|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-528 |
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: 601.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHAsDPTQTAL 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPL-DDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMMSA-RDIATIINRIRKAEKEMTDPDPDvmtkaMNRYDKAMQDFDKAGGYAAQSEAISMATSLGLPQEVMEQQLGTLS 161
Cdd:COG0488 80 DTVLDGdAELRALEAELEELEAKLAEPDED-----LERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQIDMYSL 241
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDR--GKLTLYPG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 242 SWKAYLHQRVVDEERRRREREVAEKKAERLMKQGIRLHAKASKAVAAQNMMRRAEKLLENtsEAQKAEKVADIRFPEPAP 321
Cdd:COG0488 233 NYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLERE--EPPRRDKTVEIRFPPPER 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 322 CGRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTL 401
Cdd:COG0488 311 LGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:COG0488 391 DPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEA 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489925987 482 ILKAIAKYEGAIVLVTHDEGAVEALNPeRVLLMPDGDEDLWNDSYLD 528
Cdd:COG0488 471 LEEALDDFPGTVLLVSHDRYFLDRVAT-RILEFEDGGVREYPGGYDD 516
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-499 |
2.15e-87 |
|
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: 279.90 E-value: 2.15e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 28 GDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHAsDPTQTALDR-MMSARDIATIINRIRKAEKE 104
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPgiKVGYLPQEPQL-DPTKTVRENvEEGVAEIKDALDRFNEISAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 105 MTDPDPDvMTKAMNRYDKAMQDFDKAGGYAAQSEaISMAT-SLGLPQEvmEQQLGTLSGGQRRRIELARILFSDADTLIL 183
Cdd:TIGR03719 110 YAEPDAD-FDKLAAEQAELQEIIDAADAWDLDSQ-LEIAMdALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 184 DEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNkvWHLDAQLGQIDMYSLSWKAYLHQRVVDEERRRREREV 263
Cdd:TIGR03719 186 DEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 264 AEKKAERLMkQGIRLHAKA----SKAvaaqnMMRRAEKLLENtsEAQKAEKVADIRFPePAP-CGRTPIMAKDISKAYGS 338
Cdd:TIGR03719 264 RQKTLKREL-EWVRQSPKGrqakSKA-----RLARYEELLSQ--EFQKRNETAEIYIP-PGPrLGDKVIEAENLTKAFGD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 339 NIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTLDLNATVLENLQHVAPEL 418
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKTVWEEISGGLDII 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 419 D----NTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIV 494
Cdd:TIGR03719 415 KlgkrEIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAV 494
|
....*
gi 489925987 495 LVTHD 499
Cdd:TIGR03719 495 VISHD 499
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-520 |
8.31e-82 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 264.45 E-value: 8.31e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHASDpTQT 80
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPneRLGKLRQDQFAFE-EFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALD----------RMMSARDiatiinRIRkAEKEMTDPDpdvmtkAMNRYDKAMQdFDKAGGYAAQSEAISMATSLGLPq 150
Cdd:PRK15064 81 VLDtvimghtelwEVKQERD------RIY-ALPEMSEED------GMKVADLEVK-FAEMDGYTAEARAGELLLGVGIP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 151 evMEQQLGTLSG---GQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVW 227
Cdd:PRK15064 146 --EEQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 228 HLDaqLGQIDMYSLSWKAYLHQRVVDEerrrrerevaekkaERLMKQgirlHAKASKAVAA-QNMMRR----AEKLLENT 302
Cdd:PRK15064 224 DLD--YGELRVYPGNYDEYMTAATQAR--------------ERLLAD----NAKKKAQIAElQSFVSRfsanASKAKQAT 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 303 SEAQKAEKV--AD----------IRFPEPAPCGRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLR 370
Cdd:PRK15064 284 SRAKQIDKIklEEvkpssrqnpfIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 371 LLAHIEEPDTGSVEYGHGCKIGYFAQEH-DTLDLNATVLENLQHVAPELDNTQA-RSILGSFLFSGDDAMKPAHVLSGGE 448
Cdd:PRK15064 364 TLVGELEPDSGTVKWSENANIGYYAQDHaYDFENDLTLFDWMSQWRQEGDDEQAvRGTLGRLLFSQDDIKKSVKVLSGGE 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 449 KTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTHDEGAVEALnPERVL-LMPDGDED 520
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSL-ATRIIeITPDGVVD 515
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
28-499 |
2.16e-81 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 264.29 E-value: 2.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 28 GDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHAsDPTQTALDRMMSA-RDIATIINRIRKAEKE 104
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgiKVGYLPQEPQL-DPEKTVRENVEEGvAEVKAALDRFNEIYAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 105 MTDPDPDvMTKAMNRYDKAMQDFDKAGGYAAQSEaISMA-TSLGLPQevMEQQLGTLSGGQRRRIELARILFSDADTLIL 183
Cdd:PRK11819 112 YAEPDAD-FDALAAEQGELQEIIDAADAWDLDSQ-LEIAmDALRCPP--WDAKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 184 DEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNkvWHLDAQLGQIDMYSLSWKAYLHQrvvdeerrrrerev 263
Cdd:PRK11819 188 DEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILELDRGRGIPWEGNYSSWLEQ-------------- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 264 aekKAERLMKQG----------------IRLHAKA----SKAvaaqnMMRRAEKLLenTSEAQKAEKVADIRFPePAP-C 322
Cdd:PRK11819 252 ---KAKRLAQEEkqeaarqkalkrelewVRQSPKArqakSKA-----RLARYEELL--SEEYQKRNETNEIFIP-PGPrL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 323 GRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTLD 402
Cdd:PRK11819 321 GDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 LNATVLENlqhVAPELDNTQ-------ARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD 475
Cdd:PRK11819 401 PNKTVWEE---ISGGLDIIKvgnreipSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
490 500
....*....|....*....|....*..
