|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-527 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 562.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 4 VHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI--DRGGEIGYLPQDPRSgDPDELAR 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsiPKGLRIGYLPQEPPL-DDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDA-RGLGQLVLGMQEstiamSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRILEQPLKTLS 160
Cdd:COG0488 80 DTVLDGdAELRALEAELEE-----LEAKLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDanRQVIDVYNM 240
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELD--RGKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 241 NWKNYQRQRAADEERRKKERANVEKKAGALQLQAARFGAKASKAAAAHQMVARAEKMLsgLEEVRAVDRVAKLRFPTPMA 320
Cdd:COG0488 233 NYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLE--REEPPRRDKTVEIRFPPPER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 321 CGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEHETI 400
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 401 DVKRSVLENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREE 480
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1552103373 481 ILDALAHYEGAVVLVSHDEGAVEALNPERVLIMPeGTEDHWAADYLD 527
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVATRILEFED-GGVREYPGGYDD 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
14-498 |
3.06e-80 |
|
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: 261.02 E-value: 3.06e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdliaskgtIDR--GGE--------IGYLPQDPRSgDPDELARTR 83
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG--------VDKdfNGEarpqpgikVGYLPQEPQL-DPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRilEQPLKTLSGGQ 163
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 164 RRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQVidvynmNWK 243
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGI------PWE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 244 -NY------QRQRAADEERRKKERANVEKK------AGALQLQA---ARfgakaskaaaahqmVARAEKMLSglEEVRAV 307
Cdd:TIGR03719 241 gNYsswleqKQKRLEQEEKEESARQKTLKRelewvrQSPKGRQAkskAR--------------LARYEELLS--QEFQKR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 308 DRVAKLRFPTPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHG 387
Cdd:TIGR03719 305 NETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQEHETIDVKRSVLENMVSASPNLT----ETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:TIGR03719 385 VKLAYVDQSRDALDPNKTVWEEISGGLDIIKlgkrEIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNV 464
|
490 500 510
....*....|....*....|....*....|....*
gi 1552103373 464 LLLDEPTNNLDPASREEILDALAHYEGAVVLVSHD 498
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLNFAGCAVVISHD 499
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-519 |
5.47e-80 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 259.82 E-value: 5.47e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGT--IDRGGEIGYLPQDprsgdpdE 78
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNvsLDPNERLGKLRQD-------Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LA--RTRILDA--RGLGQLVLGMQESTiAMSSSDASVSAAGMKkYGTLTDRFLALGGYAAEAEAASIASNLNLPdriLEQ 154
Cdd:PRK15064 74 FAfeEFTVLDTviMGHTELWEVKQERD-RIYALPEMSEEDGMK-VADLEVKFAEMDGYTAEARAGELLLGVGIP---EEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 155 ---PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDAN 231
Cdd:PRK15064 149 hygLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 232 RqvIDVYNMNWKNYQRqrAADEERRKKERANVEKKAGALQLQA--ARFGAKASKAAaahQMVARAEKMLS-GLEEVRAVD 308
Cdd:PRK15064 229 E--LRVYPGNYDEYMT--AATQARERLLADNAKKKAQIAELQSfvSRFSANASKAK---QATSRAKQIDKiKLEEVKPSS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 309 RVAK-LRFPTPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHG 387
Cdd:PRK15064 302 RQNPfIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQEHET-IDVKRSVLENMVS-ASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLL 465
Cdd:PRK15064 382 ANIGYYAQDHAYdFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 466 LDEPTNNLDPASREEILDALAHYEGAVVLVSHDEGAVEALnPERVL-IMPEGTED 519
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL-ATRIIeITPDGVVD 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-498 |
5.17e-78 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 257.41 E-value: 5.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--EIGYLPQDprsgdpde 78
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 larTRILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRILEQPLKT 158
Cdd:PRK10636 73 ---TPALPQPALEYVIDGDREYRQLEAQLHDANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDanRQVIDVY 238
Cdd:PRK10636 150 FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIE--QQSLFEY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 239 NMNWKNYQRQRAADEERRKKERANVEKKAGALQLQAARFgakASKAAAAHQMVARAeKMLSGLEEVRA--VDRVAKLRFP 316
Cdd:PRK10636 228 TGNYSSFEVQRATRLAQQQAMYESQQERVAHLQSYIDRF---RAKATKAKQAQSRI-KMLERMELIAPahVDNPFHFSFR 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 317 TPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQE 396
Cdd:PRK10636 304 APESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQH 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 H-ETIDVKRSVLENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDP 475
Cdd:PRK10636 384 QlEFLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
|
490 500
....*....|....*....|...
gi 1552103373 476 ASREEILDALAHYEGAVVLVSHD 498
Cdd:PRK10636 464 DMRQALTEALIDFEGALVVVSHD 486
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-498 |
5.64e-71 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 236.55 E-value: 5.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG-------DLIASKGTidrggEIGYLPQDPRSgDPDELARTRI 84
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGvdkefegEARPAPGI-----KVGYLPQEPQL-DPEKTVRENV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 85 LDarGLGQLV--------LGMQESTIAMSSSDAsvsaagMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRilEQPL 156
Cdd:PRK11819 92 EE--GVAEVKaaldrfneIYAAYAEPDADFDAL------AAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPW--DAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDielvgetvnRVFY--------- 227
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD---------RYFLdnvagwile 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 228 LDANRQVidvynmNWK-NY------QRQRAADEERRKKERANVEKK------AGALQLQA---ARfgakaskaaaahqmV 291
Cdd:PRK11819 233 LDRGRGI------PWEgNYsswleqKAKRLAQEEKQEAARQKALKRelewvrQSPKARQAkskAR--------------L 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 292 ARAEKMLSglEEVRAVDRVAKLRFPTPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRIL 371
Cdd:PRK11819 293 ARYEELLS--EEYQKRNETNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 372 GGVDQPDTGVIEAGHGLRIGYYAQEHETIDVKRSVLENMVSASPNLT----ETEARRVLGSFLFTGDDSHKPAGVLSGGE 447
Cdd:PRK11819 371 TGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKTVWEEISGGLDIIKvgnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGE 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 448 KTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHD 498
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHD 501
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-498 |
1.07e-59 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 208.27 E-value: 1.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--IGYLPQDPrsgdPDE 78
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDliVARLQQDP----PRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LARTrILD--ARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDrilEQPL 156
Cdd:PRK11147 79 VEGT-VYDfvAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP---DAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDanRQVID 236
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD--RGKLV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 237 VYNMNWKNY-----------QRQRA------ADEE---RR--KKERANVEKKAGAL-QLQAARfgakaskaaaahqmVAR 293
Cdd:PRK11147 233 SYPGNYDQYllekeealrveELQNAefdrklAQEEvwiRQgiKARRTRNEGRVRALkALRRER--------------SER 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 294 AEKMLSGLEEVRAVDRVAKLRFptpmacgrtplHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGG 373
Cdd:PRK11147 299 REVMGTAKMQVEEASRSGKIVF-----------EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 374 VDQPDTGVIEAGHGLRIGYYAQEHETIDVKRSVLEN--------MVSASPnlteteaRRVLG---SFLFTGDDSHKPAGV 442
Cdd:PRK11147 368 QLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVMDNlaegkqevMVNGRP-------RHVLGylqDFLFHPKRAMTPVKA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHD 498
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-505 |
1.13e-54 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 195.85 E-value: 1.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 11 VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAgdLIASKGtIDRGGEIGYLPQDPRSGDPDELA--------RT 82
Cdd:PLN03073 187 VGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--MHAIDG-IPKNCQILHVEQEVVGDDTTALQcvlntdieRT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 RILDARGlgQLVLGMQESTIAMSSSDASVSAAG-------MKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRILEQP 155
Cdd:PLN03073 264 QLLEEEA--QLVAQQRELEFETETGKGKGANKDgvdkdavSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKA 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 156 LKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDAnrQVI 235
Cdd:PLN03073 342 TKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG--QKL 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 236 DVYNMNWKNYQRQRAADEERRKKERANVEKKAGALQLQAARFgakaSKAAAAHQMVARAEKMLSGLEEVRAV--DRVAKL 313
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKF----RYNAKRASLVQSRIKALDRLGHVDAVvnDPDYKF 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 314 RFPTPMACGRTPLHA-ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIG 391
Cdd:PLN03073 496 EFPTPDDRPGPPIISfSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEH-ETIDVKRSVLENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:PLN03073 576 VFSQHHvDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
490 500 510
....*....|....*....|....*....|....*....
gi 1552103373 471 NNLDPASREEILDALAHYEGAVVLVSHDE----GAVEAL 505
Cdd:PLN03073 656 NHLDLDAVEALIQGLVLFQGGVLMVSHDEhlisGSVDEL 694
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
326-498 |
1.28e-46 |
|
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: 159.54 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQehetidvkrs 405
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 406 vlenmvsaspnltetearrvlgsflftgddshkpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170
....*....|...
gi 1552103373 486 AHYEGAVVLVSHD 498
Cdd:cd03221 114 KEYPGTVILVSHD 126
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-248 |
4.77e-43 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 160.62 E-value: 4.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--EIGYLPQDPRSGDPDE 78
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQEELDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 lartRILDArgLGQLVLGMQESTIAmsssdasvsaagmkkyGTLTdRFLaLGGyaaeaeaasiasnlnlpDRIlEQPLKT 158
Cdd:COG0488 395 ----TVLDE--LRDGAPGGTEQEVR----------------GYLG-RFL-FSG-----------------DDA-FKPVGV 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRqvIDVY 238
Cdd:COG0488 433 LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGG--VREY 510
|
250
....*....|
gi 1552103373 239 NMNWKNYQRQ 248
Cdd:COG0488 511 PGGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-232 |
2.08e-42 |
|
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: 148.37 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--EIGYLPQdprsgdpdel 79
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 artrildarglgqlvlgmqestiamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasnlnlpdrileqplktL 159
Cdd:cd03221 71 -------------------------------------------------------------------------------L 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANR 232
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-516 |
4.67e-37 |
|
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: 143.51 E-value: 4.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRV--GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTI-----------------DRG 61
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIsgevlldgrdllelseaLRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 62 GEIGYLPQDPRSGdpdeLARTRILDarglgQLVLGMQESTIAMSSSDasvsaagmkkygTLTDRFLALGGYaaeaeaasi 141
Cdd:COG1123 83 RRIGMVFQDPMTQ----LNPVTVGD-----QIAEALENLGLSRAEAR------------ARVLELLEAVGL--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 142 asnlnlpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIEL 217
Cdd:COG1123 133 -------ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 218 VGETVNRVFYLDANRQVIDvynmnwknyqrqraadeerrkkeranvekkagalqlqaarfgakaskaaaahqmvARAEKM 297
Cdd:COG1123 206 VAEIADRVVVMDDGRIVED-------------------------------------------------------GPPEEI 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 298 LSGLEEVRAVDRVAKLRFPTPMACGRTP--LHAENLSKSYGSL--EIFTAVD---LAIDRGSKVVILGLNGAGKTTLLRI 370
Cdd:COG1123 231 LAAPQALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRgkGGVRAVDdvsLTLRRGETLGLVGESGSGKSTLARL 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 371 LGGVDQPDTGVIE-AGHGL-------------RIGY-----YAQ--EHETidVKRSVLENMV---SASPNLTETEARRVL 426
Cdd:COG1123 311 LLGLLRPTSGSILfDGKDLtklsrrslrelrrRVQMvfqdpYSSlnPRMT--VGDIIAEPLRlhgLLSRAERRERVAELL 388
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 427 GSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH----YEGAVVLVSHDEGAV 502
Cdd:COG1123 389 ERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFISHDLAVV 468
|
570
....*....|....
gi 1552103373 503 EALNpERVLIMPEG 516
Cdd:COG1123 469 RYIA-DRVAVMYDG 481
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
326-517 |
3.88e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 3.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI---------EAGHGLR--IGYYA 394
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsaMPPPEWRrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QE----HETidvkrsVLENMVS----ASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:COG4619 81 QEpalwGGT------VRDNLPFpfqlRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 467 DEPTNNLDPASREEILDALAHY----EGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVA-DRVLTLEAGR 208
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
326-516 |
1.17e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.49 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL---------RIGYYAQ 395
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHeTIDVKRSVLENMV------SASPNLTETEARRVLGSFLFTgDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:COG1131 81 EP-ALYPDLTVRENLRffarlyGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 470 TNNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:COG1131 159 TSGLDPEARRELWELLRELaaEGkTVLLSTHYLEEAERL-CDRVAIIDKG 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
326-516 |
1.75e-33 |
|
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: 125.20 E-value: 1.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL---------RIGYYAQ 395
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EhetidvkrsvlenmVSASPNLTeteARRVLgsflftgddshkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDP 475
Cdd:cd03230 81 E--------------PSLYENLT---VRENL---------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1552103373 476 ASREEILDALAHY---EGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:cd03230 129 ESRREFWELLRELkkeGKTILLSSHILEEAERLC-DRVAILNNG 171
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
326-504 |
4.08e-33 |
|
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: 125.28 E-value: 4.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL---------RIGYYAQ 395
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwNGEPIrdaredyrrRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVkRSVLENM--------VSASPNLTETEARRV-LGSFLftgddsHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:COG4133 83 ADGLKPE-LTVRENLrfwaalygLRADREAIDEALEAVgLAGLA------DLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1552103373 467 DEPTNNLDPASREEILDALAHY---EGAVVLVSHDEGAVEA 504
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQPLELAA 196
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
329-517 |
1.70e-31 |
|
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: 121.03 E-value: 1.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLE--IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-----------AGHGLRIGYYAQ 395
Cdd:cd03225 3 KNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdgkdltklslKELRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVKRSVLENMVSASPNL---TETEARRVLGSFLFTGDDS--HKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:cd03225 83 NPDDQFFGPTVEEEVAFGLENLglpEEEIEERVEEALELVGLEGlrDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 471 NNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:cd03225 163 AGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLEL-ADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-236 |
2.94e-31 |
|
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: 121.12 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqDPRSGDPDelA 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE------DVRKEPRE--A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRI---LDARGLgqlvlgmqestiamsssdasvsaagmkkYGTLTDR----FLA----LGGYAAEAEAASIASNLNLPD 149
Cdd:COG4555 73 RRQIgvlPDERGL----------------------------YDRLTVRenirYFAelygLFDEELKKRIEELIELLGLEE 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 150 rILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG-GFIVI--SHDIELVGETVNRVF 226
Cdd:COG4555 125 -FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLfsSHIMQEVEALCDRVV 203
|
250
....*....|
gi 1552103373 227 YLDANRQVID 236
Cdd:COG4555 204 ILHKGKVVAQ 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
326-516 |
3.52e-31 |
|
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: 120.29 E-value: 3.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS----LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL------------ 388
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRvDGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 --RIGYYAQEHETIDVkRSVLEN------MVSASPNLTETEARRVLGSF-LftGDDSHKPAGVLSGGEKTRLALAMIVVS 459
Cdd:cd03255 81 rrHIGFVFQSFNLLPD-LTALENvelpllLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 460 GANVLLLDEPTNNLDPASREEILD---ALAHYEG-AVVLVSHDEGAVEALnpERVLIMPEG 516
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMEllrELNKEAGtTIVVVTHDPELAEYA--DRIIELRDG 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
327-512 |
4.85e-31 |
|
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: 119.56 E-value: 4.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 327 HAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLRIGYYAQEHET- 399
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 ----IDVKRSV---LENMVSASPNLTETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:cd03235 81 rdfpISVRDVVlmgLYGHKGLFRRLSKADKAKVDEALERVGlsELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1552103373 471 NNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALNPERVLI 512
Cdd:cd03235 161 AGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
326-498 |
1.89e-30 |
|
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: 119.38 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL----------RIGYYA 394
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLlDGRDLaslsrrelarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHET---IDVKRSVLenM-----VSASPNLTETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVL 464
Cdd:COG1120 82 QEPPApfgLTVRELVA--LgryphLGLFGRPSAEDREAVEEALERTGleHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 465 LLDEPTNNLDPASREEILD---ALAHYEG-AVVLVSHD 498
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLEllrRLARERGrTVVMVLHD 197
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-235 |
2.11e-30 |
|
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: 118.02 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 3 SVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------IGYLPQDpRSG 74
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQR-RSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 75 DPDELARTRILDARGL-GQLVLGMQESTIAMSSSDASVSAAGMKKYgtltdrflalggyaaeaeaasiasnlnlpdriLE 153
Cdd:cd03235 80 DRDFPISVRDVVLMGLyGHKGLFRRLSKADKAKVDEALERVGLSEL--------------------------------AD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 154 QPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLda 230
Cdd:cd03235 128 RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL-- 205
|
....*
gi 1552103373 231 NRQVI 235
Cdd:cd03235 206 NRTVV 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
327-517 |
4.23e-30 |
|
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: 115.42 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 327 HAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEaghglrigyyaqeHETIDVKRSV 406
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL-------------IDGKDIAKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 LEnmvsaspnltetEARRVLGsFLFTgddshkpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA 486
Cdd:cd00267 68 LE------------ELRRRIG-YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 487 HY--EG-AVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:cd00267 125 ELaeEGrTVIIVTHDPELAELA-ADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
326-516 |
4.47e-30 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.45 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS----LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL------------ 388
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLiDGQDIsslserelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 --RIGYYAQEHETIDVkRSVLEN------MVSASPNLTETEARRVLGSFLFTGDDSHKPAgVLSGGEKTRLALAMIVVSG 460
Cdd:COG1136 85 rrHIGFVFQFFNLLPE-LTALENvalpllLAGVSRKERRERARELLERVGLGDRLDHRPS-QLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDAL---AHYEG-AVVLVSHDEGAVEALNpeRVLIMPEG 516
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLrelNRELGtTIVMVTHDPELAARAD--RVIRLRDG 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
328-517 |
9.40e-30 |
|
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: 116.88 E-value: 9.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR---------IGYYAQEH 397
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILiDGEDVRkeprearrqIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ETIDvKRSVLENMVSASP----NLTETEAR--RVLGSFLFtGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTN 471
Cdd:COG4555 84 GLYD-RLTVRENIRYFAElyglFDEELKKRieELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 472 NLDPASREEILDALAHY--EGAVVLVS-HDEGAVEALNpERVLIMPEGT 517
Cdd:COG4555 162 GLDVMARRLLREILRALkkEGKTVLFSsHIMQEVEALC-DRVVILHKGK 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-235 |
2.47e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------IGYLPQDPR 72
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 73 SgDPDELARTRildarglgQLVL-GMQestiamsssdasvSAAGMKKYGTLTDRFLAlggyaaeaeaasiasnlnlpDRI 151
Cdd:COG1121 86 V-DWDFPITVR--------DVVLmGRY-------------GRRGLFRRPSRADREAV--------------------DEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 152 LEQ---------PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVG 219
Cdd:COG1121 124 LERvgledladrPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVR 203
|
250
....*....|....*.
gi 1552103373 220 ETVNRVFYLdaNRQVI 235
Cdd:COG1121 204 EYFDRVLLL--NRGLV 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
12-232 |
3.51e-29 |
|
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: 114.49 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDPRsgdpDE 78
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVFQNPD----DQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LARTRILD--ARGLGQLvlGMQESTIAMSssdasvsaagmkkygtlTDRFLALGGyaaeaeaasiasnlnlPDRILEQPL 156
Cdd:cd03225 88 FFGPTVEEevAFGLENL--GLPEEEIEER-----------------VEEALELVG----------------LEGLRDRSP 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLDANR 232
Cdd:cd03225 133 FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-512 |
4.02e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.19 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLRIGYYAQeHET 399
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQ-RAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 IDvkR----SVLEnMVSAS--------PNLTETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLL 465
Cdd:COG1121 86 VD--WdfpiTVRD-VVLMGrygrrglfRRPSRADREAVDEALERVGleDLADRPIGELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 466 LDEPTNNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALNPERVLI 512
Cdd:COG1121 163 LDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRVLLL 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
326-517 |
6.03e-29 |
|
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: 114.35 E-value: 6.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGyyaqEHETIDVKR 404
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-GKDIT----KKNLRELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 SV-----------------------LENMvsaspNLTETEAR-RV--------LGSFLftgddsHKPAGVLSGGEKTRLA 452
Cdd:COG1122 76 KVglvfqnpddqlfaptveedvafgPENL-----GLPREEIReRVeealelvgLEHLA------DRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 453 LAMIVVSGANVLLLDEPTNNLDPASREEILDALA--HYEG-AVVLVSHD-EGAVEalNPERVLIMPEGT 517
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKrlNKEGkTVIIVTHDlDLVAE--LADRVIVLDDGR 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
326-516 |
8.37e-29 |
|
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: 113.38 E-value: 8.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLRIGYYAQE 396
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvppERRNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 -----HETidvkrsVLENMVSA---SPNLTETEARRVLGSFLFTGDDSH---KPAGvLSGGEKTRLALAMIVVSGANVLL 465
Cdd:cd03259 81 yalfpHLT------VAENIAFGlklRGVPKAEIRARVRELLELVGLEGLlnrYPHE-LSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 466 LDEPTNNLDPASREEILDALAHYEGA----VVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRElgitTIYVTHDQEEALALA-DRIAVMNEG 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
326-517 |
9.14e-29 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 113.37 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEiFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR---------IGY 392
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDdlsLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYiNGYSIRtdrkaarqsLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQeHETIDVKRSVLENM--------VSASPNLTETEA-RRVLGSflftGDDSHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:cd03263 80 CPQ-FDALFDELTVREHLrfyarlkgLPKSEIKEEVELlLRVLGL----TDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 464 LLLDEPTNNLDPASREEILDALAHYEG--AVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALC-DRIAIMSDGK 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
1.16e-28 |
|
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: 112.96 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdpRSGDPDELA 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGE--------PIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILdarGLGQLvlgmqestiamsssdasvsaAGMKKYGTLTD--RFLA--LGGYAAEAEAASIASNLNLPDRiLEQPL 156
Cdd:COG4133 74 RRRLA---YLGHA--------------------DGLKPELTVREnlRFWAalYGLRADREAIDEALEAVGLAGL-ADLPV 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVI-SHD 214
Cdd:COG4133 130 RQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGAVLLtTHQ 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
328-498 |
3.97e-28 |
|
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: 110.60 E-value: 3.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL----------RIGYYAQe 396
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILlDGKDLaslspkelarKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 hetidvkrsVLENMvsaspNLTetearrvlgsflftgDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPA 476
Cdd:cd03214 81 ---------ALELL-----GLA---------------HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180
....*....|....*....|....*.
gi 1552103373 477 SREEILD---ALAHYEG-AVVLVSHD 498
Cdd:cd03214 132 HQIELLEllrRLARERGkTVVMVLHD 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-232 |
1.28e-27 |
|
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: 109.02 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYLPQ 69
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKdikkepeevkrrIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DPRsgdpdelartrildarglgqlvlgmqestiamsssdasvsaagmkKYGTLTdrflalggyaaeaeaasIASNLNlpd 149
Cdd:cd03230 81 EPS---------------------------------------------LYENLT-----------------VRENLK--- 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 150 rileqplktLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR---GGFIVISHDIELVGETVNRVF 226
Cdd:cd03230 96 ---------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVA 166
|
....*.
gi 1552103373 227 YLDANR 232
Cdd:cd03230 167 ILNNGR 172
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
322-517 |
1.92e-26 |
|
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: 112.94 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 322 GRTPLHAENLSKSY--GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR--------- 389
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlGGVDLRdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 -IGYYAQEHETIDVkrSVLENMVSASPNLTETEARRV-----LGSFLftgddSHKPAGV----------LSGGEKTRLAL 453
Cdd:COG4987 410 rIAVVPQRPHLFDT--TLRENLRLARPDATDEELWAAlervgLGDWL-----AALPDGLdtwlgeggrrLSGGERRRLAL 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDPASREEILDAL-AHYEG-AVVLVSHDEGAVEALNpeRVLIMPEGT 517
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALLADLlEALAGrTVLLITHRLAGLERMD--RILVLEDGR 546
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-229 |
3.79e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.69 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYLPQ 69
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEdvardpaevrrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DPR-----------------SGDPDELARTRIldarglgqlvlgmqestiamsssdasvsaagmkkygtltDRFLALggy 132
Cdd:COG1131 81 EPAlypdltvrenlrffarlYGLPRKEARERI---------------------------------------DELLEL--- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 133 aaeaeaasiasnLNLPDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FI 209
Cdd:COG1131 119 ------------FGLTDA-ADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVL 185
|
250 260
....*....|....*....|
gi 1552103373 210 VISHDIELVGETVNRVFYLD 229
Cdd:COG1131 186 LSTHYLEEAERLCDRVAIID 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-232 |
5.65e-26 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.28 E-value: 5.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigYLPQDPRSGDPDELAR 81
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI-------YLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRIldarglgqlVLGMQESTIAMsssdasvsaagmkkyGTLTDRFLALGGYAAEAEAASIASN----LNLPDRILEQPLK 157
Cdd:COG4619 74 RQV---------AYVPQEPALWG---------------GTVRDNLPFPFQLRERKFDRERALEllerLGLPPDILDKPVE 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLDADS----VVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANR 232
Cdd:COG4619 130 RLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
326-517 |
1.16e-25 |
|
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: 103.42 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEHETIDvkRS 405
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDELPPLR--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 406 VleNMVSASPNLTetearrvlgsflftgddSHKPAG-----VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREE 480
Cdd:cd03229 78 I--GMVFQDFALF-----------------PHLTVLenialGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRRE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1552103373 481 ILDAL----AHYEGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:cd03229 139 VRALLkslqAQLGITVVLVTHDLDEAARLA-DRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
18-236 |
1.40e-25 |
|
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: 104.72 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDPRsgdpDELARTRI 84
Cdd:COG1122 18 DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKditkknlrelrrkVGLVFQNPD----DQLFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 85 LD--ARGLGQLvlGMQESTIAmsssdasvsaagmkkygTLTDRFLALggyaaeaeaasiasnLNLPDrILEQPLKTLSGG 162
Cdd:COG1122 94 EEdvAFGPENL--GLPREEIR-----------------ERVEEALEL---------------VGLEH-LADRPPHELSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLDANRQVID 236
Cdd:COG1122 139 QKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-498 |
1.42e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 105.56 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 319 MACGRTPLHAENLSKSY----GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGL 388
Cdd:COG1116 1 MSAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 RIGYYAQEHetidvkRSVLEN------MVSASPNLTETEARRVLGSFLFTGDDSHKPAgVLSGGEKTRLALAMIVVSGAN 462
Cdd:COG1116 81 DRGVVFQEPall-pwLTVLDNvalgleLRGVPKAERRERARELLELVGLAGFEDAYPH-QLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 463 VLLLDEPTNNLDPASR----EEILDALAHYEGAVVLVSHD 498
Cdd:COG1116 159 VLLMDEPFGALDALTRerlqDELLRLWQETGKTVLFVTHD 198
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
326-516 |
2.28e-25 |
|
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: 102.46 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS--LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA-GHGLRigyyaqehetiDV 402
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLR-----------DL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRSVLENMVSASPNltetearrvlGSFLFTG---DDshkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE 479
Cdd:cd03228 70 DLESLRKNIAYVPQ----------DPFLFSGtirEN------ILSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 480 EILDALAHYEG--AVVLVSHDEGAVEalNPERVLIMPEG 516
Cdd:cd03228 134 LILEALRALAKgkTVIVIAHRLSTIR--DADRIIVLDDG 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
326-516 |
2.53e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 2.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL-------------RI 390
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvNGQDLsrlkrreipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQEHETIDvKRSVLENM------VSASPNLTETEARRVLGSF-LftGDDSHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:COG2884 82 GVVFQDFRLLP-DRTVYENValplrvTGKSRKEIRRRVREVLDLVgL--SDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 464 LLLDEPTNNLDPASREEILDALA--HYEG-AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEeiNRRGtTVLIATHDLELVDRM-PKRVLELEDG 213
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
326-504 |
1.45e-24 |
|
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: 101.28 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEHETIDV--K 403
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYlgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 RSVLENMVSASPNLT------ETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDP 475
Cdd:TIGR01189 81 LPGLKPELSALENLHfwaaihGGAQRTIEDALAAVGltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|...
gi 1552103373 476 ASRE---EILDALAHYEGAVVLVSH-DEGAVEA 504
Cdd:TIGR01189 161 AGVAllaGLLRAHLARGGIVLLTTHqDLGLVEA 193
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-187 |
1.51e-24 |
|
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: 99.64 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDPRsgdpdELARTRI 84
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltdderkSLRKEIGYVFQDPQ-----LFPRLTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 85 LDARGLGQLVLGMQESTIAMSSSDAsvsaagMKKYGtltdrflalggyaaeaeaasiasNLNLPDRILEQPLKTLSGGQR 164
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEA------LEKLG-----------------------LGDLADRPVGERPGTLSGGQR 127
|
170 180
....*....|....*....|...
gi 1552103373 165 RRIELARILFSDASTLILDEPTN 187
Cdd:pfam00005 128 QRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-276 |
1.64e-24 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 107.34 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 4 VHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--EIGYLPQDPRSGDPDelaR 81
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTklEVAYFDQHRAELDPE---K 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TrILDarglgQLVLGMQESTIAmsssdasvsaaGMKKY--GTLTDrFLALggyaaeaeaasiasnlnlPDRILeQPLKTL 159
Cdd:PRK11147 399 T-VMD-----NLAEGKQEVMVN-----------GRPRHvlGYLQD-FLFH------------------PKRAM-TPVKAL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANrQVIDVYN 239
Cdd:PRK11147 442 SGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGN-GKIGRYV 520
|
250 260 270
....*....|....*....|....*....|....*..
gi 1552103373 240 MNWKNYQRQRAADEERRKKERANVEKKAGALQLQAAR 276
Cdd:PRK11147 521 GGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKR 557
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
326-516 |
2.69e-24 |
|
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: 100.82 E-value: 2.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-------AGHGLRIGYYAQEhE 398
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 399 TIDVKRSVLENMV--SASPNLTETEARRVLGSFLFT---GDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:cd03269 80 GLYPKMKVIDQLVylAQLKGLKKEEARRRIDEWLERlelSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 474 DPASRE---EILDALAHYEGAVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:cd03269 160 DPVNVEllkDVIRELARAGKTVILSTHQMELVEEL-CDRVLLLNKG 204
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-232 |
3.20e-24 |
|
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: 98.86 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 3 SVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdPRSGDPDELART 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-------DIAKLPLEELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 RILdarglgqlvlgmqestiamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasnlnlpdrILEQplktLSGG 162
Cdd:cd00267 74 RIG-----------------------------------------------------------------YVPQ----LSGG 84
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIVISHDIELVGETVNRVFYLDANR 232
Cdd:cd00267 85 QRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEgrtVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
329-516 |
3.68e-24 |
|
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: 100.40 E-value: 3.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL-------------RIGYY 393
Cdd:TIGR02673 5 HNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRiAGEDVnrlrgrqlpllrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDvKRSVLENM-----VSASPnltETEARRVLGSFLFTGDDSHK---PAGVLSGGEKTRLALAMIVVSGANVLL 465
Cdd:TIGR02673 85 FQDFRLLP-DRTVYENValpleVRGKK---EREIQRRVGAALRQVGLEHKadaFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 466 LDEPTNNLDPASREEILDAL--AHYEGA-VVLVSHDEGAVEAlNPERVLIMPEG 516
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLkrLNKRGTtVIVATHDLSLVDR-VAHRVIILDDG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
326-498 |
5.13e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 100.90 E-value: 5.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL-------------RI 390
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvDGQDVtalrgralrrlrrRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQEHETIDvKRSVLENmV------------SASPNLTETE---ARRVLGSF-LftGDDSHKPAGVLSGGEKTRLALA 454
Cdd:COG3638 83 GMIFQQFNLVP-RLSVLTN-VlagrlgrtstwrSLLGLFPPEDrerALEALERVgL--ADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILDAL---AHYEGAVVLVS-HD 498
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLrriAREDGITVVVNlHQ 206
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
334-511 |
6.73e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 6.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 334 SYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEHETIDVKRSVLENMVS- 412
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLPLTVRDLVAm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 413 -------ASPNLTEtEARRVLGSFLFT---GDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:NF040873 81 grwarrgLWRRLTR-DDRAAVDDALERvglADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|..
gi 1552103373 483 DALA--HYEGA-VVLVSHDEGAVEALNPERVL 511
Cdd:NF040873 160 ALLAeeHARGAtVVVVTHDLELVRRADPCVLL 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
319-499 |
8.93e-24 |
|
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: 99.82 E-value: 8.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 319 MACGRTP-LHAENLSKSY----GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL---- 388
Cdd:COG4181 1 MSSSSAPiIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlAGQDLfald 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 ----------RIGYYAQEHETIDvKRSVLEN-MVSA----SPNLTETEAR---RV-LGSFLftgddSHKPAGvLSGGEKT 449
Cdd:COG4181 81 edararlrarHVGFVFQSFQLLP-TLTALENvMLPLelagRRDARARARAlleRVgLGHRL-----DHYPAQ-LSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 450 RLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDE 499
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHDP 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-498 |
2.08e-23 |
|
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: 103.73 E-value: 2.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG--DLIASKGTI----DRGGEIGYLPQDPRSGD 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyhvALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 76 PDELARTRildarglgqlvlgMQESTIAMSSSDASVSAAGMKKYGTLTDRFLAL----------------GGYAAEAEAA 139
Cdd:TIGR03269 81 PCPVCGGT-------------LEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFALygddtvldnvlealeeIGYEGKEAVG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 140 SIASNL---NLPDRILEQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSV-VWLREFLKNYRGGFIVIS 212
Cdd:TIGR03269 148 RAVDLIemvQLSHRITHIA-RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVhNALEEAVKASGISMVLTS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 213 HDIELVGETVNRVFYLDaNRQVidvynmnwknyqrqraadeerrkkeranveKKAGALQLQAARFgakaskaaaahqmva 292
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLE-NGEI------------------------------KEEGTPDEVVAVF--------------- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 293 raekmlsgLEEVRAVDRVAKLRFPTPMacgrtpLHAENLSKSYGSLE--IFTAVD---LAIDRGSKVVILGLNGAGKTTL 367
Cdd:TIGR03269 261 --------MEGVSEVEKECEVEVGEPI------IKVRNVSKRYISVDrgVVKAVDnvsLEVKEGEIFGIVGTSGAGKTTL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 368 LRILGGVDQP-----------------DTGVIEAGHGLR-IGYYAQEHeTIDVKRSVLENMVSA-SPNLTETEARR---- 424
Cdd:TIGR03269 327 SKIIAGVLEPtsgevnvrvgdewvdmtKPGPDGRGRAKRyIGILHQEY-DLYPHRTVLDNLTEAiGLELPDELARMkavi 405
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 425 VLGSFLFTGDDS----HKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR----EEILDALAHYEGAVVLVS 496
Cdd:TIGR03269 406 TLKMVGFDEEKAeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEMEQTFIIVS 485
|
..
gi 1552103373 497 HD 498
Cdd:TIGR03269 486 HD 487
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
326-516 |
2.15e-23 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 98.66 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI----EAGHGLRigyyaqEHETid 401
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgEDITGLP------PHEI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 VKR---------------SVLEN-MVSASPNLTET---------------EARRVLGsFLFTGDDSHKPAGVLSGGEKTR 450
Cdd:cd03219 73 ARLgigrtfqiprlfpelTVLENvMVAAQARTGSGlllararreereareRAEELLE-RVGLADLADRPAGELSYGQQRR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 451 LALAMIVVSGANVLLLDEPTNNLDPASREEILD---ALAHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:cd03219 152 LEIARALATDPKLLLLDEPAAGLNPEETEELAElirELRERGITVLLVEHDMDVVMSLA-DRVTVLDQG 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
2.17e-23 |
|
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: 97.12 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 3 SVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELART 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------KDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 R-----ILDARGLGQLvlgmqestiamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasnlnlpdriLEQPLK 157
Cdd:cd03214 75 IayvpqALELLGLAHL----------------------------------------------------------ADRPFN 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISHDIELV 218
Cdd:cd03214 97 ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERgktvVMVLHDLNLA 161
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
329-498 |
2.53e-23 |
|
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: 98.79 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSL-EIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA---------GHGLR-----IGYY 393
Cdd:cd03256 4 ENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdinklkGKALRqlrrqIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDvKRSVLENMVSASpnLTETEARRVLGSfLFTG----------------DDSHKPAGVLSGGEKTRLALAMIV 457
Cdd:cd03256 84 FQQFNLIE-RLSVLENVLSGR--LGRRSTWRSLFG-LFPKeekqralaalervgllDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1552103373 458 VSGANVLLLDEPTNNLDPASREEILDAL---AHYEGAVVLVS-HD 498
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLkriNREEGITVIVSlHQ 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
326-516 |
2.70e-23 |
|
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: 98.03 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSkVVILGLNGAGKTTLLRILGGVDQPDTGVIE--------AGHGLR--IGYYAQ 395
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLRrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 E---HETIDVkRSVLENMVSA---SPNLTETEARRVLgSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:cd03264 80 EfgvYPNFTV-REFLDYIAWLkgiPSKEVKARVDEVL-ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 470 TNNLDPASRE---EILDALAhyEGAVVLVS-HDEGAVEALnPERVLIMPEG 516
Cdd:cd03264 158 TAGLDPEERIrfrNLLSELG--EDRIVILStHIVEDVESL-CNQVAVLNKG 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
326-516 |
2.77e-23 |
|
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: 99.00 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEA-GHGL----------RIGYY 393
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGERRggedvwelrkRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQE-HETIDVKRSVLENMVSAS-------PNLTETE---ARRVLGSF-LftGDDSHKPAGVLSGGEKTRLALAMIVVSGA 461
Cdd:COG1119 84 SPAlQLRFPRDETVLDVVLSGFfdsiglyREPTDEQrerARELLELLgL--AHLADRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDALAHY--EG--AVVLVSHDegaVEALNPE--RVLIMPEG 516
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHH---VEEIPPGitHVLLLKDG 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
291-516 |
2.80e-23 |
|
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: 103.30 E-value: 2.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 291 VARAEKMLSGLEEVRAVDRVAKLRFPTPmacGRTPLHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLR 369
Cdd:COG4988 305 IAAAEKIFALLDAPEPAAPAGTAPLPAA---GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 370 ILGGVDQPDTGVIE-AGHGLR----------IGYYAQeHETIdVKRSVLENMVSASPNLTETEARRVL-----GSFLftg 433
Cdd:COG4988 382 LLLGFLPPYSGSILiNGVDLSdldpaswrrqIAWVPQ-NPYL-FAGTIRENLRLGRPDASDEELEAALeaaglDEFV--- 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 434 ddSHKPAGV----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY-EG-AVVLVSHDEGA 501
Cdd:COG4988 457 --AALPDGLdtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLAL 534
|
250
....*....|....*
gi 1552103373 502 VEalNPERVLIMPEG 516
Cdd:COG4988 535 LA--QADRILVLDDG 547
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
326-498 |
4.94e-23 |
|
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: 97.16 E-value: 4.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS----LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLRIGYYAQ 395
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVkRSVLEN------MVSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:cd03293 81 QDALLPW-LTVLDNvalgleLQGVPKAEARERAEELLELVGLSGFENAYPHQ-LSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 1552103373 470 TNNLDPASR----EEILDALAHYEGAVVLVSHD 498
Cdd:cd03293 159 FSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-234 |
6.33e-23 |
|
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: 97.81 E-value: 6.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYL 67
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlaslsrrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDPRSGDP----DELARTRILDARGLGQLvlgmqestiamsssdasvsaagmkkygTLTDRFLAlggyaaeaeaasias 143
Cdd:COG1120 81 PQEPPAPFGltvrELVALGRYPHLGLFGRP---------------------------SAEDREAV--------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 144 nlnlpDRILEQ---------PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVV----WLREFLKNYRGGFIV 210
Cdd:COG1120 119 -----EEALERtglehladrPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLevleLLRRLARERGRTVVM 193
|
250 260
....*....|....*....|....
