdd:cd18572 79 LLRQDIAFF--DATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALIT--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 190 akKLSGR--RRNLRGYREQK---SQGIISIINSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQ 264
Cdd:cd18572 154 --KVYGRyyRKLSKEIQDALaeaNQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
|
170 180
....*....|....*....|...
gi 2534190046 265 FGVVIIIILTSYLVLDGQMTIGA 287
Cdd:cd18572 232 GTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
373-394 |
1.12e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 40.84 E-value: 1.12e-03
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
373-394 |
1.90e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 1.90e-03
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
454-583 |
2.34e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.49 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 454 EDAAKRAYIHEQIMDLPEGYQSKALLLSGGQQQRIAIARMFLKNPPIIFLDEPTASLDAIATEQIKNSLDAIKKDRTVII 533
Cdd:NF000106 119 KDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVL 198
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2534190046 534 ISHSISQIID--ADYTYVMKQGEVVEHG-IHEDVYKMNGTYKEIFDAMAKSLN 583
Cdd:NF000106 199 LTTQYMEEAEqlAHELTVIDRGRVIADGkVDELKTKVGGRTLQIRPAHAAELD 251
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
361-511 |
3.58e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 361 KALKNINMTIQPNKITALVGLSGAGKS-TVINLLDKFY-QPDSGKILLDGidlEEYDTQFLRDNI--------------G 424
Cdd:NF040905 274 KVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYgRNISGTVFKDG---KEVDVSTVSDAIdaglayvtedrkgyG 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 425 LVLqknhifNGTIEENIRYGNVNATfeeiedaAKRAYIHEQI-MDLPEGYQSK-----------ALLLSGGQQQRIAIAR 492
Cdd:NF040905 351 LNL------IDDIKRNITLANLGKV-------SRRGVIDENEeIKVAEEYRKKmniktpsvfqkVGNLSGGNQQKVVLSK 417
|
170
....*....|....*....
gi 2534190046 493 MFLKNPPIIFLDEPTASLD 511
Cdd:NF040905 418 WLFTDPDVLILDEPTRGID 436
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
147-305 |
4.45e-03 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 39.51 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 147 FIDIL--PLFansiVALILMFNAnfYVGLVGLCIVPIYF---IITQQQAKKLSGRRRNLRGYREQKSQgiiSIINSITVI 221
Cdd:cd18586 120 FFDLPwaPLF----LAVIFLIHP--PLGWVALVGAPVLVglaWLNHRATRKPLGEANEAQAARDALAA---ETLRNAETI 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 222 KSFN-REDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFiEQFGVVIIIILTSYLVLDGQMTIGASMFHILLFNNVSA 300
Cdd:cd18586 191 KALGmLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTL-RMALQSLILGVGAYLVIDGELTIGALIAASILSGRALA 269
|
....*
gi 2534190046 301 PIRQL 305
Cdd:cd18586 270 PIDQL 274
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
346-459 |
4.77e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.60 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 346 KFEIQNvefsypngYKALKNINMTIQPNkITALVGLSGAGKSTVINLLDKFYQPDSgkilldGIDLEEYDTQFLRDNIGL 425
Cdd:COG3593 5 KIKIKN--------FRSIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSS------SRKFDEEDFYLGDDPDLP 69
|
90 100 110
....*....|....*....|....*....|....
gi 2534190046 426 VLQKNHIFNGTIEENIRYGNVNATFEEIEDAAKR 459
Cdd:COG3593 70 EIEIELTFGSLLSRLLRLLLKEEDKEELEEALEE 103
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
58-312 |
5.36e-03 |
|
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: 39.24 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 58 GLKEGLKIISFISIVLMTKEILnafitfgqkyygekLRILVSQDLAqtiiekiltyrmaFYtnQDNQAGKLQTRIDRGIE 137
Cdd:cd18590 54 GLRGGLFMCTLSRLNLRLRHQL--------------FSSLVQQDIG-------------FF--EKTKTGDLTSRLSTDTT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 138 SLTRLV-QNFFIdILPLFANSIVALILMFNANFYVGLVGLCIVPIyFIITQQQAKKLSGR-RRNLRGYREQKSQGIISII 215
Cdd:cd18590 105 LMSRSVaLNANV-LLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPL-TAIAQKVYNTYHQKlSQAVQDSIAKAGELAREAV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534190046 216 NSITVIKSFNREDIEGKKQLDLQKELTNNQMQTRKTSFFFDGLKSFIEQFGVVIIIILTSYLVLDGQMTIGASMFHILLF 295
Cdd:cd18590 183 SSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQ 262
|
250
....*....|....*..
gi 2534190046 296 NNVSAPIRQLHRIYDEM 312
Cdd:cd18590 263 KNLGSYVRTLVYIYGDM 279
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
363-391 |
5.46e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 5.46e-03
10 20
....*....|....*....|....*....
gi 2534190046 363 LKNINMTIQPNKITALVGLSGAGKSTVIN 391
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
347-408 |
9.33e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.72 E-value: 9.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534190046 347 FEIQNVEFSYpngykALKNINMTIQPNKITALVGLSGAGKSTVINLLDKFYQPDSGKILLDG 408
Cdd:PRK13545 29 FRSKDGEYHY-----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| |