gi 489925987 476 P---ASREEilkAIAKYEGAIVLVTHD 499
Cdd:PRK11819 478 VetlRALEE---ALLEFPGCAVVISHD 501
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-499 |
1.03e-79 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 262.03 E-value: 1.03e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 8 LEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHASDptQTALDRM 85
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwQLAWVNQETPALP--QPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 MSARdiatiiNRIRKAEKEMTDPDPDVMTKAMNRYDKAMqdfDKAGGYAAQSEAISMATSLGLPQEVMEQQLGTLSGGQR 165
Cdd:PRK10636 85 IDGD------REYRQLEAQLHDANERNDGHAIATIHGKL---DAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 166 RRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAQlgQIDMYSLSWKA 245
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQ--SLFEYTGNYSS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 246 YLHQRVVDEERRRREREVAEKKAERLMKQGIRLHAKASKAVAAQNMMrraeKLLENTSEAQKAEKVADIRF----PEPAP 321
Cdd:PRK10636 234 FEVQRATRLAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRI----KMLERMELIAPAHVDNPFHFsfraPESLP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 322 cgrTPIMAKD-ISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEH-D 399
Cdd:PRK10636 310 ---NPLLKMEkVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQlE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:PRK10636 387 FLRADESPLQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
490 500
....*....|....*....|
gi 489925987 480 EEILKAIAKYEGAIVLVTHD 499
Cdd:PRK10636 467 QALTEALIDFEGALVVVSHD 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
17-499 |
6.49e-66 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 225.21 E-value: 6.49e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL--GYLPQDThASDPTQTALDRmmsardIATI 94
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLivARLQQDP-PRNVEGTVYDF------VAEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 95 INRIRKAEKE--------MTDPdpdvMTKAMNRYDKAMQDFDKAGGYAAQSEAISMATSLGLPQEvmeQQLGTLSGGQRR 166
Cdd:PRK11147 91 IEEQAEYLKRyhdishlvETDP----SEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPD---AALSSLSGGWLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 167 RIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQIDMYSLSWKAY 246
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDR--GKLVSYPGNYDQY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 247 LHQRVVDEERRRREREVAEKK---AERLMKQGIrlhakasKAVAAQNMMR-RAEKLL-ENTSEAQKAEKVADIRFPEPAP 321
Cdd:PRK11147 242 LLEKEEALRVEELQNAEFDRKlaqEEVWIRQGI-------KARRTRNEGRvRALKALrRERSERREVMGTAKMQVEEASR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 322 CGRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTL 401
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENL----QHVapeLDNTQARSILG---SFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:PRK11147 395 DPEKTVMDNLaegkQEV---MVNGRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
490 500
....*....|....*....|....*
gi 489925987 475 DPASREEILKAIAKYEGAIVLVTHD 499
Cdd:PRK11147 472 DVETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
3-506 |
1.54e-64 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 223.20 E-value: 1.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG---DMLPTAGKVRvsgklgYLPQDTHASDPT- 78
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaiDGIPKNCQIL------HVEQEVVGDDTTa 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 -----QTALDRMMSARDIATIINRIRKAE----------KEMTDPDPDVMTKAMNRYDKAMQDFDkagGYAAQSEAISMA 143
Cdd:PLN03073 252 lqcvlNTDIERTQLLEEEAQLVAQQRELEfetetgkgkgANKDGVDKDAVSQRLEEIYKRLELID---AYTAEARAASIL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 144 TSLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVV 223
Cdd:PLN03073 329 AGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVV 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 224 NKVWHLDAQlgQIDMYSLSWKAYlHQRVVDEERRRREREVAEKKAERLMKQGI-RLHAKASKAVAAQNMMrraeKLLENT 302
Cdd:PLN03073 409 TDILHLHGQ--KLVTYKGDYDTF-ERTREEQLKNQQKAFESNERSRSHMQAFIdKFRYNAKRASLVQSRI----KALDRL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 303 SEAQKAEKVADIRFPEPAPCGR--TPIMA-KDISKAY-GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEP 378
Cdd:PLN03073 482 GHVDAVVNDPDYKFEFPTPDDRpgPPIISfSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQP 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 379 DTGSVEYGHGCKIGYFAQEH-DTLDLNATVLENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATL 457
Cdd:PLN03073 562 SSGTVFRSAKVRMAVFSQHHvDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKI 641
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 458 VTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTHDE----GAVEAL 506
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEhlisGSVDEL 694
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-249 |
1.38e-48 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 175.64 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDTHASDPTQT 80
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGEtvKIGYFDQHQEELDPDKT 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDRMMSARDIATiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaQSEAISMATSLGLPQEVMEQQLGTL 160
Cdd:COG0488 396 VLDELRDGAPGGT------------------------------------------EQEVRGYLGRFLFSGDDAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQIDMYS 240
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFED--GGVREYP 511
|
....*....
gi 489925987 241 LSWKAYLHQ 249
Cdd:COG0488 512 GGYDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-232 |
7.54e-48 |
|
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: 162.62 E-value: 7.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQdthasdptqt 80
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGStvKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 aldrmmsardiatiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaismatslglpqevmeqqlgtL 160
Cdd:cd03221 71 -------------------------------------------------------------------------------L 71
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAQ 232
Cdd:cd03221 72 SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
327-499 |
4.96e-44 |
|
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: 152.60 E-value: 4.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQehdtldlnat 406
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 407 vlenlqhvapeldntqarsilgsflfsgddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI 486
Cdd:cd03221 71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
|
170
....*....|...
gi 489925987 487 AKYEGAIVLVTHD 499
Cdd:cd03221 114 KEYPGTVILVSHD 126
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-517 |
4.45e-39 |
|
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: 149.28 E-value: 4.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQI--GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGkvRVSGKLGYLPQDTHASDPTQ 79
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGG--RISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 TALDRMMSARDIATIINRIRKAEkemtdpdpDVMTKAMNRydkamqdfdKAGGYAAQSEAISMATSLGLpQEVMEQQLGT 159
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPVTVGD--------QIAEALENL---------GLSRAEARARVLELLEAVGL-ERRLDRYPHQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQ 235
Cdd:COG1123 143 LSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD--GR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 236 IdmyslswkaylhqrvvdeerrrrereVAEKKAERLMKQGIRLHA---KASKAVAAQNMMRRAEKLLEntseaqkaekva 312
Cdd:COG1123 221 I--------------------------VEDGPPEEILAAPQALAAvprLGAARGRAAPAAAAAEPLLE------------ 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 313 dirfpepapcgrtpimAKDISKAYGSNI-----VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG- 386
Cdd:COG1123 263 ----------------VRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDg 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 387 -------------HGCKIGYFAQEHDTLdLNA--TV-------LENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVL 444
Cdd:COG1123 327 kdltklsrrslreLRRRVQMVFQDPYSS-LNPrmTVgdiiaepLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHEL 405
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 445 SGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA----KYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlqrELGLTYLFISHDLAVVRYIA-DRVAVMYDG 481
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
329-517 |
1.13e-36 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 133.68 E-value: 1.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC---------KIGYFAQEh 398
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIkkepeevkrRIGYLPEE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DTLDLNATVLENLQhvapeldntqarsilgsflfsgddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:cd03230 82 PSLYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 479 REEILKAIAKY---EGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03230 131 RREFWELLRELkkeGKTILLSSHILEEAERLC-DRVAILNNG 171
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
329-517 |
8.36e-36 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 8.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC-----------KIGYFAQE 397
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 HDTLDlnATVLENLQHVA----PELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALA-TLVTSRAnVLLLDEPTN 472
Cdd:COG4619 83 PALWG--GTVRDNLPFPFqlreRKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIrALLLQPD-VLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 473 NLDPASREEILKAIAKY----EGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:COG4619 160 ALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVA-DRVLTLEAG 207
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
327-533 |
2.94e-35 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 132.11 E-value: 2.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC---------KIGYFAQ 396
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EhDTLDLNATVLENLQHVAP--ELDNTQARSILGSFL--FS-GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:COG1131 81 E-PALYPDLTVRENLRFFARlyGLPRKEARERIDELLelFGlTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 472 NNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEALnPERVLLMPDG-----------DEDLWNDSYLDLVAEE 533
Cdd:COG1131 160 SGLDPEARRELwelLRELAAEGKTVLLSTHYLEEAERL-CDRVAIIDKGrivadgtpdelKARLLEDVFLELTGEE 234
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
329-505 |
1.10e-34 |
|
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: 129.52 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG----HGCKIGYFAQ-----EHD 399
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgepiRDAREDYRRRlaylgHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVA----PELDNTQARSILGSF-LfsGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:COG4133 85 GLKPELTVRENLRFWAalygLRADREAIDEALEAVgL--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 475 DPASREEILKAIAKY---EGAIVLVTHDEGAVEA 505
Cdd:COG4133 163 DAAGVALLAELIAAHlarGGAVLLTTHQPLELAA 196
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-222 |
2.13e-34 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 129.80 E-value: 2.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQ 70
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DthasdptqTALDRMMSARDIATIINRIRKAEKEmtdpdpdvmtKAMNRYDKAMQDFdkaggyaaqseaismatslGLpQ 150
Cdd:COG1131 81 E--------PALYPDLTVRENLRFFARLYGLPRK----------EARERIDELLELF-------------------GL-T 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 151 EVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHsteLLDEV 222
Cdd:COG1131 123 DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTH---YLEEA 194
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
330-517 |
2.99e-34 |
|
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: 128.35 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-----------HGCKIGYFAQ 396
Cdd:cd03225 3 KNLSFSYPDGARPAldDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkeLRRKVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLDLNATV-------LENLQhVAPELDNTQARSILGSFLFSGDDAmKPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:cd03225 83 NPDDQFFGPTVeeevafgLENLG-LPEEEIEERVEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 470 PTNNLDPASREEILKAIAKY--EG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLEL-ADRVIVLEDG 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
327-517 |
1.15e-33 |
|
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: 127.67 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGC-----------KIGYFA 395
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEdvrkeprearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHDtLDLNATVLENLQHVAP------ELDNTQARSILGSFLFSgDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:COG4555 81 DERG-LYDRLTVRENIRYFAElyglfdEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 470 PTNNLDPASRE---EILKAIAKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:COG4555 159 PTNGLDVMARRllrEILRALKKEGKTVLFSSHIMQEVEALC-DRVVILHKG 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
2.04e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 127.13 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------LGYLPQdT 72
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKpprrarrrIGYVPQ-R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 73 HASDPTQ--TALDRMMSARDIAT-IINRIRKAEKEMTDpdpdvmtKAMNRYDkaMQDFdkaggyaaqseaismatslglp 149
Cdd:COG1121 84 AEVDWDFpiTVRDVVLMGRYGRRgLFRRPSRADREAVD-------EALERVG--LEDL---------------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 150 qevMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHSTELLDEVVNKV 226
Cdd:COG1121 133 ---ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrrEGkTILVVTHDLGAVREYFDRV 209
|
....*..