gi 1552103373 211 ISHDIELVGETVNRVFYLDANRQV 234
Cdd:COG1120 194 VLHDLNLAARYADRLVLLKDGRIV 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
329-498 |
7.42e-23 |
|
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: 102.60 E-value: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLE--IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLR--IGYYAQ 395
Cdd:COG2274 477 ENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDgidlrqidpASLRrqIGVVLQ 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDvkRSVLENMVSASPNLTETEARRV-----LGSFLftgdDSHkPAG----------VLSGGEKTRLALAMIVVSG 460
Cdd:COG2274 557 DVFLFS--GTIRENITLGDPDATDEEIIEAarlagLHDFI----EAL-PMGydtvvgeggsNLSGGQRQRLAIARALLRN 629
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDALAHYEG--AVVLVSHD 498
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
339-498 |
7.73e-23 |
|
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: 95.95 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 339 EIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG--------HGL-----RIGYYAQEHETIDVKRS 405
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgepldysrKGLlerrqRVGLVFQDPDDQLFAAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 406 VLENmVSASP---NLTETEARRVLGSFLFTGDDSH---KPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE 479
Cdd:TIGR01166 86 VDQD-VAFGPlnlGLSEAEVERRVREALTAVGASGlreRPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|..
gi 1552103373 480 EILDALAHYEGA---VVLVSHD 498
Cdd:TIGR01166 165 QMLAILRRLRAEgmtVVISTHD 186
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
330-498 |
1.45e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.35 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGS-LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEHEtIDVKRSVLE 408
Cdd:PRK11819 11 RVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQ-LDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NMVSASPNLTETEAR--RVLGSFLFTGDDSHK--------------------------------------PAGVLSGGEK 448
Cdd:PRK11819 90 NVEEGVAEVKAALDRfnEIYAAYAEPDADFDAlaaeqgelqeiidaadawdldsqleiamdalrcppwdaKVTKLSGGER 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 449 TRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHD 498
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
326-516 |
1.72e-22 |
|
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: 95.67 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYYAQEHETIDVK-- 403
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKLTDDKKNINELRQKvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 -----------RSVLENMVSA-------SPNLTETEARRVLGSflfTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:cd03262 80 mvfqqfnlfphLTVLENITLApikvkgmSKAEAEERALELLEK---VGlaDKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 464 LLLDEPTNNLDPASREEILD---ALAHyEG-AVVLVSHDEG-AVEALNpeRVLIMPEG 516
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDvmkDLAE-EGmTMVVVTHEMGfAREVAD--RVIFMDDG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
328-516 |
2.03e-22 |
|
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: 95.51 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGLRigyyaqeHETIDVKRS- 405
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGrATVAGHDVV-------REPREVRRRi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 406 -VLENMVSASPNLTETE----------------ARRV--LGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:cd03265 76 gIVFQDLSVDDELTGWEnlyiharlygvpgaerRERIdeLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 467 DEPTNNLDPASRE---EILDALAHYEG-AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:cd03265 156 DEPTIGLDPQTRAhvwEYIEKLKEEFGmTILLTTHYMEEAEQL-CDRVAIIDHG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-230 |
5.62e-22 |
|
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: 94.49 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDL----ELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI----------------DR 60
Cdd:cd03257 1 LLEVKNLsvsfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIifdgkdllklsrrlrkIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 61 GGEIGYLPQDPRSG-DPdelaRTRILDarglgQLVLGMQESTIamsssdasvsaagMKKYGTLTDRFLALggyaaeaeaa 139
Cdd:cd03257 81 RKEIQMVFQDPMSSlNP----RMTIGE-----QIAEPLRIHGK-------------LSKKEARKEAVLLL---------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 140 siASNLNLPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDAdSVVW-----LREFLKNYRGGFIVISHD 214
Cdd:cd03257 129 --LVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDV-SVQAqildlLKKLQEELGLTLLFITHD 205
|
250
....*....|....*.
gi 1552103373 215 IELVGETVNRVFYLDA 230
Cdd:cd03257 206 LGVVAKIADRVAVMYA 221
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
12-232 |
5.84e-22 |
|
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: 92.83 E-value: 5.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDPRsgdpde 78
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVdlrdldleslrknIAYVPQDPF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 lartrILDarglgqlvlgmqestiamsssdasvsaagmkkyGTLTDrflalggyaaeaeaasiasnlNLpdrileqplkt 158
Cdd:cd03228 87 -----LFS---------------------------------GTIRE---------------------NI----------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLDANR 232
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
326-495 |
6.91e-22 |
|
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: 94.04 E-value: 6.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR-----------IGYY 393
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRfDGRDITglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDvKRSVLENMVSASPNLTETEAR----RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:cd03224 81 PEGRRIFP-ELTVEENLLLGAYARRRAKRKarleRVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180
....*....|....*....|....*....
gi 1552103373 470 TNNLDPASREEILDALAHY--EG-AVVLV 495
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELrdEGvTILLV 188
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
326-517 |
7.13e-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: 95.11 E-value: 7.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE--------------AGHGL--- 388
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdgrditglpphriARLGIart 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 ----------------RIGYYAQEHETIDVKRSVLENMVSASPNLTEtEARRVLGsflFTG--DDSHKPAGVLSGGEKTR 450
Cdd:COG0411 85 fqnprlfpeltvlenvLVAAHARLGRGLLAALLRLPRARREEREARE-RAEELLE---RVGlaDRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 451 LALAMIVVSGANVLLLDEPTNNLDPASREEILD---ALAHYEG-AVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAElirRLRDERGiTILLIEHDMDLVMGL-ADRIVVLDFGR 230
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
326-481 |
7.17e-22 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.53 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH------------GLRIGYY 393
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHeTIDVKRSVLENMVSA--SPNLTETEARRVLGSFLftgDD------SHKPAGVLSGGEKTRLALAMIVVSGANVLL 465
Cdd:cd03218 81 PQEA-SIFRKLTVEENILAVleIRGLSKKEREEKLEELL---EEfhithlRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170
....*....|....*.
gi 1552103373 466 LDEPTNNLDPASREEI 481
Cdd:cd03218 157 LDEPFAGVDPIAVQDI 172
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
329-498 |
8.49e-22 |
|
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: 94.11 E-value: 8.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGyYAQEHETIDVKR---- 404
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DGEDIS-GLSEAELYRLRRrmgm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 -----------SVLENMvsASP-----NLTETEARRV----LGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVL 464
Cdd:cd03261 82 lfqsgalfdslTVFENV--AFPlrehtRLSEEEIREIvlekLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 465 LLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHD 498
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHD 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
326-516 |
9.82e-22 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 94.29 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEHETIDVK-- 403
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD-GEDLTDSKKDINKLRRKvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 -----------RSVLENMVSA-------SPNLTETEARRVLGSF-LftGDDSHKPAGVLSGGEKTRL----ALAMivvsG 460
Cdd:COG1126 81 mvfqqfnlfphLTVLENVTLApikvkkmSKAEAEERAMELLERVgL--ADKADAYPAQLSGGQQQRVaiarALAM----E 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDA---LAHyEG-AVVLVSHDEG-AVEALNpeRVLIMPEG 516
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVmrdLAK-EGmTMVVVTHEMGfAREVAD--RVVFMDGG 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
344-471 |
1.08e-21 |
|
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: 91.56 E-value: 1.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI-----------EAGHGLRIGYYAQEHeTIDVKRSVLENMVS 412
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTIlldgqdltddeRKSLRKEIGYVFQDP-QLFPRLTVRENLRL 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 413 ASP---NLTETEARRV------LGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTN 471
Cdd:pfam00005 83 GLLlkgLSKREKDARAeealekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
326-497 |
1.73e-21 |
|
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: 92.56 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI----EAGHGLRIGY-----YAQE 396
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllngGPLDFQRDSIargllYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 HETIDVKRSVLENM-----VSASPNLTETEARRVLGSFlftgddSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTN 471
Cdd:cd03231 81 APGIKTTLSVLENLrfwhaDHSDEQVEEALARVGLNGF------EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 1552103373 472 NLDPASREEILDALA-HYE--GAVVLVSH 497
Cdd:cd03231 155 ALDKAGVARFAEAMAgHCArgGMVVLTTH 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-236 |
2.39e-21 |
|
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: 92.65 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDPR-----------S 73
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdirqldpaDLRRNIGYVPQDVTlfygtlrdnitL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 74 GDP--DELARTRILDARGLGQLVLGmqestiamsssdasvSAAGMkkygtltDRFLALGGYAaeaeaasiasnlnlpdri 151
Cdd:cd03245 101 GAPlaDDERILRAAELAGVTDFVNK---------------HPNGL-------DLQIGERGRG------------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 152 leqplktLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLD 229
Cdd:cd03245 141 -------LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLL-DLVDRIIVMD 212
|
....*..
gi 1552103373 230 ANRQVID 236
Cdd:cd03245 213 SGRIVAD 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
326-513 |
2.60e-21 |
|
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: 92.57 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS-LEIFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGH-------------G 387
Cdd:cd03257 2 LEVKNLSVSFPTgGGSVKALDdvsFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfDGKdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQE-----HETIDVKRSVLENMVSASPNLTETEARRVLGSFLFTGDDSHK-----PAGvLSGGEKTRLALAMIV 457
Cdd:cd03257 82 KEIQMVFQDpmsslNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryPHE-LSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 458 VSGANVLLLDEPTNNLDPASREEILDALAH----YEGAVVLVSHDEGAVEALNpERVLIM 513
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIA-DRVAVM 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
326-497 |
3.05e-21 |
|
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: 90.57 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLRIgyyaqehetidvkr 404
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILvDGKEVSF-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 svlenmvsASPNltetEARRvlgsflftgddshkpAGV-----LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE 479
Cdd:cd03216 67 --------ASPR----DARR---------------AGIamvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180
....*....|....*....|.
gi 1552103373 480 ---EILDALAHYEGAVVLVSH 497
Cdd:cd03216 120 rlfKVIRRLRAQGVAVIFISH 140
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
325-513 |
4.37e-21 |
|
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: 96.59 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 325 PLHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI-----------EAGHGLRIGY 392
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQeHETIdVKRSVLENMVSASPNLTETEARRV-----LGSFLFT-GDDSHKPAGV----LSGGEKTRLALAMIVVSGAN 462
Cdd:TIGR02857 401 VPQ-HPFL-FAGTIAENIRLARPDASDAEIREAleragLDEFVAAlPQGLDTPIGEggagLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALAHYEG--AVVLVSHDEGAVEALnpERVLIM 513
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALAALA--DRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
325-499 |
4.99e-21 |
|
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: 96.28 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 325 PLHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-----------VIEAGHGLRIGY 392
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEHETIDVkrSVLENMVSASPNLTETEARRVLGSF--------LFTGDDS--HKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:TIGR02868 414 CAQDAHLFDT--TVRENLRLARPDATDEELWAALERVgladwlraLPDGLDTvlGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 463 VLLLDEPTNNLDPASREEILDAL--AHYEGAVVLVSHDE 499
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLlaALSGRTVVLITHHL 530
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
327-517 |
6.88e-21 |
|
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: 90.78 E-value: 6.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 327 HAENLSKSYG-SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-----AGHGLR---IGYYAQEH 397
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpIKAKERrksIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ETIDVKRSVLENMVSASPNLTE--TEARRVLGSF-LFTGDDSHkPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLD 474
Cdd:cd03226 81 DYQLFTDSVREELLLGLKELDAgnEQAETVLKDLdLYALKERH-PLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 475 PASREEILDA---LAHYEGAVVLVSHD-EGAVEALNpeRVLIMPEGT 517
Cdd:cd03226 159 YKNMERVGELireLAAQGKAVIVITHDyEFLAKVCD--RVLLLANGA 203
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
351-516 |
8.19e-21 |
|
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: 90.82 E-value: 8.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 351 GSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGL---------------RIGYYAQE-----HetIDVKRSVLENM 410
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQyalfpH--LNVRENLAFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 411 VSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL----DALA 486
Cdd:cd03297 101 KRKRNREDRISVDELLDLLGLDHLLNRYPAQ-LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLpelkQIKK 179
|
170 180 190
....*....|....*....|....*....|
gi 1552103373 487 HYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLA-DRIVVMEDG 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
326-485 |
1.13e-20 |
|
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: 91.21 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS-LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI---------EAGHGLR-----I 390
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditkLRGKKLRklrrrI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQEHETIDvKRSVLENM----VSASPNL-------TETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIV 457
Cdd:TIGR02315 82 GMIFQHYNLIE-RLTVLENVlhgrLGYKPTWrsllgrfSEEDKERALSALERVGlaDKAYQRADQLSGGQQQRVAIARAL 160
|
170 180
....*....|....*....|....*...
gi 1552103373 458 VSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYL 188
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
326-516 |
1.22e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 93.29 E-value: 1.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSleiFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG----------HGLRIGY 392
Cdd:COG1118 3 IEVRNISKRFGS---FTLlddVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlppRERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQE-----HETidvkrsVLEN----MVSASPNLTETEAR--RVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGA 461
Cdd:COG1118 80 VFQHyalfpHMT------VAENiafgLRVRPPSKAEIRARveELLELVQLEGLADRYPSQ-LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 462 NVLLLDEPTNNLDPASREEI----LDALAHYEGAVVLVSHD-EGAVE-AlnpERVLIMPEG 516
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELrrwlRRLHDELGGTTVFVTHDqEEALElA---DRVVVMNQG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
326-512 |
1.32e-20 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 90.58 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLeIFTAvDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghglRIGYYAQEHETIDV-KR 404
Cdd:COG3840 2 LRLDDLTYRYGDF-PLRF-DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSG--------RILWNGQDLTALPPaER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 ---------------SVLENM---VSASPNLTETEARRV--------LGSFLftgddSHKPaGVLSGGEKTRLALAMIVV 458
Cdd:COG3840 72 pvsmlfqennlfphlTVAQNIglgLRPGLKLTAEQRAQVeqalervgLAGLL-----DRLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEILD---ALAHYEGAVVL-VSHDEGAVEALNPERVLI 512
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDlvdELCRERGLTVLmVTHDPEDAARIADRVLLV 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
326-497 |
1.55e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLRIGYYAQE-----Het 399
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKlDGGDIDDPDVAEAchylgH-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 idvkRSVLENMVSASPNLT---------ETEARRVLgSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:PRK13539 81 ----RNAMKPALTVAENLEfwaaflggeELDIAAAL-EAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1552103373 471 NNLDPASREEILDAL-AHYE--GAVVLVSH 497
Cdd:PRK13539 156 AALDAAAVALFAELIrAHLAqgGIVIAATH 185
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-232 |
1.80e-20 |
|
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: 89.94 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGdKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYLPQ 69
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DPRsGDP--------DELARTRILDARGLGQLVLGMQEstiamsssdasvsaagmkkygtltdrflalggyaaeaeaasi 141
Cdd:cd03264 80 EFG-VYPnftvreflDYIAWLKGIPSKEVKARVDEVLE------------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 142 asNLNLPDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVI--SHDIELVG 219
Cdd:cd03264 117 --LVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVE 193
|
250
....*....|...
gi 1552103373 220 ETVNRVFYLDANR 232
Cdd:cd03264 194 SLCNQVAVLNKGK 206
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
12-236 |
1.98e-20 |
|
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: 94.90 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELARtrildarglg 91
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDG------IDLRQIDPASLRR---------- 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 QLVLGMQESTIAmsssdasvsaagmkkYGTLTDRfLALGGYAAEAEAASIASNL-NLPDRILEQPL----------KTLS 160
Cdd:COG2274 550 QIGVVLQDVFLF---------------SGTIREN-ITLGDPDATDEEIIEAARLaGLHDFIEALPMgydtvvgeggSNLS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLDANRQVID 236
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI-RLADRIIVLDKGRIVED 690
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
12-234 |
3.10e-20 |
|
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: 88.85 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI----------DRGGEIGYLPQDPRsgdpDELAR 81
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngkpikakERRKSIGYVMQDVD----YQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDarglgQLVLGMQESTiamsssdasvsaagmkKYGTLTDRFLALggyaaeaeaasiasnLNLPDRILEQPLkTLSG 161
Cdd:cd03226 87 DSVRE-----ELLLGLKELD----------------AGNEQAETVLKD---------------LDLYALKERHPL-SLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLDADSVV----WLREfLKNYRGGFIVISHDIELVGETVNRVFYLDANRQV 234
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMErvgeLIRE-LAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-217 |
3.50e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.22 E-value: 3.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG------RPLADWSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRildarglgqlvlGMqestiamsssdasvsaagMKKYGTLTDRFL-----ALGGYAAEAEAASIAsnlNLPDRILEQ- 154
Cdd:PRK13548 76 RRR------------AV------------------LPQHSSLSFPFTveevvAMGRAPHGLSRAEDD---ALVAAALAQv 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 155 --------PLKTLSGGQRRRIELARIL------FSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIE 216
Cdd:PRK13548 123 dlahlagrDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDlahqHHVLRLARQLAHERGLAVIVVLHDLN 202
|
.
gi 1552103373 217 L 217
Cdd:PRK13548 203 L 203
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-230 |
3.88e-20 |
|
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: 93.67 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELR-VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYL 67
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrqIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDP-----------RSGDPD----ELARtrILDARGLGQLVLGMQEstiamsssdasvsaagmkKYGTLtdrfLALGGy 132
Cdd:COG4988 417 PQNPylfagtirenlRLGRPDasdeELEA--ALEAAGLDEFVAALPD------------------GLDTP----LGEGG- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 133 aaeaeaasiasnlnlpdrileqplKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIV 210
Cdd:COG4988 472 ------------------------RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVIL 527
|
250 260
....*....|....*....|
gi 1552103373 211 ISHDIELVGEtVNRVFYLDA 230
Cdd:COG4988 528 ITHRLALLAQ-ADRILVLDD 546
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-234 |
3.90e-20 |
|
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: 93.68 E-value: 3.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELR--VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGY 66
Cdd:COG4987 334 LELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDP-----------RSGDPD----ELARtrILDARGLGQLVLGmqestiamsssdasvsaagmkkygtltdrflalgg 131
Cdd:COG4987 414 VPQRPhlfdttlrenlRLARPDatdeELWA--ALERVGLGDWLAA----------------------------------- 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 132 yaaeaeaasiasnlnLPDRiLEQPL----KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSV-VWLREFLKNYRG 206
Cdd:COG4987 457 ---------------LPDG-LDTWLgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEqALLADLLEALAG 520
|
250 260
....*....|....*....|....*....
gi 1552103373 207 -GFIVISHDIELVgETVNRVFYLDANRQV 234
Cdd:COG4987 521 rTVLLITHRLAGL-ERMDRILVLEDGRIV 548
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
329-505 |
4.59e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.67 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIeaghglRIGyyaqeheTIDV------ 402
Cdd:COG3839 7 ENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI------LIG-------GRDVtdlppk 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KR---------------SVLENMvsASP----NLTETE-ARRV--------LGSFLftgddSHKPAGvLSGGEKTRLALA 454
Cdd:COG3839 74 DRniamvfqsyalyphmTVYENI--AFPlklrKVPKAEiDRRVreaaellgLEDLL-----DRKPKQ-LSGGQRQRVALG 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEI---LDALaHYE-GA-VVLVSHDegAVEAL 505
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMraeIKRL-HRRlGTtTIYVTHD--QVEAM 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-217 |
4.62e-20 |
|
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: 88.18 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgdpdELAR 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT--------------PLAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARGLgqLVLGMQEstiamsssdasvsaaGMKkyGTLTD----RFLA--LGGYAAEAEAASIASNLN-LPDRileq 154
Cdd:TIGR01189 67 QRDEPHENI--LYLGHLP---------------GLK--PELSAlenlHFWAaiHGGAQRTIEDALAAVGLTgFEDL---- 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 155 PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVISHDIEL 217
Cdd:TIGR01189 124 PAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlaRGGIVLLTTHQDL 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-516 |
4.78e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylPQDPRSgdpdelartrILDARGLG-----Q- 92
Cdd:COG1129 22 GVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE----PVRFRS----------PRDAQAAGiaiihQe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 ------------LVLGMQESTiamsssdasvsaAGMKKYGTLTDRFLALggyaaeaeaaSIASNLNLPdriLEQPLKTLS 160
Cdd:COG1129 88 lnlvpnlsvaenIFLGREPRR------------GGLIDWRAMRRRAREL----------LARLGLDID---PDTPVGDLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWL----REfLKNyRG-GFIVISHDIELVGE-----TVNRvfylda 230
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKA-QGvAIIYISHRLDEVFEiadrvTVLR------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 231 NRQVIDVYNMnwknyqrqRAADEErrkkeranvekkagalqlqaarfgakaskaaaahQMVaraEKMlsgleevraVDRV 310
Cdd:COG1129 215 DGRLVGTGPV--------AELTED----------------------------------ELV---RLM---------VGRE 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 311 AKLRFP-TPMACGRTPLHAENLSKSygslEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL 388
Cdd:COG1129 241 LEDLFPkRAAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRlDGKPV 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 RIGYYAQ----------E---HETIDVKRSVLENMVSA-----------SPNLTETEARRVLGSFLFTGDDSHKPAGVLS 444
Cdd:COG1129 317 RIRSPRDairagiayvpEdrkGEGLVLDLSIRENITLAsldrlsrggllDRRRERALAEEYIKRLRIKTPSPEQPVGNLS 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 445 GGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHyEG-AVVLVSHDegaveaLnPE------RVLIMP 514
Cdd:COG1129 397 GGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIyrlIRELAA-EGkAVIVISSE------L-PEllglsdRILVMR 468
|
..
gi 1552103373 515 EG 516
Cdd:COG1129 469 EG 470
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
324-516 |
7.28e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.35 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 324 TPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHglrigyyAQEHETIDVK 403
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-------APLAEAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 R------------SVLENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTN 471
Cdd:PRK11247 84 RlmfqdarllpwkKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 472 NLDPASREEILDALA----HYEGAVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:PRK11247 163 ALDALTRIEMQDLIEslwqQHGFTVLLVTHDVSEAVAM-ADRVLLIEEG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
333-516 |
7.89e-20 |
|
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: 90.14 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 333 KSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL---------RIGYYAQEHeTIDV 402
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGtARVAGYDVvreprkvrrSIGIVPQYA-SVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRSVLENMV------SASPNLTETEARRVLGSFLFtGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPA 476
Cdd:TIGR01188 80 DLTGRENLEmmgrlyGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 477 SREEILDALAHYEGA---VVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:TIGR01188 159 TRRAIWDYIRALKEEgvtILLTTHYMEEADKLC-DRIAIIDHG 200
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
326-481 |
8.07e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 88.49 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HG---LRIGYY 393
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmHErarLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEhETIDVKRSVLENMVSA---SPNLTETEARRVLGSFLFTGDDSH---KPAGVLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:TIGR04406 82 PQE-ASIFRKLTVEENIMAVleiRKDLDRAEREERLEALLEEFQISHlrdNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170
....*....|....
gi 1552103373 468 EPTNNLDPASREEI 481
Cdd:TIGR04406 161 EPFAGVDPIAVGDI 174
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-217 |
1.09e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.24 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqDPRSGDPDELA 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildarglgqlVLGMQEstiamsssdasvsaaGMKKYGTLTD--RFLA--LGGYAAEAEAASIASNLnlpDRILEQPL 156
Cdd:PRK13539 76 H------------YLGHRN---------------AMKPALTVAEnlEFWAafLGGEELDIAAALEAVGL---APLAHLPF 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVISHDIEL 217
Cdd:PRK13539 126 GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHlaQGGIVIAATHIPL 188
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-516 |
1.20e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 88.25 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG----HGLRigyyaqEHE--- 398
Cdd:COG4674 11 LYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGgtdlTGLD------EHEiar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 399 ----------TIDVKRSVLENMVSASPNlteteARRVLGSFLF----------------TG--DDSHKPAGVLSGGEKTR 450
Cdd:COG4674 85 lgigrkfqkpTVFEELTVFENLELALKG-----DRGVFASLFArltaeerdrieevletIGltDKADRLAGLLSHGQKQW 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 451 LALAMIVVSGANVLLLDEPTNNLDPASRE---EILDALAHyEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:COG4674 160 LEIGMLLAQDPKLLLLDEPVAGMTDAETErtaELLKSLAG-KHSVVVVEHDMEFVRQIA-RKVTVLHQG 226
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
328-498 |
1.32e-19 |
|
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: 87.62 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGG-----VDQPDTGVIEAGhGLRIgyYAQEHETIDV 402
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLD-GKDI--YDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRSVleNMVSASPNL-----------------------TETEARRVL-GSFLFTGDDSHKPAGVLSGGEKTRLALAMIVV 458
Cdd:cd03260 80 RRRV--GMVFQKPNPfpgsiydnvayglrlhgiklkeeLDERVEEALrKAALWDEVKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEILDALA--HYEGAVVLVSHD 498
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
326-505 |
1.42e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 90.16 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIeaghglRIGyyaqEHETIDV--- 402
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI------LLD----GRDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRSVleNMVSAS----PNLT----------------ETEARRV--------LGSFLftgddsHKPAGVLSGGEKTRLALA 454
Cdd:COG3842 76 KRNV--GMVFQDyalfPHLTvaenvafglrmrgvpkAEIRARVaellelvgLEGLA------DRYPHQLSGGQQQRVALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASRE----EILDALAHYEGAVVLVSHDEGavEAL 505
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAKLREemreELRRLQRELGITFIYVTHDQE--EAL 200
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
329-517 |
1.61e-19 |
|
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: 86.89 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEaghgLRIGYYAQEHETIDVKRSVLE 408
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT----FDGKSYQKNIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 ------NMvSASPNL---------TETEARRVLGSFLFtGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:cd03268 80 apgfypNL-TARENLrllarllgiRKKRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1552103373 474 DPAS----REEILDaLAHYEGAVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:cd03268 158 DPDGikelRELILS-LRDQGITVLISSHLLSEIQKV-ADRIGIINKGK 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
326-516 |
2.31e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.90 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLRiGYYAQE-------- 396
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRlNGRPLA-DWSPAElarrravl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 ------------HETIDVKRSVLENMVSASPNLTETEARRV-LGSFlftgddSHKPAGVLSGGEKTRLALAMIVV----- 458
Cdd:PRK13548 82 pqhsslsfpftvEEVVAMGRAPHGLSRAEDDALVAAALAQVdLAHL------AGRDYPQLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 459 -SGANVLLLDEPTNNLDPASREEILDA---LAHYEG-AVVLVSHDegaveaLN-----PERVLIMPEG 516
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLarqLAHERGlAVIVVLHD------LNlaaryADRIVLLHQG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-214 |
2.50e-19 |
|
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: 91.15 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--EIGYLPQDPRSGDPDEL 79
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtvKLAYVDQSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARTRILDarGLGQLVLGMQEstiamsssdasvsaAGMKKYgtlTDRFlalggyaaeaeaasiasNLNLPDRilEQPLKTL 159
Cdd:TIGR03719 403 VWEEISG--GLDIIKLGKRE--------------IPSRAY---VGRF-----------------NFKGSDQ--QKKVGQL 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHD 214
Cdd:TIGR03719 445 SGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHD 499
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-238 |
2.92e-19 |
|
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: 87.40 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLPqdprsgdPDEL 79
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfDGRDITGLP-------PHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARtrildaRGLG---Q-------------LVLGMQESTIAMSSSDASVSAAGMKKYGTLTDR------FLALGGYaaeae 137
Cdd:COG0411 77 AR------LGIArtfQnprlfpeltvlenVLVAAHARLGRGLLAALLRLPRARREEREARERaeelleRVGLADR----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 138 aasiasnlnlpdriLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISH 213
Cdd:COG0411 146 --------------ADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgitiLLIEH 211
|
250 260 270
....*....|....*....|....*....|....*....
gi 1552103373 214 DIELVGETVNRVFYLD--------------ANRQVIDVY 238
Cdd:COG0411 212 DMDLVMGLADRIVVLDfgrviaegtpaevrADPRVIEAY 250
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
329-516 |
4.75e-19 |
|
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: 86.14 E-value: 4.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghglRIGYYAQEHETIDV-KRSVl 407
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSG--------EILLDGKDITNLPPhKRPV- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 eNMVSAS----PNLTETE----------------ARRVLGSFLFTGDDSH---KPAGvLSGGEKTRLALAMIVVSGANVL 464
Cdd:cd03300 75 -NTVFQNyalfPHLTVFEniafglrlkklpkaeiKERVAEALDLVQLEGYanrKPSQ-LSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 465 LLDEPTNNLDPASREEI---LDALAHYEG-AVVLVSHDEGavEALN-PERVLIMPEG 516
Cdd:cd03300 153 LLDEPLGALDLKLRKDMqleLKRLQKELGiTFVFVTHDQE--EALTmSDRIAVMNKG 207
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-274 |
5.88e-19 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 90.23 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID--RGGEIGYLPQDPRsgdpdELARTrilDARG 89
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlaKGIKLGYFAQHQL-----EFLRA---DESP 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 90 LGQLV-LGMQEStiamsssdasvsAAGMKKYgtltdrflaLGGYAAEAeaasiasnlnlpDRILEqPLKTLSGGQRRRIE 168
Cdd:PRK10636 395 LQHLArLAPQEL------------EQKLRDY---------LGGFGFQG------------DKVTE-ETRRFSGGEKARLV 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 169 LARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRvFYLDANRQViDVYNMNWKNYQrQ 248
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDD-LYLVHDGKV-EPFDGDLEDYQ-Q 517
|
250 260
....*....|....*....|....*.
gi 1552103373 249 RAADEERRKKERANVEKKAGALQLQA 274
Cdd:PRK10636 518 WLSDVQKQENQTDEAPKENNANSAQA 543
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
326-516 |
7.45e-19 |
|
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: 84.29 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLE--IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIeaghglrigyYAQEHETIDVK 403
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI----------TLDGVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 RSVLENM--VSASPNLTETEARRVLGSflftgddshkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEI 481
Cdd:cd03247 71 KALSSLIsvLNQRPYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 482 LDALAHY--EGAVVLVSHDEGAVEALNpeRVLIMPEG 516
Cdd:cd03247 138 LSLIFEVlkDKTLIWITHHLTGIEHMD--KILFLENG 172
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-233 |
7.49e-19 |
|
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: 84.19 E-value: 7.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVG--ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGY 66
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdpnELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDprsgdpDELartriLDarglgqlvlgmqestiamsssdasvsaagmkkyGTLTDrflalggyaaeaeaasiasnlN 146
Cdd:cd03246 81 LPQD------DEL-----FS---------------------------------GSIAE---------------------N 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 LpdrileqplktLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF---IVISHDIELVgETVN 223
Cdd:cd03246 96 I-----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGatrIVIAHRPETL-ASAD 163
|
250
....*....|
gi 1552103373 224 RVFYLDANRQ 233
Cdd:cd03246 164 RILVLEDGRV 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
326-516 |
8.11e-19 |
|
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: 85.47 E-value: 8.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTaVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL--------RIGYYAQE 396
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGkILLNGKDItnlppekrDISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 HETIDvKRSVLENMVSASPNLTE---TEARRVLGSFLFTGDDS--HKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTN 471
Cdd:cd03299 80 YALFP-HMTVYKNIAYGLKKRKVdkkEIERKVLEIAEMLGIDHllNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 472 NLDPASREEILDALA----HYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:cd03299 159 ALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWALA-DKVAIMLNG 206
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
329-498 |
8.48e-19 |
|
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: 85.80 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLrigYYAQEHETIDVKR--- 404
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvDGQDI---TGLSEKELYELRRrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 ------------SVLENMvsASP-----NLTETEARR----VLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANV 463
Cdd:COG1127 86 mlfqggalfdslTVFENV--AFPlrehtDLSEAEIRElvleKLELVGLPGAADKMPSE-LSGGMRKRVALARALALDPEI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 464 LLLDEPTNNLDPASREEIlDAL-----AHYEGAVVLVSHD 498
Cdd:COG1127 163 LLYDEPTAGLDPITSAVI-DELirelrDELGLTSVVVTHD 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
329-516 |
1.12e-18 |
|
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: 85.47 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI------EAGHGLR---IGYYAQeHET 399
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggedATDVPVQernVGFVFQ-HYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 IDVKRSVLENM--------VSASPNLTETEAR--RVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:cd03296 85 LFRHMTVFDNVafglrvkpRSERPPEAEIRAKvhELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 470 TNNLDPASREEILDALA--HYEGAV--VLVSHDEGavEALN-PERVLIMPEG 516
Cdd:cd03296 164 FGALDAKVRKELRRWLRrlHDELHVttVFVTHDQE--EALEvADRVVVMNKG 213
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
313-513 |
1.61e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.51 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 313 LRFPTPmACGRTPLHAENLSKSYGSLEIFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG--------- 380
Cdd:cd03220 8 KSYPTY-KGGSSSLKKLGILGRKGEVGEFWAlkdVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGtvtvrgrvs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 381 -VIEAGHGLRIGYyaqehetidvkrSVLEN--MVSASPNLTETEARRVLGSFL-FT--GDDSHKPAGVLSGGEKTRLALA 454
Cdd:cd03220 87 sLLGLGGGFNPEL------------TGRENiyLNGRLLGLSRKEIDEKIDEIIeFSelGDFIDLPVKTYSSGMKARLAFA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILDALAHY---EGAVVLVSHDEGAVEALNpERVLIM 513
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELlkqGKTVILVSHDPSSIKRLC-DRALVL 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
326-516 |
1.88e-18 |
|
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: 84.34 E-value: 1.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLE-IFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEaghglrIGYYAQEHETID 401
Cdd:cd03266 2 ITADALTKRFRDVKkTVQAVDgvsFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT------VDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 VKRSV--------LENMVSASPNL-----------TETEAR-RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGA 461
Cdd:cd03266 76 ARRRLgfvsdstgLYDRLTARENLeyfaglyglkgDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERL-CDRVVVLHRG 212
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-225 |
2.63e-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: 83.42 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDrggeigylpQDPRSGDPDELAR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---------FDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRI---LDARGLgqlvlgmqestiamsssdasvsaagmkkYGTLTDR-FLALGGYAAEAEAASIasnlnlpDRILE---- 153
Cdd:cd03268 72 RRIgalIEAPGF----------------------------YPNLTAReNLRLLARLLGIRKKRI-------DEVLDvvgl 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 154 -----QPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR---GGFIVISHDIELVGETVNRV 225
Cdd:cd03268 117 kdsakKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRdqgITVLISSHLLSEIQKVADRI 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
329-516 |
3.26e-18 |
|
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: 83.46 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEHETIDV------ 402
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIG-GRDVTDLPPKDRDIAMvfqnya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 ---KRSVLENMVSA-------SPNLTE--TEARRVLG-SFLFtgddSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:cd03301 83 lypHMTVYDNIAFGlklrkvpKDEIDErvREVAELLQiEHLL----DRKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 470 TNNLDP----ASREEILDALAHYEGAVVLVSHDEgaVEALN-PERVLIMPEG 516
Cdd:cd03301 158 LSNLDAklrvQMRAELKRLQQRLGTTTIYVTHDQ--VEAMTmADRIAVMNDG 207
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
344-517 |
3.93e-18 |
|
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: 84.43 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG------------HGLR--IGYYAQ--EH----ETI--D 401
Cdd:TIGR04521 24 VSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDgrditakkkkklKDLRkkVGLVFQfpEHqlfeETVykD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 V----KrsvleNMvsaspNLTETEA-RRVLGSFLFTG-DDSHK---PAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNN 472
Cdd:TIGR04521 104 IafgpK-----NL-----GLSEEEAeERVKEALELVGlDEEYLersPFE-LSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 473 LDPASREEILDALAHY---EG-AVVLVSHDEGAVeALNPERVLIMPEGT 517
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLhkeKGlTVILVTHSMEDV-AEYADRVIVMHKGK 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-236 |
4.00e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 83.54 E-value: 4.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYlpqdprsgdpdelaRTRILDARGLGqLVLG 96
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPW--------------KRRKKFLRRIG-VVFG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 mQESTIAMSSSDASVSAAGMKKYGTLTDRFlalggyaaEAEAASIASNLNLpDRILEQPLKTLSGGQRRRIELARILFSD 176
Cdd:cd03267 102 -QKTQLWWDLPVIDSFYLLAAIYDLPPARF--------KKRLDELSELLDL-EELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 177 ASTLILDEPTNHLDADSVVWLREFLKNY---RGGFIVI-SHDIELVGETVNRVFYLDANRQVID 236
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYnreRGTTVLLtSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-236 |
4.24e-18 |
|
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: 87.61 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDPR-----------S 73
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVlldgvdirqidpaDLRRNIGYVPQDPRlfygtlrdniaL 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 74 GDP--DELARTRILDARGLGQLVlgmqestiamsssdasvsaagmkkygtltdRFLALGgyaaeaeaasiasnLNLPdrI 151
Cdd:TIGR03375 562 GAPyaDDEEILRAAELAGVTEFV------------------------------RRHPDG--------------LDMQ--I 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 152 LEQPLkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLD 229
Cdd:TIGR03375 596 GERGR-SLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRTSLL-DLVDRIIVMD 673
|
....*..
gi 1552103373 230 ANRQVID 236
Cdd:TIGR03375 674 NGRIVAD 680
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-232 |
5.77e-18 |
|
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: 83.31 E-value: 5.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARL----LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------- 63
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 64 IGYLPQDPR-SGDPdelaRTRILD--ARGLGQLVLGMQESTIAMSssdasvsaagMKKYGtLTDRFLalggyaaeaeaas 140
Cdd:COG1124 81 VQMVFQDPYaSLHP----RHTVDRilAEPLRIHGLPDREERIAEL----------LEQVG-LPPSFL------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 141 iasnlnlpDRILEQplktLSGGQRRRIELARILFSDASTLILDEPTNHLDAdSV---VW--LREFLKNYRGGFIVISHDI 215
Cdd:COG1124 133 --------DRYPHQ----LSGGQRQRVAIARALILEPELLLLDEPTSALDV-SVqaeILnlLKDLREERGLTYLFVSHDL 199
|
250
....*....|....*..