gi 489925987 227 WHLDAQL 233
Cdd:COG1121 210 LLLNRGL 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-231 |
4.37e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 125.31 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGYLP 69
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrrqVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 70 QDTHASDPTqtaldrmmsARDIATIINRIRKAEkemtdPDPDVMTKAMNRydkamqdfdkaggyaaqseaismatsLGLP 149
Cdd:COG4619 81 QEPALWGGT---------VRDNLPFPFQLRERK-----FDRERALELLER--------------------------LGLP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 150 QEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGYLKKYEGGFLVISHSTELLDEVVNK 225
Cdd:COG4619 121 PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADR 200
|
....*.
gi 489925987 226 VWHLDA 231
Cdd:COG4619 201 VLTLEA 206
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-226 |
1.70e-32 |
|
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: 124.58 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQ 70
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DTHASDptqtaldrMMSARDIATIINRIRKAEKEmtdpdpdvmtKAMNRYDKAMQDFDkaggyaaqseaisMatslglpQ 150
Cdd:COG4555 82 ERGLYD--------RLTVRENIRYFAELYGLFDE----------ELKKRIEELIELLG-------------L-------E 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 151 EVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY---EGGFLVISHSTELLDEVVNKV 226
Cdd:COG4555 124 EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRV 202
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-222 |
3.08e-32 |
|
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: 122.59 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASD---- 76
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRlayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 PTQTALDRMMSARDIATIINRIRKAEKEMTDPDpdvmtkamnrydkamqdfdkaggyaaqsEAISMatsLGLpQEVMEQQ 156
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAID----------------------------EALEA---VGL-AGLADLP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 157 LGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGG-FLVISHSTELLDEV 222
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlaRGGaVLLTTHQPLELAAA 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
327-517 |
9.08e-32 |
|
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: 122.06 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY-GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-----------HGCKIGYF 394
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkditkknlreLRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHDTLDLNATVLENlqhVA--PE---LDNTQARSILgsflfsgDDAM----------KPAHVLSGGEKTRLALATLVT 459
Cdd:COG1122 81 FQNPDDQLFAPTVEED---VAfgPEnlgLPREEIRERV-------EEALelvglehladRPPHELSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 460 SRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHD-EGAVEalNPERVLLMPDG 517
Cdd:COG1122 151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDlDLVAE--LADRVIVLDDG 210
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
329-517 |
1.28e-31 |
|
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: 119.27 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHgckigyfaqehdtldlnatvl 408
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 409 enlqHVAPELDNTQARSILGsFLFSgddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAK 488
Cdd:cd00267 61 ----KDIAKLPLEELRRRIG-YVPQ----------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 489 Y--EG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd00267 126 LaeEGrTVIIVTHDPELAELA-ADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-233 |
2.15e-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: 120.72 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 4 EAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------LGYLPQdTHAS 75
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKplekerkrIGYVPQ-RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 76 DPTQ--TALDRMMSARDIAT-IINRIRKAEKEmtdpdpdvmtKAMnrydkamqdfdkaggyaaqsEAISMatsLGLpQEV 152
Cdd:cd03235 80 DRDFpiSVRDVVLMGLYGHKgLFRRLSKADKA----------KVD--------------------EALER---VGL-SEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 153 MEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGyLKKYEGGFLVISHSTELLDEVVNKVWH 228
Cdd:cd03235 126 ADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqediYELLRE-LRREGMTILVVTHDLGLVLEYFDRVLL 204
|
....*
gi 489925987 229 LDAQL 233
Cdd:cd03235 205 LNRTV 209
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-517 |
2.51e-31 |
|
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: 120.69 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGCK---------IGYF 394
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYiNGYSIRtdrkaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQeHDTLDLNATVLENLQHVA-----PELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:cd03263 81 PQ-FDALFDELTVREHLRFYArlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 470 PTNNLDPASREEILKAIAKYEG--AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALC-DRIAIMSDG 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
327-517 |
8.22e-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: 119.13 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------- 389
Cdd:cd03255 1 IELKNLSKTYggGGEKVQAlkGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-GTdisklsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 ---KIGYFAQEHDTLDlNATVLEN------LQHVAPELDNTQARSILGSF-LfsGDDAMKPAHVLSGGEKTRLALATLVT 459
Cdd:cd03255 80 rrrHIGFVFQSFNLLP-DLTALENvelpllLAGVPKKERRERAEELLERVgL--GDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 460 SRANVLLLDEPTNNLDPASREEI---LKAIAKYEG-AIVLVTHDEGAVEALnpERVLLMPDG 517
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVmelLRELNKEAGtTIVVVTHDPELAEYA--DRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
327-517 |
8.28e-31 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 119.38 E-value: 8.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GH-------------- 387
Cdd:COG1136 5 LELRNLTKSYgtGEGEVTAlrGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQdisslserelarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 388 GCKIGYFAQEH---DTLdlnaTVLEN------LQHVAPELDNTQARSILGSF-LfsGDDAMKPAHVLSGGEKTRLALA-T 456
Cdd:COG1136 85 RRHIGFVFQFFnllPEL----TALENvalpllLAGVSRKERRERARELLERVgL--GDRLDHRPSQLSGGQQQRVAIArA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 457 LVTsRANVLLLDEPTNNLDPASREEI---LKAIAKYEG-AIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:COG1136 159 LVN-RPKLILADEPTGNLDSKTGEEVlelLRELNRELGtTIVMVTHDPELAARAD--RVIRLRDG 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
329-499 |
1.01e-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: 120.15 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------KIGYFAQ 396
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD-GRdlaslsrrelarRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTlDLNATVLE-----------NLQHVAPElDNTQARSIL-----GSFlfsgddAMKPAHVLSGGEKTRLALATLVTS 460
Cdd:COG1120 83 EPPA-PFGLTVRElvalgryphlgLFGRPSAE-DREAVEEALertglEHL------ADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 461 RANVLLLDEPTNNLDPASREEIL---KAIAKYEG-AIVLVTHD 499
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLellRRLARERGrTVVMVLHD 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
330-517 |
1.28e-30 |
|
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: 117.29 E-value: 1.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-------------HGCKIGYFAQ 396
Cdd:cd03229 4 KNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedltdledelppLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHdTLDLNATVLENLqhvapeldntqarsilgsflfsgddamkpAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDP 476
Cdd:cd03229 84 DF-ALFPHLTVLENI-----------------------------ALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 477 ASREEI---LKAIAKYEG-AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03229 134 ITRREVralLKSLQAQLGiTVVLVTHDLDEAARLA-DRVVVLRDG 177
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
330-517 |
2.10e-30 |
|
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: 118.01 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HGCKIGYFAQeHDT 400
Cdd:cd03259 4 KGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrdvtgvppERRNIGMVFQ-DYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLNATVLEN----LQHVAPELDNTQARSILGSFLFS-GDDAMKPAHVLSGGEKTRLALA-TLVTsRANVLLLDEPTNNL 474
Cdd:cd03259 83 LFPHLTVAENiafgLKLRGVPKAEIRARVRELLELVGlEGLLNRYPHELSGGQQQRVALArALAR-EPSLLLLDEPLSAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 475 DPASREEILKAIAKYEGA----IVLVTHDEGavEALN-PERVLLMPDG 517
Cdd:cd03259 162 DAKLREELREELKELQRElgitTIYVTHDQE--EALAlADRIAVMNEG 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-191 |
2.27e-29 |
|
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: 116.30 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGYL 68
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRdlaslsrrelarrIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQDTHASDPtqtaldrmMSARDIAtiinrirkaekemtdpdpdvmtkAMNR--YDKAMQDFDKAgGYAAQSEAISMatsL 146
Cdd:COG1120 81 PQEPPAPFG--------LTVRELV-----------------------ALGRypHLGLFGRPSAE-DREAVEEALER---T 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 147 GLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG1120 126 GL-EHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-188 |
5.12e-29 |
|
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: 111.97 E-value: 5.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHaSDPTQTALDR 84
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslrkEIGYVFQDPQ-LFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMSARDIATIINRIRKAEkemtdpdpdvMTKAMNRYDkaMQDFDKaggyaaqseaismatslglpqEVMEQQLGTLSGGQ 164
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR----------AEEALEKLG--LGDLAD---------------------RPVGERPGTLSGGQ 126
|
170 180
....*....|....*....|....