gi 1552103373 216 ELVGETVNRVFYLDANR 232
Cdd:COG1124 200 AVVAHLCDRVAVMQNGR 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
329-516 |
6.41e-18 |
|
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: 82.64 E-value: 6.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFT--AVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGLR----------IGYYAQ 395
Cdd:cd03245 6 RNVSFSYPNQEIPAldNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsVLLDGTDIRqldpadlrrnIGYVPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIdvKRSVLENMVSASPNLTETE---ARRVLGSFLFTGDDshkPAGV----------LSGGEKTRLALAMIVVSGAN 462
Cdd:cd03245 86 DVTLF--YGTLRDNITLGAPLADDERilrAAELAGVTDFVNKH---PNGLdlqigergrgLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALAHYEG--AVVLVSHDEGAVEALNpeRVLIMPEG 516
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVD--RIIVMDSG 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-190 |
7.31e-18 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.24 E-value: 7.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG------RPLAAWSPWELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRildArglgqlVLgMQESTIAmsssdasvsaagmkkygtltdrF-------LALGGYAAEAEAASiasNLNLPDRILE 153
Cdd:COG4559 75 RRR---A------VL-PQHSSLA----------------------FpftveevVALGRAPHGSSAAQ---DRQIVREALA 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 154 Q----PLK-----TLSGGQRRRIELARIL-------FSDASTLILDEPTNHLD 190
Cdd:COG4559 120 LvglaHLAgrsyqTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALD 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
326-516 |
7.70e-18 |
|
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: 87.10 E-value: 7.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYG-SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLR--IGYY 393
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslkdidrHTLRqfINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDvkRSVLENMV-SASPNLTETEARRVLgSFLFTGDDSHK-----------PAGVLSGGEKTRLALAMIVVSGA 461
Cdd:TIGR01193 554 PQEPYIFS--GSILENLLlGAKENVSQDEIWAAC-EIAEIKDDIENmplgyqtelseEGSSISGGQKQRIALARALLTDS 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDALAH-YEGAVVLVSHDEGAveALNPERVLIMPEG 516
Cdd:TIGR01193 631 KVLILDESTSNLDTITEKKIVNNLLNlQDKTIIFVAHRLSV--AKQSDKIIVLDHG 684
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
326-516 |
1.65e-17 |
|
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: 80.34 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLE--IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI-----------EAGHGLRIGY 392
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisqwdPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEHETIDvkRSVLENmvsaspnltetearrvlgsflftgddshkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNN 472
Cdd:cd03246 81 LPQDDELFS--GSIAEN--------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 473 LDPASREEILDALAHYEGA---VVLVSHDEGAVEALnpERVLIMPEG 516
Cdd:cd03246 127 LDVEGERALNQAIAALKAAgatRIVIAHRPETLASA--DRILVLEDG 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
326-516 |
1.78e-17 |
|
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: 81.86 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS-LEIFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE---------AGHGLR--- 389
Cdd:cd03258 2 IELKNVSKVFGDtGGKVTAlkdVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllSGKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 --IGYYAQeHETIDVKRSVLENMvsASP----NLTETE-ARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSG 460
Cdd:cd03258 82 rrIGMIFQ-HFNLLSSRTVFENV--ALPleiaGVPKAEiEERVLELLELVGleDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDALAHYEG----AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRI-CDRVAVMEKG 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-229 |
1.82e-17 |
|
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: 81.71 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLPqdprsgdPDELA 80
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfDGEDITGLP-------PHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildaRGLG---Q-------------LVLGMQESTiaMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeaasiasn 144
Cdd:cd03219 74 R------LGIGrtfQiprlfpeltvlenVMVAAQART--GSGLLLARARREEREARERAEELLER--------------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 LNLPDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRG-GFIVISHDIELVGET 221
Cdd:cd03219 131 VGLADL-ADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRelRERGiTVLLVEHDMDVVMSL 209
|
....*...
gi 1552103373 222 VNRVFYLD 229
Cdd:cd03219 210 ADRVTVLD 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-498 |
1.99e-17 |
|
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: 85.22 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 30 VGLVGRNGAGKTTLTKVLAGDLIASKGTID------------RGGEIG-YL-------------PQ--D--PR--SGDPD 77
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrfRGTELQdYFkklangeikvahkPQyvDliPKvfKGTVR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 78 ELARTriLDARGlgqlvlgmqestiamsssdasvsaagmkKYGTLTDRflalggyaaeaeaasiasnLNLpDRILEQPLK 157
Cdd:COG1245 182 ELLEK--VDERG----------------------------KLDELAEK-------------------LGL-ENILDRDIS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLD------ADSVVwlREFLKNYRGgFIVISHDI---ELVGETVNrVFY- 227
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnVARLI--RELAEEGKY-VLVVEHDLailDYLADYVH-ILYg 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 228 ----------LDANRQVIDVYnmnWKNYQRqraadEErrkkeraNVekkagalqlqaaRFgakaskaaaahqmvaRAEKM 297
Cdd:COG1245 288 epgvygvvskPKSVRVGINQY---LDGYLP-----EE-------NV------------RI---------------RDEPI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 298 LSgleEVRAVDRVAKlrfptpmacGRTPLHAENLSKSYG--SLEIFTAvdlAIDRGSKVVILGLNGAGKTTLLRILGGVD 375
Cdd:COG1245 326 EF---EVHAPRREKE---------EETLVEYPDLTKSYGgfSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 376 QPDTGVIEAghGLRIGYYAQEHEtIDVKRSVLENMVSASP-----NLTETEARRVLG-SFLFtgddsHKPAGVLSGGEKT 449
Cdd:COG1245 391 KPDEGEVDE--DLKISYKPQYIS-PDYDGTVEEFLRSANTddfgsSYYKTEIIKPLGlEKLL-----DKNVKDLSGGELQ 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 450 RLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY----EGAVVLVSHD 498
Cdd:COG1245 463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHD 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
329-516 |
2.32e-17 |
|
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: 80.91 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG-------HGLRIGYYAQEHETI 400
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 401 --DVK----RSVLENmVSASPNLTET---EARRVLGSFLFTGDDSHK----PAGvLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:cd03292 84 fqDFRllpdRNVYEN-VAFALEVTGVpprEIRKRVPAALELVGLSHKhralPAE-LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 468 EPTNNLDPASREEILDAL--AHYEGAVVLVS-HDEGAVEALNPeRVLIMPEG 516
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLkkINKAGTTVVVAtHAKELVDTTRH-RVIALERG 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
325-485 |
2.77e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 325 PLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE---------AGHG-LRIGYYA 394
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrARHArQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QeHETIDVKRSVLENMVSASP--NLTETEARRVLGSFL-FTGDDSHKPAGV--LSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:PRK13537 87 Q-FDNLDPDFTVRENLLVFGRyfGLSAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170
....*....|....*.
gi 1552103373 470 TNNLDPASREEILDAL 485
Cdd:PRK13537 166 TTGLDPQARHLMWERL 181
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
326-498 |
4.63e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 4.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY--GSL--EIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL------------ 388
Cdd:PRK11629 6 LQCDNLCKRYqeGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQPMsklssaakaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 --RIGYYAQEHETIDvKRSVLENMV------SASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSG 460
Cdd:PRK11629 86 nqKLGFIYQFHHLLP-DFTALENVAmplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDALAHYE----GAVVLVSHD 498
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNrlqgTAFLVVTHD 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
335-517 |
6.07e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 80.07 E-value: 6.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 335 YGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG----------HGLRIGYYAQEHETIDVKR 404
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpwkrrkkFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 SVLE--NMVSASPNLTETEARRVLGSF---LFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE 479
Cdd:cd03267 111 PVIDsfYLLAAIYDLPPARFKKRLDELselLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 480 EI----LDALAHYEGAVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:cd03267 191 NIrnflKEYNRERGTTVLLTSHYMKDIEAL-ARRVLVIDKGR 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
329-516 |
6.56e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.56 E-value: 6.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG-----------------HGLR-- 389
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtarslsqqkgliRQLRqh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 IGYYAQEHETIDvKRSVLENMVSAsPNLTETE--------ARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGA 461
Cdd:PRK11264 87 VGFVFQNFNLFP-HRTVLENIIEG-PVIVKGEpkeeatarARELLAKVGLAGKETSYPRR-LSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 462 NVLLLDEPTNNLDPASREEILD---ALAHYEGAVVLVSHDEG-AVEALNpeRVLIMPEG 516
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNtirQLAQEKRTMVIVTHEMSfARDVAD--RAIFMDQG 220
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
329-498 |
6.90e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.54 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQE-HETIDVKRSVl 407
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlYLDTTLPLTV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 ENMVSASPNLTETEA----RRVLGSFLFtgddsHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLD---PASREE 480
Cdd:PRK09544 87 NRFLRLRPGTKKEDIlpalKRVQAGHLI-----DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvngQVALYD 161
|
170
....*....|....*....
gi 1552103373 481 ILDALAHYEG-AVVLVSHD 498
Cdd:PRK09544 162 LIDQLRRELDcAVLMVSHD 180
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-225 |
6.97e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.08 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdPRSGDPDELA 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGE-------PIRRQRDEYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTrildarglgQLVLGMQestiamsssdasvsaAGMKkyGTLTD----RFL-ALGGYAAEAEAASIASNLNLPDRiLEQP 155
Cdd:PRK13538 74 QD---------LLYLGHQ---------------PGIK--TELTAlenlRFYqRLHGPGDDEALWEALAQVGLAGF-EDVP 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 156 LKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVIS--HDIELVGETVNRV 225
Cdd:PRK13538 127 VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeQGGMVILTthQDLPVASDKVRKL 200
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
324-517 |
7.27e-17 |
|
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: 79.79 E-value: 7.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 324 TPLHAENLSKSY-----GSLEI--FTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI---EAGHGLRIGYy 393
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGWVDLAQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDVKRSVLeNMVS---------------ASPNLT--------ETEARRVLGSF-----LFtgddsHKPAGVLSG 445
Cdd:COG4778 82 ASPREILALRRRTI-GYVSqflrviprvsaldvvAEPLLErgvdreeaRARARELLARLnlperLW-----DLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 446 GEKTRLALAMIVVSGANVLLLDEPTNNLDPASR----EEILDALAhyEG-AVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKA--RGtAIIGIFHDEEVREAV-ADRVVDVTPFS 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
326-481 |
8.50e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 79.69 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE--------------AGHGlrIG 391
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldgedithlpmhkrARLG--IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEHeTIDVKRSVLENMVSA--SPNLTETEARRVLGSFLftgDD------SHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:COG1137 82 YLPQEA-SIFRKLTVEDNILAVleLRKLSKKEREERLEELL---EEfgithlRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170
....*....|....*...
gi 1552103373 464 LLLDEPTNNLDPASREEI 481
Cdd:COG1137 158 ILLDEPFAGVDPIAVADI 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
326-495 |
9.25e-17 |
|
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: 79.64 E-value: 9.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE--------------AGHGlrIG 391
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdgeditglpphriARLG--IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEhetidvkR------SVLENMVSASPNLTETEARR-----------VLGSFLftgddsHKPAGVLSGGEKTRLALA 454
Cdd:COG0410 82 YVPEG-------RrifpslTVEENLLLGAYARRDRAEVRadlervyelfpRLKERR------RQRAGTLSGGEQQMLAIG 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILDALA--HYEG-AVVLV 495
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRrlNREGvTILLV 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-225 |
1.13e-16 |
|
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: 77.47 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylPQDPRSgdpdelar 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK----EVSFAS-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 trILDARGLG-QLVlgMQestiamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasnlnlpdrileqplktLS 160
Cdd:cd03216 69 --PRDARRAGiAMV--YQ------------------------------------------------------------LS 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRV 225
Cdd:cd03216 85 VGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFEIADRV 152
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-234 |
1.19e-16 |
|
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: 82.87 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDP------- 71
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreELGRHIGYLPQDVelfdgti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 -----RSGDPDelaRTRILDArglGQLVlGMQEsTIamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasnLN 146
Cdd:COG4618 423 aeniaRFGDAD---PEKVVAA---AKLA-GVHE-MI------------------------------------------LR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 LPD----RILEQPLkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKN--YRGG-FIVISHDIELVG 219
Cdd:COG4618 453 LPDgydtRIGEGGA-RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAlkARGAtVVVITHRPSLLA 531
|
250
....*....|....*
gi 1552103373 220 EtVNRVFYLDANRQV 234
Cdd:COG4618 532 A-VDKLLVLRDGRVQ 545
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-218 |
1.20e-16 |
|
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: 82.72 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDP------- 71
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrdqIAWVPQHPflfagti 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 ----RSGDPD--ELARTRILDARGLGQLVLGMQEStiamsssdasvsaagmkkYGTLTDRflalGGyaaeaeaasiasnl 145
Cdd:TIGR02857 413 aeniRLARPDasDAEIREALERAGLDEFVAALPQG------------------LDTPIGE----GG-------------- 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 146 nlpdrileqplKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELV 218
Cdd:TIGR02857 457 -----------AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA 520
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
345-517 |
1.21e-16 |
|
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: 78.69 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 345 DLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhglrigyyAQEHETIDVKR----------------SVLE 408
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN--------GVDVTAAPPADrpvsmlfqennlfahlTVEQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NM-VSASPNLTETEARR-----VLGSFLFTGDDSHKPaGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:cd03298 90 NVgLGLSPGLKLTAEDRqaievALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 483 DAL----AHYEGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:cd03298 169 DLVldlhAETKMTVLMVTHQPEDAKRLA-QRVVFLDNGR 206
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-218 |
1.42e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 10 RVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--IGYLPQdpRSGDPDEL-ARTRILD 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGarVAYVPQ--RSEVPDSLpLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 87 ARGLGQlvlgmqestiamsssdasvsAAGMKKYGTLTDRflalggyaaeAEAASIASNLNLpDRILEQPLKTLSGGQRRR 166
Cdd:NF040873 79 AMGRWA--------------------RRGLWRRLTRDDR----------AAVDDALERVGL-ADLAGRQLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 167 IELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELV 218
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV 182
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
330-516 |
1.84e-16 |
|
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: 80.93 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIftAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--------EAGHGL-------RIGYYA 394
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfDSRKGIflppekrRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QE-----HETidVKRSVLENMVSASPNLTETEARRVLgSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:TIGR02142 82 QEarlfpHLS--VRGNLRYGMKRARPSERRISFERVI-ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 470 TNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:TIGR02142 159 LAALDDPRKYEILPYLerlhAEFGIPILYVSHSLQEVLRL-ADRVVVLEDG 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
330-498 |
1.88e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 78.90 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLRIGYYAQEHETIDVKR---- 404
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiAGHQFDFSQKPSEKAIRLLRQkvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 -----------SVLENMVSASPN---LTETEAR---RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:COG4161 87 vfqqynlwphlTVMENLIEAPCKvlgLSKEQARekaMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 468 EPTNNLDP---ASREEILDALAHYEGAVVLVSHD 498
Cdd:COG4161 167 EPTAALDPeitAQVVEIIRELSQTGITQVIVTHE 200
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
326-497 |
2.06e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.21 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--EAGHGLR-----IGYYAQE-- 396
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIifDGHPWTRkdlhkIGSLIESpp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 -------HETIDVKRSVLenmvsaspNLTETEARRVLgSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:TIGR03740 81 lyenltaRENLKVHTTLL--------GLPDSRIDEVL-NIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190
....*....|....*....|....*....|.
gi 1552103373 470 TNNLDPASREEILDALAHYEG---AVVLVSH 497
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEqgiTVILSSH 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-229 |
2.58e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.96 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 9 LRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPqDPRSG-DPDELARTRILda 87
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL-GLGGGfNPELTGRENIY-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 88 rgLGQLVLGMQESTIAmsssdasvsaagmKKYGTLTDrFLALGGYaaeaeaasiasnlnlpdriLEQPLKTLSGGQRRRI 167
Cdd:cd03220 107 --LNGRLLGLSRKEID-------------EKIDEIIE-FSELGDF-------------------IDLPVKTYSSGMKARL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 168 ELARILFSDASTLILDEPTNHLDAD----SVVWLREFLKNYRGGFIViSHDIELVGETVNRVFYLD 229
Cdd:cd03220 152 AFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLE 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
330-500 |
2.84e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLR-------------ILGGVDQPDTGVIEAGHGLRIGYYAQE 396
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGLKVNDPKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 -----HETidvkrsVLENMV-------SASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVL 464
Cdd:PRK09493 86 fylfpHLT------ALENVMfgplrvrGASKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 465 LLDEPTNNLDPASREEIL---DALAHyEG-AVVLVSHDEG 500
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLkvmQDLAE-EGmTMVIVTHEIG 197
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
326-505 |
4.04e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-------GSL------------EIFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE 383
Cdd:COG1134 5 IEVENVSKSYrlyhepsRSLkelllrrrrtrrEEFWAlkdVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 384 AgHGlRIGyyaqehetidvkrSVLENMVSASPNLT-----------------ETEARRV-------LGSFLftgddsHKP 439
Cdd:COG1134 85 V-NG-RVS-------------ALLELGAGFHPELTgreniylngrllglsrkEIDEKFDeivefaeLGDFI------DQP 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 440 AGVLSGGEKTRLALAMIVVSGANVLLLDEptnNL---DPASRE---EILDALAHYEGAVVLVSHDEGAVEAL 505
Cdd:COG1134 144 VKTYSSGMRARLAFAVATAVDPDILLVDE---VLavgDAAFQKkclARIRELRESGRTVIFVSHSMGAVRRL 212
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
329-516 |
4.62e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.22 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL-------------RIGYY 393
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfSGHDItrlknrevpflrrQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIdVKRSVLENMvsASPNL-----TETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:PRK10908 85 FQDHHLL-MDRTVYDNV--AIPLIiagasGDDIRRRVSAALDKVGllDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 467 DEPTNNLDPASREEILDALAHYE--GAVVLV-SHDEGAVEALNpERVLIMPEG 516
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNrvGVTVLMaTHDIGLISRRS-YRMLTLSDG 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
326-497 |
5.88e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 76.38 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI----EAGHGLRIGYYAQ----EH 397
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwqgEPIRRQRDEYHQDllylGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ET-IDVKRSVLENMVSASP---NLTETEARRVLGSFLFTGDDsHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:PRK13538 82 QPgIKTELTALENLRFYQRlhgPGDDEALWEALAQVGLAGFE-DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*..
gi 1552103373 474 DPASREEILDALA-HYE--GAVVLVSH 497
Cdd:PRK13538 161 DKQGVARLEALLAqHAEqgGMVILTTH 187
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
326-511 |
7.02e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.43 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA-GHGLRIG------YYAQEHE 398
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGdrsrfmAYLGHLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 399 TIDVKRSVLENMVSASpNLTETEARRVLGSFL-FTGDDSHKPAGV--LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDP 475
Cdd:PRK13543 92 GLKADLSTLENLHFLC-GLHGRRAKQMPGSALaIVGLAGYEDTLVrqLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 476 AS---REEILDALAHYEGAVVLVSHdeGAVEALN-PERVL 511
Cdd:PRK13543 171 EGitlVNRMISAHLRGGGAALVTTH--GAYAAPPvRTRML 208
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-226 |
7.27e-16 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 80.67 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPRSGDPDELARTRILDArglg 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYM---- 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 qlvlgmqestiamsssdasvsaagMKKY-GTLTDRFLA-LGGYAAEAeaasiasNLNLpdrileQPLKTLSGGQRRRIEL 169
Cdd:PLN03073 596 ------------------------MRCFpGVPEQKLRAhLGSFGVTG-------NLAL------QPMYTLSGGQKSRVAF 638
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 170 ARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVF 226
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELW 695
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-516 |
8.65e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 77.75 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHglrigyYAQEHETI-DVKRSV---------------- 406
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG------MVLSEETVwDVRRQVgmvfqnpdnqfvgatv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 -------LEN-------MVsasPNLTETEARRVLGSFLftgddSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNN 472
Cdd:PRK13635 100 qddvafgLENigvpreeMV---ERVDQALRQVGMEDFL-----NREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1552103373 473 LDPASREEILDA---LAHYEGAVVL-VSHDegAVEALNPERVLIMPEG 516
Cdd:PRK13635 171 LDPRGRREVLETvrqLKEQKGITVLsITHD--LDEAAQADRVIVMNKG 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
329-516 |
8.76e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 77.47 E-value: 8.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY--GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRigyYAQEHETIDVKRSV 406
Cdd:TIGR04520 4 ENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLD---TLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 -----------------------LENM-VSaspnlTETEARRV--------LGSFLftgddSHKPAgVLSGGEKTRLALA 454
Cdd:TIGR04520 80 gmvfqnpdnqfvgatveddvafgLENLgVP-----REEMRKRVdealklvgMEDFR-----DREPH-LLSGGQKQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILD---ALAHYEG-AVVLVSHD-EGAVEAlnpERVLIMPEG 516
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLEtirKLNKEEGiTVISITHDmEEAVLA---DRVIVMNKG 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-239 |
1.08e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLpQDPRSG-DPD----ELARtrildargLGQL 93
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSAL-LELGAGfHPEltgrENIY--------LNGR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 VLGMQESTIAmsssdasvsaagmKKYGTLTDrFLALGGYaaeaeaasiasnlnlpdriLEQPLKTLSGGQRrrielARIL 173
Cdd:COG1134 115 LLGLSRKEID-------------EKFDEIVE-FAELGDF-------------------IDQPVKTYSSGMR-----ARLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 174 FS-----DASTLILDEPTNHLDAD----SVVWLREFLKNYRgGFIVISHDIELVGETVNRVFYLDANR--------QVID 236
Cdd:COG1134 157 FAvatavDPDILLVDEVLAVGDAAfqkkCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRlvmdgdpeEVIA 235
|
...
gi 1552103373 237 VYN 239
Cdd:COG1134 236 AYE 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-498 |
1.19e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 79.85 E-value: 1.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 26 DGDKVGLVGRNGAGKTTLTKVLAGDLI------ASKGTID------RGGEIG-YLpQDPRSGD------P---DELARtr 83
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIpnlgdyEEEPSWDevlkrfRGTELQnYF-KKLYNGEikvvhkPqyvDLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ILDARgLGQLVLGMQEStiamsssdasvsaagmKKYGTLTDRflalggyaaeaeaasiasnLNLpDRILEQPLKTLSGGQ 163
Cdd:PRK13409 175 VFKGK-VRELLKKVDER----------------GKLDEVVER-------------------LGL-ENILDRDISELSGGE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 164 RRRIELARILFSDASTLILDEPTNHLD-------ADSVvwlREFLKN-YrggFIVISHDI---ELVGETVN--------- 223
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDirqrlnvARLI---RELAEGkY---VLVVEHDLavlDYLADNVHiaygepgay 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 224 -RVFYLDANRQVIDVY--------NMnwknyqrqRAADEERRKKERAnvekkagalqlqaarfgakaskaaaahqmvara 294
Cdd:PRK13409 292 gVVSKPKGVRVGINEYlkgylpeeNM--------RIRPEPIEFEERP--------------------------------- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 295 ekmlsgleEVRAVDRVAKLRFPtpmacgrtplhaeNLSKSYG--SLEIFTAvdlAIDRGSKVVILGLNGAGKTTLLRILG 372
Cdd:PRK13409 331 --------PRDESERETLVEYP-------------DLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 373 GVDQPDTGVIEAghGLRIGYYAQEHETiDVKRSVLENMVSASPNLT----ETEARRVLG-SFLFTgddshKPAGVLSGGE 447
Cdd:PRK13409 387 GVLKPDEGEVDP--ELKISYKPQYIKP-DYDGTVEDLLRSITDDLGssyyKSEIIKPLQlERLLD-----KNVKDLSGGE 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 448 KTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY----EGAVVLVSHD 498
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHD 513
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-236 |
1.28e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE---------IGYLPQDp 71
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEpldpedrrrIGYLPEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 RSGDPDELARTRILDargLGQLVlGMQESTIamsssdasvsaagMKKYGTLTDRFlalggyaaeaeaasiasnlNLPDRi 151
Cdd:COG4152 80 RGLYPKMKVGEQLVY---LARLK-GLSKAEA-------------KRRADEWLERL-------------------GLGDR- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 152 LEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR-GGFIVI--SHDIELVGETVNRVFYL 228
Cdd:COG4152 123 ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAaKGTTVIfsSHQMELVEELCDRIVII 202
|
....*...
gi 1552103373 229 DANRQVID 236
Cdd:COG4152 203 NKGRKVLS 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-235 |
1.47e-15 |
|
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: 75.39 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE---------IGYLPQDpR 72
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEE-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 73 SGDPDElartRILD-ARGLGQLvlgmqestiamsssdasvsaAGMKKYGTL--TDRFLalggyaaeaeaasiaSNLNLPD 149
Cdd:cd03269 80 GLYPKM----KVIDqLVYLAQL--------------------KGLKKEEARrrIDEWL---------------ERLELSE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 150 RiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG-GFIVI--SHDIELVGETVNRVF 226
Cdd:cd03269 121 Y-ANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVIlsTHQMELVEELCDRVL 199
|
....*....
gi 1552103373 227 YLDANRQVI 235
Cdd:cd03269 200 LLNKGRAVL 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
2.21e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 77.49 E-value: 2.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYLPQ 69
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRdlftnlpprerrVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 D----------------PRSGDPDELARTRIldARGLGQLVlGMQEstiamsssdasvsaagmkkygtLTDRFlalggya 133
Cdd:COG1118 83 HyalfphmtvaeniafgLRVRPPSKAEIRAR--VEELLELV-QLEG----------------------LADRY------- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 134 aeaeaasiasnlnlPDrileQplktLSGGQRRRIELARILFSDASTLILDEPTNHLDAdSV-----VWLREFLKNYRGGF 208
Cdd:COG1118 131 --------------PS----Q----LSGGQRQRVALARALAVEPEVLLLDEPFGALDA-KVrkelrRWLRRLHDELGGTT 187
|
....*...
gi 1552103373 209 IVISHDIE 216
Cdd:COG1118 188 VFVTHDQE 195
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
10-234 |
3.16e-15 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 75.62 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 10 RVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgdpDELARTRILDARg 89
Cdd:TIGR03873 10 SAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGV-------------DLHGLSRRARAR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 90 lgQLVLGMQESTIAMSSSDASVSAAGMKKYGTL-----------TDRFLALGGYAaeaeaasiasnlNLPDRileqPLKT 158
Cdd:TIGR03873 76 --RVALVEQDSDTAVPLTVRDVVALGRIPHRSLwagdsphdaavVDRALARTELS------------HLADR----DMST 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG-GFIVIS--HDIELVGETVNRVFYLDANRQV 234
Cdd:TIGR03873 138 LSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtGVTVVAalHDLNLAASYCDHVVVLDGGRVV 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
344-517 |
3.31e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.04 E-value: 3.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH-----------GLR--IGYYAQEHETIDVKRSVLENM 410
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidysrkglmKLResVGMVFQDPDNQLFSASVYQDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 411 VSASPNLTETE---ARRVLGSFLFTGDD--SHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:PRK13636 105 SFGAVNLKLPEdevRKRVDNALKRTGIEhlKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLL 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 1552103373 486 AHYEG----AVVLVSHDEGAVeALNPERVLIMPEGT 517
Cdd:PRK13636 185 VEMQKelglTIIIATHDIDIV-PLYCDNVFVMKEGR 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
330-516 |
4.05e-15 |
|
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: 76.68 E-value: 4.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIftAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------------HGLRIGYYA 394
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsargiflppHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QE-----HetidvkRSVLENMVSASPNlTETEARRV----------LGSFLftgddSHKPAGvLSGGEKTRLALAMIVVS 459
Cdd:COG4148 84 QEarlfpH------LSVRGNLLYGRKR-APRAERRIsfdevvellgIGHLL-----DRRPAT-LSGGERQRVAIGRALLS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 460 GANVLLLDEPTNNLDPASREEILDALA--HYEGA--VVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:COG4148 151 SPRLLLMDEPLAALDLARKAEILPYLErlRDELDipILYVSHSLDEVARL-ADHVVLLEQG 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
326-498 |
4.84e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.84 E-value: 4.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY----GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL------RIGYYA 394
Cdd:PRK10535 5 LELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRvAGQDVatldadALAQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDVKRSVLENMVSASPNL--------TETEARRVLGSFLFT----GDDSHKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQNVevpavyagLERKQRLLRAQELLQrlglEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 463 VLLLDEPTNNLDPASREE---ILDALAHYEGAVVLVSHD 498
Cdd:PRK10535 165 VILADEPTGALDSHSGEEvmaILHQLRDRGHTVIIVTHD 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-186 |
5.76e-15 |
|
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: 74.25 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLPqdprsgdPDEL 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfDGEDITGLP-------PHRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARtrildaRGLGQLvlgMQESTIamsssdasvsaagmkkYGTLTDR-FLALGGYAAEAEAASIASnlnlPDRILE----- 153
Cdd:COG0410 76 AR------LGIGYV---PEGRRI----------------FPSLTVEeNLLLGAYARRDRAEVRAD----LERVYElfprl 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 154 -----QPLKTLSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:COG0410 127 kerrrQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
329-486 |
7.35e-15 |
|
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: 73.80 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLE-IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLR--IGYYAQE 396
Cdd:cd03254 6 ENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDgidirdisrKSLRsmIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 heTIDVKRSVLENMVSASPNLTETE---ARRVLGSFLF-----TGDDSH-KPAG-VLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:cd03254 86 --TFLFSGTIMENIRLGRPNATDEEvieAAKEAGAHDFimklpNGYDTVlGENGgNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180
....*....|....*....|
gi 1552103373 467 DEPTNNLDPASREEILDALA 486
Cdd:cd03254 164 DEATSNIDTETEKLIQEALE 183
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
329-516 |
7.35e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 7.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGL----------RIGYYAQeHE 398
Cdd:PRK10851 6 ANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-HGTdvsrlhardrKVGFVFQ-HY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 399 TIDVKRSVLENMV--------SASPNLTETEAR--RVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDE 468
Cdd:PRK10851 84 ALFRHMTVFDNIAfgltvlprRERPNAAAIKAKvtQLLEMVQLAHLADRYPAQ-LSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 469 PTNNLDPASREEI---LDALaHYE--GAVVLVSHD-EGAVEALNpeRVLIMPEG 516
Cdd:PRK10851 163 PFGALDAQVRKELrrwLRQL-HEElkFTSVFVTHDqEEAMEVAD--RVVVMSQG 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-190 |
7.73e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.42 E-value: 7.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpqDPRSGdpdela 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-------DDVEA------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 rtriLDARGLGQLVLGM-QESTIAMSSSDASVSAAGMKKYgtlTDRFLALGgyAAEAEAASIASNLNLPDRILEQPLKTL 159
Cdd:PRK09536 70 ----LSARAASRRVASVpQDTSLSFEFDVRQVVEMGRTPH---RSRFDTWT--ETDRAAVERAMERTGVAQFADRPVTSL 140
|
170 180 190
....*....|....*....|....*....|.
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
323-485 |
9.92e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 9.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 323 RTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGV----DQPDTGVIEAGHGLR--------- 389
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRTVQregrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 ------IGYYAQEHETIDvKRSVLENM----VSASPN-------LTETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTR 450
Cdd:PRK09984 82 rksranTGYIFQQFNLVN-RLSVLENVligaLGSTPFwrtcfswFTREQKQRALQALTRVGmvHFAHQRVSTLSGGQQQR 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 451 LALAMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
325-474 |
1.02e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 325 PLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH-----------GLRIGYY 393
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraaSRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHE---TIDVkRSVLEnmVSASPNL------TETEARRVLGSFLFTGDD--SHKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:PRK09536 83 PQDTSlsfEFDV-RQVVE--MGRTPHRsrfdtwTETDRAAVERAMERTGVAqfADRPVTSLSGGERQRVLLARALAQATP 159
|
170
....*....|..
gi 1552103373 463 VLLLDEPTNNLD 474
Cdd:PRK09536 160 VLLLDEPTASLD 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-186 |
1.05e-14 |
|
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: 73.24 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPqdprsgdPDELA 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRdITGLP-------PHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildaRGLGQLvlgMQestiamsssdasvsaaGMKKYGTLTDR-FLALGGYAAEAEAASIAsnlnlPDRILE------ 153
Cdd:cd03224 74 R------AGIGYV---PE----------------GRRIFPELTVEeNLLLGAYARRRAKRKAR-----LERVYElfprlk 123
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 154 ----QPLKTLSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:cd03224 124 errkQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-505 |
1.06e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.76 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSleiFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-------AGHGLRIGY--- 392
Cdd:COG4152 2 LELKGLTKRFGD---KTAVDdvsFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 ----YAqehetidvKRSVLENMV--SASPNLTETEARRVLgSFLFT----GDDSHKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:COG4152 79 erglYP--------KMKVGEQLVylARLKGLSKAEAKRRA-DEWLErlglGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALAHY--EGA-VVLVSHDEGAVEAL 505
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELaaKGTtVIFSSHQMELVEEL 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
324-498 |
1.29e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 1.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 324 TPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH-----------GLRIGY 392
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEH---ETIDVKRSVlenMVSASP------NLTETEARRVLGSFLFTGDD--SHKPAGVLSGGEKTRLALAMIVVSGA 461
Cdd:PRK11231 81 LPQHHltpEGITVRELV---AYGRSPwlslwgRLSAEDNARVNQAMEQTRINhlADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDALAHYEGA---VVLVSHD 498
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHD 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-236 |
1.39e-14 |
|
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: 73.58 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKG-TI-----DRGGE--------IGY 66
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVrlfgeRRGGEdvwelrkrIGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 ----LPQDPRsgdPDELARTRIL----DARGLGQLVLGMQEstiamsssdasvsaagmkkygTLTDRFLALggyaaeaea 138
Cdd:COG1119 83 vspaLQLRFP---RDETVLDVVLsgffDSIGLYREPTDEQR---------------------ERARELLEL--------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 139 asiasnLNLpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG----FIVISHD 214
Cdd:COG1119 130 ------LGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTHH 202
|
250 260
....*....|....*....|..
gi 1552103373 215 IELVGETVNRVFYLDANRQVID 236
Cdd:COG1119 203 VEEIPPGITHVLLLKDGRVVAA 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-228 |
1.62e-14 |
|
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: 72.52 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELARTR--------------- 83
Cdd:cd03255 22 GVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDG------TDISKLSEKELAAFRrrhigfvfqsfnllp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ILDAR---GLGQLVLGMQESTIamsssdasvsaagMKKYGTLTDRflalggyaaeaeaasiasnLNLPDRiLEQPLKTLS 160
Cdd:cd03255 96 DLTALenvELPLLLAGVPKKER-------------RERAEELLER-------------------VGLGDR-LNHYPSELS 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADS--VVW--LREFLKNYRGGFIVISHDIELVgETVNRVFYL 228
Cdd:cd03255 143 GGQQQRVAIARALANDPKIILADEPTGNLDSETgkEVMelLRELNKEAGTTIVVVTHDPELA-EYADRIIEL 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-225 |
1.90e-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: 72.14 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigYLPQDPRSGDPDELAR 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-------LLNGGPLDFQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 trildarglGQLVLGMQEstiamsssdasvsaaGMKkyGTLTD----RFLALGGYAAEAEAASIASNLN-LPDRileqPL 156
Cdd:cd03231 74 ---------GLLYLGHAP---------------GIK--TTLSVlenlRFWHADHSDEQVEEALARVGLNgFEDR----PV 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVIS--HDIELVGETVNRV 225
Cdd:cd03231 124 AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcaRGGMVVLTthQDLGLSEAGAREL 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-516 |
2.25e-14 |
|
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: 75.63 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdlIASKGTIDrgGEIGYlpqdprSGDPDELARTRILDARGlgqLVLG 96
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG--VYPHGTWD--GEIYW------SGSPLKASNIRDTERAG---IVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 MQESTIAMSSSDASVSAAG--------MKKYGTLTDRFLALggyaaeaeaasiASNLNLPDRILEQPLKTLSGGQRRRIE 168
Cdd:TIGR02633 84 HQELTLVPELSVAENIFLGneitlpggRMAYNAMYLRAKNL------------LRELQLDADNVTRPVGDYGGGQQQLVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 169 LARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLDANRQVidvynmnwkNY 245
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDGQHV---------AT 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 246 QRQRAADEERrkkeranvekkagalqlqaarfgakaskaaAAHQMVARaekmlsgleEVRAVdrvaklrFPT-PMACGRT 324
Cdd:TIGR02633 223 KDMSTMSEDD------------------------------IITMMVGR---------EITSL-------YPHePHEIGDV 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 325 PLHAENLSKSYGSLEIFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGV--DQPDTGVIEAGHGLRIGYYAQ--EH 397
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAypGKFEGNVFINGKPVDIRNPAQaiRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ETI----DVKRSVLENMVSASPNLTETearrVLGSFLFTG--DDSHK--------------------PAGVLSGGEKTRL 451
Cdd:TIGR02633 337 GIAmvpeDRKRHGIVPILGVGKNITLS----VLKSFCFKMriDAAAElqiigsaiqrlkvktaspflPIGRLSGGNQQKA 412
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 452 ALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIyklINQLAQEGVAIIVVSSELAEVLGLS-DRVLVIGEG 479
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-226 |
2.90e-14 |
|
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: 72.08 E-value: 2.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLE------LRVGARL-LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI---DRGG-------- 62
Cdd:COG4778 4 LLEVENLSktftlhLQGGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrHDGGwvdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 63 ----------EIGYLPQDPRsgdpdELARTRILD--ARGLgqLVLGMQESTiamsssdasvsaaGMKKYGTLTDRflalg 130
Cdd:COG4778 84 preilalrrrTIGYVSQFLR-----VIPRVSALDvvAEPL--LERGVDREE-------------ARARARELLAR----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 131 gyaaeaeaasiasnLNLPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS---VVWLREFLKNyRGG 207
Cdd:COG4778 139 --------------LNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKA-RGT 203
|
250 260
....*....|....*....|
gi 1552103373 208 FIV-ISHDIELVGETVNRVF 226
Cdd:COG4778 204 AIIgIFHDEEVREAVADRVV 223
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
316-485 |
3.13e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 3.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 316 PTPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA----------G 385
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 386 HGLRIGYYAQeHETIDVKRSVLENMVSASP--NLTETEARRVLGSFL-FTGDDSHKPAGV--LSGGEKTRLALAMIVVSG 460
Cdd:PRK13536 112 ARARIGVVPQ-FDNLDLEFTVRENLLVFGRyfGMSTREIEAVIPSLLeFARLESKADARVsdLSGGMKRRLTLARALIND 190
|
170 180
....*....|....*....|....*
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDAL 485
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERL 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
329-498 |
3.20e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 72.42 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEhetiDVKR--SV 406
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-GLDVATTPSR----ELAKrlAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 L--ENMVSAS------------P----NLTETEARRVLGS--FLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:COG4604 80 LrqENHINSRltvrelvafgrfPyskgRLTAEDREIIDEAiaYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1552103373 467 DEPTNNLDPA-SRE--EILDALAHYEG-AVVLVSHD 498
Cdd:COG4604 160 DEPLNNLDMKhSVQmmKLLRRLADELGkTVVIVLHD 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
330-516 |
3.32e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 74.21 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI------------EAGH----------- 386
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRImldgqdithvpaENRHvntvfqsyalf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 387 -----------GLRIgyyaQEHETIDVKRSVLE--NMVSaspnlTETEARRvlgsflftgddshKPAGvLSGGEKTRLAL 453
Cdd:PRK09452 99 phmtvfenvafGLRM----QKTPAAEITPRVMEalRMVQ-----LEEFAQR-------------KPHQ-LSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEG-AVVLVSHDEGavEALN-PERVLIMPEG 516
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMqneLKALQRKLGiTFVFVTHDQE--EALTmSDRIVVMRDG 221
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
344-497 |
3.85e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 72.84 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGL---------------RIGYYAQEHETIDVKRSVLE 408
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPESQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NMVSASPN--LTETEARRVLGSFL----FTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:PRK13643 105 DVAFGPQNfgIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170
....*....|....*...