gi 489925987 165 RRRIELARILFSDADTLILDEPTN 188
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
327-517 |
1.30e-28 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 113.22 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC---------------K 390
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-GQdlsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQEHDTLDlNATVLENL------QHVAPELDNTQARSILGSF-LfsGDDAMKPAHVLSGGEKTRLALAtlvtsRA- 462
Cdd:COG2884 81 IGVVFQDFRLLP-DRTVYENValplrvTGKSRKEIRRRVREVLDLVgL--SDKAKALPHELSGGEQQRVAIA-----RAl 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 463 -N---VLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:COG2884 153 vNrpeLLLADEPTGNLDPETSWEImelLEEINRRGTTVLIATHDLELVDRM-PKRVLELEDG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
329-517 |
1.56e-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: 111.76 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhgckigyfaqEHDTLDLNATVL 408
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD----------GKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 409 enLQHVA--PeldntQARSILGSFLFsgddAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL--- 483
Cdd:cd03214 72 --ARKIAyvP-----QALELLGLAHL----ADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLell 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 484 KAIAKYEG-AIVLVTHDegaveaLNP-----ERVLLMPDG 517
Cdd:cd03214 141 RRLARERGkTVVMVLHD------LNLaaryaDRVILLKDG 174
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
317-517 |
2.06e-28 |
|
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: 119.10 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 317 PEPAPcGRTPIMAKDISKAY--GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC----- 389
Cdd:COG4987 325 PAPAP-GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG-GVdlrdl 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 -------KIGYFAQEHDTLDlnATVLENLQHVAPELDNTQARSI-----LGSFLFS---------GDDAMKpahvLSGGE 448
Cdd:COG4987 403 deddlrrRIAVVPQRPHLFD--TTLRENLRLARPDATDEELWAAlervgLGDWLAAlpdgldtwlGEGGRR----LSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 449 KTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EGAIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLERMD--RILVLEDG 545
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-230 |
3.65e-28 |
|
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: 110.03 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 4 EAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptqtald 83
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 84 rmmsarDIATIINRIRKAEkemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaISMatslgLPQevmeqqlgtLSGG 163
Cdd:cd00267 62 ------DIAKLPLEELRRR-------------------------------------IGY-----VPQ---------LSGG 84
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY-EGG--FLVISHSTELLDEVVNKVWHLD 230
Cdd:cd00267 85 QRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaEEGrtVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-236 |
5.42e-28 |
|
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: 109.79 E-value: 5.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQ 70
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGkdikkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DthasdptqTALDRMMSARDIAtiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaismatslglpq 150
Cdd:cd03230 81 E--------PSLYENLTVRENL---------------------------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 151 evmeqqlgTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGG-FLVISHSTELLDEVVNKVW 227
Cdd:cd03230 95 --------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkEGKtILLSSHILEEAERLCDRVA 166
|
....*....
gi 489925987 228 HLDAqlGQI 236
Cdd:cd03230 167 ILNN--GRI 173
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-517 |
6.03e-28 |
|
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: 117.21 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG--DMLPTAGKV--RVS--GKLGYL-------- 68
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIiyHVAlcEKCGYVerpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 ----------PQDTHASDPTQTALDRMMsaRDIATIINRIRKAEKEMTdpdpdVMTKAMNrydkAMQDFdkagGYAAQsE 138
Cdd:TIGR03269 81 pcpvcggtlePEEVDFWNLSDKLRRRIR--KRIAIMLQRTFALYGDDT-----VLDNVLE----ALEEI----GYEGK-E 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 139 AISMATSLgLPQEVMEQQLG----TLSGGQRRRIELARILFSDADTLILDEPTNHLD---ADSI-EWLRGYLKKYEGGFL 210
Cdd:TIGR03269 145 AVGRAVDL-IEMVQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtAKLVhNALEEAVKASGISMV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 211 VISHSTELLDEVVNK-VWhldaqlgqidmyslswkaylhqrvvdeerrrrerevaekkaerLMKQGIRLHAKASKAVAaq 289
Cdd:TIGR03269 224 LTSHWPEVIEDLSDKaIW-------------------------------------------LENGEIKEEGTPDEVVA-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 290 nmmrraeKLLENTSEAQKAEKVAdirfpepapCGRTPIMAKDISKAYGS---NIVFA--GVNLAIDKGSRVVILGYNGAG 364
Cdd:TIGR03269 259 -------VFMEGVSEVEKECEVE---------VGEPIIKVRNVSKRYISvdrGVVKAvdNVSLEVKEGEIFGIVGTSGAG 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 365 KTTTLRLLAHIEEPDTGSVEYGHGCK------------------IGYFAQEHDtLDLNATVLENLQ-----HVAPELDNT 421
Cdd:TIGR03269 323 KTTLSKIIAGVLEPTSGEVNVRVGDEwvdmtkpgpdgrgrakryIGILHQEYD-LYPHRTVLDNLTeaiglELPDELARM 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 422 QARSILGSFLFSGDDAM----KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR----EEILKAIAKYEGAI 493
Cdd:TIGR03269 402 KAVITLKMVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEMEQTF 481
|
570 580
....*....|....*....|....