gi 1552103373 483 DALA--HYEG-AVVLVSH 497
Cdd:PRK13643 185 QLFEsiHQSGqTVVLVTH 202
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
326-514 |
4.33e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.42 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLRIGYYAQeHET 399
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpvEGPGAERGVVFQ-NEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 IDVKRSVLEN------MVSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:PRK11248 81 LLPWRNVQDNvafglqLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 474 DPASRE---EILDALAHYEG-AVVLVSHD-EGAVeALNPERVLIMP 514
Cdd:PRK11248 160 DAFTREqmqTLLLKLWQETGkQVLLITHDiEEAV-FMATELVLLSP 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-232 |
4.37e-14 |
|
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: 70.29 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigyLPQDPRSGDPDElaR 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE---DLTDLEDELPPL--R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRIldarglgqlvlGM--QESTIamsssdasvsaagmkkYGTLTDRflalggyaaeaeaasiaSNLNLPdrileqplktL 159
Cdd:cd03229 76 RRI-----------GMvfQDFAL----------------FPHLTVL-----------------ENIALG----------L 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISHDIELVGETVNRVFYLDANR 232
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLgitvVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
345-500 |
5.27e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 5.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 345 DLAIDRGSKVVILGLNGAGKTTLLRILGGvDQP---------------------------------DTGVIEAGHGLRIg 391
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNG-EVLlddgriiyeqdlivarlqqdpprnvegtvydfvAEGIEEQAEYLKR- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEHetiDVKRSVLENMVSASPNLTET---------EAR--RVLGSFlftGDDSHKPAGVLSGGEKTRLALAMIVVSG 460
Cdd:PRK11147 101 YHDISH---LVETDPSEKNLNELAKLQEQldhhnlwqlENRinEVLAQL---GLDPDAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHDEG 500
Cdd:PRK11147 175 PDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRS 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
329-517 |
5.51e-14 |
|
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: 71.56 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSleIFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR----------IGYYA 394
Cdd:cd03295 4 ENVTKRYGG--GKKAVNnlnLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFiDGEDIReqdpvelrrkIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QE-----HetidvkRSVLENmVSASPNLT----ETEARRV--------LGSFLFTGDDSHKpagvLSGGEKTRLALAMIV 457
Cdd:cd03295 82 QQiglfpH------MTVEEN-IALVPKLLkwpkEKIRERAdellalvgLDPAEFADRYPHE----LSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 458 VSGANVLLLDEPTNNLDPASREEILDALAHYEGA----VVLVSHDegAVEALN-PERVLIMPEGT 517
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgktIVFVTHD--IDEAFRlADRIAIMKNGE 213
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-213 |
5.80e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.43 E-value: 5.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGYLPQDP------- 71
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTflfsgti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 ----RSGDPDElARTRILDARGLGQLvlgmqestiamsssdasvsaagmkkygtltDRFLAlggyaaeaeaasiasnlNL 147
Cdd:COG1132 431 reniRYGRPDA-TDEEVEEAAKAAQA------------------------------HEFIE-----------------AL 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 148 PDRiLEQPL----KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISH 213
Cdd:COG1132 463 PDG-YDTVVgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
344-517 |
5.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.36 E-value: 5.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH-------------GLR--IGYYAQ--EHETIDvkRSV 406
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkknkklkPLRkkVGIVFQfpEHQLFE--ETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 LENMVSASPN--LTETEARR----VLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREE 480
Cdd:PRK13634 104 EKDICFGPMNfgVSEEDAKQkareMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 481 ILDALA--HYEG--AVVLVSH--DEGAVEAlnpERVLIMPEGT 517
Cdd:PRK13634 184 MMEMFYklHKEKglTTVLVTHsmEDAARYA---DQIVVMHKGT 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-236 |
6.30e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.17 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTidRG----GEIGYLPQDPRSGDP 76
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAP--RGarvtGDVTLNGEPLAAIDA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 77 DELARTR-ILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGyaaeaeaasiasnlnlPDRILEQP 155
Cdd:PRK13547 79 PRLARLRaVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAG----------------ATALVGRD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 156 LKTLSGGQRRRIELARIL---------FSDASTLILDEPTNHLD-------ADSVvwlREFLKNYRGGFIVISHDIELVG 219
Cdd:PRK13547 143 VTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlahqhrlLDTV---RRLARDWNLGVLAIVHDPNLAA 219
|
250
....*....|....*..
gi 1552103373 220 ETVNRVFYLDANRQVID 236
Cdd:PRK13547 220 RHADRIAMLADGAIVAH 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
326-499 |
6.30e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGS----LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI------------EAGHGLR 389
Cdd:PRK10584 7 VEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhqmdeEARAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 ---IGYYAQEHETIDVkRSVLEN------MVSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSG 460
Cdd:PRK10584 87 akhVGFVFQSFMLIPT-LNALENvelpalLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDE 499
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDL 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-237 |
6.76e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 70.85 E-value: 6.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRV-GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE---------------- 63
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQdlsrlkrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 64 IGYLPQDprsgdpdelarTRILDAR------GLGQLVLGMQESTIAMSSSDAsvsaagMKKYGtLTDRFLAlggyaaeae 137
Cdd:COG2884 81 IGVVFQD-----------FRLLPDRtvyenvALPLRVTGKSRKEIRRRVREV------LDLVG-LSDKAKA--------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 138 aasiasnlnLPDrileqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVI-SHD 214
Cdd:COG2884 134 ---------LPH--------ELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeiNRRGTTVLIaTHD 196
|
250 260
....*....|....*....|...
gi 1552103373 215 IELVGETVNRVFYLDANRQVIDV 237
Cdd:COG2884 197 LELVDRMPKRVLELEDGRLVRDE 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
329-516 |
7.27e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 71.20 E-value: 7.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLRIGYYAQEHETIDVKR--- 404
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNiAGNHFDFSKTPSDKAIRELRRnvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 ------------SVLENMVSASPN---LTETEAR---RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:PRK11124 86 mvfqqynlwphlTVQQNLIEAPCRvlgLSKDQALaraEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 467 DEPTNNLDP---ASREEILDALAHYEGAVVLVSHdEGAVEALNPERVLIMPEG 516
Cdd:PRK11124 166 DEPTAALDPeitAQIVSIIRELAETGITQVIVTH-EVEVARKTASRVVYMENG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
329-517 |
8.39e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI------------EAGHGLRIGYYAQE 396
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 HETIDvKRSVLENM---------VSASPNLTETEARRVLGSFLFTGD---DSHKPAGVLSGGEKTRLALAMIVVSGANVL 464
Cdd:PRK09700 89 LSVID-ELTVLENLyigrhltkkVCGVNIIDWREMRVRAAMMLLRVGlkvDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 465 LLDEPTNNLDPASREE---ILDALAHYEGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYlflIMNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDGS 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-236 |
8.95e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIgylPQDPRSgdpdELARtRIldarGL-----GQ 92
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV---PFKRRK----EFAR-RI----GVvfgqrSQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 LV--LGMQES--------TIamsssdasvsaaGMKKYGTLTDRFLALggyaaeaeaasiasnLNLpDRILEQPLKTLSGG 162
Cdd:COG4586 107 LWwdLPAIDSfrllkaiyRI------------PDAEYKKRLDELVEL---------------LDL-GELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVI--SHDIELVGETVNRVFYLDANRQVID 236
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILltSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
1-193 |
1.04e-13 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 70.78 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAG------HDLRRAPRAALA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILdarglgqlvlgMQESTIAMSSSDASVSaagmkkygtltdRFLA----LGGYAAEAEAASIASNLNLPDRILEQpL 156
Cdd:TIGR03864 75 RLGVV-----------FQQPTLDLDLSVRQNL------------RYHAalhgLSRAEARARIAELLARLGLAERADDK-V 130
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS 193
Cdd:TIGR03864 131 RELNGGHRRRVEIARALLHRPALLLLDEPTVGLDPAS 167
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
329-516 |
1.23e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 71.17 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQP----------DTGVIEAGHGLR--IGYYAQ 395
Cdd:PRK13644 5 ENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPqkgkvlvsgiDTGDFSKLQGIRklVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVKRSVLENMVSASPNLT--ETEARRVLGSFLFT---GDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:PRK13644 85 NPETQFVGRTVEEDLAFGPENLClpPIEIRKRVDRALAEiglEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 471 NNLDPASREEILDALA--HYEG-AVVLVSHDegaVEALN-PERVLIMPEG 516
Cdd:PRK13644 165 SMLDPDSGIAVLERIKklHEKGkTIVYITHN---LEELHdADRIIVMDRG 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-232 |
1.24e-13 |
|
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: 69.81 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGAR-----LLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDP--RSG 74
Cdd:cd03250 1 ISVEDASFTWDSGeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPwiQNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 75 ------------DPDELARTriLDARGLgqlvlgmqestiamsssdasvsaagmkkygtltDRFLALggyaaeaeaasia 142
Cdd:cd03250 81 tirenilfgkpfDEERYEKV--IKACAL---------------------------------EPDLEI------------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 143 snlnLPDRIL----EQPLkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWL-----REFLKNYRgGFIVISH 213
Cdd:cd03250 113 ----LPDGDLteigEKGI-NLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLNNK-TRILVTH 186
|
250
....*....|....*....
gi 1552103373 214 DIELVGEtVNRVFYLDANR 232
Cdd:cd03250 187 QLQLLPH-ADQIVVLDNGR 204
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-236 |
1.24e-13 |
|
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: 71.33 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELARTR-------------- 83
Cdd:TIGR04521 22 DDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG------RDITAKKKKKLKDLRkkvglvfqfpehql 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ----ILDARGLGQLVLGMQESTIAMSSSDAsvsaagMKKYGtltdrflalggyaaeaeaasiasnlnLPDRILEQPLKTL 159
Cdd:TIGR04521 96 feetVYKDIAFGPKNLGLSEEEAEERVKEA------LELVG--------------------------LDEEYLERSPFEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG----GFIVISHDIELVGETVNRVFYLDANRQVI 235
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKekglTVILVTHSMEDVAEYADRVIVMHKGKIVL 223
|
.
gi 1552103373 236 D 236
Cdd:TIGR04521 224 D 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
1.62e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------------IGY 66
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDPrSgdpdelartrILdaRGLG-----QLVLGMQESTIAMSssdasvsaagMKKYGTLTDRFlalggyaaeaeaasi 141
Cdd:COG1137 83 LPQEA-S----------IF--RKLTvedniLAVLELRKLSKKER----------EERLEELLEEF--------------- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1552103373 142 asNLnlpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEP 185
Cdd:COG1137 125 --GI---THLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
344-517 |
1.74e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.96 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEHETIDVKRSVleNMVSASP-------- 415
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPVRKRI--GMVFQFPesqlfedt 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 416 --------------NLTETEAR--RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE 479
Cdd:PRK13646 103 vereiifgpknfkmNLDEVKNYahRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 480 EILDALAHYE----GAVVLVSHDEGAVeALNPERVLIMPEGT 517
Cdd:PRK13646 183 QVMRLLKSLQtdenKTIILVSHDMNEV-ARYADEVIVMKEGS 223
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-233 |
1.75e-13 |
|
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: 72.77 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI----------DR---GGEIGYLPQDPR--SGDP 76
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVrldgadlkqwDRetfGKHIGYLPQDVElfPGTV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 77 DE-LAR-TRILDAR---------GLGQLVLGMQestiamsssdasvsaagmKKYgtltDRFLALGGyaaeaeaasiasnl 145
Cdd:TIGR01842 409 AEnIARfGENADPEkiieaaklaGVHELILRLP------------------DGY----DTVIGPGG-------------- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 146 nlpdrileqplKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREF---LKNYRGGFIVISHDIELVGeTV 222
Cdd:TIGR01842 453 -----------ATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAikaLKARGITVVVITHRPSLLG-CV 520
|
250
....*....|.
gi 1552103373 223 NRVFYLDANRQ 233
Cdd:TIGR01842 521 DKILVLQDGRI 531
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
328-517 |
1.90e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.27 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSY----------GSL--------EIFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGh 386
Cdd:COG4586 4 VENLSKTYrvyekepglkGALkglfrreyREVEAVDdisFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 387 glriGYYAQEHETIDVKR---------------SVLE--NMVSASPNLTETEARRV---------LGSFLftgddsHKPA 440
Cdd:COG4586 83 ----GYVPFKRRKEFARRigvvfgqrsqlwwdlPAIDsfRLLKAIYRIPDAEYKKRldelvelldLGELL------DTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 441 GVLSGGEKTR--LALAMIvvSGANVLLLDEPTNNLDPASREEILDALAHY---EGA-VVLVSHDEGAVEALNpERVLIMP 514
Cdd:COG4586 153 RQLSLGQRMRceLAAALL--HRPKILFLDEPTIGLDVVSKEAIREFLKEYnreRGTtILLTSHDMDDIEALC-DRVIVID 229
|
...
gi 1552103373 515 EGT 517
Cdd:COG4586 230 HGR 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
344-516 |
2.07e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL----------RIGYYAQEHETIDVKRSVLENMVS 412
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvMGREVnaenekwvrsKVGLVFQDPDDQVFSSTVWDDVAF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 413 ASPNLTETEA---RRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE---EILDA 484
Cdd:PRK13647 104 GPVNMGLDKDeveRRVEEALKAVRmwDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQEtlmEILDR 183
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 485 LaHYEGAVVLVS-HD-EGAVEAlnPERVLIMPEG 516
Cdd:PRK13647 184 L-HNQGKTVIVAtHDvDLAAEW--ADQVIVLKEG 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
2.10e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYLPQ 69
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEpvpsrarharqrVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DPRSgDPDELARTRIldarglgqLVLGmqestiamsssdasvsaagmkkygtltdRFLALGGYAAEAEAASIASNLNLPD 149
Cdd:PRK13537 88 FDNL-DPDFTVRENL--------LVFG----------------------------RYFGLSAAAARALVPPLLEFAKLEN 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 150 RIlEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD--ADSVVW--LREFLKnyRGGFIVI-SHDIELVGETVNR 224
Cdd:PRK13537 131 KA-DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLA--RGKTILLtTHFMEEAERLCDR 207
|
250
....*....|
gi 1552103373 225 VFYLDANRQV 234
Cdd:PRK13537 208 LCVIEEGRKI 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-229 |
2.10e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--IGYLPQDPRSGDPDE 78
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKlrIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LARTRILDARGlgqlvlgmqestiamsssdasvsaaGMKKygtlTDRFLALGGYAAEaeaasiasnlnlpdRILEQPLKT 158
Cdd:PRK09544 84 LTVNRFLRLRP-------------------------GTKK----EDILPALKRVQAG--------------HLIDAPMQK 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG----GFIVISHDIELVGETVNRVFYLD 229
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
316-517 |
2.16e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 316 PTPMACGRtplhaeNLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------- 385
Cdd:PRK15439 8 APPLLCAR------SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgnpcarltpa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 386 --HGLRIGYYAQEhETIDVKRSVLENMVSASPNLTETEAR-----RVLGSFLftgdDSHKPAGVLSGGEKTRLALAMIVV 458
Cdd:PRK15439 82 kaHQLGIYLVPQE-PLLFPNLSVKENILFGLPKRQASMQKmkqllAALGCQL----DLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQL-ADRISVMRDGT 217
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-185 |
2.46e-13 |
|
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: 69.49 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------------IGYL 67
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDP---RSgdpdelartrildarglgqlvLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFlalggyaaeaeaasiasN 144
Cdd:cd03218 81 PQEAsifRK---------------------LTVEENILAVLEIRGLSKKEREEKLEELLEEF-----------------H 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1552103373 145 LnlpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEP 185
Cdd:cd03218 123 I---THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-235 |
2.52e-13 |
|
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: 68.11 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVG--ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE------------IGYL 67
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVpvsdlekalsslISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDPRsgdpdeLARTRILDarglgqlvlgmqestiamsssdasvsaagmkkygtltdrflalggyaaeaeaasiasNLNL 147
Cdd:cd03247 81 NQRPY------LFDTTLRN---------------------------------------------------------NLGR 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 148 PdrileqplktLSGGQRRRIELARILFSDASTLILDEPTNHLDADS-VVWLREFLKNYRGGFIV-ISHdiELVG-ETVNR 224
Cdd:cd03247 98 R----------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDKTLIwITH--HLTGiEHMDK 165
|
250
....*....|.
gi 1552103373 225 VFYLDaNRQVI 235
Cdd:cd03247 166 ILFLE-NGKII 175
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
344-516 |
3.25e-13 |
|
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: 69.98 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQEhETIDVK----------------RSVL 407
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID-GQDIAAMSRK-ELRELRrkkismvfqsfallphRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 ENMV------SASPNLTETEARRVLGSFLFTGDDSHKPaGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR--- 478
Cdd:cd03294 121 ENVAfglevqGVPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRrem 199
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 479 -EEILDALAHYEGAVVLVSHDegAVEALN-PERVLIMPEG 516
Cdd:cd03294 200 qDELLRLQAELQKTIVFITHD--LDEALRlGDRIAIMKDG 237
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
17-225 |
3.26e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 71.76 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRggeigylpqdpRSGDPDELARTRILDARGLGQLVLG 96
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV-----------RVGDEWVDMTKPGPDGRGRAKRYIG 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 M--QESTIAMSSSDAsvsaagmkkyGTLTDrflALGgyaaeaeaasiasnLNLPDR----------------------IL 152
Cdd:TIGR03269 369 IlhQEYDLYPHRTVL----------DNLTE---AIG--------------LELPDElarmkavitlkmvgfdeekaeeIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 153 EQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD-------ADSVVWLREFLKNyrgGFIVISHDIELVGETVNRV 225
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRA 498
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
17-225 |
4.21e-13 |
|
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: 68.55 E-value: 4.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKG--TIDrGGEIGYLPQDPRsgdpdelartrildaRGLGQLv 94
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGfaTVD-GFDVVKEPAEAR---------------RRLGFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 95 lgmqestiamsssdasvsAAGMKKYGTLTDR--------FLALGGYAAEAEAASIASNLNLPDrILEQPLKTLSGGQRRR 166
Cdd:cd03266 84 ------------------SDSTGLYDRLTARenleyfagLYGLKGDELTARLEELADRLGMEE-LLDRRVGGFSTGMRQK 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 167 IELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIVISHDIELVGETVNRV 225
Cdd:cd03266 145 VAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFSTHIMQEVERLCDRV 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-517 |
4.23e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--------------------------- 382
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqqrdicmvfqsyalf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 383 -------EAGHGLRIGYYAQEHETIDVKRSvLEnMVsaspNLTETEARRVlgsflftgdDShkpagvLSGGEKTRLALAM 455
Cdd:PRK11432 91 phmslgeNVGYGLKMLGVPKEERKQRVKEA-LE-LV----DLAGFEDRYV---------DQ------ISGGQQQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 456 IVVSGANVLLLDEPTNNLDP----ASREEILDALAHYEGAVVLVSHDEGAVEALNPErVLIMPEGT 517
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQSEAFAVSDT-VIVMNKGK 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
326-499 |
4.45e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL---RIGYYAQ----EH 397
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfERQSIkkdLCTYQKQlcfvGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ET-----IDVKRSVLENMVSASPNLTETEARRV--LGSFLftgddsHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:PRK13540 82 RSginpyLTLRENCLYDIHFSPGAVGITELCRLfsLEHLI------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|..
gi 1552103373 471 NNLDPASREEILDALAHYE---GAVVLVSHDE 499
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
329-517 |
4.51e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTA--VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLR-----IGYYAQ 395
Cdd:PRK13648 11 KNVSFQYQSDASFTLkdVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFynnqaiTDDNFEklrkhIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVKRSV-------LENMVSASPNLTEtEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDE 468
Cdd:PRK13648 91 NPDNQFVGSIVkydvafgLENHAVPYDEMHR-RVSEALKQVDMLERADYEPNA-LSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 469 PTNNLDPASREEILDALAHY--EGAVVLVSHDEGAVEALNPERVLIMPEGT 517
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGT 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
344-517 |
4.91e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 69.69 E-value: 4.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--------EAGHGL-----RIGYYAQ--EH----ETIdvkr 404
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditDKKVKLsdirkKVGLVFQypEYqlfeETI---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 svlENMVSASP---NLTETE-ARRVLGSFLFTGDD----SHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPA 476
Cdd:PRK13637 102 ---EKDIAFGPinlGLSEEEiENRVKRAMNIVGLDyedyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1552103373 477 SREEILDALA----HYEGAVVLVSHDEGAVEALnPERVLIMPEGT 517
Cdd:PRK13637 179 GRDEILNKIKelhkEYNMTIILVSHSMEDVAKL-ADRIIVMNKGK 222
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
301-517 |
4.94e-13 |
|
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: 71.61 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 301 LEEVRAVDRVAKLrfPTPmacgRTPLHAENLS--KSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPD 378
Cdd:TIGR01842 298 LANYPSRDPAMPL--PEP----EGHLSVENVTivPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 379 TGVIEAG-----------HGLRIGYYAQEHETIDvkRSVLENMVSASPNLTE---TEARRVLG------SFLFTGDDSHK 438
Cdd:TIGR01842 372 SGSVRLDgadlkqwdretFGKHIGYLPQDVELFP--GTVAENIARFGENADPekiIEAAKLAGvhelilRLPDGYDTVIG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 439 PAGV-LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYE---GAVVLVSHDEGAVEALNpeRVLIMP 514
Cdd:TIGR01842 450 PGGAtLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKargITVVVITHRPSLLGCVD--KILVLQ 527
|
...
gi 1552103373 515 EGT 517
Cdd:TIGR01842 528 DGR 530
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
5.23e-13 |
|
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: 68.31 E-value: 5.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-----------IGYLPQD 70
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 71 PRSgdpdeLARTRILDARGLGQLVLGMQESTIAMSSsdasvsaagmkkygtltDRFLALGGYaaeaeaasiasnlnlpDR 150
Cdd:cd03259 81 YAL-----FPHLTVAENIAFGLKLRGVPKAEIRARV-----------------RELLELVGL----------------EG 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 151 ILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISHDIE 216
Cdd:cd03259 123 LLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQE 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
330-505 |
5.82e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 70.44 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQpdtgvIEAGHgLRIGyyaqEHETIDV---KRSV 406
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLED-----ITSGD-LFIG----EKRMNDVppaERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 leNMVSAS----PNLTETE----------------ARRV--------LGSFLftgddSHKPAGvLSGGEKTRLALAMIVV 458
Cdd:PRK11000 78 --GMVFQSyalyPHLSVAEnmsfglklagakkeeiNQRVnqvaevlqLAHLL-----DRKPKA-LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 459 SGANVLLLDEPTNNLDPA----SREEILDALAHYEGAVVLVSHDEgaVEAL 505
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAAlrvqMRIEISRLHKRLGRTMIYVTHDQ--VEAM 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
344-516 |
6.28e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 69.47 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL--------------RIGYYAQEHETIDVKRSVLE 408
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiAGYHItpetgnknlkklrkKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NMVSASPNL--TETEARRVLGSFL----FTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:PRK13641 106 DVEFGPKNFgfSEDEAKEKALKWLkkvgLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 483 DALAHYEGA---VVLVSHDEGAVeALNPERVLIMPEG 516
Cdd:PRK13641 186 QLFKDYQKAghtVILVTHNMDDV-AEYADDVLVLEHG 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
6.58e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.96 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELR----VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------IGYLP 68
Cdd:COG1116 7 ALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgpdRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 69 QDPR-----------------SGDPDELARTRildARGLGQLVlgmqestiamsssdasvsaaGMKKYGtltDRFlalgg 131
Cdd:COG1116 87 QEPAllpwltvldnvalglelRGVPKAERRER---ARELLELV--------------------GLAGFE---DAY----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 132 yaaeaeaasiasnlnlpdrileqPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDA-------DsvvWLREFLKNY 204
Cdd:COG1116 136 -----------------------P-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrerlqD---ELLRLWQET 188
|
250
....*....|..
gi 1552103373 205 RGGFIVISHDIE 216
Cdd:COG1116 189 GKTVLFVTHDVD 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-213 |
8.06e-13 |
|
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: 66.41 E-value: 8.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGA-RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDR--GGEIGYLPQDPrsgdpde 78
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpeGEDLLFLPQRP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 lartrildarglgqlvlgmqestiamsssdasvsaagmkkygtltdrFLALGgyaaeaeaasiasnlNLPDRILEQPLKT 158
Cdd:cd03223 74 -----------------------------------------------YLPLG---------------TLREQLIYPWDDV 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISH 213
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
344-520 |
8.28e-13 |
|
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: 67.88 E-value: 8.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG--------VIEAGHGLRIGYyaqEHETIDVKRSVLENMV---- 411
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGgvilegkqITEPGPDRMVVF---QNYSLLPWLTVRENIAlavd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 412 SASPNLTETEARRVLGSFLFT---GDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH- 487
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEHIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQi 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 488 ---YEGAVVLVSHDegAVEALN-PERVLIMPEGTEDH 520
Cdd:TIGR01184 161 weeHRVTVLMVTHD--VDEALLlSDRVVMLTNGPAAN 195
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-216 |
9.50e-13 |
|
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: 67.32 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVgDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--------EIGYLPQDprsgdpdelartrildaRGL 90
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkKINLPPQQ-----------------RKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 91 GQLVlgmQESTIAMSSSDASVSAAGMKKYGTLTDRFLAlggyaaeaeaASIASNLNLpDRILEQPLKTLSGGQRRRIELA 170
Cdd:cd03297 78 GLVF---QQYALFPHLNVRENLAFGLKRKRNREDRISV----------DELLDLLGL-DHLLNRYPAQLSGGEKQRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 171 RILFSDASTLILDEPTNHLDADS----VVWLREFLKNYRGGFIVISHDIE 216
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLS 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
326-497 |
9.51e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.43 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AG-------------HGLRIG 391
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILlDGepvrfrsprdaqaAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YyaQEHETIDvKRSVLENMVSASP---------NLTETEARRVLGSFLFTgDDSHKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:COG1129 85 H--QELNLVP-NLSVAENIFLGREprrgglidwRAMRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 463 VLLLDEPTNNLDPASRE---EILDALAHyEG-AVVLVSH 497
Cdd:COG1129 161 VLILDEPTASLTEREVErlfRIIRRLKA-QGvAIIYISH 198
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
329-497 |
9.58e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.58 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGLR----------IGYYAQE 396
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILiDGVDIRdltleslrrqIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 heTIDVKRSVLENMVSASPNLTETEARRVL-----GSFLftgddSHKPAGV----------LSGGEKTRLALAMIVVSGA 461
Cdd:COG1132 423 --TFLFSGTIRENIRYGRPDATDEEVEEAAkaaqaHEFI-----EALPDGYdtvvgergvnLSGGQRQRIAIARALLKDP 495
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDALAHY-EGA-VVLVSH 497
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLmKGRtTIVIAH 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
326-497 |
1.02e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.44 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSleiFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------------AGHGLRI 390
Cdd:COG3845 6 LELRGITKRFGG---VVAnddVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILidgkpvrirsprDAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQeH----ETIdvkrSVLENMV-----SASPNLTETEARRVLGSFlftGD------DSHKPAGVLSGGEKTRL---- 451
Cdd:COG3845 83 GMVHQ-HfmlvPNL----TVAENIVlglepTKGGRLDRKAARARIREL---SErygldvDPDAKVEDLSVGEQQRVeilk 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 452 ALAmivvSGANVLLLDEPTNNLDPASREE---ILDALAHyEG-AVVLVSH 497
Cdd:COG3845 155 ALY----RGARILILDEPTAVLTPQEADElfeILRRLAA-EGkSIIFITH 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-192 |
1.04e-12 |
|
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: 70.47 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqDPRSGDPDELART--------R 83
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV------PVSSLDQDEVRRRvsvcaqdaH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ILDARGLGQLVLGMQESTiamsssdASVSAAGMKKYGtLTDRFLAL-GGYaaeaeaasiasnlnlpDRILEQPLKTLSGG 162
Cdd:TIGR02868 420 LFDTTVRENLRLARPDAT-------DEELWAALERVG-LADWLRALpDGL----------------DTVLGEGGARLSGG 475
|
170 180 190
....*....|....*....|....*....|
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDAD 192
Cdd:TIGR02868 476 ERQRLALARALLADAPILLLDEPTEHLDAE 505
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-228 |
1.11e-12 |
|
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: 68.93 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDL--ELRVGARLLM--ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTID----------------- 59
Cdd:COG0444 1 LLEVRNLkvYFPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGITSgeilfdgedllklseke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 60 ----RGGEIGYLPQDPRS------------GDPdeLARTRILDARGLGQLVLGMqestiamsssdasvsaagMKKYGtlt 123
Cdd:COG0444 80 lrkiRGREIQMIFQDPMTslnpvmtvgdqiAEP--LRIHGGLSKAEARERAIEL------------------LERVG--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 124 drflalggyaaeaeaasiasnLNLPDRILEQ-PlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDAdSVVW-----L 197
Cdd:COG0444 137 ---------------------LPDPERRLDRyP-HELSGGMRQRVMIARALALEPKLLIADEPTTALDV-TIQAqilnlL 193
|
250 260 270
....*....|....*....|....*....|...
gi 1552103373 198 REFLKNYRGGFIVISHDIELVGETVNR--VFYL 228
Cdd:COG0444 194 KDLQRELGLAILFITHDLGVVAEIADRvaVMYA 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-225 |
1.13e-12 |
|
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: 67.14 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI------------DRGGEIGYLPQDprsgD--PDEL----- 79
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrkAARQSLGYCPQF----DalFDELtvreh 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ----ARTRILDARGLGQLVLGMQESTiamsssdasvsaaGMKKYgtltdrflalggyaaeaeaasiasnlnlpdriLEQP 155
Cdd:cd03263 96 lrfyARLKGLPKSEIKEEVELLLRVL-------------GLTDK--------------------------------ANKR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 156 LKTLSGGQRRRIELARILFSDASTLILDEPTNHLD--ADSVVWlrEFLKNYRGG--FIVISHDIELVGETVNRV 225
Cdd:cd03263 131 ARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDpaSRRAIW--DLILEVRKGrsIILTTHSMDEAEALCDRI 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-497 |
1.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.02 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 323 RTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQ--PDTGVieAGHGLRIGYYAQEHETI 400
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEARV--SGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 401 DVKR---------------SVLENmVSASPNLT---------ETEARRVLGSFLF---TGDDSHKPAGVLSGGEKTRLAL 453
Cdd:PRK14247 79 ELRRrvqmvfqipnpipnlSIFEN-VALGLKLNrlvkskkelQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQRLCI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDP---ASREEILDALAHyEGAVVLVSH 497
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPentAKIESLFLELKK-DMTIVLVTH 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-213 |
1.16e-12 |
|
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: 66.78 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDliaSKGTIDRgGEIGYLPQDPRSGDPDELAR 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH---PKYEVTE-GEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 trildaRGLGqlvLGMQEStiamsssdasVSAAGMKkygtlTDRFLalggyaaeaeaasiaSNLNlpdrileqplKTLSG 161
Cdd:cd03217 77 ------LGIF---LAFQYP----------PEIPGVK-----NADFL---------------RYVN----------EGFSG 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISH 213
Cdd:cd03217 108 GEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
345-516 |
1.53e-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: 65.64 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 345 DLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghglRIGYYAQEHetidvkrsVLenMVSASPNLTETEARR 424
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG--------RIGMPEGED--------LL--FLPQRPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 425 VLgsfLFTGDDshkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHDEgAVEA 504
Cdd:cd03223 83 QL---IYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRP-SLWK 152
|
170
....*....|..
gi 1552103373 505 LNPERVLIMPEG 516
Cdd:cd03223 153 FHDRVLDLDGEG 164
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
344-516 |
1.57e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 67.90 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGV----DQPDTGVIEAGHGL----------RIGYYAQEHETIDVKRSV--- 406
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLllpdDNPNSKITVDGITLtaktvwdireKVGIVFQNPDNQFVGATVgdd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 ----LENMVSASPNLTETeARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:PRK13640 106 vafgLENRAVPRPEMIKI-VRDVLADVGMLDYIDSEPAN-LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQIL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 483 DALAHYEG----AVVLVSHDEGavEALNPERVLIMPEG 516
Cdd:PRK13640 184 KLIRKLKKknnlTVISITHDID--EANMADQVLVLDDG 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-215 |
1.61e-12 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 67.30 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPQDPRsgdpdelA 80
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdITHLPMHER-------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildaRGLGQLvlgMQESTIamsssdasvsaagMKKYgTLTDRFLALGGYAAEAEAASIASNL-NLPD-----RILEQ 154
Cdd:TIGR04406 75 R------LGIGYL---PQEASI-------------FRKL-TVEENIMAVLEIRKDLDRAEREERLeALLEefqisHLRDN 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 155 PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLR---EFLKNYRGGFIVISHDI 215
Cdd:TIGR04406 132 KAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKkiiKHLKERGIGVLITDHNV 195
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-234 |
1.63e-12 |
|
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: 67.13 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 10 RVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELARtrildarg 89
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG------HDLALADPAWLRR-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 90 lgQLVLGMQESTIAMsssdasvsaagmkkyGTLTDRfLALGGYAAEAEAASIASNL-NLPDRILEQPL----------KT 158
Cdd:cd03252 77 --QVGVVLQENVLFN---------------RSIRDN-IALADPGMSMERVIEAAKLaGAHDFISELPEgydtivgeqgAG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLDANRQV 234
Cdd:cd03252 139 LSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTV-KNADRIIVMEKGRIV 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
316-516 |
1.90e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.71 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 316 PTPMACGR---TPL-HAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIG 391
Cdd:PRK11607 6 PRPQAKTRkalTPLlEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEHETIDV---------KRSVLENMVSA--SPNLTETEARRVLGSFL-------FTGDDSHKpagvLSGGEKTRLAL 453
Cdd:PRK11607 85 HVPPYQRPINMmfqsyalfpHMTVEQNIAFGlkQDKLPKAEIASRVNEMLglvhmqeFAKRKPHQ----LSGGQRQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDPASRE----EILDALAHYEGAVVLVSHDEGavEALN-PERVLIMPEG 516
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERVGVTCVMVTHDQE--EAMTmAGRIAIMNRG 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-218 |
2.14e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 27 GDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPrSGDPDELARTRILDARGlgqlvlGMQESTIAmss 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYI-SPDYDGTVEEFLRSANT------DDFGSSYY--- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 107 sdasvsaagmkkYGTLTDRflalggyaaeaeaasiasnLNLpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:COG1245 436 ------------KTEIIKP-------------------LGL-EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190
....*....|....*....|....*....|....*.
gi 1552103373 187 NHLDADSVV----WLREFLKNYRGGFIVISHDIELV 218
Cdd:COG1245 484 AHLDVEQRLavakAIRRFAENRGKTAMVVDHDIYLI 519
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
345-485 |
2.43e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 2.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 345 DLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghGLRIGyyAQEH-ETIDVKR--SVL--ENMVSA------ 413
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASG------SLTLN--GQDHtTTPPSRRpvSMLfqENNLFShltvaq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 414 ------SPNLTETE---------ARRV-LGSFLftgddSHKPaGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPAS 477
Cdd:PRK10771 91 niglglNPGLKLNAaqreklhaiARQMgIEDLL-----ARLP-GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
....*...
gi 1552103373 478 REEILDAL 485
Cdd:PRK10771 165 RQEMLTLV 172
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
326-516 |
2.46e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI---------EAGHGLR--IGYY 393
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkENIREVRkfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 394 AQEHETIDVKRSVLENMVSASPNL---TETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDE 468
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAFGPINLgldEETVAHRVSSALHMLGleELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 469 PTNNLDPASREEILD---ALAHYEGAVVLVSHDEGAVEALNPERVLIMPEG 516
Cdd:PRK13652 164 PTAGLDPQGVKELIDflnDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
326-516 |
2.58e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.02 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY---------GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI------------EA 384
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnrAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 385 GHGLR----------IGYYAQEHETIDVKRSVLENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALA 454
Cdd:PRK10419 84 RKAFRrdiqmvfqdsISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILD---ALAHYEG-AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRllkKLQQQFGtACLFITHDLRLVERF-CQRVMVMDNG 228
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
326-516 |
2.62e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.41 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYyaQEHETIDVKR 404
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKY--DKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 SV---------------LENMVSASP---NLTETE-ARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANV 463
Cdd:PRK13639 79 TVgivfqnpddqlfaptVEEDVAFGPlnlGLSKEEvEKRVKEALKAVGmeGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 464 LLLDEPTNNLDPASREEILDALA--HYEGAVVLVS-HDEGAVeALNPERVLIMPEG 516
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHDVDLV-PVYADKVYVMSDG 213
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
326-485 |
3.68e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.06 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG-------HGLRIGYYA---- 394
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkditdwQTAKIMREAvaiv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDVKRSVLENMVS----ASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPT 470
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMggffAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170
....*....|....*
gi 1552103373 471 NNLDPASREEILDAL 485
Cdd:PRK11614 166 LGLAPIIIQQIFDTI 180
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
326-483 |
4.39e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.26 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY--GSLE---IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAqEHeti 400
Cdd:COG1101 2 LELKNLSKTFnpGTVNekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILID-GKDVTKLP-EY--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 401 dvKRS-----VLEN-MVSASPNLTETE---------ARRVLGSFLFTGDDSH-----------------KPAGVLSGGEK 448
Cdd:COG1101 77 --KRAkyigrVFQDpMMGTAPSMTIEEnlalayrrgKRRGLRRGLTKKRRELfrellatlglglenrldTKVGLLSGGQR 154
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 449 TRLALAMIVVSGANVLLLDEPTNNLDPASREEILD 483
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLE 189
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
355-506 |
5.70e-12 |
|
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: 64.94 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 355 VILGLNGAGKTTLLRIL-------------GGVDQPD-TGVIEAGHGLRIGYYAQEHETIDVKRS--VLENMVsaspnlt 418
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkyaltgelppnskGGAHDPKlIREGEVRAQVKLAFENANGKKYTITRSlaILENVI------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 419 etearrvlgsFLFTGDdSHKPA----GVLSGGEKT------RLALAMIVVSGANVLLLDEPTNNLDPASRE----EILDA 484
Cdd:cd03240 99 ----------FCHQGE-SNWPLldmrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaEIIEE 167
|
170 180
....*....|....*....|...
gi 1552103373 485 LAHYEG-AVVLVSHDEGAVEALN 506
Cdd:cd03240 168 RKSQKNfQLIVITHDEELVDAAD 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
326-498 |
5.74e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.15 E-value: 5.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH-----------GLRIGYYA 394
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 Q------------EHETIDVKRSVLENMVSASPN---LTETEAR----RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAM 455
Cdd:PRK10619 86 QlrllrtrltmvfQHFNLWSHMTVLENVMEAPIQvlgLSKQEAReravKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 456 IVVSGANVLLLDEPTNNLDPASREE---ILDALAHYEGAVVLVSHD 498
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEvlrIMQQLAEEGKTMVVVTHE 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
17-228 |
7.18e-12 |
|
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: 64.74 E-value: 7.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgDPDELARTRI-LDARGLGqlvL 95
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ-----------DVSDLRGRAIpYLRRKIG---V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 96 GMQESTIAMSSSDASVSAAGMkkygtltdRFLALGGYAAEAEAASIASNLNLPDRILEQPLKtLSGGQRRRIELARILFS 175
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFAL--------EVTGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 176 DASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVIS-HDIELVGETVNRVFYL 228
Cdd:cd03292 154 SPTILIADEPTGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELVDTTRHRVIAL 209
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-200 |
7.64e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.81 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIA---SKGTIDRGGE-----------IGY 66
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltalpaeqrrIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDP----------------RSGDPDELARTRILDArgLGQLVLGmqestiamsssdasvsaagmkkygTLTDRFLAlg 130
Cdd:COG4136 81 LFQDDllfphlsvgenlafalPPTIGRAQRRARVEQA--LEEAGLA------------------------GFADRDPA-- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 131 gyaaeaeaasiasnlnlpdrileqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREF 200
Cdd:COG4136 133 ---------------------------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREF 175
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-517 |
8.50e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 67.54 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY--GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhGLRIGYYAQE--HETIDV-- 402
Cdd:PRK11160 342 NNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQPIADYSEAalRQAISVvs 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KR------SVLENMVSASPNLTETEARRVLG----SFLFTGD--------DSHKPagvLSGGEKTRLALAMIVVSGANVL 464
Cdd:PRK11160 421 QRvhlfsaTLRDNLLLAAPNASDEALIEVLQqvglEKLLEDDkglnawlgEGGRQ---LSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 465 LLDEPTNNLDPASREEILDAL-AHYEG-AVVLVSHDEGAVEALNpeRVLIMPEGT 517
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLaEHAQNkTVLMITHRLTGLEQFD--RICVMDNGQ 550
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-215 |
8.68e-12 |
|
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: 65.12 E-value: 8.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRvgDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPQDPRsgdPDelartrildarglgq 92
Cdd:cd03237 14 TLEVEGGSIS--ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDtVSYKPQYIK---AD--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 lvlgmQESTIAMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeaasiasnlnlpDRILEQPLKTLSGGQRRRIELARI 172
Cdd:cd03237 74 -----YEGTVRDLLSSITKDFYTHPYFKTEIAKPLQI-------------------EQILDREVPELSGGELQRVAIAAC 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 173 LFSDASTLILDEPTNHLDADSVVW----LREFLKNYRGGFIVISHDI 215
Cdd:cd03237 130 LSKDADIYLLDEPSAYLDVEQRLMaskvIRRFAENNEKTAFVVEHDI 176
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-216 |
9.17e-12 |
|
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: 64.80 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDL----ELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------IGYLPQ 69
Cdd:cd03293 1 LEVRNVsktyGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DPRSgdpdeLARTRILDARGLGQLVLGMQESTIAMSssdasvsaagmkkygtlTDRFLALGGyaaeaeaasiasnlnLPD 149
Cdd:cd03293 81 QDAL-----LPWLTVLDNVALGLELQGVPKAEARER-----------------AEELLELVG---------------LSG 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 150 RILEQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGGFIVISHDIE 216
Cdd:cd03293 124 FENAYP-HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHDID 193
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-234 |
9.47e-12 |
|
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: 65.60 E-value: 9.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELR------VGAR---LLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDP 71
Cdd:TIGR02769 2 LLEVRDVTHTyrtgglFGAKqraPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRG------QDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 RSGDPDELARTRildaRGLgQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTD-----RFLALggyaaeaeaasiASNLN 146
Cdd:TIGR02769 76 YQLDRKQRRAFR----RDV-QLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDEseqkaRIAEL------------LDMVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 LPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETV 222
Cdd:TIGR02769 139 LRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFC 218
|
250
....*....|..
gi 1552103373 223 NRVFYLDANRQV 234
Cdd:TIGR02769 219 QRVAVMDKGQIV 230
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
329-486 |
1.00e-11 |
|
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: 64.94 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYG-SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLR--IGYYAQE 396
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdirevtlDSLRraIGVVPQD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 ----HETIdvkrsvLENMVSASPNLTETEARRV---------LGSFLFTGDDSHKPAGV-LSGGEKTRLALAMIVVSGAN 462
Cdd:cd03253 84 tvlfNDTI------GYNIRYGRPDATDEEVIEAakaaqihdkIMRFPDGYDTIVGERGLkLSGGEKQRVAIARAILKNPP 157
|
170 180
....*....|....*....|....
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALA 486
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALR 181
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
326-517 |
1.05e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 65.01 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI----EAGHGL------RIGYYAQ 395
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIllrgQHIEGLpghqiaRMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 -EHETIDVKRSVLENMVSASpnlteteaRRVLGSFLFTG----------------------------DDSHKPAGVLSGG 446
Cdd:PRK11300 86 fQHVRLFREMTVIENLLVAQ--------HQQLKTGLFSGllktpafrraesealdraatwlervgllEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 447 EKTRLALAMIVVSGANVLLLDEPTNNLDPASREEiLDAL-----AHYEGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKE-LDELiaelrNEHNVTVLLIEHDMKLVMGIS-DRIYVVNQGT 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
326-485 |
1.15e-11 |
|
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: 63.72 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSK------SYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGG--VDQPDTGVIEA-GHGL-------R 389
Cdd:cd03213 4 LSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGRPLdkrsfrkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 IGYYAQEhetiDVkrsvlenmvsASPNLTETEArrvlgsFLFTgddshkpAGV--LSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:cd03213 84 IGYVPQD----DI----------LHPTLTVRET------LMFA-------AKLrgLSGGERKRVSIALELVSNPSLLFLD 136
|
170
....*....|....*...
gi 1552103373 468 EPTNNLDPASREEILDAL 485
Cdd:cd03213 137 EPTSGLDSSSALQVMSLL 154
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
324-498 |
1.16e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 324 TPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--EAGH---------GLRIGY 392
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwlDGEHiqhyaskevARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEHET---IDVKRSVLENMVSASPNLT---ETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVL 464
Cdd:PRK10253 86 LAQNATTpgdITVQELVARGRYPHQPLFTrwrKEDEEAVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 465 LLDEPTNNLDPASREEILDALAH------YEGAVVLvsHD 498
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSElnrekgYTLAAVL--HD 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
329-516 |
1.38e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 65.01 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLE--IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLR-----IGYYAQ 395
Cdd:PRK13632 11 ENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiSKENLKeirkkIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVKRSV-------LENMvsaspNLTETEARRVLgsflftgDDSHKPAGV----------LSGGEKTRLALAMIVV 458
Cdd:PRK13632 91 NPDNQFIGATVeddiafgLENK-----KVPPKKMKDII-------DDLAKKVGMedyldkepqnLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEILDALA--HYEGAVVLVS--HDEGavEALNPERVLIMPEG 516
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISitHDMD--EAILADKVIVFSEG 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-215 |
1.66e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.76 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 27 GDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPRSgDPDelartrildarGLGQLVLGMQEStiamss 106
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQYIKP-DYD-----------GTVEDLLRSITD------ 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 107 sdasvsaagmkKYGT------LTDRflalggyaaeaeaasiasnLNLpDRILEQPLKTLSGGQRRRIELARILFSDASTL 180
Cdd:PRK13409 427 -----------DLGSsyykseIIKP-------------------LQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1552103373 181 ILDEPTNHLD------ADSVvwLREFLKNYRGGFIVISHDI 215
Cdd:PRK13409 476 LLDEPSAHLDveqrlaVAKA--IRRIAEEREATALVVDHDI 514
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-516 |
1.68e-11 |
|
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: 63.22 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 322 GRTPLHAENLSKSYGsleiFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------------AGHGLR 389
Cdd:cd03215 1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITldgkpvtrrsprDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 IGYYAQE--HETIDVKRSVLENMVsaspnltetearrvLGSFLftgddshkpagvlSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:cd03215 77 IAYVPEDrkREGLVLDLSVAENIA--------------LSSLL-------------SGGNQQKVVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 468 EPTNNLDPASREEI---LDALAHYEGAVVLVSHDegavealNPE------RVLIMPEG 516
Cdd:cd03215 130 EPTRGVDVGAKAEIyrlIRELADAGKAVLLISSE-------LDEllglcdRILVMYEG 180
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
326-516 |
1.77e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--------------EAGHGlrIG 391
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRG--IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEhETIDVKRSVLENMVSA---SPNLTETEARRVLGSFLFTGDDSHKPAGV---LSGGEKTRLALAMIVVSGANVLL 465
Cdd:PRK10895 82 YLPQE-ASIFRRLSVYDNLMAVlqiRDDLSAEQREDRANELMEEFHIEHLRDSMgqsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 466 LDEPTNNLDPASREEILDALAHYE--GAVVLVShDEGAVEALNP-ERVLIMPEG 516
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRdsGLGVLIT-DHNVRETLAVcERAYIVSQG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-211 |
1.82e-11 |
|
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: 63.34 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRV------GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLI--ASKGTIDRGG----------E 63
Cdd:cd03213 4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGrpldkrsfrkI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 64 IGYLPQDprsgdpDELartrildarglgqlvlgmqestiamsssdasvsaagmkkYGTLTDR----FLALggyaaeaeaa 139
Cdd:cd03213 84 IGYVPQD------DIL---------------------------------------HPTLTVRetlmFAAK---------- 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 140 siasnlnlpdrileqpLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR-GGFIVI 211
Cdd:cd03213 109 ----------------LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdTGRTII 165
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
344-516 |
2.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGG----------VDQPDTGVIEAGHGLR--IGYYAQEHETIDVKRSVLENMV 411
Cdd:PRK13633 29 VNLEVKKGEFLVILGRNGSGKSTIAKHMNAllipsegkvyVDGLDTSDEENLWDIRnkAGMVFQNPDNQIVATIVEEDVA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 412 SASPNL--TETEAR-RVlgsflftgDDSHKPAG----------VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR 478
Cdd:PRK13633 109 FGPENLgiPPEEIReRV--------DESLKKVGmyeyrrhaphLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 479 EEILDAL----AHYEGAVVLVSH-DEGAVEAlnpERVLIMPEG 516
Cdd:PRK13633 181 REVVNTIkelnKKYGITIILITHyMEEAVEA---DRIIVMDSG 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
326-498 |
2.10e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 64.50 E-value: 2.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYG----SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE------AGHGLRIGYYAQ 395
Cdd:COG4525 4 LTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITldgvpvTGPGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHeTIDVKRSVLENM--------VSASPNltETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:COG4525 84 KD-ALLPWLNVLDNVafglrlrgVPKAER--RARAEELLALVGLADFARRRIWQ-LSGGMRQRVGIARALAADPRFLLMD 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 468 EPTNNLDPASREE----ILDALAHYEGAVVLVSHD 498
Cdd:COG4525 160 EPFGALDALTREQmqelLLDVWQRTGKGVFLITHS 194
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
340-517 |
2.36e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 340 IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQE----HETIdvkRSVLenmvsASP 415
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRpylpLGTL---REAL-----LYP 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 416 N----LTETEARRV-----LGSF---LFTGDDSHKpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILD 483
Cdd:COG4178 450 AtaeaFSDAELREAleavgLGHLaerLDEEADWDQ---VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
170 180 190
....*....|....*....|....*....|....*.
gi 1552103373 484 ALAH--YEGAVVLVSHDEgAVEALNPERVLIMPEGT 517
Cdd:COG4178 527 LLREelPGTTVISVGHRS-TLAAFHDRVLELTGDGS 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-236 |
2.38e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 64.68 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG---------------EIGYLPQDPRSgdpdELAR 81
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPEY----QLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARGLGQLVLGMQESTIAMSSSDAsvsaagMK----KYGTLTDRflalggyaaeaeaasiasnlnlpdrileQPLK 157
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRA------MNivglDYEDYKDK----------------------------SPFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 158 tLSGGQRRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQ 233
Cdd:PRK13637 145 -LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
...
gi 1552103373 234 VID 236
Cdd:PRK13637 224 ELQ 226
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-516 |
2.49e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.09 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgdPDELARTRilDARGLG------- 91
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------------EMRFASTT--AALAAGvaiiyqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 -QLVlgmQESTIAMSSSDasvsaagmkkyGTLTDRFLALGGYAAEAEAASIASNLNL---PDrileQPLKTLSGGQRRRI 167
Cdd:PRK11288 88 lHLV---PEMTVAENLYL-----------GQLPHKGGIVNRRLLNYEAREQLEHLGVdidPD----TPLKYLSIGQRQMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 168 ELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR--GGFIV-ISHDIELVGETVNRVFYLDANRQVIDVYNMnwkn 244
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaeGRVILyVSHRMEEIFALCDAITVFKDGRYVATFDDM---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 245 yqrqraadeerrkkerANVEKKagalQLQAArfgakaskaaaahqMVARAEKMLSG-----LEEVR-AVDRVAKLRFPTP 318
Cdd:PRK11288 226 ----------------AQVDRD----QLVQA--------------MVGREIGDIYGyrprpLGEVRlRLDGLKGPGLREP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 319 macgrtplhaenlsksygsleiftaVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE----------AGHGL 388
Cdd:PRK11288 272 -------------------------ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidirsPRDAI 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 RIGYYA----QEHETIDVKRSVLENM-VSASPNL----------TETE-ARRVLGSFLFTGDDSHKPAGVLSGGEKTRLA 452
Cdd:PRK11288 327 RAGIMLcpedRKAEGIIPVHSVADNInISARRHHlragclinnrWEAEnADRFIRSLNIKTPSREQLIMNLSGGNQQKAI 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 453 LAMIVVSGANVLLLDEPTNNLDPASREEILD---ALAHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK11288 407 LGRWLSEDMKVILLDEPTRGIDVGAKHEIYNviyELAAQGVAVLFVSSDLPEVLGVA-DRIVVMREG 472
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
326-516 |
2.51e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 64.34 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY---GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA-GHGL----------RIG 391
Cdd:PRK13642 5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLtaenvwnlrrKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEHETIDVKRSVLENMVSASPNL---TETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:PRK13642 85 MVFQNPDNQFVGATVEDDVAFGMENQgipREEMIKRVDEALLAVNmlDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 467 DEPTNNLDPASREEILDALAH----YEGAVVLVSHDEGavEALNPERVLIMPEG 516
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEikekYQLTVLSITHDLD--EAASSDRILVMKAG 216
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
348-498 |
2.54e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.97 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 348 IDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYYAQEHEtIDVKRSVLENMVSASPNltetearrvLG 427
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIK-ADYEGTVRDLLSSITKD---------FY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 428 SFLFTGDDSHKPAGV----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY----EGAVV 493
Cdd:cd03237 91 THPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAF 170
|
....*
gi 1552103373 494 LVSHD 498
Cdd:cd03237 171 VVEHD 175
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
340-512 |
2.56e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.44 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 340 IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGG--VDQPDTGVIEAghglrigyyaqEHETIDVKRSVLENMvsaSPNL 417
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV-----------PDNQFGREASLIDAI---GRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 418 TETEARRVLGS------FLFTgddshKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREE----ILDALAH 487
Cdd:COG2401 111 DFKDAVELLNAvglsdaVLWL-----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARR 185
|
170 180
....*....|....*....|....*
gi 1552103373 488 YEGAVVLVSHDEGAVEALNPERVLI 512
Cdd:COG2401 186 AGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-516 |
2.73e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdlIASKGTidrgGEIGYLPQDPRSGDPdelartRILDARGLG----- 91
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTG--IYTRDA----GSILYLGKEVTFNGP------KSSQEAGIGiihqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 -QLV--LGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLAlggyaaeaeaasiasNLNLPDRIlEQPLKTLSGGQRRRIE 168
Cdd:PRK10762 88 lNLIpqLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLA---------------RLNLRFSS-DKLVGELSIGEQQMVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 169 LARILFSDASTLILDEPTNHL-DAD-----SVVwlREfLKNYRGGFIVISHDIELVGETVNRVFYLdANRQVIDvynmnw 242
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTEteslfRVI--RE-LKSQGRGIVYISHRLKEIFEICDDVTVF-RDGQFIA------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 243 knyQRQRAADEERRKKERanvekkagalqlqaarfgakaskaaaahqMVARAekmlsgLEEvrAVDRVAKLRfptpmacG 322
Cdd:PRK10762 222 ---EREVADLTEDSLIEM-----------------------------MVGRK------LED--QYPRLDKAP-------G 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 323 RTPLHAENLSKSyGsleiFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGH----------GLRIGY 392
Cdd:PRK10762 255 EVRLKVDNLSGP-G----VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGhevvtrspqdGLANGI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 -YAQEhetiDVKR-------SVLENM--------VSASPNLTETEARRVLGSF--LFT--GDDSHKPAGVLSGGEKTRLA 452
Cdd:PRK10762 330 vYISE----DRKRdglvlgmSVKENMsltalryfSRAGGSLKHADEQQAVSDFirLFNikTPSMEQAIGLLSGGNQQKVA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 453 LAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY--EG-AVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaEGlSIILVSSEMPEVLGMS-DRILVMHEG 471
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-212 |
2.89e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.98 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGA-RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdlI--ASKGTIDR--GGEIGYLPQ------ 69
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--LwpYGSGRIARpaGARVLFLPQrpylpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 -----------DPRSGDPDELArtRILDARGLGQLVlgmqestiamsssdasvsaagmkkygtltDRflalggyaaeaea 138
Cdd:COG4178 440 gtlreallypaTAEAFSDAELR--EALEAVGLGHLA-----------------------------ER------------- 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 139 asiasnlnlpdriLEQPL---KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVIS 212
Cdd:COG4178 476 -------------LDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVIS 539
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
3.24e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 3.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE---------------IGYLPQDPrsgdPDELAR 81
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktVGIVFQNP----DDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARGLGQLVLGMQESTIAMSSSDasvsaaGMKKYGtltdrflaLGGYAaeaeaasiasnlnlpdrilEQPLKTLSG 161
Cdd:PRK13639 94 PTVEEDVAFGPLNLGLSKEEVEKRVKE------ALKAVG--------MEGFE-------------------NKPPHHLSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVIS-HDIELVGETVNRVFYL 228
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHDVDLVPVYADKVYVM 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
329-529 |
5.35e-11 |
|
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: 64.82 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQ--PDTGVIEAGHGL-----RIGYYAQEHETID 401
Cdd:TIGR03269 4 KNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHVALcekcgYVERPSKVGEPCP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 VKRSVLENMVSASPNLTETEARRVLG--------SFLFTGDD---------------------------------SHKPA 440
Cdd:TIGR03269 84 VCGGTLEPEEVDFWNLSDKLRRRIRKriaimlqrTFALYGDDtvldnvlealeeigyegkeavgravdliemvqlSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 441 GV---LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEALNPERVL-- 511
Cdd:TIGR03269 164 HIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALeeavKASGISMVLTSHWPEVIEDLSDKAIWle 243
|
250 260
....*....|....*....|.
gi 1552103373 512 ---IMPEGTEDHWAADYLDLI 529
Cdd:TIGR03269 244 ngeIKEEGTPDEVVAVFMEGV 264
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-516 |
6.74e-11 |
|
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: 65.42 E-value: 6.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 357 LGLNGAGKTTLLRILGGVDQPDTGVIEAG--------HGLR--IGYYAQeHETIDVKRSVLENMV--SASPNLTETEARR 424
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGgkdietnlDAVRqsLGMCPQ-HNILFHHLTVAEHILfyAQLKGRSWEEAQL 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 425 VLGSFLFTGDDSHK---PAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGA--VVLVSHDE 499
Cdd:TIGR01257 1041 EMEAMLEDTGLHHKrneEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGrtIIMSTHHM 1120
|
170
....*....|....*..
gi 1552103373 500 GAVEALNpERVLIMPEG 516
Cdd:TIGR01257 1121 DEADLLG-DRIAIISQG 1136
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-229 |
6.82e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-----------------EIGYLPQDPRSgdpdEL 79
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFPEA----QL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARTRILDARGLGQLVLGMQEStiamssSDASVSAAGMKKYGtltdrflalggyaaeaeaasiasnlnLPDRILEQPLKTL 159
Cdd:PRK13641 99 FENTVLKDVEFGPKNFGFSED------EAKEKALKWLKKVG--------------------------LSEDLISKSPFEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY-RGG--FIVISHDIELVGETVNRVFYLD 229
Cdd:PRK13641 147 SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGhtVILVTHNMDDVAEYADDVLVLE 219
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
149-218 |
6.95e-11 |
|
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: 61.85 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 149 DRILEQPLKTLSGGQRR------RIELARILFSDASTLILDEPTNHLDADSVVW-LREFLKNYRGGF----IVISHDIEL 217
Cdd:cd03240 106 NWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKnfqlIVITHDEEL 185
|
.
gi 1552103373 218 V 218
Cdd:cd03240 186 V 186
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-235 |
7.82e-11 |
|
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: 62.30 E-value: 7.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG------QDITGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRildaRGLG---Q-------------LVLGMQEstiamsssdasvsaagmkkYGTLTDRFLAlggyaaeaeaasiasn 144
Cdd:COG1127 79 ELR----RRIGmlfQggalfdsltvfenVAFPLRE-------------------HTDLSEAEIR---------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 lnlpDRILEQpLKT-------------LSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVVWL-REFLKNYRGG 207
Cdd:COG1127 120 ----ELVLEK-LELvglpgaadkmpseLSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELiRELRDELGLT 194
|
250 260
....*....|....*....|....*...
gi 1552103373 208 FIVISHDIELVGETVNRVFYLdANRQVI 235
Cdd:COG1127 195 SVVVTHDLDSAFAIADRVAVL-ADGKII 221
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-235 |
8.80e-11 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 61.79 E-value: 8.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 22 FRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--------EIGYLPQDprsgdpDELARTRILDARglgQL 93
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGaspgkgwrHIGYVPQR------HEFAWDFPISVA---HT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 VLGMQESTIamsssdasvsaaGMKKYGTLTDrFLALGGYAAEAEAAsiasnlNLPDRileqPLKTLSGGQRRRIELARIL 173
Cdd:TIGR03771 72 VMSGRTGHI------------GWLRRPCVAD-FAAVRDALRRVGLT------ELADR----PVGELSGGQRQRVLVARAL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 174 FSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLdaNRQVI 235
Cdd:TIGR03771 129 ATRPSVLLLDEPFTGLDMPTQELLTELFIELAGagtAILMTTHDLAQAMATCDRVVLL--NGRVI 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-228 |
8.83e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.72 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigylpqdprsgdpdeLA 80
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV--------------------LW 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDARGLGQLVLGMQESTIAMSSSdasvsaagMKKYGTLTDRFLALG----GYAAEAEAASIASNLNLPD--RILEQ 154
Cdd:PRK13638 61 QGKPLDYSKRGLLALRQQVATVFQDPE--------QQIFYTDIDSDIAFSlrnlGVPEAEITRRVDEALTLVDaqHFRHQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 155 PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVI-SHDIELVGETVNRVFYL 228
Cdd:PRK13638 133 PIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIsSHDIDLIYEISDAVYVL 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-236 |
9.01e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigYLPQDPRsgdpdeLARTRILDARGLG 91
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV--PVPARAR------LARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 QLVLGMqestiamsssdasvsaagmkkygTLTDRFLALGGYAAEAEAASIASNLNLPD-----RILEQPLKTLSGGQRRR 166
Cdd:PRK13536 124 NLDLEF-----------------------TVRENLLVFGRYFGMSTREIEAVIPSLLEfarleSKADARVSDLSGGMKRR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 167 IELARILFSDASTLILDEPTNHLD--ADSVVW--LREFLKnyRGGFIVI-SHDIELVGETVNRVFYLDANRQVID 236
Cdd:PRK13536 181 LTLARALINDPQLLILDEPTTGLDphARHLIWerLRSLLA--RGKTILLtTHFMEEAERLCDRLCVLEAGRKIAE 253
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
326-497 |
9.15e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.84 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTA-----VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGL------------ 388
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 ---RIGYYAQEHETIDVKRSVLENMV------SASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVS 459
Cdd:PRK13649 83 irkKVGLVFQFPESQLFEETVLKDVAfgpqnfGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1552103373 460 GANVLLLDEPTNNLDPASREEILDALA--HYEG-AVVLVSH 497
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKklHQSGmTIVLVTH 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
328-498 |
9.34e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGS-----LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEaghglrigyYAQEHETIDv 402
Cdd:PRK13651 5 VKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE---------WIFKDEKNK- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRSVLENMVSASPNLTET---------EARRVLG------------------------SFLFTGDDSHKPA-------GV 442
Cdd:PRK13651 75 KKTKEKEKVLEKLVIQKTrfkkikkikEIRRRVGvvfqfaeyqlfeqtiekdiifgpvSMGVSKEEAKKRAakyielvGL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 443 -----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA--HYEG-AVVLVSHD 498
Cdd:PRK13651 155 desylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDnlNKQGkTIILVTHD 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
344-516 |
1.00e-10 |
|
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: 61.86 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA-GHGLR----------IGYYAQEheTIDVKRSVLENMVS 412
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVRdytlaslrrqIGLVSQD--VFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 413 ASPNLTETEARRV-----LGSFLFTGDDS-HKPAGV----LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:cd03251 99 GRPGATREEVEEAaraanAHEFIMELPEGyDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQ 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1552103373 483 DALAH-YEGAVVLV-SHDEGAVEalNPERVLIMPEG 516
Cdd:cd03251 179 AALERlMKNRTTFViAHRLSTIE--NADRIVVLEDG 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-190 |
1.25e-10 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 62.00 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELR-VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDEL 79
Cdd:COG3638 2 MLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDG------QDVTALRGRAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 --ARTRI-----------------------LDARGLGQLVLGMQestiamsssdasvsaagmkkygTLTDRFLALggyaa 134
Cdd:COG3638 76 rrLRRRIgmifqqfnlvprlsvltnvlagrLGRTSTWRSLLGLF----------------------PPEDRERAL----- 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 135 eaeaaSIASNLNLPDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:COG3638 129 -----EALERVGLADK-AYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-498 |
1.34e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.98 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGhglRIGYYAQE--HETIDVK 403
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEG---RVEFFNQNiyERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 RSVLE-NMVSASPNL-------------------TETEARRVLGSFLFTGD-------DSHKPAGVLSGGEKTRLALAMI 456
Cdd:PRK14258 85 RLRRQvSMVHPKPNLfpmsvydnvaygvkivgwrPKLEIDDIVESALKDADlwdeikhKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 457 VVSGANVLLLDEPTNNLDPASREEIlDALAH-----YEGAVVLVSHD 498
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKV-ESLIQslrlrSELTMVIVSHN 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
332-516 |
1.42e-10 |
|
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: 60.74 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 332 SKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVieAGHGLRIGY-YAQEHETidVKRSVLenM 410
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV--EGDIHYNGIpYKEFAEK--YPGEII--Y 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 411 VSAS----PNLTETE----ARRVLGSFLFTGddshkpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:cd03233 88 VSEEdvhfPTLTVREtldfALRCKGNEFVRG---------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 483 DAL---AHYEGAVVLVSHDEGAVEALNP-ERVLIMPEG 516
Cdd:cd03233 159 KCIrtmADVLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
326-498 |
1.52e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.95 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL---RIGYYA--QEHET 399
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGaVLWQGKPLdysKRGLLAlrQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 I--DVKRSVL-----ENMVSASPNLTETE---ARRVLGSFLFTGDDS--HKPAGVLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:PRK13638 82 VfqDPEQQIFytdidSDIAFSLRNLGVPEaeiTRRVDEALTLVDAQHfrHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 468 EPTNNLDPASREE---ILDALAHYEGAVVLVSHD 498
Cdd:PRK13638 162 EPTAGLDPAGRTQmiaIIRRIVAQGNHVIISSHD 195
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-235 |
1.79e-10 |
|
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: 60.98 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELAR 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG------EDISGLSEAELYR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRI-----------LDARGLGQLV-------LGMQESTIAMSSSdasvsaagMKkygtltdrfLALGGyaaeaeaasias 143
Cdd:cd03261 75 LRRrmgmlfqsgalFDSLTVFENVafplrehTRLSEEEIREIVL--------EK---------LEAVG------------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 144 nlnLPDRILEQPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVVWL-REFLKNYRGGFIVISHDIELVG 219
Cdd:cd03261 126 ---LRGAEDLYPAE-LSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLiRSLKKELGLTSIMVTHDLDTAF 201
|
250
....*....|....*.
gi 1552103373 220 ETVNRVFYLdANRQVI 235
Cdd:cd03261 202 AIADRIAVL-YDGKIV 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
344-517 |
1.79e-10 |
|
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: 60.56 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLR-ILGGVDQPDtGVIEagHGLRIGYYAQE----HETIdvkrsvLENMVSASPnLT 418
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLS-GSVS--VPGSIAYVSQEpwiqNGTI------RENILFGKP-FD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 419 ETEARRVLGSFLFTGDDSHKPAG----------VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILD----- 483
Cdd:cd03250 94 EERYEKVIKACALEPDLEILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncilg 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 484 ALAHyEGAVVLVSHdegAVEALNP-ERVLIMPEGT 517
Cdd:cd03250 174 LLLN-NKTRILVTH---QLQLLPHaDQIVVLDNGR 204
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-190 |
1.96e-10 |
|
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: 63.61 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVG-ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI----------DRG---GEIGYL 67
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdiDRHtlrQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDPRsgdpdelartrILDARGLGQLVLGMQEstiamsssdasvsaagmkkyGTLTDRFLALGGYAAEAEAASiasnlNL 147
Cdd:TIGR01193 554 PQEPY-----------IFSGSILENLLLGAKE--------------------NVSQDEIWAACEIAEIKDDIE-----NM 597
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 148 P---DRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:TIGR01193 598 PlgyQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-213 |
2.41e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKgtidrgGEIGYLPQdprSGDPDELA 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEK------GEILFERQ---SIKKDLCT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRildarglgQLVLGMQEStiamsssdasvsaaGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRILEQPLKTLS 160
Cdd:PRK13540 72 YQK--------QLCFVGHRS--------------GINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLS 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR---GGFIVISH 213
Cdd:PRK13540 130 SGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSH 185
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
329-517 |
3.44e-10 |
|
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: 59.46 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVdqPDTGVIEAghglrigyyaqeheTIDVKRSVLE 408
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEG--------------EILFKGEDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NMvsaspnltETEARRVLGSFLftgdDSHKPA---GV------------LSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:cd03217 68 DL--------PPEERARLGIFL----AFQYPPeipGVknadflryvnegFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 474 DPASREEILDALAHYEG---AVVLVSHDEGAVEALNPERVLIMPEGT 517
Cdd:cd03217 136 DIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHVLYDGR 182
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
317-497 |
3.57e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 60.44 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 317 TPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLR------------------ILGGVD--Q 376
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgarvegeiLLDGEDiyD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 377 PDTGVIEaghgLR--IGYYAQehetidvK-----RSVLENmVSASPNLTETEARRVL---------GSFLF--TGDDSHK 438
Cdd:COG1117 83 PDVDVVE----LRrrVGMVFQ-------KpnpfpKSIYDN-VAYGLRLHGIKSKSELdeiveeslrKAALWdeVKDRLKK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 439 PAGVLSGGEKTRL----ALAMivvsGANVLLLDEPTNNLDPASR---EEILDALA-HYegAVVLVSH 497
Cdd:COG1117 151 SALGLSGGQQQRLciarALAV----EPEVLLMDEPTSALDPISTakiEELILELKkDY--TIVIVTH 211
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-234 |
3.71e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 5 HDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgDPDELARTRI 84
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGE-----------PLAKLNRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 85 LDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRflalggyAAEAEAASIASNLNLPDRILEQPLKTLSGGQR 164
Cdd:PRK10419 85 KAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKA-------ERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 165 RRIELARILFSDASTLILDEPTNHLD---ADSVVWLREFLKNYRG-GFIVISHDIELVGETVNRVFYLDANRQV 234
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQQQFGtACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
292-517 |
3.80e-10 |
|
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: 62.46 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 292 ARAEKMLSGLEEvravdRVAKLRFPTPmacgRTPLHAENLSKSY--GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLR 369
Cdd:COG4618 306 RRLNELLAAVPA-----EPERMPLPRP----KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLAR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 370 ILGGVDQPDTGVI-----------EAGHGLRIGYYAQEHETIDvkRSVLEN---MVSASPNLTETEARRVlgsflftgdD 435
Cdd:COG4618 377 LLVGVWPPTAGSVrldgadlsqwdREELGRHIGYLPQDVELFD--GTIAENiarFGDADPEKVVAAAKLA---------G 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 436 SHK-----PAG----------VLSGGEKTRLALA-------MIVVsganvllLDEPTNNLDPASREEILDALAH--YEGA 491
Cdd:COG4618 446 VHEmilrlPDGydtrigeggaRLSGGQRQRIGLAralygdpRLVV-------LDEPNSNLDDEGEAALAAAIRAlkARGA 518
|
250 260
....*....|....*....|....*..
gi 1552103373 492 -VVLVSHDEGAVEALNpeRVLIMPEGT 517
Cdd:COG4618 519 tVVVITHRPSLLAAVD--KLLVLRDGR 543
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
326-516 |
3.98e-10 |
|
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: 60.59 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSY---------GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL----RIG 391
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfRGQDLyqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 YYAQEHE----------TIDVKRSV-------LENMVSASPNLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALA 454
Cdd:TIGR02769 83 RRAFRRDvqlvfqdspsAVNPRMTVrqiigepLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 455 MIVVSGANVLLLDEPTNNLD---PASREEILDALAHYEG-AVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDmvlQAVILELLRKLQQAFGtAYLFITHDLRLVQSFC-QRVAVMDKG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
4.34e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.41 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD------KPISMLSSRQLA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildarglgQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRfLALGGYAAEAEAASIASNLNLPDRileqPLKTLS 160
Cdd:PRK11231 76 R----------RLALLPQHHLTPEGITVRELVAYGRSPWLSLWGR-LSAEDNARVNQAMEQTRINHLADR----RLTDLS 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDadsvvwlreflknyrggfivISHDIELVG 219
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLD--------------------INHQVELMR 179
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
329-516 |
4.52e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 60.79 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLEIF-----TAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEHETIDVK 403
Cdd:PRK13645 10 DNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 RSV---------------LENMVSASP-NLTET--EARRVLGSFL----FTGDDSHKPAGVLSGGEKTRLALAMIVVSGA 461
Cdd:PRK13645 90 KEIglvfqfpeyqlfqetIEKDIAFGPvNLGENkqEAYKKVPELLklvqLPEDYVKRSPFELSGGQKRRVALAGIIAMDG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEALNPErVLIMPEG 516
Cdd:PRK13645 170 NTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADE-VIVMHEG 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
347-498 |
4.82e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 4.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 347 AIDRGSKVVILGLNGAGKTTLLRILGGV----------DQPDTGVIEAGHGLRIGYYAQEhetidvkRSVLENM------ 410
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLlpgsgsiqfaGQPLEAWSAAELARHRAYLSQQ-------QTPPFAMpvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 411 ---VSASPNLTETEAR-RVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVV-------SGANVLLLDEPTNNLDPASR- 478
Cdd:PRK03695 91 tlhQPDKTRTEAVASAlNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQa 170
|
170 180
....*....|....*....|..
gi 1552103373 479 --EEILDALAHYEGAVVLVSHD 498
Cdd:PRK03695 171 alDRLLSELCQQGIAVVMSSHD 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-213 |
6.45e-10 |
|
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: 59.55 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGYLPQDPRsgdpdeLARTRIL 85
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTF------LFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 86 DarglgQLVLGMQEST---IAMSSSDASVSAAGMKkygtLTDrflalgGYaaeaeaasiasnlnlpDRILEQPLKTLSGG 162
Cdd:cd03254 95 E-----NIRLGRPNATdeeVIEAAKEAGAHDFIMK----LPN------GY----------------DTVLGENGGNLSQG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG--FIVISH 213
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
344-516 |
6.64e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 60.13 E-value: 6.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL----------RIGYYAQEHETIDVKRSV------ 406
Cdd:PRK13650 26 VSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGqIIIDGDLLteenvwdirhKIGMVFQNPDNQFVGATVeddvaf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 -LENMVSASPNLTE--TEARRVLGSFLFTgddSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILD 483
Cdd:PRK13650 106 gLENKGIPHEEMKErvNEALELVGMQDFK---EREPAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1552103373 484 ALA----HYEGAVVLVSHDEGAVeALNpERVLIMPEG 516
Cdd:PRK13650 182 TIKgirdDYQMTVISITHDLDEV-ALS-DRVLVMKNG 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
329-516 |
6.94e-10 |
|
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: 59.42 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYG--SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL----------RIGYYAQ 395
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrVLVDGHDLaladpawlrrQVGVVLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDvkRSVLENMVSASPNLTE---TEARRVLGSFLFTgddSHKPAGV----------LSGGEKTRLALAMIVVSGAN 462
Cdd:cd03252 84 ENVLFN--RSIRDNIALADPGMSMervIEAAKLAGAHDFI---SELPEGYdtivgeqgagLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 463 VLLLDEPTNNLDPASREEIL----DALAHYegAVVLVSHDEGAVEalNPERVLIMPEG 516
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMrnmhDICAGR--TVIIIAHRLSTVK--NADRIIVMEKG 212
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
326-516 |
7.86e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.55 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE---AGHGLRIGYYAQEHETIDV 402
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmRDGQLRDLYALSEAERRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 KRS----VLEN------M-VSASPNLTET----------EARRVLGSFLFTG-------DDshkPAGVLSGGEKTRLALA 454
Cdd:PRK11701 87 LRTewgfVHQHprdglrMqVSAGGNIGERlmavgarhygDIRATAGDWLERVeidaariDD---LPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEgAVEALNPERVLIMPEG 516
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrglvRELGLAVVIVTHDL-AVARLLAHRLLVMKQG 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-190 |
1.05e-09 |
|
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: 61.46 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 16 LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPrsgdpdelartrildarglgQLVL 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTS--------------------WIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 96 GMQESTIAmsssdasvsaagmkkYGTLTDRFLalggYAAEAEAASIASNLN-LPDR---ILEQPLKTLSGGQRRRIELAR 171
Cdd:TIGR01271 501 GTIKDNII---------------FGLSYDEYR----YTSVIKACQLEEDIAlFPEKdktVLGEGGITLSGGQRARISLAR 561
|
170
....*....|....*....
gi 1552103373 172 ILFSDASTLILDEPTNHLD 190
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLD 580
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
1.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggEIGYLPQDPRS--------GDPDELARTR---IL 85
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI----EWIFKDEKNKKktkekekvLEKLVIQKTRfkkIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 86 DARGLGQLV--------LGMQESTIAMSSSDasvsaaGMKKYGT-------LTDRFLALGGyaaeaeaasiasnlnLPDR 150
Cdd:PRK13651 99 KIKEIRRRVgvvfqfaeYQLFEQTIEKDIIF------GPVSMGVskeeakkRAAKYIELVG---------------LDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 151 ILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKN-YRGG--FIVISHDIELVGETVNRVFY 227
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGktIILVTHDLDNVLEWTKRTIF 237
|
....*....
gi 1552103373 228 LDANRQVID 236
Cdd:PRK13651 238 FKDGKIIKD 246
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-186 |
1.69e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylPQDPRSgdPdelartriLDARGLG-----Q- 92
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK----PVRIRS--P--------RDAIALGigmvhQh 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 ------------LVLGMQEStiamsssdasvsAAGMKKYGTLTDRFLALGG-YaaeaeaasiasNLNL-PDRILEQplkt 158
Cdd:COG3845 89 fmlvpnltvaenIVLGLEPT------------KGGRLDRKAARARIRELSErY-----------GLDVdPDAKVED---- 141
|
170 180
....*....|....*....|....*...