gi 489925987 494 VLVTHDEGAVEALNpERVLLMPDG 517
Cdd:TIGR03269 482 IIVSHDMDFVLDVC-DRAALMRDG 504
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-230 |
1.90e-27 |
|
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: 109.48 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPTQTAldrmmsaRDIA 92
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK------DLTKLSLKELR-------RKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIinrirkaekeMTDPD---------PDVMTKAMNRYDKAmqdfdkaggyAAQSEAISMATSLGLPQEVMEQQLGTLSGG 163
Cdd:cd03225 79 LV----------FQNPDdqffgptveEEVAFGLENLGLPE----------EEIEERVEEALELVGLEGLRDRSPFTLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHSTELLDEVVNKVWHLD 230
Cdd:cd03225 139 QKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaEGkTIIIVTHDLDLLLELADRVIVLE 208
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-514 |
2.73e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.18 E-value: 2.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG------HGCKIGYFAQeHDT 400
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQ-RAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLN--ATVLE----------NLQHVAPELDNTQARSILgsflfsgdDAM-------KPAHVLSGGEKTRLALATLVTSR 461
Cdd:COG1121 86 VDWDfpITVRDvvlmgrygrrGLFRRPSRADREAVDEAL--------ERVgledladRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 462 ANVLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEALNPeRVLLM 514
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALyelLRELRREGKTILVVTHDLGAVREYFD-RVLLL 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
327-517 |
2.75e-26 |
|
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: 105.16 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI--VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK----------IGY 393
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLRdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQehDTLDLNATVLENLqhvapeldntqarsilgsflfsgddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNN 473
Cdd:cd03228 81 VPQ--DPFLFSGTIRENI--------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 474 LDPASREEILKAIAKYEG--AIVLVTHDEGAVEalNPERVLLMPDG 517
Cdd:cd03228 127 LDPETEALILEALRALAKgkTVIVIAHRLSTIR--DADRIIVLDDG 170
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
327-499 |
1.32e-25 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 105.52 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY-GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHG-------------CKI 391
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILvDGQDvtalrgralrrlrRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 GYFAQEHDtLDLNATVLEN-----LQHVAPeldntqARSILGsfLFSGDD----------------AMKPAHVLSGGEKT 450
Cdd:COG3638 83 GMIFQQFN-LVPRLSVLTNvlagrLGRTST------WRSLLG--LFPPEDreralealervgladkAYQRADQLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 451 RLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVT-HD 499
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVmdlLRRIAREDGITVVVNlHQ 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-227 |
1.91e-25 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 110.43 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 4 EAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL--GYLPQDTHASDPTQTA 81
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLevAYFDQHRAELDPEKTV 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 LDrmmsardiatiinrirkaekEMTDPDPDVMTKAMNR----YdkaMQDFdkaggyaaqseaismatsLGLPQEVMeQQL 157
Cdd:PRK11147 401 MD--------------------NLAEGKQEVMVNGRPRhvlgY---LQDF------------------LFHPKRAM-TPV 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVW 227
Cdd:PRK11147 439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECW 508
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
327-499 |
1.97e-25 |
|
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: 104.09 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY------GHGCKIGYFAQ 396
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLDLnATVLEN------LQHVAPELDNTQARSILGSFLFSGDDAMKPaHVLSGGEKTRLALA-TLVTsRANVLLLDE 469
Cdd:cd03293 81 QDALLPW-LTVLDNvalgleLQGVPKAEARERAEELLELVGLSGFENAYP-HQLSGGMRQRVALArALAV-DPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 470 PTNNLDPASR----EEILKAIAKYEGAIVLVTHD 499
Cdd:cd03293 158 PFSALDALTReqlqEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
344-472 |
3.01e-25 |
|
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: 101.57 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC-----------KIGYFAQeHDTLDLNATVLENLQ 412
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQ-DPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 413 HVAPELDNT---------QARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTN 472
Cdd:pfam00005 82 LGLLLKGLSkrekdaraeEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
329-514 |
4.38e-25 |
|
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: 103.00 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY------GHGCKIGYFAQEHDTL- 401
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRSIDr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLE-----NLQHVAP----------ELDNTQARSILGSFlfsgddAMKPAHVLSGGEKTRLALATLVTSRANVLL 466
Cdd:cd03235 82 DFPISVRDvvlmgLYGHKGLfrrlskadkaKVDEALERVGLSEL------ADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 467 LDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEGAVEALNPeRVLLM 514
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELrrEGmTILVVTHDLGLVLEYFD-RVLLL 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-236 |
5.55e-25 |
|
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: 108.69 E-value: 5.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQ-IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGY 67
Cdd:COG4988 336 SIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdldpaswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQDTHasdptqtaldrmmsardI--ATIINRIRkaekeMTDPDPDvmtkamnryDKAMQDfdkAggyAAQSEAISMATS 145
Cdd:COG4988 416 VPQNPY-----------------LfaGTIRENLR-----LGRPDAS---------DEELEA---A---LEAAGLDEFVAA 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 146 L--GLPQEVMEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDE 221
Cdd:COG4988 459 LpdGLDTPLGEGGRG-LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ 537
|
250
....*....|....*
gi 489925987 222 vVNKVWHLDAqlGQI 236
Cdd:COG4988 538 -ADRILVLDD--GRI 549
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
327-517 |
5.89e-25 |
|
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: 102.61 E-value: 5.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQEHDTL----- 401
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKLTDDKKNINELrqkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 ------DL--NATVLENL-------QHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLL 466
Cdd:cd03262 80 mvfqqfNLfpHLTVLENItlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQ-LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 467 LDEPTNNLDPASREEIL---KAIAKyEG-AIVLVTHDEG-AVEALNpeRVLLMPDG 517
Cdd:cd03262 159 FDEPTSALDPELVGEVLdvmKDLAE-EGmTMVVVTHEMGfAREVAD--RVIFMDDG 211
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
327-517 |
8.96e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 102.76 E-value: 8.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGCKIGyfAQEHDTLDL--- 403
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD-GEDLT--DSKKDINKLrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 ------------NATVLENL-------QHVAPELDNTQARSILGSF-LfsGDDAMK-PAHvLSGGEKTRLALAtlvtsRA 462
Cdd:COG1126 79 vgmvfqqfnlfpHLTVLENVtlapikvKKMSKAEAEERAMELLERVgL--ADKADAyPAQ-LSGGQQQRVAIA-----RA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 463 -----NVLLLDEPTNNLDPASREEILKAI---AKyEG-AIVLVTHDEG-AVEALNpeRVLLMPDG 517
Cdd:COG1126 151 lamepKVMLFDEPTSALDPELVGEVLDVMrdlAK-EGmTMVVVTHEMGfAREVAD--RVVFMDGG 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-236 |
1.19e-24 |
|
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: 102.41 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDthasdP-T 78
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVFQN-----PdD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 Q----TALDrmmsarDIATIINRIRKAEKEMTDpdpdvmtkamnRYDKAMQDFDkAGGYAAQSeaismatslglPQEvme 154
Cdd:COG1122 87 QlfapTVEE------DVAFGPENLGLPREEIRE-----------RVEEALELVG-LEHLADRP-----------PHE--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 155 qqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHSTELLDEVVNKVWHLDA 231
Cdd:COG1122 135 -----LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkEGkTVIIVTHDLDLVAELADRVIVLDD 209
|
....*
gi 489925987 232 qlGQI 236
Cdd:COG1122 210 --GRI 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
329-517 |
1.31e-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: 101.59 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-------YGHGCKIGYFAQEHDtL 401
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldIAARNRIGYLPEERG-L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENLQHVAP--ELDNTQARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDP 476
Cdd:cd03269 82 YPKMKVIDQLVYLAQlkGLKKEEARRRIDEWLERlelSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 477 ASREEILKAIAKYEGA---IVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03269 162 VNVELLKDVIRELARAgktVILSTHQMELVEEL-CDRVLLLNKG 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
13-238 |
1.82e-24 |
|
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: 107.16 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGYLPQDTHASDptq 79
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVdlrdldeddlrrrIAVVPQRPHLFD--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 taldrmmsardiATIINRIRKAEKEMTDpdpDVMTKAMnrydkamqdfDKAG-GYAAQSEAISMATSLGlpqevmeqQLG 158
Cdd:COG4987 423 ------------TTLRENLRLARPDATD---EELWAAL----------ERVGlGDWLAALPDGLDTWLG--------EGG 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 159 -TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDEvVNKVWHLDAqlGQ 235
Cdd:COG4987 470 rRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLER-MDRILVLED--GR 546
|
...
gi 489925987 236 IDM 238
Cdd:COG4987 547 IVE 549
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
330-499 |
2.23e-24 |
|
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: 106.56 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN-IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDtLDLNATVL 408
Cdd:TIGR03719 8 NRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQ-LDPTKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 409 ENLQHVAPELDNTQARSILGSFLFSGDD-------------------------------AMK---------PAHVLSGGE 448
Cdd:TIGR03719 87 ENVEEGVAEIKDALDRFNEISAKYAEPDadfdklaaeqaelqeiidaadawdldsqleiAMDalrcppwdaDVTKLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 449 KTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTHD 499
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHD 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
327-517 |
3.61e-24 |
|
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: 100.35 E-value: 3.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSrVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK---------IGYFAQ 396
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLDlNATVLENLQHVA--PELDNTQARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:cd03264 80 EFGVYP-NFTVREFLDYIAwlKGIPSKEVKARVDEVLELvnlGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 472 NNLDPASRE---EILKAIAkyEGAIVLV-THDEGAVEALnPERVLLMPDG 517
Cdd:cd03264 159 AGLDPEERIrfrNLLSELG--EDRIVILsTHIVEDVESL-CNQVAVLNKG 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
335-513 |
5.79e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.23 E-value: 5.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 335 AYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQeHDTLD--LNATVLENL- 411
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPdsLPLTVRDLVa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 ----QHVAPELDNT-QARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:NF040873 80 mgrwARRGLWRRLTrDDRAAVDDALERvglADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 484 KAIAKYEG---AIVLVTHDEGAVEALNPeRVLL 513
Cdd:NF040873 160 ALLAEEHArgaTVVVVTHDLELVRRADP-CVLL 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
22-236 |
7.13e-24 |
|
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: 105.69 E-value: 7.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDthasdptqtalDRMMSa 88
Cdd:COG2274 495 SLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIGVVLQD-----------VFLFS- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 89 rdiATIINRIRkaekeMTDPDPDvmtkamnryDKAMQdfdkaggyaaqsEAISMAtslGLPQEVMEQQLG---------- 158
Cdd:COG2274 563 ---GTIRENIT-----LGDPDAT---------DEEII------------EAARLA---GLHDFIEALPMGydtvvgeggs 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDEvVNKVWHLDAqlGQI 236
Cdd:COG2274 611 NLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTIRL-ADRIIVLDK--GRI 687
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-499 |
7.73e-24 |
|
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: 105.69 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 292 MRRAEKLLENTSEAQKAEKVADIRFPEPApcgrtpIMAKDISKAYG--SNIVFAGVNLAIDKGSRVVILGYNGAGKTTTL 369
Cdd:COG2274 445 LERLDDILDLPPEREEGRSKLSLPRLKGD------IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 370 RLLAHIEEPDTGSVEYGhGC------------KIGYFAQEhDTLdLNATVLENLQHVAPELDNTQARSILgsfLFSG--D 435
Cdd:COG2274 519 KLLLGLYEPTSGRILID-GIdlrqidpaslrrQIGVVLQD-VFL-FSGTIRENITLGDPDATDEEIIEAA---RLAGlhD 592
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 436 DAMK-P----------AHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEG--AIVLVTHD 499
Cdd:COG2274 593 FIEAlPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
279-517 |
8.32e-24 |
|
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: 105.23 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 279 HAKASkAVAAqnmMRRAEKLLENTSEAQKAEKVadirfPEPAPcGRTPIMAKDISKAY-GSNIVFAGVNLAIDKGSRVVI 357
Cdd:COG4988 299 HARAN-GIAA---AEKIFALLDAPEPAAPAGTA-----PLPAA-GPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVAL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 358 LGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------KIGYFAQeHDTLdLNATVLENLQHVAPELDNTQ--- 422
Cdd:COG4988 369 VGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVdlsdldpaswrrQIAWVPQ-NPYL-FAGTIRENLRLGRPDASDEElea 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 423 --ARSILGSFLFS---------GDDAMKpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY-E 490
Cdd:COG4988 446 alEAAGLDEFVAAlpdgldtplGEGGRG----LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaK 521
|
250 260
....*....|....*....|....*...
gi 489925987 491 GAIVL-VTHDEGAVEalNPERVLLMPDG 517
Cdd:COG4988 522 GRTVIlITHRLALLA--QADRILVLDDG 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
342-517 |
9.68e-24 |
|
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: 99.29 E-value: 9.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 342 FAGVNLAID---KGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC---------------KIGYFAQEHdTLDL 403
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLVFQQY-ALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 NATVLENLQHVAPELDNT----QARSILGSFlfsGDDAMKPAHV--LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPA 477
Cdd:cd03297 89 HLNVRENLAFGLKRKRNRedriSVDELLDLL---GLDHLLNRYPaqLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 478 SREEI---LKAIAK-YEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03297 166 LRLQLlpeLKQIKKnLNIPVIFVTHDLSEAEYLA-DRIVVMEDG 208
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-191 |
2.70e-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: 96.74 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 4 EAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdPTQTald 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGK------------DLAS--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 84 rmMSARDIATIINrirkaekemtdpdpdVMTKAMNRYDkaMQDFDkaggyaaqseaismatslglpqevmEQQLGTLSGG 163
Cdd:cd03214 66 --LSPKELARKIA---------------YVPQALELLG--LAHLA-------------------------DRPFNELSGG 101
|
170 180
....*....|....*....|....*...
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:cd03214 102 ERQRVLLARALAQEPPILLLDEPTSHLD 129
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
330-517 |
3.01e-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: 98.62 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV------EYGhGC-------KIGYFAQ 396
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRG-GEdvwelrkRIGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 E-HDTLDLNATVLENL-----------QHVAPElDNTQARSILGSF-LfsGDDAMKPAHVLSGGEKTRLALA-TLVTSRA 462
Cdd:COG1119 86 AlQLRFPRDETVLDVVlsgffdsiglyREPTDE-QRERARELLELLgL--AHLADRPFGTLSQGEQRRVLIArALVKDPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 463 nVLLLDEPTNNLDPASREEILKAIAKY--EG--AIVLVTHDegaVEALNPE--RVLLMPDG 517
Cdd:COG1119 163 -LLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTHH---VEEIPPGitHVLLLKDG 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
327-498 |
4.30e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 97.25 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCKIG-YFAQEH-----D 399
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPdVAEACHylghrN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVApeldntqarSILGSFLFSGDDAMK----------PAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:PRK13539 83 AMKPALTVAENLEFWA---------AFLGGEELDIAAALEavglaplahlPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 470 PTNNLDPASREEILKAIAKY---EGAIVLVTH 498
Cdd:PRK13539 154 PTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-226 |
5.12e-23 |
|
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: 96.90 E-value: 5.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgyLPQDTHAsdptqtAL 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIE------AL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRM------------MSARD----IATIINRIRKAEKEMTDpdpdvmTKAMNRYDKamqdfDKAGGYaaqseaismatSL 146
Cdd:cd03268 72 RRIgalieapgfypnLTAREnlrlLARLLGIRKKRIDEVLD------VVGLKDSAK-----KKVKGF-----------SL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 147 GlpqevMEQQLGtlsggqrrrieLARILFSDADTLILDEPTNHLDADSIEWLRGY---LKKYEGGFLVISHSTELLDEVV 223
Cdd:cd03268 130 G-----MKQRLG-----------IALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVA 193
|
...