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:COG3845 142 LSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-232 |
1.90e-09 |
|
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: 57.76 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 4 VHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG------------EIGYLPQDP 71
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 rSGDPDELARTRI-LDARGLGqlvLGMQESTiamsssdasvsaagmKKYGTLTDrFLALGGYAaeaeaasiasnlnlpDR 150
Cdd:cd03265 83 -SVDDELTGWENLyIHARLYG---VPGAERR---------------ERIDELLD-FVGLLEAA---------------DR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 151 IleqpLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD--ADSVVW--LREFLKNYRGGFIVISHDIELVGETVNRVF 226
Cdd:cd03265 128 L----VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDpqTRAHVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVA 203
|
....*.
gi 1552103373 227 YLDANR 232
Cdd:cd03265 204 IIDHGR 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
329-485 |
1.90e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 59.32 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLE-IFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE---------AGHGLR-----I 390
Cdd:COG1135 5 ENLSKTFPTKGgPVTAlddVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLvdgvdltalSERELRaarrkI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQeH----ETidvkRSVLENMvsASP----NLTETEARRVLGSFL-FTG--DDSHK-PAGvLSGGEKTRLALAMIVV 458
Cdd:COG1135 85 GMIFQ-HfnllSS----RTVAENV--ALPleiaGVPKAEIRKRVAELLeLVGlsDKADAyPSQ-LSGGQKQRVGIARALA 156
|
170 180
....*....|....*....|....*..
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLL 183
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-232 |
2.08e-09 |
|
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: 57.89 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRV--GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGY 66
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVdiskiglhdlrsrISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDP-------RSG-DP----DELARTRILDARGLGQLVLGMQestiamsssdasvsaagmkkyGTLTDRfLALGGyaa 134
Cdd:cd03244 83 IPQDPvlfsgtiRSNlDPfgeySDEELWQALERVGLKEFVESLP---------------------GGLDTV-VEEGG--- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 135 eaeaasiasnlnlpdrileqplKTLSGGQRRRIELARILFSDASTLILDEPTNHLD--ADSVVW--LREFLKNYRggFIV 210
Cdd:cd03244 138 ----------------------ENLSVGQRQLLCLARALLRKSKILVLDEATASVDpeTDALIQktIREAFKDCT--VLT 193
|
250 260
....*....|....*....|....*
gi 1552103373 211 ISHDIelvgETV---NRVFYLDANR 232
Cdd:cd03244 194 IAHRL----DTIidsDRILVLDKGR 214
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
12-234 |
2.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.66 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDPrsgdPDE 78
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfVGLVFQNP----DDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LARTRILDARGLGQLVLGMQESTIAMSssdasvsaagmkkygtlTDRFLALGGYAaeaeaasiasnlNLPDRILEQplkt 158
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHR-----------------VSSALHMLGLE------------ELRDRVPHH---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYrgGFIVI--SHDIELVGETVNRVFYLDANR 232
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETY--GMTVIfsTHQLDLVPEMADYIYVMDKGR 215
|
..
gi 1552103373 233 QV 234
Cdd:PRK13652 216 IV 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-190 |
2.11e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI---DRGGEI------------- 64
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrMRDGQLrdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 65 ------GYLPQDPRSGdpdelARTRILDARGLGQLVLGMqestiamsssdasvsaaGMKKYGTLTDRFLA-LGGYAAEae 137
Cdd:PRK11701 86 llrtewGFVHQHPRDG-----LRMQVSAGGNIGERLMAV-----------------GARHYGDIRATAGDwLERVEID-- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 138 aasiasnlnlPDRILEQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK11701 142 ----------AARIDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
19-228 |
2.20e-09 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 57.75 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdliaskgtIDR--GGEIGYLPQDPRSGDPDELARTR---I--------- 84
Cdd:COG1136 26 GVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--------LDRptSGEVLIDGQDISSLSERELARLRrrhIgfvfqffnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 85 ---LDAR---GLGQLVLGMQESTIAmsssdasvsaagmKKYGTLTDRflalggyaaeaeaasiasnLNLPDRILEQPlKT 158
Cdd:COG1136 98 lpeLTALenvALPLLLAGVSRKERR-------------ERARELLER-------------------VGLGDRLDHRP-SQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADS--VVW--LREFLKNYRGGFIVISHDIELVgETVNRVFYL 228
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeEVLelLRELNRELGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-191 |
2.29e-09 |
|
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: 57.83 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVG---ARL-LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDP 76
Cdd:COG4181 8 IIELRGLTKTVGtgaGELtILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG------QDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 77 DELARTRildARGLG------QLVlgmqestiamsssdasvsaagmkkyGTLTdrflALggyaaeaeaasiaSNLNLP-- 148
Cdd:COG4181 82 DARARLR---ARHVGfvfqsfQLL-------------------------PTLT----AL-------------ENVMLPle 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 149 -----------DRILEQ----------PlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDA 191
Cdd:COG4181 117 lagrrdararaRALLERvglghrldhyP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-225 |
3.09e-09 |
|
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: 57.35 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLmENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-----------IGYLPQD 70
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 71 ----PRSGDPDELA---RTRILDARGLGQLVLGMQEStiamsssdasvsaagmkkygtltdrflalggyaaeaeaasias 143
Cdd:cd03299 80 yalfPHMTVYKNIAyglKKRKVDKKEIERKVLEIAEM------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 144 nLNLpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK----NYRGGFIVISHDIELVG 219
Cdd:cd03299 117 -LGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAW 194
|
....*.
gi 1552103373 220 ETVNRV 225
Cdd:cd03299 195 ALADKV 200
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-239 |
3.33e-09 |
|
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: 57.35 E-value: 3.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 4 VHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-----------IGYLPQD-- 70
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 71 ------------------PRSGDPDELA-RTRILDARGLGQLVlgmqestiamsssdasvsaagmkkygtltdrflalgg 131
Cdd:cd03296 85 lfrhmtvfdnvafglrvkPRSERPPEAEiRAKVHELLKLVQLD------------------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 132 yaaeaeaasiasnlNLPDRILEQplktLSGGQRRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGG 207
Cdd:cd03296 128 --------------WLADRYPAQ----LSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVT 189
|
250 260 270
....*....|....*....|....*....|....*..
gi 1552103373 208 FIVISHDIELVGETVNRVFYLDANR--QV---IDVYN 239
Cdd:cd03296 190 TVFVTHDQEEALEVADRVVVMNKGRieQVgtpDEVYD 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-236 |
3.91e-09 |
|
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: 57.19 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE----------------IGYLPQDPRSgdPDEL-A 80
Cdd:cd03256 18 KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkalrqlrrqIGMIFQQFNL--IERLsV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDARgLGQLvlgmqeSTIamsssdasvsaAGMKKYGTLTDRFLALggyaaeaeaaSIASNLNLPDRILeQPLKTLS 160
Cdd:cd03256 96 LENVLSGR-LGRR------STW-----------RSLFGLFPKEEKQRAL----------AALERVGLLDKAY-QRADQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK---NYRGGFIVIS-HDIELVGETVNRVFYLDANRQVID 236
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinREEGITVIVSlHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-193 |
3.95e-09 |
|
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: 56.65 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARL--LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGY 66
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDPrsgdpdelartrildarglgQLVLGMQESTiamsssdasvsaagMKKYGTLTDR--FLALggyaaeaeaasiasn 144
Cdd:cd03369 87 IPQDP--------------------TLFSGTIRSN--------------LDPFDEYSDEeiYGAL--------------- 117
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 145 lnlpdRILEQPLkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS 193
Cdd:cd03369 118 -----RVSEGGL-NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-497 |
4.17e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 57.54 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIG--YYAQEHETIDVK 403
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGrnIYSPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 404 RSV------------------------LENMVSASPNLTETEARRVLGSFLF--TGDDSHKPAGVLSGGEKTRLALAMIV 457
Cdd:PRK14267 85 REVgmvfqypnpfphltiydnvaigvkLNGLVKSKKELDERVEWALKKAALWdeVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 458 VSGANVLLLDEPTNNLDPASR---EEILDALAHyEGAVVLVSH 497
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTakiEELLFELKK-EYTIVLVTH 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
356-496 |
5.20e-09 |
|
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: 56.51 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 356 ILGLNGAGKTTLLRILGGVDQPD---TGVI-----EAGHGL---RIGYYAQE---HETIDVKRSVLENMVSASPNLTETE 421
Cdd:cd03234 38 ILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqPRKPDQfqkCVAYVRQDdilLPGLTVRETLTYTAILRLPRKSSDA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 422 ARRVLGSFLFTGDDSHKPAG-----VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY--EGAVVL 494
Cdd:cd03234 118 IRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarRNRIVI 197
|
..
gi 1552103373 495 VS 496
Cdd:cd03234 198 LT 199
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
316-498 |
5.63e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 57.10 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 316 PTPMACGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVD------QPDTGVIEAGHGLr 389
Cdd:PRK14243 1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgfRVEGKVTFHGKNL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 390 igyYAQEHETIDVKRSVleNMVSASPN-----LTETEA--RRVLGsflFTGD-------------------DSHKPAGV- 442
Cdd:PRK14243 80 ---YAPDVDPVEVRRRI--GMVFQKPNpfpksIYDNIAygARING---YKGDmdelverslrqaalwdevkDKLKQSGLs 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR---EEILDALAHyEGAVVLVSHD 498
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTlriEELMHELKE-QYTIIIVTHN 209
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
347-517 |
6.28e-09 |
|
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: 58.87 E-value: 6.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 347 AIDR-------GSKVVILGLNGAGKTTLLRILGGvdqpDTGVIE-----AGHGL---------RIGYYAQeHETIDVKRS 405
Cdd:TIGR01257 1954 AVDRlcvgvrpGECFGLLGVNGAGKTTTFKMLTG----DTTVTSgdatvAGKSIltnisdvhqNMGYCPQ-FDAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 406 VLENMV--SASPNLTETEARRV-------LGSFLFtgddSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPA 476
Cdd:TIGR01257 2029 GREHLYlyARLRGVPAEEIEKVanwsiqsLGLSLY----ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1552103373 477 SREEILD---ALAHYEGAVVLVSHDEGAVEALNpERVLIMPEGT 517
Cdd:TIGR01257 2105 ARRMLWNtivSIIREGRAVVLTSHSMEECEALC-TRLAIMVKGA 2147
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-516 |
6.48e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdlIASKGTIDrgGEIGYlpqdprSGDPDELARTRILDARGLG----Q 92
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG--VYPHGTYE--GEIIF------EGEELQASNIRDTERAGIAiihqE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 LVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeaasiASNLNLpDRILEQPLKTLSGGQRRRIELARI 172
Cdd:PRK13549 91 LALVKELSVLENIFLGNEITPGGIMDYDAMYLRAQKL------------LAQLKL-DINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 173 LFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVfyldanrQVIdvynmnwknyqrqr 249
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHKLNEVKAISDTI-------CVI-------------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 250 aadeerRKKERANVEKKAGALQLQAARfgakaskaaaahQMVARaekmlsgleEVRAvdrvaklRFPT-PMACGRTPLHA 328
Cdd:PRK13549 217 ------RDGRHIGTRPAAGMTEDDIIT------------MMVGR---------ELTA-------LYPRePHTIGEVILEV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLS---KSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQpdtGVIEA-----GHGLRIGYYAQEHE-- 398
Cdd:PRK13549 263 RNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRWEGeifidGKPVKIRNPQQAIAqg 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 399 ----TIDVKR-------SVLENMVSAspnltetearrVLGSFLFTG--DDSHK--------------------PAGVLSG 445
Cdd:PRK13549 340 iamvPEDRKRdgivpvmGVGKNITLA-----------ALDRFTGGSriDDAAElktilesiqrlkvktaspelAIARLSG 408
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 446 GEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK13549 409 GNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIyklINQLVQQGVAIIVISSELPEVLGLS-DRVLVMHEG 481
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
290-516 |
7.59e-09 |
|
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: 58.19 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 290 MVARAEKMLSGLEEVRAVDrvaKLRFPTPMACGRtpLHAENLSKSYGSLEI--FTAVDLAIDRGSKVVILGLNGAGKTTL 367
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPEKD---TGTRAIERARGD--VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTL 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 368 LRILGGVDQPDTGVIeaghgLRIGYYAQEHETIDVKR--------------SVLENMVSASP-NLTETEARRVLG----- 427
Cdd:TIGR02203 375 VNLIPRFYEPDSGQI-----LLDGHDLADYTLASLRRqvalvsqdvvlfndTIANNIAYGRTeQADRAEIERALAaayaq 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 428 SFLFTGDDS-HKPAGV----LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH-YEGAVVLV-SHDEG 500
Cdd:TIGR02203 450 DFVDKLPLGlDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERlMQGRTTLViAHRLS 529
|
250
....*....|....*.
gi 1552103373 501 AVEalNPERVLIMPEG 516
Cdd:TIGR02203 530 TIE--KADRIVVMDDG 543
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-234 |
7.95e-09 |
|
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: 56.09 E-value: 7.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 13 ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG--DLIASKGTID----RG-------GEIGYLPQDP-------- 71
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfyDVDSGRILIDghdvRDytlaslrRQIGLVSQDVflfndtva 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 ---RSGDPDElARTRILDAR---GLGQLVLGMQEstiamsssdasvsaagmkkygtltdrflalgGYaaeaeaasiasnl 145
Cdd:cd03251 94 eniAYGRPGA-TREEVEEAAraaNAHEFIMELPE-------------------------------GY------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 146 nlpDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS--VVW--LREFLKNyRGGFiVISHDIELVgET 221
Cdd:cd03251 129 ---DTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESerLVQaaLERLMKN-RTTF-VIAHRLSTI-EN 202
|
250
....*....|...
gi 1552103373 222 VNRVFYLDANRQV 234
Cdd:cd03251 203 ADRIVVLEDGKIV 215
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
17-236 |
8.00e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 56.92 E-value: 8.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigyLPQDPRSGDPDELArtrilDARGLGQLVLG 96
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV--------LVSGIDTGDFSKLQ-----GIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 MQESTIAmsssdasvsaagmkkyGTLTDRFLALGgyaaeaeaasiASNLNLP--------DRILEQ---------PLKTL 159
Cdd:PRK13644 85 NPETQFV----------------GRTVEEDLAFG-----------PENLCLPpieirkrvDRALAEiglekyrhrSPKTL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADS-VVWLREFLKNYRGG--FIVISHDIELVgETVNRVFYLDANRQVID 236
Cdd:PRK13644 138 SGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGktIVYITHNLEEL-HDADRIIVMDRGKIVLE 216
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-218 |
8.20e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 7 LELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdliASKGTIDRG-GEIGYLPQD---------PRSGDP 76
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---ALKGTPVAGcVDVPDNQFGreaslidaiGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 77 DelARTRILDARGLGQLVLgmqestiamsssdasvsaagmkkygtltdrFLAlggyaaeaeaasiasnlnlpdrileqPL 156
Cdd:COG2401 113 K--DAVELLNAVGLSDAVL------------------------------WLR--------------------------RF 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS--VVW--LREFLKNYRGGFIVISHDIELV 218
Cdd:COG2401 135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakRVArnLQKLARRAGITLVVATHHYDVI 200
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
326-485 |
9.04e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 56.32 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQ--PD---TG-VIEAGHGLrigyYAQEHET 399
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGsIVYNGHNI----YSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 400 IDVKRSVleNMVSASPN------------------------LTETEARRVLGSFLF--TGDDSHKPAGVLSGGEKTRLAL 453
Cdd:PRK14239 82 VDLRKEI--GMVFQQPNpfpmsiyenvvyglrlkgikdkqvLDEAVEKSLKGASIWdeVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190
....*....|....*....|....*....|..
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-215 |
9.24e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.06 E-value: 9.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPQDPRsgdpdelARtrildaRGLGQ 92
Cdd:PRK10895 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdISLLPLHAR-------AR------RGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 93 LVlgmQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPdrileqplKTLSGGQRRRIELARI 172
Cdd:PRK10895 83 LP---QEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG--------QSLSGGERRRVEIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1552103373 173 LFSDASTLILDEPTNHLDADSVVWLR---EFLKNYRGGFIVISHDI 215
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDIKriiEHLRDSGLGVLITDHNV 197
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
329-485 |
1.06e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG---------HGLR--IGYYAQE 396
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvtrASLRrnIAVVFQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 397 HETIDvkRSVLENMVSASPNLTETEARRVLGS-----FLFTGDDSHKP-AG----VLSGGEKTRLALAMIVVSGANVLLL 466
Cdd:PRK13657 418 AGLFN--RSIEDNIRVGRPDATDEEMRAAAERaqahdFIERKPDGYDTvVGergrQLSGGERQRLAIARALLKDPPILIL 495
|
170
....*....|....*....
gi 1552103373 467 DEPTNNLDPASREEILDAL 485
Cdd:PRK13657 496 DEATSALDVETEAKVKAAL 514
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
11-214 |
1.06e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.09 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 11 VGARLLmeNVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTIDRGGeigylpQDPRSGDPDELARTRILdargl 90
Cdd:PRK03695 8 VSTRLG--PLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAG------QPLEAWSAAELARHRAY----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 91 gqlvLGMQESTIAMsssdasvsaagMKKYgtltdRFLALGGYAAEAEAASIAS------NLNLPDRiLEQPLKTLSGGQR 164
Cdd:PRK03695 74 ----LSQQQTPPFA-----------MPVF-----QYLTLHQPDKTRTEAVASAlnevaeALGLDDK-LGRSVNQLSGGEW 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 165 RRIELA-------RILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVIS-HD 214
Cdd:PRK03695 133 QRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELcqQGIAVVMSsHD 192
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
329-485 |
1.46e-08 |
|
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: 55.62 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGS---LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEA-GHGLR----------IGYYA 394
Cdd:cd03249 4 KNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDvkRSVLENMVSASPNLTETEARRVLG-----SFLFT---GDDSH-KPAGV-LSGGEKTRLALAMIVVSGANVL 464
Cdd:cd03249 84 QEPVLFD--GTIAENIRYGKPDATDEEVEEAAKkanihDFIMSlpdGYDTLvGERGSqLSGGQKQRIAIARALLRNPKIL 161
|
170 180
....*....|....*....|.
gi 1552103373 465 LLDEPTNNLDPASREEILDAL 485
Cdd:cd03249 162 LLDEATSALDAESEKLVQEAL 182
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
340-499 |
1.62e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 53.90 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 340 IFTAVDLAIDRGSKVVILGLNGAGKTTLLRilggvdqpDTGVIEAGHGLRIGYYAQEHETIDVKRSVLENMvsaspnlte 419
Cdd:cd03227 10 YFVPNDVTFGEGSLTIITGPNGSGKSTILD--------AIGLALGGAQSATRRRSGVKAGCIVAAVSAELI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 420 tearrvlgsFLFTGddshkpagvLSGGEKTRLALAMIV----VSGANVLLLDEPTNNLDPASREEILDALAHY--EGAVV 493
Cdd:cd03227 73 ---------FTRLQ---------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQV 134
|
....*..
gi 1552103373 494 LV-SHDE 499
Cdd:cd03227 135 IViTHLP 141
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
329-486 |
1.67e-08 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.35 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSY-GSLEIFTA---VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGH--------GLR-----I 390
Cdd:PRK11153 5 KNISKVFpQGGRTIHAlnnVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGrVLVDGQdltalsekELRkarrqI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQeHETIDVKRSVLENMvsASP----NLTETE-ARRVLGSFLFTGDDSHK---PAGvLSGGEKTRLALAMIVVSGAN 462
Cdd:PRK11153 85 GMIFQ-HFNLLSSRTVFDNV--ALPlelaGTPKAEiKARVTELLELVGLSDKAdryPAQ-LSGGQKQRVAIARALASNPK 160
|
170 180
....*....|....*....|....
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALA 486
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLK 184
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
149-516 |
1.68e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 149 DRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVIS------HDIElvgETV 222
Cdd:PRK10938 126 TALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlvlnrfDEIP---DFV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 223 NRVFYLdANRQVIdvynmnwknyqrqraadeerRKKERANVEKKAGALQLqaarfgakaskaaaahqmvARAEKmLSGLE 302
Cdd:PRK10938 203 QFAGVL-ADCTLA--------------------ETGEREEILQQALVAQL-------------------AHSEQ-LEGVQ 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 303 EVRAVDRVAKLRFPTpmacGRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGvDQPDtgvi 382
Cdd:PRK10938 242 LPEPDEPSARHALPA----NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQ---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 383 eaGH-------GLRIGyyaqEHETI-DVKRSVleNMVSASPNL---TETEARRVLGSFLFtgdDS--------------- 436
Cdd:PRK10938 313 --GYsndltlfGRRRG----SGETIwDIKKHI--GYVSSSLHLdyrVSTSVRNVILSGFF---DSigiyqavsdrqqkla 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 437 --------------HKPAGVLSGGEKtRLAL-AMIVVSGANVLLLDEPTNNLDPASREEI---LDAL-AHYEGAVVLVSH 497
Cdd:PRK10938 382 qqwldilgidkrtaDAPFHSLSWGQQ-RLALiVRALVKHPTLLILDEPLQGLDPLNRQLVrrfVDVLiSEGETQLLFVSH 460
|
410 420
....*....|....*....|
gi 1552103373 498 -DEGAVEALNpERVLIMPEG 516
Cdd:PRK10938 461 hAEDAPACIT-HRLEFVPDG 479
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
344-497 |
1.88e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 56.78 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVdQPDTGVIEA-GHGLR----------IGYYAQE----HETIdvkrsvLE 408
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKInGIELReldpeswrkhLSWVGQNpqlpHGTL------RD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 409 NMVSASPNLTETEARRVL-----GSFLftgddSHKPAGV----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:PRK11174 442 NVLLGNPDASDEQLQQALenawvSEFL-----PLLPQGLdtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180
....*....|....*....|....*.
gi 1552103373 474 DPASREEILDALAHYEGA--VVLVSH 497
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRqtTLMVTH 542
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
145-237 |
1.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.78 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 LNLPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGGFIVISHDIELVGE 220
Cdd:PRK13645 137 VQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNKEYKKRIIMVTHNMDQVLR 216
|
90
....*....|....*..
gi 1552103373 221 TVNRVFYLDANRqVIDV 237
Cdd:PRK13645 217 IADEVIVMHEGK-VISI 232
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-186 |
2.08e-08 |
|
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: 54.84 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPqdprsgdPDELA 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEdITKLP-------PHERA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RtrildaRGLGQLVLGmQEStiamsssdasvsaagmkkYGTLTDR------FLALGGyaaeaeaasiaSNLNLPDRILEQ 154
Cdd:TIGR03410 74 R------AGIAYVPQG-REI------------------FPRLTVEenlltgLAALPR-----------RSRKIPDEIYEL 117
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 155 -P-LKT--------LSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:TIGR03410 118 fPvLKEmlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
326-498 |
2.22e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.72 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL----------RIGYYA 394
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGtLLFEGEDIstlkpeiyrqQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDvkRSVLENMV------SASPNltETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDE 468
Cdd:PRK10247 88 QTPTLFG--DTVYDNLIfpwqirNQQPD--PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 469 PTNNLDPASREEILDALAHY----EGAVVLVSHD 498
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvreqNIAVLWVTHD 197
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-234 |
2.40e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.51 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGYLPQDPrsgdPDELARTR 83
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGrevnaenekwvrsKVGLVFQDP----DDQVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ILDARGLGQLVLGMQESTIaMSSSDASVSAAGMKKYGtltdrflalggyaaeaeaasiasnlnlpdrilEQPLKTLSGGQ 163
Cdd:PRK13647 97 VWDDVAFGPVNMGLDKDEV-ERRVEEALKAVRMWDFR--------------------------------DKPPYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 164 RRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVIS-HDIELVGETVNRVFYLDANRQV 234
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDrlHNQGKTVIVAtHDVDLAAEWADQVIVLKEGRVL 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-218 |
2.68e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 7 LELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAgDLIASKGtidrggEIGYlpqdprSGDP-DELARTRIL 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALL-RLINSQG------EIWF------DGQPlHNLNRRQLL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 86 DARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTltdrflALGGYAAEAEAASIASNLNL-PDRILEQPlKTLSGGQR 164
Cdd:PRK15134 359 PVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQP------TLSAAQREQQVIAVMEEVGLdPETRHRYP-AEFSGGQR 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 165 RRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELV 218
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHDLHVV 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
330-497 |
3.00e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG--------------HGLRIGYyaQ 395
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfasttaalaAGVAIIY--Q 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDvKRSVLEN-MVSASPN--------LTETEARRVLGSFlftGD--DSHKPAGVLSGGEKTRLALAMIVVSGANVL 464
Cdd:PRK11288 87 ELHLVP-EMTVAENlYLGQLPHkggivnrrLLNYEAREQLEHL---GVdiDPDTPLKYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 465 LLDEPTNNLdpASRE-EILDALAHY---EGAVVL-VSH 497
Cdd:PRK11288 163 AFDEPTSSL--SAREiEQLFRVIRElraEGRVILyVSH 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
3.10e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 54.87 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELR----VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdPRSG-D 75
Cdd:COG4525 3 MLTVRHVSVRypggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-------PVTGpG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 76 PDE---------LARTRILDARGLGQLVLGMQESTIAMsssdasvsaagmkkygtLTDRFLALGGyaaeaeaasiasnln 146
Cdd:COG4525 76 ADRgvvfqkdalLPWLNVLDNVAFGLRLRGVPKAERRA-----------------RAEELLALVG--------------- 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 147 LPDRIlEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFL----KNYRGGFIVISHDIE 216
Cdd:COG4525 124 LADFA-RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHSVE 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
319-498 |
3.13e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 319 MACGRTPLHAENLSKSYGSLE---IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGG-VDQPDTGVIEAGHGLRIGYYA 394
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINdkaILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRlIEIYDSKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDVKRSVleNMVSASPN----------------------------LTETEARRVlGSFLFTGDDSHKPAGVLSGG 446
Cdd:PRK14246 81 FQIDAIKLRKEV--GMVFQQPNpfphlsiydniayplkshgikekreikkIVEECLRKV-GLWKEVYDRLNSPASQLSGG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 447 EKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY--EGAVVLVSHD 498
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELknEIAIVIVSHN 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-271 |
3.67e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDprSGDPDELARTRILDARGlgqLVLG 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAIS--SGLNGQLTGIENIELKG---LMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 MQESTIamsssdasvsaagmKKYGTLTDRFLALGgyaaeaeaasiasnlnlpdRILEQPLKTLSGGQRRRIELARILFSD 176
Cdd:PRK13545 115 LTKEKI--------------KEIIPEIIEFADIG-------------------KFIYQPVKTYSSGMKSRLGFAISVHIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 177 ASTLILDEP--------TNH-LDAdsvvwLREFLKNYRGGFIvISHDIELVGETVNRVFYL---------DANrQVIDVY 238
Cdd:PRK13545 162 PDILVIDEAlsvgdqtfTKKcLDK-----MNEFKEQGKTIFF-ISHSLSQVKSFCTKALWLhygqvkeygDIK-EVVDHY 234
|
250 260 270
....*....|....*....|....*....|...
gi 1552103373 239 NMNWKNYQRQRAADEERRKKERANvEKKAGALQ 271
Cdd:PRK13545 235 DEFLKKYNQMSVEERKDFREEQIS-QFQHGLLQ 266
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
346-516 |
3.84e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 55.42 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 346 LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGLRIGYYAQEHETIDVKRSVLENMVSASPNLT------ 418
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGqVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTvldnta 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 419 ----------ETEARRVLGSFLFTG--DDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL- 485
Cdd:PRK10070 129 fgmelaginaEERREKALDALRQVGleNYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELv 208
|
170 180 190
....*....|....*....|....*....|....
gi 1552103373 486 ---AHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK10070 209 klqAKHQRTIVFISHDLDEAMRIG-DRIAIMQNG 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
3.89e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 55.10 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-----------IGYLPQ 69
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 DP-----------------RSGDPDELARTRILDArgLgQLVlgmqestiamsssdasvsaaGMKKYGtltDRFlalggy 132
Cdd:COG3842 85 DYalfphltvaenvafglrMRGVPKAEIRARVAEL--L-ELV--------------------GLEGLA---DRY------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 133 aaeaeaasiasnlnlPDrileqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY---RGG-F 208
Cdd:COG3842 133 ---------------PH--------QLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLqreLGItF 189
|
....*.
gi 1552103373 209 IVISHD 214
Cdd:COG3842 190 IYVTHD 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-234 |
4.06e-08 |
|
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: 55.88 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigylpqdprSGDPDELARTRILDARGlgQLVLG 96
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI--------------LLDGHDLADYTLASLRR--QVALV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 MQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAasiasnlNLPDRiLEQPLKT----LSGGQRRRIELARI 172
Cdd:TIGR02203 412 SQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVD-------KLPLG-LDTPIGEngvlLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 173 LFSDASTLILDEPTNHLDADS----VVWLREFLKNYRGgfIVISHDIELVgETVNRVFYLDANRQV 234
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESerlvQAALERLMQGRTT--LVIAHRLSTI-EKADRIVVMDDGRIV 546
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
346-498 |
4.40e-08 |
|
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: 54.29 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 346 LAIDRGSKVV-ILGLNGAGKTTLLRILGGVDQPDTG----------VIEAGHGLRIGYYAQEHETIDVKRSVLENMVSAS 414
Cdd:cd03236 20 LPVPREGQVLgLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 415 PN---------LTETEARRVLGSFLFTGDDSH---KPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR---E 479
Cdd:cd03236 100 PKavkgkvgelLKKKDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaA 179
|
170
....*....|....*....
gi 1552103373 480 EILDALAHYEGAVVLVSHD 498
Cdd:cd03236 180 RLIRELAEDDNYVLVVEHD 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-226 |
4.45e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.23 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLP--QDPRSGdpd 77
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlRGQHIEGLPghQIARMG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 78 eLARTRildarglgQLVLGMQESTIAMSSSdasvsaagMKKYGTLTDRFLAlGGYAAEAEAASIASNLNLPDRILEQ--- 154
Cdd:PRK11300 82 -VVRTF--------QHVRLFREMTVIENLL--------VAQHQQLKTGLFS-GLLKTPAFRRAESEALDRAATWLERvgl 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 155 ------PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIV----ISHDIELVGETVNR 224
Cdd:PRK11300 144 lehanrQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVtvllIEHDMKLVMGISDR 223
|
..
gi 1552103373 225 VF 226
Cdd:PRK11300 224 IY 225
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
344-484 |
4.95e-08 |
|
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: 54.48 E-value: 4.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEagHGLRIGYYAQEHETIdvKRSVLENMVsASPNLTETEAR 423
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQFSWIM--PGTIKENII-FGVSYDEYRYK 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 424 RVLGSFLFTGDDSHKP---------AGV-LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDA 484
Cdd:cd03291 131 SVVKACQLEEDITKFPekdntvlgeGGItLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
329-498 |
6.05e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.57 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGSLeiFTAVDLA-IDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYyaqehetidvkrsvl 407
Cdd:cd03222 4 PDCVKRYGVF--FLLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 enmvsaspnltetearrvlgsflftgddshKPAGV-LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA 486
Cdd:cd03222 66 ------------------------------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170
....*....|....*.
gi 1552103373 487 HY----EGAVVLVSHD 498
Cdd:cd03222 116 RLseegKKTALVVEHD 131
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
289-486 |
6.68e-08 |
|
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: 55.21 E-value: 6.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 289 QMVARAEKMLSGLEEVRAV-DRVAklrfPTPMACGRTPLHAENLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTT 366
Cdd:COG5265 324 QALADMERMFDLLDQPPEVaDAPD----APPLVVGGGEVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKST 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 367 LLRILGGVDQPDTGVIE-AGHGLR----------IGYYAQEheTIDVKRSVLENMVSASPNLTETEARRV-----LGSFL 430
Cdd:COG5265 400 LARLLFRFYDVTSGRILiDGQDIRdvtqaslraaIGIVPQD--TVLFNDTIAYNIAYGRPDASEEEVEAAaraaqIHDFI 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 431 ftgddSHKPAGV----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA 486
Cdd:COG5265 478 -----ESLPDGYdtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-190 |
7.35e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 7.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGA-----RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLP------ 68
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPeykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 69 ------QDPRSGD-PD----E---LARTRIlDARGLGqlvlgmqestiamsssdasvsaAGMKKygTLTDRFLALggyaa 134
Cdd:COG1101 81 yigrvfQDPMMGTaPSmtieEnlaLAYRRG-KRRGLR----------------------RGLTK--KRRELFREL----- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 135 eaeaaSIASNLNLPDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:COG1101 131 -----LATLGLGLENR-LDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
159-213 |
7.36e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 55.22 E-value: 7.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADS----VVWLREFLKNYRggFIVISH 213
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQNKT--VLMITH 532
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-190 |
7.47e-08 |
|
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: 53.39 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDP--------- 71
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtldslrraIGVVPQDTvlfndtigy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 --RSGDPD-------ELARTRILDARglgqlVLGMQEstiamsssdasvsaagmkKYGTLtdrflaLGgyaaeaeaasia 142
Cdd:cd03253 94 niRYGRPDatdeeviEAAKAAQIHDK-----IMRFPD------------------GYDTI------VG------------ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1552103373 143 snlnlpdrilEQPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:cd03253 133 ----------ERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-229 |
7.78e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 53.87 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRV--GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGY 66
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDP------------------RSGDPDELARTRILDArgLGQlvLGMQEstiamsssdasvsaagmkkygtltdrfla 128
Cdd:PRK13635 86 VFQNPdnqfvgatvqddvafgleNIGVPREEMVERVDQA--LRQ--VGMED----------------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 129 lggyaaeaeaasiasnlnlpdrILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNY 204
Cdd:PRK13635 133 ----------------------FLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQK 190
|
250 260
....*....|....*....|....*
gi 1552103373 205 RGGFIVISHDIELVGETvNRVFYLD 229
Cdd:PRK13635 191 GITVLSITHDLDEAAQA-DRVIVMN 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
330-498 |
8.94e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 53.62 E-value: 8.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL----RIGYYAQEHETIDVKR 404
Cdd:PRK11831 12 GVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfDGENIpamsRSRLYTVRKRMSMLFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 S--------VLENM-------VSASPNLTETEARRVLGSFLFTGDDSHKPAGvLSGGEKTRLALAMIVVSGANVLLLDEP 469
Cdd:PRK11831 92 SgalftdmnVFDNVayplrehTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE-LSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 1552103373 470 TNNLDPASRE---EILDALAHYEGAV-VLVSHD 498
Cdd:PRK11831 171 FVGQDPITMGvlvKLISELNSALGVTcVVVSHD 203
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
14-216 |
9.43e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.46 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDPR-----SGD 75
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkeirkkIGIIFQNPDnqfigATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 76 PDELA---RTRILDARGLGQLVLGMQESTiamsssdasvsaaGMKKYgtltdrflalggyaaeaeaasiasnlnlpdriL 152
Cdd:PRK13632 102 EDDIAfglENKKVPPKKMKDIIDDLAKKV-------------GMEDY--------------------------------L 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 153 EQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG----FIVISHDIE 216
Cdd:PRK13632 137 DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTrkktLISITHDMD 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-232 |
9.76e-08 |
|
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: 52.95 E-value: 9.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTIDRGGEIGYLPQDPRSGDPDELA- 80
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR-LNDLIPGAPDEGEVLLDGKDIYDLDVDVLEl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTR--------------ILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYgtLTDRFLALGgyaaeaeaasiasnln 146
Cdd:cd03260 80 RRRvgmvfqkpnpfpgsIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDE--VKDRLHALG---------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 lpdrileqplktLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF--IVISHDIELVGETVNR 224
Cdd:cd03260 142 ------------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYtiVIVTHNMQQAARVADR 209
|
....*...
gi 1552103373 225 VFYLDANR 232
Cdd:cd03260 210 TAFLLNGR 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-213 |
1.04e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDpdela 80
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG------KTATRGD----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDArgLGQLvlgmqestiamsssdasvsaAGMKK-YGTLTD-RFL-ALGGYAAEAEAASIASNLNLPDRilEQPL- 156
Cdd:PRK13543 80 RSRFMAY--LGHL--------------------PGLKAdLSTLENlHFLcGLHGRRAKQMPGSALAIVGLAGY--EDTLv 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY---RGGFIVISH 213
Cdd:PRK13543 136 RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-516 |
1.08e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeIGYLPQDPRsgdpdelartrilDARGLGQLVLg 96
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNKLDHK-------------LAAQLGIGII- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 MQESTIAMSSSDASVSAAGMkkygTLTDRFLALGGYAAEAEAASIASNLNLPD--RILEQPLKTLSGGQRRRIELARILF 174
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGR----HLTKKVCGVNIIDWREMRVRAAMMLLRVGlkVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 175 SDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIELVGETVNRVFYLD-----ANRQVIDVYNmnwknyq 246
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKdgssvCSGMVSDVSN------- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 247 rqraaDEERRkkeranvekkagalqlqaarfgakaskaaaahQMVARAEKmlsgleevravDRVAKLRFPTPMACGRTPL 326
Cdd:PRK09700 235 -----DDIVR--------------------------------LMVGRELQ-----------NRFNAMKENVSNLAHETVF 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 327 HAENL-SKSYGSLEiftAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIgyyAQEHETIDVKR- 404
Cdd:PRK09700 267 EVRNVtSRDRKKVR---DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL-NGKDI---SPRSPLDAVKKg 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 -----------------SVLENMvSASPNLTETEARRVLGsfLFTGDDSHKPA------------------GVLSGGEKT 449
Cdd:PRK09700 340 mayitesrrdngffpnfSIAQNM-AISRSLKDGGYKGAMG--LFHEVDEQRTAenqrellalkchsvnqniTELSGGNQQ 416
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 450 RLALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIykvMRQLADDGKVILMVSSELPEIITVC-DRIAVFCEG 485
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-190 |
1.08e-07 |
|
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: 53.32 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 16 LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQdprsgdpdelartrildargLGQLVL 95
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ--------------------FSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 96 GMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeaasiasnlnlPDR---ILEQPLKTLSGGQRRRIELARI 172
Cdd:cd03291 112 GTIKENIIFGVSYDEYRYKSVVKACQLEEDITKF------------------PEKdntVLGEGGITLSGGQRARISLARA 173
|
170
....*....|....*...
gi 1552103373 173 LFSDASTLILDEPTNHLD 190
Cdd:cd03291 174 VYKDADLYLLDSPFGYLD 191
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
1.20e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.31 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE---------------IGYLPQDPrsgdPDELAR 81
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresVGMVFQDP----DNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARGLGQLVLGMQESTIAMSssdasvsaagmkkygtlTDRFLALGGYaaeaeaasiasnlnlpDRILEQPLKTLSG 161
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKR-----------------VDNALKRTGI----------------EHLKDKPTHCLSF 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISHDIELVGETVNRVFYLDANRQVID 236
Cdd:PRK13636 145 GQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgltiIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
356-504 |
1.51e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 356 ILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYYAQEHET-------IDVKRSVLENMVSASPNLTETEARRVLGS 428
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNINNIAKPYCTyighnlgLKLEMTVFENLKFWSEIYNSAETLYAAIH 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 429 FLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASReEILDAL----AHYEGAVVLVSHDEGAVEA 504
Cdd:PRK13541 110 YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR-DLLNNLivmkANSGGIVLLSSHLESSIKS 188
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
330-479 |
1.60e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 53.34 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSYGSLEIftAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-AGHGL--------------RIGYYA 394
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVlNGRVLfdaekgiclppekrRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QE-----HETidVKRSVLENMVSASP-------NLTETEArrVLGSFLFTgddshkpagvLSGGEKTRLALAMIVVSGAN 462
Cdd:PRK11144 83 QDarlfpHYK--VRGNLRYGMAKSMVaqfdkivALLGIEP--LLDRYPGS----------LSGGEKQRVAIGRALLTAPE 148
|
170
....*....|....*...