gi 489925987 224 NKV 226
Cdd:cd03268 194 DRI 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
330-517 |
5.88e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 96.94 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDT--------L 401
Cdd:cd03301 4 ENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIamvfqnyaL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLEN------LQHVAPELDNTQARS---ILG-SFLFSgddaMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:cd03301 84 YPHMTVYDNiafglkLRKVPKDEIDERVREvaeLLQiEHLLD----RKPKQ-LSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 472 NNLDP----ASREEILKAIAKYEGAIVLVTHDEgaVEALN-PERVLLMPDG 517
Cdd:cd03301 159 SNLDAklrvQMRAELKRLQQRLGTTTIYVTHDQ--VEAMTmADRIAVMNDG 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
327-499 |
5.88e-23 |
|
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: 97.25 E-value: 5.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEE-----PDTGSVEYG-------------HG 388
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDgkdiydldvdvleLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 389 CKIGYFAQEHDTLDlnATVLEN------LQHVAP--ELDNTQARSILGSFLFsgDDAMKPAHV--LSGGEKTRLALA-TL 457
Cdd:cd03260 81 RRVGMVFQKPNPFP--GSIYDNvayglrLHGIKLkeELDERVEEALRKAALW--DEVKDRLHAlgLSGGQQQRLCLArAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 458 VTsRANVLLLDEPTNNLDPASREEILKAIAKY--EGAIVLVTHD 499
Cdd:cd03260 157 AN-EPEVLLLDEPTSALDPISTAKIEELIAELkkEYTIVIVTHN 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
329-518 |
7.99e-23 |
|
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: 96.17 E-value: 7.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK-------IGYFAQEHD 399
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKakerrksIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVAPELD--NTQARSILGSFLFSGDDAMKPaHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPA 477
Cdd:cd03226 82 YQLFTDSVREELLLGLKELDagNEQAETVLKDLDLYALKERHP-LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 478 SREEILKAI---AKYEGAIVLVTHD-EGAVEALNpeRVLLMPDGD 518
Cdd:cd03226 161 NMERVGELIrelAAQGKAVIVITHDyEFLAKVCD--RVLLLANGA 203
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
329-505 |
8.94e-23 |
|
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: 95.89 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTL----DLN 404
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylgHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 A-----TVLENLQHVAPELDNTQaRSILGSFLFSG--DDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPA 477
Cdd:TIGR01189 83 GlkpelSALENLHFWAAIHGGAQ-RTIEDALAAVGltGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 478 SRE---EILKAIAKYEGAIVLVTH-DEGAVEA 505
Cdd:TIGR01189 162 GVAllaGLLRAHLARGGIVLLTTHqDLGLVEA 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
330-499 |
9.46e-23 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.73 E-value: 9.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN-IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDtLDLNATVL 408
Cdd:PRK11819 10 NRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQ-LDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 409 ENLQHVAPELDNTQAR--SIlgSFLFSGDD-------------------------------AM---------KPAHVLSG 446
Cdd:PRK11819 89 ENVEEGVAEVKAALDRfnEI--YAAYAEPDadfdalaaeqgelqeiidaadawdldsqleiAMdalrcppwdAKVTKLSG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 447 GEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTHD 499
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHD 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
330-506 |
1.21e-22 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 99.40 E-value: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HGCKIGYFAQeHDT 400
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvtglppEKRNVGMVFQ-DYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLNATVLEN------LQHVAPELDNTQARSILgsflfsgddAM---------KPAHvLSGGEKTRLALA-TLVTsRANV 464
Cdd:COG3842 88 LFPHLTVAENvafglrMRGVPKAEIRARVAELL---------ELvglegladrYPHQ-LSGGQQQRVALArALAP-EPRV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 465 LLLDEPTNNLDPASREEI---LKAIAKYEGA-IVLVTHDEGavEAL 506
Cdd:COG3842 157 LLLDEPLSALDAKLREEMreeLRRLQRELGItFIYVTHDQE--EAL 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
328-506 |
1.25e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 99.38 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 328 MA----KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhgckigyfaqEHDTLDL 403
Cdd:COG3839 1 MAslelENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG----------GRDVTDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 ------------------NATVLEN------LQHVAPELDNTQARSI-----LGSFLfsgddAMKPAHvLSGGEKTRLAL 454
Cdd:COG3839 71 ppkdrniamvfqsyalypHMTVYENiafplkLRKVPKAEIDRRVREAaellgLEDLL-----DRKPKQ-LSGGQRQRVAL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 455 A-TLVTsRANVLLLDEPTNNLDPASREEI---LKAIAKYEGA-IVLVTHDegAVEAL 506
Cdd:COG3839 145 GrALVR-EPKVFLLDEPLSNLDAKLRVEMraeIKRLHRRLGTtTIYVTHD--QVEAM 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-222 |
1.29e-22 |
|
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: 101.17 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRV--SGKLGYLPQDTHASDPTQT 80
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgeTVKLAYVDQSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDRMMSARDIATIINRirkaekemtdpdpDVMTKAmnrYDKAmqdFDKAGGyaaqseaismatslglpqevmEQQ--LG 158
Cdd:TIGR03719 403 VWEEISGGLDIIKLGKR-------------EIPSRA---YVGR---FNFKGS---------------------DQQkkVG 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEV 222
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI 506
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
341-499 |
1.31e-22 |
|
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: 95.18 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-------------HGCKIGYFAQEHDTLDLNATV 407
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgepldysrkglleRRQRVGLVFQDPDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 LENLQhVAPE---LDNTQARSILGSFLFSGDD---AMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:TIGR01166 87 DQDVA-FGPLnlgLSEAEVERRVREALTAVGAsglRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGREQ 165
|
170 180
....*....|....*....|.
gi 489925987 482 ILKAIAKYEGA---IVLVTHD 499
Cdd:TIGR01166 166 MLAILRRLRAEgmtVVISTHD 186
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-236 |
1.54e-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: 96.04 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK----------------LGYLPQDthasd 76
Cdd:cd03257 16 GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkirrkeIQMVFQD----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 PtQTALDRMMSardIATIInrirkAEkemtdpdpdvmtkamnrydkAMQDFDKAGGYAAQSEAISMA-TSLGLPQEVMEQ 155
Cdd:cd03257 91 P-MSSLNPRMT---IGEQI-----AE--------------------PLRIHGKLSKKEARKEAVLLLlVGVGLPEEVLNR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 156 QLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDA 231
Cdd:cd03257 142 YPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA 221
|
....*
gi 489925987 232 qlGQI 236
Cdd:cd03257 222 --GKI 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
278-500 |
2.00e-22 |
|
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: 100.51 E-value: 2.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 278 LHAKASKAVAAQNMMRRAEKLLENTSEAQKAEKVADirfpEPAPCGRTPIMAKDISKAY-GSNIVFAGVNLAIDKGSRVV 356
Cdd:TIGR02868 290 LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAA----GAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLRLLAHIEEPDTGSV--------EYGHG---CKIGYFAQEHDTLDlnATVLENLQHVAP-----ELDN 420
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvsSLDQDevrRRVSVCAQDAHLFD--TTVRENLRLARPdatdeELWA 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 421 TQARSILGSFLFSGDDAMKP-----AHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI--AKYEGAI 493
Cdd:TIGR02868 444 ALERVGLADWLRALPDGLDTvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLlaALSGRTV 523
|
....*..
gi 489925987 494 VLVTHDE 500
Cdd:TIGR02868 524 VLITHHL 530
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-219 |
4.52e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 4.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQdthasdptQTALDRMM--SA 88
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQ--------RSEVPDSLplTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 89 RDIATI-INRIRKAEKEMTDPDPDVMTKAMNRYDkaMQDFDKaggyaaqseaismatslglpqevmeQQLGTLSGGQRRR 167
Cdd:NF040873 75 RDLVAMgRWARRGLWRRLTRDDRAAVDDALERVG--LADLAG-------------------------RQLGELSGGQRQR 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 168 IELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEG---GFLVISHSTELL 219
Cdd:NF040873 128 ALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHDLELV 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
275-514 |
4.91e-22 |
|
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: 99.28 E-value: 4.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 275 GIRLHAKASkAVAAQNMMRRaekLLENTS--EAQKAEKVADirfpePAPcgrtPIMAKDISKAY-GSNIVFAGVNLAIDK 351
Cdd:TIGR02857 281 GAQYHARAD-GVAAAEALFA---VLDAAPrpLAGKAPVTAA-----PAS----SLEFSGVSVAYpGRRPALRPVSFTVPP 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 352 GSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----------EYGHGCKIGYFAQeHDTLdLNATVLENLQHVAP---- 416
Cdd:TIGR02857 348 GERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvpladadADSWRDQIAWVPQ-HPFL-FAGTIAENIRLARPdasd 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 417 -ELDNTQARSILGSF---LFSGDDAM--KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY- 489
Cdd:TIGR02857 426 aEIREALERAGLDEFvaaLPQGLDTPigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALa 505
|
250 260
....*....|....*....|....*.