gi 1552103373 463 VLLLDEPTNNLD-PASRE 479
Cdd:PRK11144 149 LLLMDEPLASLDlPRKRE 166
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-211 |
1.66e-07 |
|
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: 52.27 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTIdrGGEIgYLPQDPRSGDpdeLARTRILDARGLGQL 93
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEGGGTT--SGQI-LFNGQPRKPD---QFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 VLGMqesTIamsssdasvsaagmkkYGTLTdrFLAL--------GGYAAEAEAASIASNLNLpDRILEQPLKTLSGGQRR 165
Cdd:cd03234 93 LPGL---TV----------------RETLT--YTAIlrlprkssDAIRKKRVEDVLLRDLAL-TRIGGNLVKGISGGERR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1552103373 166 RIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY-RGGFIVI 211
Cdd:cd03234 151 RVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVI 197
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
322-498 |
1.99e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.48 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 322 GRTPLHAENLSksygsleiFTAvdlaidrGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGL----------RI 390
Cdd:PRK10575 23 GRTLLHPLSLT--------FPA-------GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGeILLDAQPLeswsskafarKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 391 GYYAQE---HETIDVKRSVLENMV---SASPNLTETEARRVLGSFLFTGDD--SHKPAGVLSGGEKTRLALAMIVVSGAN 462
Cdd:PRK10575 88 AYLPQQlpaAEGMTVRELVAIGRYpwhGALGRFGAADREKVEEAISLVGLKplAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 463 VLLLDEPTNNLDPASREEIL---DALAHYEG-AVVLVSHD 498
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLalvHRLSQERGlTVIAVLHD 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
346-498 |
2.18e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.66 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 346 LAIDRGSKVV-ILGLNGAGKTTLLRILGGVDQPDTG----------VIEAGHGLRIGYYAQEHETIDVKRSVLENMVSAS 414
Cdd:PRK13409 93 LPIPKEGKVTgILGPNGIGKTTAVKILSGELIPNLGdyeeepswdeVLKRFRGTELQNYFKKLYNGEIKVVHKPQYVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 415 PN---------LTETEARRVLG---SFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEIL 482
Cdd:PRK13409 173 PKvfkgkvrelLKKVDERGKLDevvERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVA 252
|
170
....*....|....*...
gi 1552103373 483 DALAHY--EGAVVLVSHD 498
Cdd:PRK13409 253 RLIRELaeGKYVLVVEHD 270
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
326-531 |
2.19e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.29 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVdQP----DTGVIEAGHGL---------RIGY 392
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPhgtwDGEIYWSGSPLkasnirdteRAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEHETIDVKR-SVLENMVSASP----------NLTETEARRVLGSFLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGA 461
Cdd:TIGR02633 81 VIIHQELTLVPElSVAENIFLGNEitlpggrmayNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 462 NVLLLDEPTNNLDPASREEILDA---LAHYEGAVVLVSHDEGAVEALNpERVLIMPEG----TEDHWAADYLDLITL 531
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVC-DTICVIRDGqhvaTKDMSTMSEDDIITM 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-222 |
2.20e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG--------EIGYLPQDPRS 73
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTaplaeareDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 74 gdpdeLARTRILDARGLGqlvlgmqestiamsssdasvsaagMKkyGTLTDRFL-ALggyaaeaeaasiaSNLNLPDRIL 152
Cdd:PRK11247 93 -----LPWKKVIDNVGLG------------------------LK--GQWRDAALqAL-------------AAVGLADRAN 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 153 EQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIV--ISHDielVGETV 222
Cdd:PRK11247 129 EWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVllVTHD---VSEAV 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
351-487 |
2.63e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.51 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 351 GSKVVILGLNGAGKTTLL-----RILGGVD-QPDTGV----IEAGHGLRIGYYAQEHETIDVKRSVLEN-MVSAS---PN 416
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMnalafRSPKGVKgSGSVLLngmpIDAKEMRAISAYVQQDDLFIPTLTVREHlMFQAHlrmPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 417 LTETEARRVLGSFLFT----GDDSHKPAGV------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA 486
Cdd:TIGR00955 131 RVTKKEKRERVDEVLQalglRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLK 210
|
.
gi 1552103373 487 H 487
Cdd:TIGR00955 211 G 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-216 |
2.77e-07 |
|
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: 53.76 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRV--GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAgDLIASKGTIDRGG-------------EIGY 66
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQ-------------DPRSGDPDElARTRILDARGLGQLVlgmqestiamsssdasvsaagmKKYGTLTDRFLALGGYa 133
Cdd:TIGR01271 1297 IPQkvfifsgtfrknlDPYEQWSDE-EIWKVAEEVGLKSVI----------------------EQFPDKLDFVLVDGGY- 1352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 134 aeaeaasiasnlnlpdrileqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVI-- 211
Cdd:TIGR01271 1353 ------------------------VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIls 1408
|
....*
gi 1552103373 212 SHDIE 216
Cdd:TIGR01271 1409 EHRVE 1413
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
158-213 |
2.82e-07 |
|
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: 51.77 E-value: 2.82e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF--IVISH 213
Cdd:cd03249 139 QLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRttIVIAH 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-232 |
2.95e-07 |
|
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: 52.42 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 20 VSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigyLPQDPRSGD--PDELARTRIL--DARGL----- 90
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGR---TLFDSRKGIflPPEKRRIGYVfqEARLFphlsv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 91 -GQLVLGMQESTIAMSSSDAsvsaagmkkygtltDRFLALggyaaeaeaasiasnLNLpDRILEQPLKTLSGGQRRRIEL 169
Cdd:TIGR02142 93 rGNLRYGMKRARPSERRISF--------------ERVIEL---------------LGI-GHLLGRLPGRLSGGEKQRVAI 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 170 ARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF----IVISHDIELVGETVNRVFYLDANR 232
Cdd:TIGR02142 143 GRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFgipiLYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-228 |
3.32e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPRsgdpdelAR 81
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKD-------GQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARglgQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALGGYAAEAEAASIASNLNLPDRILEQPLKTLSG 161
Cdd:PRK10619 79 LKVADKN---QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLDAD---SVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYL 228
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
159-219 |
4.08e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 50.97 E-value: 4.08e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVVWLREFLKNYRG-GFIVISHDIELVG 219
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGtAFLVVTHDLQLAK 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
322-496 |
4.44e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 322 GRTPLHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLlRILGGVDQPDTGVIEAGHGLRIGYYAQEHETID 401
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 VKRSVL----------EN--MVSASPNLTETEAR----RVLGSFLFTgDDSHKPAGVLSGGEKTRLALAMIVVSGANVLL 465
Cdd:NF000106 89 *HRPVR*grresfsgrENlyMIGR*LDLSRKDARaradELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190
....*....|....*....|....*....|...
gi 1552103373 466 LDEPTNNLDPASREEILDALAHY--EGAVVLVS 496
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLT 200
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-228 |
4.58e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 20 VSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASkgtidrGGEIGYLPQDPRSGDPDELARTR------------ILDA 87
Cdd:PRK15079 40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT------DGEVAWLGKDLLGMKDDEWRAVRsdiqmifqdplaSLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 88 R-GLGQLV----------LGMQEstiamsssDASVSAAGMKKYGTLtdrflalggyaaeaeaasiasnlnlPDRILEQPl 156
Cdd:PRK15079 114 RmTIGEIIaeplrtyhpkLSRQE--------VKDRVKAMMLKVGLL-------------------------PNLINRYP- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVF--YL 228
Cdd:PRK15079 160 HEFSGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLvmYL 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-186 |
5.36e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 5.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgDPDELA 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-----------DITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRIldarglgqlvlgMQESTiamsssdaSVSAAGMKKYGTLT-DRFLALGGYAAEAEAASIASN--LNLPDRILE---Q 154
Cdd:PRK11614 74 TAKI------------MREAV--------AIVPEGRRVFSRMTvEENLAMGGFFAERDQFQERIKwvYELFPRLHErriQ 133
|
170 180 190
....*....|....*....|....*....|..
gi 1552103373 155 PLKTLSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:PRK11614 134 RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
351-516 |
5.53e-07 |
|
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: 50.55 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 351 GSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAGHGLRIGYYAQEHETIDV--------KRSVLENM---VSASPNLT 418
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQGGqVLLDGKPISQYEHKYLHSKVSLvgqepvlfARSLQDNIaygLQSCSFEC 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 419 ETEARRVLGSFLFTGDDSHKP-------AGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL--AHYE 489
Cdd:cd03248 120 VKEAAQKAHAHSFISELASGYdtevgekGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALydWPER 199
|
170 180
....*....|....*....|....*..
gi 1552103373 490 GAVVLVSHDEGAVEalNPERVLIMPEG 516
Cdd:cd03248 200 RTVLVIAHRLSTVE--RADQILVLDGG 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
159-232 |
5.74e-07 |
|
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: 50.55 E-value: 5.74e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVISHDIELVgETVNRVFYLDANR 232
Cdd:cd03248 151 LSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-202 |
6.34e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 51.61 E-value: 6.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGgeIGYL 67
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIliggrdvtdlppkDRN--IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 68 PQDP------------------RSGDPDELARtRILDARGLgqlvLGMQEstiamsssdasvsaagmkkygtLTDRflal 129
Cdd:COG3839 81 FQSYalyphmtvyeniafplklRKVPKAEIDR-RVREAAEL----LGLED----------------------LLDR---- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 130 ggyaaeaeaasiasnlnLPdrileqplKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK 202
Cdd:COG3839 130 -----------------KP--------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIK 177
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
159-193 |
6.86e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 6.86e-07
10 20 30
....*....|....*....|....*....|....*
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADS 193
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-234 |
7.06e-07 |
|
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: 50.27 E-value: 7.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDEL--ARTRI---------LD 86
Cdd:cd03258 22 KDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG------TDLTLLSGKELrkARRRIgmifqhfnlLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 87 ARG-LGQLVLGMQestiamsssdasVSAAGMKKYGTLTDRFLALggyaaeaeaasiasnLNLPDRILEQPlKTLSGGQRR 165
Cdd:cd03258 96 SRTvFENVALPLE------------IAGVPKAEIEERVLELLEL---------------VGLEDKADAYP-AQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 166 RIELARILFSDASTLILDEPTNHLDA---DSVV-WLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQV 234
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPettQSILaLLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-214 |
8.36e-07 |
|
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: 49.95 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-IGYLPQDPRsgdpdELA 80
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdVTDLPPKDR-----DIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 ----------RTRILDARGLGQLVLGMQESTIamsssdasvsaagmKKYGTLTDRFLALGGYaaeaeaasiasnlnlpdr 150
Cdd:cd03301 76 mvfqnyalypHMTVYDNIAFGLKLRKVPKDEI--------------DERVREVAELLQIEHL------------------ 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 151 iLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGG--FIVISHD 214
Cdd:cd03301 124 -LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLqqRLGttTIYVTHD 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
353-498 |
9.03e-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: 51.71 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 353 KVV-ILGLNGAGKTTLLRILGGVDQPDTG----------VIEAGHGLRIGYY-----------AQEHETIDVKRSVLENM 410
Cdd:COG1245 100 KVTgILGPNGIGKSTALKILSGELKPNLGdydeepswdeVLKRFRGTELQDYfkklangeikvAHKPQYVDLIPKVFKGT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 411 VSASpnLTETEARRVLGSFLFTGDDSH---KPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASR---EEILDA 484
Cdd:COG1245 180 VREL--LEKVDERGKLDELAEKLGLENildRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvARLIRE 257
|
170
....*....|....
gi 1552103373 485 LAHYEGAVVLVSHD 498
Cdd:COG1245 258 LAEEGKYVLVVEHD 271
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-216 |
9.29e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI--------DRGGEIGYLPQDpr 72
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSItldgkpveGPGAERGVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 73 sgdpDELARTR-ILDARGLGQLVLGMQEStiamssSDASVSAAGMKKYGtltdrflaLGGYAaeaeaasiasnlnlpdri 151
Cdd:PRK11248 79 ----EGLLPWRnVQDNVAFGLQLAGVEKM------QRLEIAHQMLKKVG--------LEGAE------------------ 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 152 lEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFL----KNYRGGFIVISHDIE 216
Cdd:PRK11248 123 -KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlklwQETGKQVLLITHDIE 190
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-64 |
1.01e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 1.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEI 64
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV 87
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
421-516 |
1.09e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 421 EARRVLGSFLFTgddshkpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA-----HYEGaVVLV 495
Cdd:PRK10418 129 NAARVLKLYPFE----------MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLEsivqkRALG-MLLV 197
|
90 100
....*....|....*....|.
gi 1552103373 496 SHDEGAVEALnPERVLIMPEG 516
Cdd:PRK10418 198 THDMGVVARL-ADDVAVMSHG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
328-478 |
1.14e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.66 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 328 AENLSKSYGSleiFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILggvdqpdTGVIEAGHG----------------- 387
Cdd:NF033858 269 ARGLTMRFGD---FTAVDhvsFRIRRGEIFGFLGSNGCGKSTTMKML-------TGLLPASEGeawlfgqpvdagdiatr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQ------EhetidvkRSVLENMVsaspnL---------TETEAR--RVLGSF-LftGDDSHKPAGVLSGGEKT 449
Cdd:NF033858 339 RRVGYMSQafslygE-------LTVRQNLE-----LharlfhlpaAEIAARvaEMLERFdL--ADVADALPDSLPLGIRQ 404
|
170 180
....*....|....*....|....*....
gi 1552103373 450 RLALAMIVVSGANVLLLDEPTNNLDPASR 478
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
12-225 |
1.14e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.85 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgDPDEL-ARTR------- 83
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----------DVSRLhARDRkvgfvfq 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ---------ILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLAlggyaaeaeaasiasnlnlpdrileq 154
Cdd:PRK10851 82 hyalfrhmtVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPA-------------------------- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 155 plkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADsvV------WLREFLKNYRGGFIVISHDIELVGETVNRV 225
Cdd:PRK10851 136 ---QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ--VrkelrrWLRQLHEELKFTSVFVTHDQEEAMEVADRV 207
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
159-505 |
1.17e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.24 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQV 234
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 235 idvynmNWKNYQRQRAADEERRKKERANVEKKAGALQLQaarfgakaskaaaahqmvARAEKMLsgleevravdRVAKLR 314
Cdd:PRK15134 237 ------EQNRAATLFSAPTHPYTQKLLNSEPSGDPVPLP------------------EPASPLL----------DVEQLQ 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 315 FPTPMACGRtplhaenLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTT----LLRIL---GGV---DQPDtgviea 384
Cdd:PRK15134 283 VAFPIRKGI-------LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLInsqGEIwfdGQPL------ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 385 gHGL----------RIGYYAQEHET-----IDVKRSVLENMVSASPNLT--ETEAR--RVLGSFLFTGDDSHKPAGVLSG 445
Cdd:PRK15134 350 -HNLnrrqllpvrhRIQVVFQDPNSslnprLNVLQIIEEGLRVHQPTLSaaQREQQviAVMEEVGLDPETRHRYPAEFSG 428
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 446 GEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEAL 505
Cdd:PRK15134 429 GQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLkslqQKHQLAYLFISHDLHVVRAL 492
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
336-485 |
1.18e-06 |
|
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: 49.16 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 336 GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGvdQPDTGVIE-----AGHGL------RIGYYAQEhetiDVKr 404
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeiliNGRPLdknfqrSTGYVEQQ----DVH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 svlenmvsaSPNLTETEARRVlgSFLFTGddshkpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDA 484
Cdd:cd03232 91 ---------SPNLTVREALRF--SALLRG---------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRF 150
|
.
gi 1552103373 485 L 485
Cdd:cd03232 151 L 151
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
442-517 |
1.55e-06 |
|
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: 49.85 E-value: 1.55e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 442 VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH-YEGAVVLVShdEGAVEA-LNPERVLIMPEGT 517
Cdd:cd03289 138 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQaFADCTVILS--EHRIEAmLECQRFLVIEENK 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
12-216 |
1.56e-06 |
|
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: 49.61 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqDPRSGDPDELART--------- 82
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE------DIREQDPVELRRKigyviqqig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 -----RILDARGLGQLVLGMQEstiamsssdasvsaagmKKYGTLTDRFLALGGYAAEaeaasiasnlNLPDRILEQplk 157
Cdd:cd03295 86 lfphmTVEENIALVPKLLKWPK-----------------EKIRERADELLALVGLDPA----------EFADRYPHE--- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 158 tLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWL-REFLKNYR--GGFIV-ISHDIE 216
Cdd:cd03295 136 -LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLqEEFKRLQQelGKTIVfVTHDID 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-236 |
1.95e-06 |
|
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: 49.22 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVG-ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLpqdprSGDPDE 78
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILlEGTDITKL-----RGKKLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 LARTRIldarglgqlvlGM--QESTIAMSSSDASVSAAG----MKKYGTLTDRFlalggyaaeaEAASIASNLNLPDR-- 150
Cdd:TIGR02315 76 KLRRRI-----------GMifQHYNLIERLTVLENVLHGrlgyKPTWRSLLGRF----------SEEDKERALSALERvg 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 151 ILEQPLK---TLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVIS--HDIELVGETVN 223
Cdd:TIGR02315 135 LADKAYQradQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKriNKEDGITVIInlHQVDLAKKYAD 214
|
250
....*....|...
gi 1552103373 224 RVFYLDANRQVID 236
Cdd:TIGR02315 215 RIVGLKAGEIVFD 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-193 |
2.46e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 50.23 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLmENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLiASKGTIDRGG-------------EIGYLPQDPrsgdpde 78
Cdd:PRK11174 362 GKTLA-GPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldpeswrkHLSWVGQNP------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 79 lartrildarglgQLVlgmqestiamsssdasvsaagmkkYGTLTDRfLALGgyaaeaeaasiasNLNLPDRILEQPLK- 157
Cdd:PRK11174 433 -------------QLP------------------------HGTLRDN-VLLG-------------NPDASDEQLQQALEn 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 158 -----------------------TLSGGQRRRIELARILFSDASTLILDEPTNHLDADS 193
Cdd:PRK11174 462 awvseflpllpqgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
145-229 |
2.52e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.46 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 LNLPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIVISHDIELVGET 221
Cdd:PRK13631 163 MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnktVFVITHTMEHVLEV 242
|
....*...
gi 1552103373 222 VNRVFYLD 229
Cdd:PRK13631 243 ADEVIVMD 250
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-213 |
2.65e-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: 50.13 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 16 LMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG--DLIASKGTIDRGGEIGYLPQDPRsgdpdelartrildaRGLGQL 93
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElwPVYGGRLTKPAKGKLFYVPQRPY---------------MTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 vlgmQESTIAMSSSDAsvsaagMKKYGtLTDRFLalggyaaeaeaASIASNLNLpDRILEQP---------LKTLSGGQR 164
Cdd:TIGR00954 532 ----RDQIIYPDSSED------MKRRG-LSDKDL-----------EQILDNVQL-THILEREggwsavqdwMDVLSGGEK 588
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 165 RRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISH 213
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
343-497 |
2.84e-06 |
|
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: 50.33 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 343 AVDLAIDRGSKVVILGLNGAGKTTLLR-ILGGVDQPDTGVIEAGhglRIGYYAQEHETIDVkrSVLENMVSASPnLTETE 421
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKG---SVAYVPQQAWIQND--SLRENILFGKA-LNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 422 ARRVLGSFLFTGDDSHKPAG----------VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGA 491
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGV 809
|
170
....*....|.
gi 1552103373 492 V-----VLVSH 497
Cdd:TIGR00957 810 LknktrILVTH 820
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
443-516 |
3.13e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 49.08 E-value: 3.13e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREE----ILDALAHYEGAVVLVSHDEGAVEAlnPERVLIMPEG 516
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmmqlILDAKANNKTVFVITHTMEHVLEV--ADEVIVMDKG 252
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
147-233 |
3.16e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 LPDR---ILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG----FIVISHDIELVg 219
Cdd:PTZ00265 565 LPDKyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTI- 643
|
90
....*....|....
gi 1552103373 220 ETVNRVFYLdANRQ 233
Cdd:PTZ00265 644 RYANTIFVL-SNRE 656
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-516 |
3.27e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgdpdELA 80
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--------------PCA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDARGLGqLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeAASIASNLNLpdrilEQPLKTLS 160
Cdd:PRK15439 77 RLTPAKAHQLG-IYLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQL--------LAALGCQLDL-----DSSAGSLE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWL----REFLKnyRG-GFIVISHDIELVGETVNRVFYLDANRQVI 235
Cdd:PRK15439 143 VADRQIVEILRGLMRDSRILILDEPTASLTPAETERLfsriRELLA--QGvGIVFISHKLPEIRQLADRISVMRDGTIAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 236 dvynmnwknyqrQRAADEERRKKERANVEKKAGALQLQAARfgakaskaaaahqmvaraeKMLSGLEEVRAVDrvaklrf 315
Cdd:PRK15439 221 ------------SGKTADLSTDDIIQAITPAAREKSLSASQ-------------------KLWLELPGNRRQQ------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 316 ptpmACGRTPLHAENLSKsygslEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghglRIGYYAQ 395
Cdd:PRK15439 263 ----AAGAPVLTVEDLTG-----EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGG--------RIMLNGK 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 396 EHETIDVKRSVLENMVSASpnltetEARRVLGSFL---------------------------------------FTGDDs 436
Cdd:PRK15439 326 EINALSTAQRLARGLVYLP------EDRQSSGLYLdaplawnvcalthnrrgfwikparenavleryrralnikFNHAE- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 437 hKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNpERVLIM 513
Cdd:PRK15439 399 -QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIyqlIRSIAAQNVAVLFISSDLEEIEQMA-DRVLVM 476
|
...
gi 1552103373 514 PEG 516
Cdd:PRK15439 477 HQG 479
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
330-474 |
3.39e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.07 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 330 NLSKSY-GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQpdtgvIEAGHgLRIG----------------- 391
Cdd:PRK11650 8 AVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLER-----ITSGE-IWIGgrvvnelepadrdiamv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 392 ---YYAQEHetidvkRSVLENMVSASPN--LTETE-ARRV--------LGSFLftgddSHKPAGvLSGGEKTRLALAMIV 457
Cdd:PRK11650 82 fqnYALYPH------MSVRENMAYGLKIrgMPKAEiEERVaeaarileLEPLL-----DRKPRE-LSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 1552103373 458 VSGANVLLLDEPTNNLD 474
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
327-478 |
3.40e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 3.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 327 HAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE--------AGH----GLRIGY-- 392
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadARHrravCPRIAYmp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 -------YAqeheTIdvkrSVLENM--------VSASpnltETEAR--RVLGSflfTGDDS--HKPAGVLSGGEKTRLAL 453
Cdd:NF033858 83 qglgknlYP----TL----SVFENLdffgrlfgQDAA----ERRRRidELLRA---TGLAPfaDRPAGKLSGGMKQKLGL 147
|
170 180
....*....|....*....|....*
gi 1552103373 454 AMIVVSGANVLLLDEPTNNLDPASR 478
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSR 172
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
348-502 |
3.48e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 48.73 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 348 IDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIE-----AGHGLR---IGYYAQEHEtIDVKRSVL-ENMVSASP--- 415
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQknlVAYVPQSEE-VDWSFPVLvEDVVMMGRygh 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 416 ----NLTETEARRVLGSFLFTGDDS---HKPAGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHY 488
Cdd:PRK15056 109 mgwlRRAKKRDRQIVTAALARVDMVefrHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL 188
|
170
....*....|....*..
gi 1552103373 489 --EGAVVLVS-HDEGAV 502
Cdd:PRK15056 189 rdEGKTMLVStHNLGSV 205
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
329-516 |
3.56e-06 |
|
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: 47.79 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 329 ENLSKSYGS--LEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAgHGLRIGYYAQEhetiDVKRSV 406
Cdd:cd03369 10 ENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLE----DLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 407 leNMVSASPNLTETEARRVLGSF-LFTGDDSHKPAGV------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPAS-- 477
Cdd:cd03369 85 --TIIPQDPTLFSGTIRSNLDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATda 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1552103373 478 ------REEILDAlahyegAVVLVSHDEGAVeaLNPERVLIMPEG 516
Cdd:cd03369 163 liqktiREEFTNS------TILTIAHRLRTI--IDYDKILVMDAG 199
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
159-234 |
3.62e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 3.62e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIvISHDIELVGEtVNRVFYLDANRQV 234
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGrttFI-IAHRLSTVRN-ADRILVFDNGRVV 548
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
337-516 |
4.39e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.34 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 337 SLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG-VIEAG--------HGLRIGYYAQEHETIDVKRSVL 407
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGqVLLDGvplvqydhHYLHRQVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 ENMVSASPNLTETEARRV---------LGSFLFTGDDSHKPAGV-LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPAS 477
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAakaanahdfIMEFPNGYDTEVGEKGSqLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652
|
170 180 190
....*....|....*....|....*....|....*....
gi 1552103373 478 REEILDALAHYEGAVVLVSHDEGAVEalNPERVLIMPEG 516
Cdd:TIGR00958 653 EQLLQESRSRASRTVLLIAHRLSTVE--RADQILVLKKG 689
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
326-498 |
4.50e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQEH-ETIDVKR 404
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYrDVLEFRR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 405 SVleNMVSASPN----------LTETEARRVLGSFLFTGDDSHKPAGV----------------LSGGEKTRLALAMIVV 458
Cdd:PRK14271 102 RV--GMLFQRPNpfpmsimdnvLAGVRAHKLVPRKEFRGVAQARLTEVglwdavkdrlsdspfrLSGGQQQLLCLARTLA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1552103373 459 SGANVLLLDEPTNNLDPASREEILDALAHYEG--AVVLVSHD 498
Cdd:PRK14271 180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-218 |
5.06e-06 |
|
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: 49.30 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdLIASKGTID-RGGEIGYLP---------------QDP-RSGDPdelaR 81
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRfDGQDLDGLSrralrplrrrmqvvfQDPfGSLSP----R 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRILDARGLGQLVLGMQEStiamSSSDASVSAAGMKKYGtltdrflalggyaaeaeaasiasnlnLPDRILEQPLKTLSG 161
Cdd:COG4172 379 MTVGQIIAEGLRVHGPGLS----AAERRARVAEALEEVG--------------------------LDPAARHRYPHEFSG 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 162 GQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELV 218
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFISHDLAVV 489
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-217 |
5.20e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.25 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 3 SVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG-------------EIGYLPQ 69
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafarKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 70 D-PrsgdPDELARTRILDARG-------LGQLVLGMQEStiamsssdasvsaagmkkygtlTDRFLALGGYAAeaeaasi 141
Cdd:PRK10575 93 QlP----AAEGMTVRELVAIGrypwhgaLGRFGAADREK----------------------VEEAISLVGLKP------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 142 asnlnLPDRILEqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDAD---SVVWLREFLKNYRG-GFIVISHDIEL 217
Cdd:PRK10575 140 -----LAHRLVD----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINM 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-216 |
5.38e-06 |
|
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: 48.31 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRV--GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAgDLIASKGTIDRGG-------------EIGY 66
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwrkAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQ-------------DPRSGDPDElARTRILDARGLGQLVlgmqestiamsssdasvsaagmKKYGTLTDRFLALGGYa 133
Cdd:cd03289 82 IPQkvfifsgtfrknlDPYGKWSDE-EIWKVAEEVGLKSVI----------------------EQFPGQLDFVLVDGGC- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 134 aeaeaasiasnlnlpdrileqplkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVI-- 211
Cdd:cd03289 138 ------------------------VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVIls 193
|
....*
gi 1552103373 212 SHDIE 216
Cdd:cd03289 194 EHRIE 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-215 |
5.63e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 48.06 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 7 LELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgDPDELARTRIld 86
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-----------HIQHYASKEV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 87 ARGLGQLVlgmQESTIAMSSSDASVSAAGMKKYGTLTDRFlalggYAAEAEAASIASNLNLPDRILEQPLKTLSGGQRRR 166
Cdd:PRK10253 80 ARRIGLLA---QNATTPGDITVQELVARGRYPHQPLFTRW-----RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 167 IELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIV--ISHDI 215
Cdd:PRK10253 152 AWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSelNREKGYTLaaVLHDL 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
145-225 |
5.98e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 48.24 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 LNLPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR----GGFIVISHDIELVGE 220
Cdd:PRK13646 132 LGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVAR 211
|
....*
gi 1552103373 221 TVNRV 225
Cdd:PRK13646 212 YADEV 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
159-228 |
6.31e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 48.95 E-value: 6.31e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVgETVNRVFYL 228
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVL 686
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-190 |
6.89e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.77 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDELA 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG------LDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RT-RILdaRglgqlvlgmQESTIAMSSSDASVSAAGMKKY--GTLT--DR--------FLALGgyaaeaeaasiasnlNL 147
Cdd:COG4604 75 KRlAIL--R---------QENHINSRLTVRELVAFGRFPYskGRLTaeDReiideaiaYLDLE---------------DL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1552103373 148 PDRILEQplktLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:COG4604 129 ADRYLDE----LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
149-224 |
6.93e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.78 E-value: 6.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 149 DRILEQPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGGFIVISHDIELVGETVNR 224
Cdd:PRK14271 155 DRLSDSPFR-LSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHNLAQAARISDR 231
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
14-236 |
8.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigYLPqdprsgDPDELARTRILDARGLGQL 93
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-------YVD------GLDTSDEENLWDIRNKAGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 VLGMQESTIAmsssdasvsaagmkkyGTLTDRFLALGgyaaeaeaasiASNLNL-PDRI---LEQPLKT----------- 158
Cdd:PRK13633 90 VFQNPDNQIV----------------ATIVEEDVAFG-----------PENLGIpPEEIrerVDESLKKvgmyeyrrhap 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 --LSGGQRRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGGFIVISHDIELVGETvNRVFYLDANR 232
Cdd:PRK13633 143 hlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGK 221
|
....
gi 1552103373 233 QVID 236
Cdd:PRK13633 222 VVME 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-221 |
9.09e-06 |
|
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: 48.79 E-value: 9.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQdpRSGDPDELARTRILDARGLgqlvlg 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQ--QAWIQNDSLRENILFGKAL------ 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 97 mQESTIAMSssdasvsaagMKKYGTLTDRFLALGGyaaeaeaasiasnlnlpDR--ILEQPLkTLSGGQRRRIELARILF 174
Cdd:TIGR00957 726 -NEKYYQQV----------LEACALLPDLEILPSG-----------------DRteIGEKGV-NLSGGQKQRVSLARAVY 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 175 SDASTLILDEPTNHLDA-------DSVVWLREFLKNYRGgfIVISHDIELVGET 221
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAhvgkhifEHVIGPEGVLKNKTR--ILVTHGISYLPQV 828
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-192 |
1.10e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 46.63 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLPQDPRSGDPDEL 79
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLfEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARTRILdargLGQ-----LVLGMQestiamsssdASVSAAGMKKYGTLTDRFlalggyaaeaeaasiasnlNLPDRILEQ 154
Cdd:PRK10247 87 AQTPTL----FGDtvydnLIFPWQ----------IRNQQPDPAIFLDDLERF-------------------ALPDTILTK 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 1552103373 155 PLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDAD 192
Cdd:PRK10247 134 NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
340-516 |
1.12e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 48.34 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 340 IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPD--TGVIEAGHG-------LRIGYYAQE-----HETI----- 400
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRkptkqilKRTGFVTQDdilypHLTVretlv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 401 -------------DVKRSVLENMVSaSPNLTETEARRVLGSFLftgddshkpAGVlSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:PLN03211 163 fcsllrlpksltkQEKILVAESVIS-ELGLTKCENTIIGNSFI---------RGI-SGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 468 EPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNPERVLIMPEG 516
Cdd:PLN03211 232 EPTSGLDATAAYRLvltLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-232 |
1.22e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 46.93 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPRSGDpdelartrildARGLGQLVlGM- 97
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKA-----------IRLLRQKV-GMv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 98 -QES------TIAMSSSDASVSAAGMKKYGTL--TDRFLAlggyaaeaeaasiasNLNLPDRILEQPLKtLSGGQRRRIE 168
Cdd:COG4161 88 fQQYnlwphlTVMENLIEAPCKVLGLSKEQARekAMKLLA---------------RLRLTDKADRFPLH-LSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 169 LARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFI---VISHDIELVGETVNRVFYLDANR 232
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGR 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
344-499 |
1.28e-05 |
|
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: 45.78 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRilggvdqpdTGVIEAGHGLRIGYY--AQEHETIDVKRsvLENMVSASpnltete 421
Cdd:cd03238 14 LDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLpkFSRNKLIFIDQ--LQFLIDVG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 422 arrvLGsFLFTGddshKPAGVLSGGEKTRLALA--MIVVSGANVLLLDEPTNNLDPASREEILDA---LAHYEGAVVLVS 496
Cdd:cd03238 76 ----LG-YLTLG----QKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVikgLIDLGNTVILIE 146
|
...
gi 1552103373 497 HDE 499
Cdd:cd03238 147 HNL 149
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
19-229 |
1.32e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 47.04 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdRGGEIGYL---------PQDPRSGDPDELARTRILDARG 89
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV-TVGDIVVSstskqkeikPVRKKVGVVFQFPESQLFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 90 LGQLVLGMQESTIAMSSSDASVsaagmkkygtlTDRFLALGgyaaeaeaasiasnlnLPDRILEQPLKTLSGGQRRRIEL 169
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIA-----------AEKLEMVG----------------LADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 170 ARILFSDASTLILDEPTNHLDADSVVWLREFLKN-YRGG--FIVISHDIELVGETVNRVFYLD 229
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESiHQSGqtVVLVTHLMDDVADYADYVYLLE 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
326-513 |
1.54e-05 |
|
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: 46.97 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLE-IFTAVD---LAIDRGSKVVILGLNGAGKTTLLRILGGVDQPdtGVIEAGH--------------- 386
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDgvsFDVRRGETLGLVGESGSGKSTLARAILGLLPP--PGITSGEilfdgedllklseke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 387 -----GLRIGYYAQE-----HETIDVKRSVLENMVSASPnLTETEAR-RVLGSFLFTGDDShkPAGV-------LSGGEK 448
Cdd:COG0444 80 lrkirGREIQMIFQDpmtslNPVMTVGDQIAEPLRIHGG-LSKAEAReRAIELLERVGLPD--PERRldrypheLSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 449 TRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH----YEGAVVLVSHDEGAVEALNpERVLIM 513
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlqreLGLAILFITHDLGVVAEIA-DRVAVM 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
389-505 |
1.60e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 389 RIGYYAQEHETIDVKRSVLENmVSASPNLTETEARRVLgsflFTGDDSHKPAGVLSGGEKT------RLALAMIVVSGAN 462
Cdd:TIGR00606 1151 RSTYRGQDIEYIEIRSDADEN-VSASDKRRNYNYRVVM----LKGDTALDMRGRCSAGQKVlasliiRLALAETFCLNCG 1225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 463 VLLLDEPTNNLDPASREEILDALAHY--------EGAVVLVSHDEGAVEAL 505
Cdd:TIGR00606 1226 IIALDEPTTNLDRENIESLAHALVEIiksrsqqrNFQLLVITHDEDFVELL 1276
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-228 |
1.72e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 46.58 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPRSGD----- 75
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDaiklr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 76 ---------PDELARTRILDarglgQLVLGMQESTIAMSSSDASVSAAGMKKYGTLTDRFlalggyaaeaeaasiasnln 146
Cdd:PRK14246 90 kevgmvfqqPNPFPHLSIYD-----NIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVY-------------------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 147 lpDRiLEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG--GFIVISHDIELVGETVNR 224
Cdd:PRK14246 145 --DR-LNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADY 221
|
....
gi 1552103373 225 VFYL 228
Cdd:PRK14246 222 VAFL 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-186 |
1.90e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.32 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLelRVGARLlmENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE--------------IGY 66
Cdd:COG1129 256 VLEVEGL--SVGGVV--RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 67 LPQDpRSGD----------------PDELARTRILDARGLGQLVLGMqestiamsssdasvsaagMKKYGTLTDRflalg 130
Cdd:COG1129 332 VPED-RKGEglvldlsirenitlasLDRLSRGGLLDRRRERALAEEY------------------IKRLRIKTPS----- 387
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 131 gyaaeaeaasiasnlnlpdriLEQPLKTLSGGQRRRIELARILFSDASTLILDEPT 186
Cdd:COG1129 388 ---------------------PEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-190 |
2.09e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGD--------LI------ASKGTI-DRGGEIGY----LPQDPRSG 74
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndLTlfgrrrGSGETIwDIKKHIGYvsssLHLDYRVS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 75 DPdelARTRIL----DARGLGQLVLGMQEStiamsssdasvsaagmkkygtLTDRFLALggyaaeaeaasiasnLNLPDR 150
Cdd:PRK10938 353 TS---VRNVILsgffDSIGIYQAVSDRQQK---------------------LAQQWLDI---------------LGIDKR 393
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 151 ILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK10938 394 TADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-214 |
2.09e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLagdliaskGTIDR--GGEIGYLPQDPRSGDPDELARTR------ILDAR 88
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNIL--------GCLDKptSGTYRVAGQDVATLDADALAQLRrehfgfIFQRY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 89 GLGQLVLGMQESTIAMSssdasvsaagmkkygtltdrFLALGGYAAEAEAASIASNLNLPDRILEQPlKTLSGGQRRRIE 168
Cdd:PRK10535 96 HLLSHLTAAQNVEVPAV--------------------YAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVS 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1552103373 169 LARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHD 214
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHD 203
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-229 |
2.12e-05 |
|
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: 45.60 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggEIGYLPQDPRSGDPDELaR 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI----IIDGLKLTDDKKNINEL-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRI---------------LDARGLGQL-VLGMQESTiamsssdasVSAAGMKkygtltdrFLALGGyaaeaeaasiasnl 145
Cdd:cd03262 76 QKVgmvfqqfnlfphltvLENITLAPIkVKGMSKAE---------AEERALE--------LLEKVG-------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 146 nLPDRILEQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVvwlREFLKNYRG------GFIVISHDIELVG 219
Cdd:cd03262 125 -LADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELV---GEVLDVMKDlaeegmTMVVVTHEMGFAR 199
|
250
....*....|
gi 1552103373 220 ETVNRVFYLD 229
Cdd:cd03262 200 EVADRVIFMD 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
11-232 |
2.15e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 45.64 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 11 VGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGG----------------EIGYLPQDPRSg 74
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDHHL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 75 dpdeLARTRILDARGLGQLVLGMQESTIAMSSSDasvsaaGMKKYGTLtdrflalggyaaeaeaasiasnlnlpDRILEQ 154
Cdd:PRK10908 91 ----LMDRTVYDNVAIPLIIAGASGDDIRRRVSA------ALDKVGLL--------------------------DKAKNF 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 155 PLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD-ADSVVWLREFLKNYRGGFIVI--SHDIELVGETVNRVFYLDAN 231
Cdd:PRK10908 135 PIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdALSEGILRLFEEFNRVGVTVLmaTHDIGLISRRSYRMLTLSDG 213
|
.
gi 1552103373 232 R 232
Cdd:PRK10908 214 H 214
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
334-497 |
2.48e-05 |
|
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: 45.78 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 334 SYGS-LEIFTAVDLAIDRGSKVVILGLNGAGKTTLL-RILGGV--------------DQPDTGVIEAGHGLRIGYYAQEH 397
Cdd:cd03290 9 SWGSgLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMqtlegkvhwsnkneSEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 398 ETIDVkrSVLENMVSASPnLTETEARRVLGSFLFTGDDSHKPAG----------VLSGGEKTRLALAMIVVSGANVLLLD 467
Cdd:cd03290 89 WLLNA--TVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFGdqteigergiNLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 468 EPTNNL-----DPASREEILDALAHYEGAVVLVSH 497
Cdd:cd03290 166 DPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTH 200
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-190 |
2.62e-05 |
|
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: 45.62 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 21 SFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGeigylpQDPRSGDPDElartrildaRGLGQLvlgMQES 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND------QSHTGLAPYQ---------RPVSML---FQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 101 TIAMSSSDASVSAAGMKKYGTLTdrflALGGYAAEAEAASIASNlNLPDRILEQplktLSGGQRRRIELARILFSDASTL 180
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGLHPGLKLN----AEQQEKVVDAAQQVGIA-DYLDRLPEQ----LSGGQRQRVALARCLVRPNPIL 150
|
170
....*....|
gi 1552103373 181 ILDEPTNHLD 190
Cdd:TIGR01277 151 LLDEPFSALD 160
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
439-499 |
2.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 2.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 439 PAGVLSGGEKT------RLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYE---GAVVLVSHDE 499
Cdd:PRK03918 785 PLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLrkiPQVIIVSHDE 854
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-234 |
2.67e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.78 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 2 LSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDPrsgDPDELAR 81
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTP---SDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 82 TRildaRGLGQL----------------------VLGMQEStiamsssdasvsaAGMKKYGTLTDRfLALGGYAaeaeaa 139
Cdd:PRK11124 80 LR----RNVGMVfqqynlwphltvqqnlieapcrVLGLSKD-------------QALARAEKLLER-LRLKPYA------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 140 siasnlnlpDRIleqPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREfLKNYRGGFIVISHDI 215
Cdd:PRK11124 136 ---------DRF---PLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIRE-LAETGITQVIVTHEV 201
|
250
....*....|....*....
gi 1552103373 216 ELVGETVNRVFYLDANRQV 234
Cdd:PRK11124 202 EVARKTASRVVYMENGHIV 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-71 |
2.67e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.08 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 6 DLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTL-------TKVLAGDLIASkgtidrGGEIG------------Y 66
Cdd:PTZ00243 1315 QMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLlltfmrmVEVCGGEIRVN------GREIGayglrelrrqfsM 1388
|
....*
gi 1552103373 67 LPQDP 71
Cdd:PTZ00243 1389 IPQDP 1393
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
326-483 |
2.78e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGvDQPDTGvieAGHGLRI-GYYAQEHE---TID 401
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGG---APRGARVtGDVTLNGEplaAID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 402 VKRsvLENMVSASPNLTET----EARRV--LGSF---LFTGDDSHKPAGV--------------------LSGGEKTRLA 452
Cdd:PRK13547 78 APR--LARLRAVLPQAAQPafafSAREIvlLGRYphaRRAGALTHRDGEIawqalalagatalvgrdvttLSGGELARVQ 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1552103373 453 LAMIV---------VSGANVLLLDEPTNNLDPASREEILD 483
Cdd:PRK13547 156 FARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLD 195
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
228-315 |
2.80e-05 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 42.56 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 228 LDANRQVIDVYNMNWKNYQRQRAADEERRKKERANVEKKAGALQLQAARFGAKAskaaaahQMVARA---EKMLSGLEEV 304
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKA-------SKAKQAqsrIKALEKMERI 73
|
90
....*....|..
gi 1552103373 305 RAVDR-VAKLRF 315
Cdd:pfam12848 74 EKPERdKPKLRF 85
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-225 |
2.82e-05 |
|
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: 44.73 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLelRVGARLlmENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEigylpqdprsgdPDELA 80
Cdd:cd03215 4 VLEVRGL--SVKGAV--RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK------------PVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDARGLGqLVLGmqestiamsssdasvsaaGMKKYGTLTDRFLAlggyaaeaeaasiaSNLNLPDRileqplktLS 160
Cdd:cd03215 68 SPRDAIRAGIA-YVPE------------------DRKREGLVLDLSVA--------------ENIALSSL--------LS 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR---GGFIVISHDIELVGETVNRV 225
Cdd:cd03215 107 GGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRI 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
318-486 |
3.02e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.63 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 318 PMACGRTPLhaENLSKSYGSLE-IFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI--------EAGHG- 387
Cdd:PRK10790 335 PLQSGRIDI--DNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIrldgrplsSLSHSv 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQEHETIDVKRSVLENmVSASPNLTETEARRVLGSFLFT------GDDSHKPAG----VLSGGEKTRLALAMIV 457
Cdd:PRK10790 413 LRQGVAMVQQDPVVLADTFLAN-VTLGRDISEEQVWQALETVQLAelarslPDGLYTPLGeqgnNLSVGQKQLLALARVL 491
|
170 180
....*....|....*....|....*....
gi 1552103373 458 VSGANVLLLDEPTNNLDPASREEILDALA 486
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALA 520
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
350-512 |
3.55e-05 |
|
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: 43.90 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 350 RGSKVVILGLNGAGKTTLLRILGG-VDQPDTGVIEaghglrigyyaqehetidvkrsvlenmVSASPNLTETEARRVLGS 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAReLGPPGGGVIY---------------------------IDGEDILEEVLDQLLLII 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 429 FLFTGddshkpaGVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEGAVVLVSHDEGAVEALNPE 508
Cdd:smart00382 54 VGGKK-------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDE 126
|
....
gi 1552103373 509 RVLI 512
Cdd:smart00382 127 KDLG 130
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
344-468 |
3.60e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGvieaghglrigyyaqeheTIDVKRSV--------LENMVSASP 415
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKG------------------TVDIKGSAaliaissgLNGQLTGIE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 416 N---------LTETEARRVLGS---FLFTGDDSHKPAGVLSGGEKTRLALAMIVVSGANVLLLDE 468
Cdd:PRK13545 105 NielkglmmgLTKEKIKEIIPEiieFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
149-214 |
4.29e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.79 E-value: 4.29e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 149 DRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLR----EFLKNYRGGFIVISHD 214
Cdd:PRK11000 124 AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRieisRLHKRLGRTMIYVTHD 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
442-516 |
4.30e-05 |
|
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: 46.44 E-value: 4.30e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 442 VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH-YEGAVVLVShdEGAVEALNPERVLIMPEG 516
Cdd:TIGR01271 1353 VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILS--EHRVEALLECQQFLVIEG 1426
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
159-240 |
4.45e-05 |
|
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: 44.92 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNY--RGG--FIVISHDIELVGETVNRVFYLDANR-- 232
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqkELGitFVFVTHDQEEALTMSDRIAVMNKGKiq 210
|
90
....*....|.
gi 1552103373 233 QV---IDVYNM 240
Cdd:cd03300 211 QIgtpEEIYEE 221
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-49 |
4.73e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 45.02 E-value: 4.73e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG 49
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
13-215 |
5.66e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 45.13 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 13 ARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDPrsgdpdel 79
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeKLRKHIGIVFQNP-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 artrilDARGLGQLVlgmqestiamsssdASVSAAGMKKYGTLTDRFlalggyaaEAEAASIASNLNLPDRILEQPlKTL 159
Cdd:PRK13648 93 ------DNQFVGSIV--------------KYDVAFGLENHAVPYDEM--------HRRVSEALKQVDMLERADYEP-NAL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWL----REFLKNYRGGFIVISHDI 215
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLldlvRKVKSEHNITIISITHDL 203
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-234 |
5.91e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.12 E-value: 5.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 19 NVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIgyLPQDPRSGDpdelartrILDARGLGQLVLGMQ 98
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTL--ITSTSKNKD--------IKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 99 ESTIAMSSSDASVSAaGMKKYG-------TLTDRFLALGGyaaeaeaasiasnlnLPDRILEQPLKTLSGGQRRRIELAR 171
Cdd:PRK13649 95 ESQLFEETVLKDVAF-GPQNFGvsqeeaeALAREKLALVG---------------ISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 172 ILFSDASTLILDEPTNHLDADSVVWLREFLKN-YRGGF--IVISHDIELVGETVNRVFYLDANRQV 234
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMtiVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-71 |
6.18e-05 |
|
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: 46.09 E-value: 6.18e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 7 LELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTI-------------DRGGEIGYLPQDP 71
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIiidglniakiglhDLRFKITIIPQDP 1369
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
149-231 |
6.19e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 44.77 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 149 DRILEQPLkTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGF--IVISHDIELVGETVNRV- 225
Cdd:PRK14239 140 DRLHDSAL-GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYtmLLVTRSMQQASRISDRTg 218
|
....*.
gi 1552103373 226 FYLDAN 231
Cdd:PRK14239 219 FFLDGD 224
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
156-217 |
6.36e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 6.36e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 156 LKTLSGGQRRRIELARIL----FSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIVISHDIEL 217
Cdd:cd03227 75 RLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKgaqVIVITHLPEL 143
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-190 |
6.66e-05 |
|
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: 45.58 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDP------- 71
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQdirdvtqaslraaIGIVPQDTvlfndti 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 72 ----RSGDPDelA-RTRILDARGLGQLvlgmqestiamsssdasvsaagmkkygtltDRFLAlggyaaeaeaasiasnlN 146
Cdd:COG5265 449 ayniAYGRPD--AsEEEVEAAARAAQI------------------------------HDFIE-----------------S 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1552103373 147 LPD----RILEQPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:COG5265 480 LPDgydtRVGERGLK-LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
157-193 |
7.01e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 7.01e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS 193
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
160-232 |
7.46e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.10 E-value: 7.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANR 232
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
147-190 |
7.84e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.63 E-value: 7.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1552103373 147 LPDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK13634 134 LPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
344-517 |
8.78e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.35 E-value: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 344 VDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIeaghglrigyyaqeheTIDVKRSVLENMvsaspnltetEAR 423
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI----------------LLDGKPVTAEQP----------EDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 424 RVLGSFLFTgdDSH-------------KPAGV------------------------LSGGEKTRLALAMIVVSGANVLLL 466
Cdd:PRK10522 396 RKLFSAVFT--DFHlfdqllgpegkpaNPALVekwlerlkmahkleledgrisnlkLSKGQKKRLALLLALAEERDILLL 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 467 DEPTNNLDPASR----EEILDALAHYEGAVVLVSHDEGAVEalNPERVLIMPEGT 517
Cdd:PRK10522 474 DEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHDDHYFI--HADRLLEMRNGQ 526
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
326-516 |
1.01e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGvdQPDTGVIE------------------AGHG 387
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILEgdilfkgesildlepeerAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 -------------------LRIGYYAQEHETIDVKRSVLE---------NMVSASPNLTEteaRRVLGSFlftgddshkp 439
Cdd:CHL00131 86 iflafqypieipgvsnadfLRLAYNSKRKFQGLPELDPLEfleiineklKLVGMDPSFLS---RNVNEGF---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 440 agvlSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEI---LDALAHYEGAVVLVSHDEGAVEALNPERVLIMPEG 516
Cdd:CHL00131 153 ----SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNG 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
156-195 |
1.02e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.02e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1552103373 156 LKTLSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVV 195
Cdd:TIGR00955 164 VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsfmAYSVV 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-477 |
1.41e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.02 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 395 QEHETIDVKRSVL-ENMVSASPNLTETearrvlgsflFTGDDSHKpagvLSGGEKTRLALAMIVVSGANVLLLDEPTNNL 473
Cdd:PTZ00265 545 KDSEVVDVSKKVLiHDFVSALPDKYET----------LVGSNASK----LSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
....
gi 1552103373 474 DPAS 477
Cdd:PTZ00265 611 DNKS 614
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-72 |
1.45e-04 |
|
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: 43.94 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVhDLELRVGARLLmeNVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE----------------- 63
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrrr 78
|
....*....
gi 1552103373 64 IGYLPQDPR 72
Cdd:COG4148 79 IGYVFQEAR 87
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
157-234 |
1.59e-04 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 43.59 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVvwlREFLKNYRG------GFIVISHDIELVGETVNRVFYLDA 230
Cdd:PRK11264 143 RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV---GEVLNTIRQlaqekrTMVIVTHEMSFARDVADRAIFMDQ 219
|
....
gi 1552103373 231 NRQV 234
Cdd:PRK11264 220 GRIV 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
158-216 |
1.66e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 43.20 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIE 216
Cdd:COG3840 129 QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDPE 191
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-203 |
1.75e-04 |
|
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: 42.62 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 12 GARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIAskGTIdrGGEIgYLPQDPRsgdPDELARTrildargLG 91
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTA--GVI--TGEI-LINGRPL---DKNFQRS-------TG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 ---QLVLGMQESTIAMSSsdasvsaagmkkygtltdRFLALggyaaeaeaasiasnlnlpdrileqpLKTLSGGQRRRIE 168
Cdd:cd03232 83 yveQQDVHSPNLTVREAL------------------RFSAL--------------------------LRGLSVEQRKRLT 118
|
170 180 190
....*....|....*....|....*....|....*
gi 1552103373 169 LARILFSDASTLILDEPTNHLDADSVVWLREFLKN 203
Cdd:cd03232 119 IGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
324-516 |
1.92e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 43.24 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 324 TPLHAENLSKSY---------GSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTG--VIEaGHGLRIGY 392
Cdd:PRK15112 3 TLLEVRNLSKTFryrtgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGelLID-DHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 393 YAQEHETI-----DVKRS---------VLENMVSASPNLTETE-ARRVLGSFLFTG---DDSHKPAGVLSGGEKTRLALA 454
Cdd:PRK15112 82 YSYRSQRIrmifqDPSTSlnprqrisqILDFPLRLNTDLEPEQrEKQIIETLRQVGllpDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 455 MIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMlelqEKQGISYIYVTQHLGMMKHIS-DQVLVMHQG 226
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
152-218 |
1.98e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 1.98e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 152 LEQPLKTLSGGQRRRIELARILF--SDASTL-ILDEPTNHLDADSVVWLREFLKNYRGG---FIVISHDIELV 218
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSkrSTGRTLyILDEPTTGLHFDDIKKLLEVLQRLVDKgntVVVIEHNLDVI 895
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
443-516 |
2.16e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 2.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA----HYEGAVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEI-ADRVLVMYQG 245
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
154-211 |
2.17e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 43.08 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 154 QPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLK--NYRGGFIVI 211
Cdd:PRK09984 148 QRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVV 207
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
152-217 |
2.27e-04 |
|
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: 41.92 E-value: 2.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 152 LEQPLKTLSGGQRRRIELARILFSDA--STLILDEPTNHLDADSVVWLREFLKNYRG---GFIVISHDIEL 217
Cdd:cd03238 81 LGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDV 151
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
160-218 |
2.40e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.41 E-value: 2.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELV 218
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDvsvqAQVLNLMMDLQQELGLSYVFISHDLSVV 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
158-236 |
2.59e-04 |
|
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: 42.48 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 158 TLSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANRQ 233
Cdd:cd03298 128 ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
...
gi 1552103373 234 VID 236
Cdd:cd03298 208 AAQ 210
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
341-484 |
2.94e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 341 FTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQP--DTGVIEAGhglRIGYYAQEHETIDVkrSVLENMVSASPNLT 418
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaeTSSVVIRG---SVAYVPQVSWIFNA--TVRENILFGSDFES 707
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 419 ETEARRVLGSFL------FTGDDSHK--PAGV-LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDA 484
Cdd:PLN03232 708 ERYWRAIDVTALqhdldlLPGRDLTEigERGVnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDS 782
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
340-516 |
3.08e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 43.56 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 340 IFTAVDLAIDRGSKVVILGLNGAGKTTLLR-ILGGVDQPDTGVieaghGLRIGY--YAQE----HETIDV---------- 402
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKtIASNTDGFHIGV-----EGVITYdgITPEeikkHYRGDVvynaetdvhf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 403 -KRSVLENMVSA----SP-----NLTETEARRVLGSFLFT------------GDDSHKpaGVlSGGEKTRLALAMIVVSG 460
Cdd:TIGR00956 151 pHLTVGETLDFAarckTPqnrpdGVSREEYAKHIADVYMAtyglshtrntkvGNDFVR--GV-SGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 461 ANVLLLDEPTNNLDPASREEILDAL---AHYEGAVVLVSHDEGAVEALNP-ERVLIMPEG 516
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALktsANILDTTPLVAIYQCSQDAYELfDKVIVLYEG 287
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
410-498 |
3.14e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.76 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 410 MVSASPNLTETEARRVLGSFLFTGDDSHK---PAGVLSGGEKTRLALAMIVVSGAN---VLLLDEPTNNLDPASREEILD 483
Cdd:pfam13304 201 DLGEGIEKSLLVDDRLRERGLILLENGGGgelPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLE 280
|
90
....*....|....*...
gi 1552103373 484 ALAHYE---GAVVLVSHD 498
Cdd:pfam13304 281 LLKELSrngAQLILTTHS 298
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
148-234 |
3.15e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 42.38 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 148 PDRILEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS---VVWLREFLKNYRG-GFIVISHDIELVGETVN 223
Cdd:PRK10418 130 AARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqarILDLLESIVQKRAlGMLLVTHDMGVVARLAD 209
|
90
....*....|.
gi 1552103373 224 RVFYLDANRQV 234
Cdd:PRK10418 210 DVAVMSHGRIV 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
326-516 |
3.35e-04 |
|
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: 43.13 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLSKSYGSLEIFTA----VDLAIDRGSKVVILGLNGAGKT----TLLRILggvdqPDTGVIEAGH----------- 386
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEavkgVSFDIAAGETLALVGESGSGKSvtalSILRLL-----PDPAAHPSGSilfdgqdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 387 ---------GLRIGYYAQE---------------HETIDVKRSvlenmvsaspnLTETEAR-RVLGSFLFTG-DDSHKPA 440
Cdd:COG4172 82 serelrrirGNRIAMIFQEpmtslnplhtigkqiAEVLRLHRG-----------LSGAAARaRALELLERVGiPDPERRL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 441 GV----LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA---HYEG-AVVLVSHDEGAVEALnPERVLI 512
Cdd:COG4172 151 DAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlqRELGmALLLITHDLGVVRRF-ADRVAV 229
|
....
gi 1552103373 513 MPEG 516
Cdd:COG4172 230 MRQG 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-218 |
3.46e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 42.80 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE-------------IGYLPQDPRSgdpdelartr 83
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwdirhkIGMVFQNPDN---------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 84 ildarglgQLVLGMQESTIAMSSSDASVSAAGMKKYgtlTDRFLALGGYaaeaeaasiasnLNLPDRileQPLKtLSGGQ 163
Cdd:PRK13650 93 --------QFVGATVEDDVAFGLENKGIPHEEMKER---VNEALELVGM------------QDFKER---EPAR-LSGGQ 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 164 RRRIELARILFSDASTLILDEPTNHLDA----DSVVWLREFLKNYRGGFIVISHDIELV 218
Cdd:PRK13650 146 KQRVAIAGAVAMRPKIIILDEATSMLDPegrlELIKTIKGIRDDYQMTVISITHDLDEV 204
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-49 |
3.51e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|..
gi 1552103373 18 ENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG 49
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-57 |
3.64e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 3.64e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 5 HDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGT 57
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE 322
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-216 |
4.03e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 42.48 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIaskgtidrggeigylpqdprsgdPDELARTRI-LDARGLG---- 91
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLL-----------------------PDDNPNSKItVDGITLTaktv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 92 ----------------QLVLGMQESTIAMSSSDASVSAAGMKKygtLTDRFLAlggyaaeaeaasiasNLNLPDRILEQP 155
Cdd:PRK13640 80 wdirekvgivfqnpdnQFVGATVGDDVAFGLENRAVPRPEMIK---IVRDVLA---------------DVGMLDYIDSEP 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 156 lKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADS----VVWLREFLKNYRGGFIVISHDIE 216
Cdd:PRK13640 142 -ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqiLKLIRKLKKKNNLTVISITHDID 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-191 |
4.10e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.43 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLI-ASKGTIDRGGEIGYLPQDPRsgdpdelartrILDARGLGQLVL 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELShAETSSVVIRGSVAYVPQVSW-----------IFNATVRENILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 96 GMQESTiamsssdasvsaagmKKYGTLTDrflalggyaaeaeAASIASNLNL-PDRILEQPLK---TLSGGQRRRIELAR 171
Cdd:PLN03232 702 GSDFES---------------ERYWRAID-------------VTALQHDLDLlPGRDLTEIGErgvNISGGQKQRVSMAR 753
|
170 180
....*....|....*....|
gi 1552103373 172 ILFSDASTLILDEPTNHLDA 191
Cdd:PLN03232 754 AVYSNSDIYIFDDPLSALDA 773
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
159-236 |
4.37e-04 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 42.00 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADsvvwLR-EFLKNYRG------GFIVISHDIELVGETVNRVFYLDAN 231
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE----LRhEVLKVMQDlaeegmTMVIVTHEIGFAEKVASRLIFIDKG 212
|
....*
gi 1552103373 232 RQVID 236
Cdd:PRK09493 213 RIAED 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-253 |
4.78e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.78 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIdrggeigYLPQDPRSGdpdelartriLDARGLGQL 93
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-------RLDGRPLSS----------LSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 94 VLGMQESTIamsssdasvsaagmkkygTLTDRFLA---LGG-------YAAEAEAASIASNLNLPD----RILEQPlKTL 159
Cdd:PRK10790 417 VAMVQQDPV------------------VLADTFLAnvtLGRdiseeqvWQALETVQLAELARSLPDglytPLGEQG-NNL 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYR--GGFIVISH--------DIELV---GETVNRvf 226
Cdd:PRK10790 478 SVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRehTTLVVIAHrlstiveaDTILVlhrGQAVEQ-- 555
|
250 260
....*....|....*....|....*..
gi 1552103373 227 ylDANRQVIDVYNMNWKNYQRQRAADE 253
Cdd:PRK10790 556 --GTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
388-498 |
5.39e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 388 LRIGYYAQEHETIDVKRSVLENMVSASPNLTETEARRVLgsfLFTGDDshkPAGVLSGGEKTRLALAMIVvsganVLLLD 467
Cdd:COG0419 110 LGLEIYEELKERLKELEEALESALEELAELQKLKQEILA---QLSGLD---PIETLSGGERLRLALADLL-----SLILD 178
|
90 100 110
....*....|....*....|....*....|.
gi 1552103373 468 epTNNLDPASREEILDALAhyegAVVLVSHD 498
Cdd:COG0419 179 --FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
159-216 |
5.53e-04 |
|
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: 41.55 E-value: 5.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVVW--LREFLKNYRGGFIVISHDIE 216
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQegILKFLQDDKRTLVLVTHKLQ 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-215 |
6.11e-04 |
|
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: 41.58 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 26 DGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID------------RGGEIGYLPQDPRSGDPDELARTRILD-----AR 88
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefRGSELQNYFTKLLEGDVKVIVKPQYVDlipkaVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 89 G-LGQLVLGMQEstiamsssdasvsaAGMKKYgtLTDRflalggyaaeaeaasiasnLNLpDRILEQPLKTLSGGQRRRI 167
Cdd:cd03236 105 GkVGELLKKKDE--------------RGKLDE--LVDQ-------------------LEL-RHVLDRNIDQLSGGELQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 168 ELARILFSDASTLILDEPTNHLD------ADSVVwlREFLKNYRgGFIVISHDI 215
Cdd:cd03236 149 AIAAALARDADFYFFDEPSSYLDikqrlnAARLI--RELAEDDN-YVLVVEHDL 199
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
152-218 |
6.40e-04 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 6.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 152 LEQPLKTLSGGQRRRIELARILF--SDASTL-ILDEPTNHLDADSVVWLREFLKN--YRGG-FIVISHDIELV 218
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSkrSTGKTLyILDEPTTGLHFHDVKKLLEVLQRlvDKGNtVVVIEHNLDVI 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
159-236 |
7.36e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 41.65 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDANrQV 234
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAG-QV 232
|
..
gi 1552103373 235 ID 236
Cdd:PRK11022 233 VE 234
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
149-192 |
7.80e-04 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 41.63 E-value: 7.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1552103373 149 DRILEQplktLSGGQRRRIELARILFSDASTLILDEPTNHLDAD 192
Cdd:PRK11432 131 DRYVDQ----ISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
444-516 |
8.29e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 41.63 E-value: 8.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 444 SGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL----AHYEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHDLGVVAGIC-DKVLVMYAG 238
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
159-225 |
8.52e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 42.15 E-value: 8.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRV 225
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
152-201 |
9.38e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.05 E-value: 9.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 152 LEQPLKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFL 201
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLF 189
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
159-190 |
9.52e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 40.72 E-value: 9.52e-04
10 20 30
....*....|....*....|....*....|..
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK10771 130 LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
156-212 |
9.70e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 9.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1552103373 156 LKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKN--YRGGFIVIS 212
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSlaQKGKTIVTS 262
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
443-516 |
1.01e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 41.61 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEG----AVVLVSHDEGAVEALnPERVLIMPEG 516
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKL-ADRVAVMQNG 233
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
329-382 |
1.02e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 1.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 329 ENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVI 382
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
434-512 |
1.07e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 434 DDSHKPAGVLSGGE------KTRLALAMIV--VSGANV--LLLDEPTNNLDPASRE---EILDALAHYEGAVVLVSHDEG 500
Cdd:TIGR00618 942 TGSVRPSATLSGGEtflaslSLALALADLLstSGGTVLdsLFIDEGFGSLDEDSLDraiGILDAIREGSKMIGIISHVPE 1021
|
90
....*....|..
gi 1552103373 501 AVEALnPERVLI 512
Cdd:TIGR00618 1022 FRERI-PHRILV 1032
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-69 |
1.08e-03 |
|
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: 40.25 E-value: 1.08e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1552103373 24 VGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID-RGGEIGYLPQ 69
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEwDGITPVYKPQ 68
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
154-215 |
1.23e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 40.38 E-value: 1.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 154 QPLKTLSGGQRRRIELARILfsdasTLILDepTNHLDADSVVWLREFLKNYRggfiVISHDI 215
Cdd:COG0419 154 DPIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA----IITHVI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
370-519 |
1.25e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 370 ILGGVDQPDTGVIEaghgLRIGYYAQEHETIDVKRSVLENMVSASPNLTETEARRV---------LGSFLFTGDDSHKPA 440
Cdd:PTZ00265 1280 LLDGVDICDYNLKD----LRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRAckfaaidefIESLPNKYDTNVGPY 1355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 441 G-VLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPAS----REEILDALAHYEGAVVLVSHDEGAVEAL-------NPE 508
Cdd:PTZ00265 1356 GkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliEKTIVDIKDKADKTIITIAHRIASIKRSdkivvfnNPD 1435
|
170
....*....|...
gi 1552103373 509 RV--LIMPEGTED 519
Cdd:PTZ00265 1436 RTgsFVQAHGTHE 1448
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-202 |
1.28e-03 |
|
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: 40.32 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDL---IASKGTIDRGGEigylpqdprsgDPDELARTRILDARGL 90
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTegnVSVEGDIHYNGI-----------PYKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 91 GQLVLGMQESTIAMsssdasvsaagmkkygTLTDRFLALGGyaaeaeaasiasnlnlpdrileQPLKTLSGGQRRRIELA 170
Cdd:cd03233 89 SEEDVHFPTLTVRE----------------TLDFALRCKGN----------------------EFVRGISGGERKRVSIA 130
|
170 180 190
....*....|....*....|....*....|..
gi 1552103373 171 RILFSDASTLILDEPTNHLDADSVVwlrEFLK 202
Cdd:cd03233 131 EALVSRASVLCWDNSTRGLDSSTAL---EILK 159
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-225 |
1.37e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGE----------------IGYLPQDP-RSGDPDEL 79
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqalrrdIQFIFQDPyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 80 ARTRILDARGLGQLVLGmqestiamsssdasvsAAGMKKYGTLTDRfLALggyaaeaeaasiasnlnLPDRILEQPlKTL 159
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPG----------------KAAAARVAWLLER-VGL-----------------LPEHAWRYP-HEF 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLD----ADSVVWLREFLKNYRGGFIVISHDIELVGETVNRV 225
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDvsirGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
157-211 |
1.48e-03 |
|
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: 41.54 E-value: 1.48e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVI 211
Cdd:TIGR01257 1060 QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTII 1114
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-229 |
1.49e-03 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 40.15 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGAR----LLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdliaskgtIDRG--GEIGYLPQDPRSG 74
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAG--------LDDGssGEVSLVGQPLHQM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 75 DPDELARTRildARGLGQLVLG-MQESTIAMSSSDASVSAAGMKKYGTLTDRFLALggyaaeaeaasiASNLNLPDRILE 153
Cdd:PRK10584 78 DEEARAKLR---AKHVGFVFQSfMLIPTLNALENVELPALLRGESSRQSRNGAKAL------------LEQLGLGKRLDH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 154 QPLKtLSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVV-WLREFLKNYRGGFIVISHDIELVGETVNRVFYLD 229
Cdd:PRK10584 143 LPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtGDKIAdLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
159-191 |
1.91e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.26 E-value: 1.91e-03
10 20 30
....*....|....*....|....*....|...
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDA 191
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-191 |
2.04e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 14 RLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTIDRGGEIGYLPQDP-------RSG----DPDELARt 82
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAwimnatvRGNilffDEEDAAR- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 rILDARGLGQLVLGMQEstiamsssdasvsaagmkkygtltdrflaLGGyaaeaeaasiasnlNLPDRILEQPLkTLSGG 162
Cdd:PTZ00243 752 -LADAVRVSQLEADLAQ-----------------------------LGG--------------GLETEIGEKGV-NLSGG 786
|
170 180
....*....|....*....|....*....
gi 1552103373 163 QRRRIELARILFSDASTLILDEPTNHLDA 191
Cdd:PTZ00243 787 QKARVSLARAVYANRDVYLLDDPLSALDA 815
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
149-201 |
2.07e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 40.21 E-value: 2.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1552103373 149 DRILEQPlKTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFL 201
Cdd:PRK14267 141 DRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-216 |
2.36e-03 |
|
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: 39.76 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAG-DLIASKGTIDRGGEIgylpQDPrsgDPDEL-------------ART 82
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKQI----TEP---GPDRMvvfqnysllpwltVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 83 RILDA--RGLGQLVLGMQESTIamsssdasvsaagmkkygtltDRFLALGGYAaeaeaasiasnlnlpdRILEQPLKTLS 160
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIV---------------------EEHIALVGLT----------------EAADKRPGQLS 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 161 GGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKN----YRGGFIVISHDIE 216
Cdd:TIGR01184 117 GGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQiweeHRVTVLMVTHDVD 176
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
159-190 |
2.60e-03 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 40.20 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|..
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD 190
Cdd:PRK11607 150 LSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
159-237 |
2.61e-03 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 40.06 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLD---ADSVVwlrEFLK--NYRGG--FIVISHDIELVGETVNRVFYLDAN 231
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSIL---DLLKdiNRELGltIVLITHEMDVVRRICDRVAVLENG 217
|
90
....*....|.
gi 1552103373 232 R-----QVIDV 237
Cdd:COG1135 218 RiveqgPVLDV 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
144-217 |
2.62e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.66 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 144 NLNLPDRILEQPLKTLSGGQRR------RIELARILFSDASTLILDEPTNHLDADSVVWLREF----LKNYRG--GFIVI 211
Cdd:PRK01156 787 NITVSRGGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIieysLKDSSDipQVIMI 866
|
....*.
gi 1552103373 212 SHDIEL 217
Cdd:PRK01156 867 SHHREL 872
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
145-218 |
2.67e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 40.07 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 145 LNLPDRILEQPLKTLSGGQRRRIELARILFSDA---STLILDEPTNHLDADSVVWLREFLK---NYRGGFIVISHDIELV 218
Cdd:pfam13304 223 LLENGGGGELPAFELSDGTKRLLALLAALLSALpkgGLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSPLLL 302
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-218 |
2.76e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 144 NLNLPDRILEQPLKTLSGGQRRRIELARILFSDAS--TLILDEPTNHL---DADSVVWLREFLKNYRGGFIVISHDIELV 218
Cdd:PRK00635 462 DLGLPYLTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMI 541
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
443-485 |
2.85e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.39 E-value: 2.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
443-516 |
2.86e-03 |
|
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: 40.44 E-value: 2.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAH----YEGAVVLVSHDEGAVEALNpERVLIMPEG 516
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDlqreHGLAYLFISHDLAVVRALA-HRVMVMKDG 502
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-213 |
3.00e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 1 MLSVHDLELRVGARLLMENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGdliASKGTIDrGGEIGYLPQDPRSGDPDELA 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG---REDYEVT-GGTVEFKGKDLLELSPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 81 RTRILDARGLGQLVLGMQESTIAMSSSDASVSAAGMKKYgtltDRFlalggyAAEAEAASIASNLNLPDRILEQPLKT-L 159
Cdd:PRK09580 77 GEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQEPL----DRF------DFQDLMEEKIALLKMPEDLLTRSVNVgF 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1552103373 160 SGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGG---FIVISH 213
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkrsFIIVTH 203
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
326-424 |
3.24e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 39.60 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 326 LHAENLsKSYGSLEIftavDLAIDRGSkVVILGLNGAGKTTLLRI----LGGVDQPDTGVieAGHGLRIGYYAQEHET-- 399
Cdd:COG3950 6 LTIENF-RGFEDLEI----DFDNPPRL-TVLVGENGSGKTTLLEAialaLSGLLSRLDDV--KFRKLLIRNGEFGDSAkl 77
|
90 100
....*....|....*....|....*...
gi 1552103373 400 ---IDVKRSVLENMVSASPNLTETEARR 424
Cdd:COG3950 78 ilyYGTSRLLLDGPLKKLERLKEEYFSR 105
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
292-497 |
3.34e-03 |
|
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: 40.12 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 292 ARAEKMLSGLeevravDRVAKLRFPTPM----ACGRTPLHAENLSKSYGSLE------IFTAVDLA-------------- 347
Cdd:TIGR00954 401 ARVDTLLQVL------DDVKSGNFKRPRveeiESGREGGRNSNLVPGRGIVEyqdngiKFENIPLVtpngdvlieslsfe 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 348 IDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAGHGLRIGYYAQE--------HETI-------DVKR-----SVL 407
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRpymtlgtlRDQIiypdsseDMKRrglsdKDL 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 408 ENMvsaspnLTETEARRVL---GSFLFTGDDSHkpagVLSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDA 484
Cdd:TIGR00954 555 EQI------LDNVQLTHILereGGWSAVQDWMD----VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRL 624
|
250
....*....|...
gi 1552103373 485 LAHYEGAVVLVSH 497
Cdd:TIGR00954 625 CREFGITLFSVSH 637
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
29-63 |
3.52e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 37.86 E-value: 3.52e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1552103373 29 KVGLVGRNGAGKTTLTKVLAGD---------LIASKGTIDRGGE 63
Cdd:COG4917 3 RIMLIGRSGAGKTTLTQALNGEeleyrktqaVEYYDNIIDTPGE 46
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
443-516 |
3.59e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 3.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALAHYEG----AVVLVSHDEGAVeALNPERVLIMPEG 516
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQkenmALVLITHDLALV-AEAAHKIIVMYAG 230
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-220 |
3.68e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.48 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 17 MENVSFRVGDGDKVGLVGRNGAGKTTLTKVLAGDLIASKGTID----------RGGEIGYLPQdprSGDPDELARTRILD 86
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptrqalQKNLVAYVPQ---SEEVDWSFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 87 arglgqLVLgmqestiamsssdasvsaagMKKYGTLTdrFLALGGYAAEAEAASIASNLNLPDRILEQpLKTLSGGQRRR 166
Cdd:PRK15056 100 ------VVM--------------------MGRYGHMG--WLRRAKKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1552103373 167 IELARILFSDASTLILDEPTNHLD----ADSVVWLREfLKNYRGGFIVISHDIELVGE 220
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDvkteARIISLLRE-LRDEGKTMLVSTHNLGSVTE 207
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
438-504 |
4.57e-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: 4.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552103373 438 KPAGVLSGGEKTRLALAMIVVSG-ANVL-LLDEPTNNLDPASREEILDALAHYE---GAVVLVSHDEGAVEA 504
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRLRdlgNTLIVVEHDEDTIRA 555
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
154-186 |
4.59e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 4.59e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1552103373 154 QPLKTLSGGQRRRIELARILfSDAST----LILDEPT 186
Cdd:COG0178 822 QPATTLSGGEAQRVKLASEL-SKRSTgktlYILDEPT 857
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
444-513 |
5.02e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 39.18 E-value: 5.02e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552103373 444 SGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDALA----HYEGAVVLVSHDEGAVEALNPErVLIM 513
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMdlqqELGLSYVFISHDLSVVEHIADE-VMVM 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
326-374 |
5.47e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 5.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1552103373 326 LHAENLSKSYGSLEIFTAVDLAIDRGSKVVILGLNGAGKTTLLRILGGV 374
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV 54
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
159-216 |
7.07e-03 |
|
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: 38.63 E-value: 7.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDEPTNHLDADsvvwLREFLKN------YRGG--FIVISHDIE 216
Cdd:TIGR01187 101 LSGGQQQRVALARALVFKPKILLLDEPLSALDKK----LRDQMQLelktiqEQLGitFVFVTHDQE 162
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
345-495 |
7.20e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 345 DLAIDRGSKVVILGLNGAGKTTLLRILGGVDQPDTGVIEAG--HGLRIGYYAQEHETIDVKRSVLENMVSASPNLTETEA 422
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfsHITRLSFEQLQKLVSDEWQRNNTDMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 423 RRVLGsflftgDDSHKPA---------GV----------LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASRE---E 480
Cdd:PRK10938 103 AEIIQ------DEVKDPArceqlaqqfGItalldrrfkyLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQqlaE 176
|
170
....*....|....*
gi 1552103373 481 ILDALAHYEGAVVLV 495
Cdd:PRK10938 177 LLASLHQSGITLVLV 191
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
355-514 |
8.09e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.02 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 355 VILGLNGAGKTTLL-----------RILGGVDQPDTgVIEAGHG-LRIG-YYAQEHETIDVKRSvlenmvsasPNLTETE 421
Cdd:cd03279 32 LICGPTGAGKSTILdaityalygktPRYGRQENLRS-VFAPGEDtAEVSfTFQLGGKKYRVERS---------RGLDYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552103373 422 ARRVLgsFLFTGDDSH---KPAGVLSGGE--KTRLALAMIVVS------GANV--LLLDEPTNNLDPASREEILDALA-- 486
Cdd:cd03279 102 FTRIV--LLPQGEFDRflaRPVSTLSGGEtfLASLSLALALSEvlqnrgGARLeaLFIDEGFGTLDPEALEAVATALEli 179
|
170 180
....*....|....*....|....*....
gi 1552103373 487 HYEGAVVLV-SHDEGAVEALnPERVLIMP 514
Cdd:cd03279 180 RTENRMVGViSHVEELKERI-PQRLEVIK 207
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
157-231 |
8.17e-03 |
|
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: 36.97 E-value: 8.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1552103373 157 KTLSGGQRRRIELARILFSDASTLILDEPTNHLDADSVVWLREFLKNYRGGFIVISHDIELVGETVNRVFYLDAN 231
Cdd:smart00382 59 ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAL 133
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
443-485 |
8.24e-03 |
|
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: 37.86 E-value: 8.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1552103373 443 LSGGEKTRLALAMIVVSGANVLLLDEPTNNLDPASREEILDAL 485
Cdd:cd03244 140 LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
159-205 |
8.97e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 38.93 E-value: 8.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1552103373 159 LSGGQRRRIELARILFSDASTLILDeptnhlDADSVVWLR---EFLKNYR 205
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILD------DALSAVDGRtehQILHNLR 495
|
|
| |