gi 489925987 490 EGAIVL-VTHDEGAVEALnpERVLLM 514
Cdd:TIGR02857 506 QGRTVLlVTHRLALAALA--DRIVVL 529
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
327-517 |
6.93e-22 |
|
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: 94.01 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIV-FAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-------HGCKIGYFAQEH 398
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvsdlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DT------LDLNATVLENLQ------HVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLL 466
Cdd:cd03292 81 GVvfqdfrLLPDRNVYENVAfalevtGVPPREIRKRVPAALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489925987 467 LDEPTNNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEALNPeRVLLMPDG 517
Cdd:cd03292 160 ADEPTGNLDPDTTWEImnlLKKINKAGTTVVVATHAKELVDTTRH-RVIALERG 212
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
330-499 |
7.05e-22 |
|
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: 94.56 E-value: 7.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN-IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGC-------------KIGYF 394
Cdd:cd03256 4 ENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLiDGTDInklkgkalrqlrrQIGMI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHDtLDLNATVLENLQHVA--------------PELDNTQARSILGSFLFSgDDAMKPAHVLSGGEKTRLALATLVTS 460
Cdd:cd03256 84 FQQFN-LIERLSVLENVLSGRlgrrstwrslfglfPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 461 RANVLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVT-HD 499
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVmdlLKRINREEGITVIVSlHQ 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
329-517 |
9.23e-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: 94.11 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAY--GSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGCK 390
Cdd:cd03257 4 VKNLSVSFptGGGSVKAldDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrkiRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQEHDTlDLNAT------VLENLQHVAPELDNTQARSILGSFLFSGDDA-----MKPaHVLSGGEKTRLALATLVT 459
Cdd:cd03257 84 IQMVFQDPMS-SLNPRmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnRYP-HELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 460 SRANVLLLDEPTNNLDPASREEILKAIAK----YEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDLGVVAKIA-DRVAVMYAG 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
327-517 |
2.11e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG----------HGCKIGYFAQ 396
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlppRERRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDtldL--NATVLENLQ---HVAPeLDNTQARSILGSFLfsgdDAM--------KPAHvLSGGEKTRLALATLVTSRAN 463
Cdd:COG1118 83 HYA---LfpHMTVAENIAfglRVRP-PSKAEIRARVEELL----ELVqlegladrYPSQ-LSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 464 VLLLDEPTNNLDPASREEI---LKAI-AKYEGAIVLVTHD-EGAVE-AlnpERVLLMPDG 517
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELrrwLRRLhDELGGTTVFVTHDqEEALElA---DRVVVMNQG 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
13-230 |
2.20e-21 |
|
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: 91.29 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHasdptq 79
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPF------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 taldrMMSArdiaTIINRIrkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaismatslglpqevmeqqlgt 159
Cdd:cd03228 87 -----LFSG----TIRENI------------------------------------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDEvVNKVWHLD 230
Cdd:cd03228 97 LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLD 168
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
327-517 |
2.47e-21 |
|
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: 92.43 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGS-VEYGHGC---------KIGYFAQ 396
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHdTLDLNATVLENLQHVA-------PELDNTQARSIlgSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:cd03265 81 DL-SVDDELTGWENLYIHArlygvpgAERRERIDELL--DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 470 PTNNLDPASRE---EILKAIAKYEG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03265 158 PTIGLDPQTRAhvwEYIEKLKEEFGmTILLTTHYMEEAEQL-CDRVAIIDHG 208
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-222 |
2.58e-21 |
|
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: 97.63 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDT------------ 72
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdirqidpadlrrNIGYVPQDPrlfygtlrdnia 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 73 ----HASDptqtalDRMMSARDIATIINRIRKaekemtdpDPDvmtkamnrydkamqdfdkaggyaaqseaismatslGL 148
Cdd:TIGR03375 561 lgapYADD------EEILRAAELAGVTEFVRR--------HPD-----------------------------------GL 591
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 149 PQEVMEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDEV 222
Cdd:TIGR03375 592 DMQIGERGRS-LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGktLVLVTHRTSLLDLV 666
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-239 |
3.04e-21 |
|
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: 97.13 E-value: 3.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGYLPQDTHASDPTq 79
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAdlsqwdreelgrhIGYLPQDVELFDGT- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 taldrmmsardIATIINRirkaekeMTDPDPDVMTKAmnrydkAMqdfdKAGGYaaqsEAIsmatsLGLPQ---EVMEQQ 156
Cdd:COG4618 422 -----------IAENIAR-------FGDADPEKVVAA------AK----LAGVH----EMI-----LRLPDgydTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 157 LGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLK--KYEGG-FLVISHSTELLdEVVNKVWHLDAql 233
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRalKARGAtVVVITHRPSLL-AAVDKLLVLRD-- 541
|
....*.
gi 489925987 234 GQIDMY 239
Cdd:COG4618 542 GRVQAF 547
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-229 |
3.21e-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: 96.97 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEI-QIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGY 67
Cdd:TIGR02857 321 SLEFSGVSVaYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQDthasdPTQTAldrmmsardiATIINRIRKAEKemtDPDPDVMTKAMNRydKAMQDFDKAGGyaaqseaismatsLG 147
Cdd:TIGR02857 401 VPQH-----PFLFA----------GTIAENIRLARP---DASDAEIREALER--AGLDEFVAALP-------------QG 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 LPQEVMEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLdEVVNK 225
Cdd:TIGR02857 448 LDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALA-ALADR 525
|
....
gi 489925987 226 VWHL 229
Cdd:TIGR02857 526 IVVL 529
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
332-517 |
3.43e-21 |
|
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: 91.93 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 332 ISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGC-------------KIGYFAQ 396
Cdd:TIGR02673 7 VSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRiAGEDVnrlrgrqlpllrrRIGVVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLdLNATVLENLQhVAPELDNTQARSI------LGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEP 470
Cdd:TIGR02673 87 DFRLL-PDRTVYENVA-LPLEVRGKKEREIqrrvgaALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 471 TNNLDPASREEIL---KAIAKYEGAIVLVTHDEGAVEAlNPERVLLMPDG 517
Cdd:TIGR02673 165 TGNLDPDLSERILdllKRLNKRGTTVIVATHDLSLVDR-VAHRVIILDDG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
327-517 |
3.83e-21 |
|
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: 93.26 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHG-----------CKIG 392
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAlkNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTvDGLDtldeenlweirKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 393 YFAQEHDTLDLNATV-------LENLQhVAPE-----LDNTQARSILGSFLfsgddaMKPAHVLSGGEKTRLALATLVTS 460
Cdd:TIGR04520 81 MVFQNPDNQFVGATVeddvafgLENLG-VPREemrkrVDEALKLVGMEDFR------DREPHLLSGGQKQRVAIAGVLAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 461 RANVLLLDEPTNNLDPASREEILKAIA---KYEG-AIVLVTHD-EGAVEAlnpERVLLMPDG 517
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRklnKEEGiTVISITHDmEEAVLA---DRVIVMNKG 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-204 |
4.41e-21 |
|
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: 92.45 E-value: 4.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGK-VRVSG-------------KLG 66
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGerrggedvwelrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQDTHAS-DPTQTALDRMMSARDiATIInRIRKAEKEMTdpdpdvmtkamnryDKAMQdfdkaggyaaqseaisMATS 145
Cdd:COG1119 82 LVSPALQLRfPRDETVLDVVLSGFF-DSIG-LYREPTDEQR--------------ERARE----------------LLEL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 146 LGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:COG1119 130 LGL-AHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDK 187
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
330-517 |
4.63e-21 |
|
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: 91.91 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HGCKIGYFAQeHDT 400
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkditnlppHKRPVNTVFQ-NYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLNATVLENL---------------QHVAPELDNTQarsiLGSFlfsgddAMKPAHVLSGGEKTRLALATLVTSRANVL 465
Cdd:cd03300 83 LFPHLTVFENIafglrlkklpkaeikERVAEALDLVQ----LEGY------ANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 466 LLDEPTNNLDPASREEI---LKAIAKYEG-AIVLVTHDEGavEALN-PERVLLMPDG 517
Cdd:cd03300 153 LLDEPLGALDLKLRKDMqleLKRLQKELGiTFVFVTHDQE--EALTmSDRIAVMNKG 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
329-498 |
5.94e-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: 91.02 E-value: 5.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV------------EYGHGCK-IGYFA 395
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdSIARGLLyLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHDTLdlnaTVLENLQHVAPELDNTQARSILGSFLFSG-DDAmkPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:cd03231 83 GIKTTL----SVLENLRFWHADHSDEQVEEALARVGLNGfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*..
gi 489925987 475 DPASREEILKAIAKY---EGAIVLVTH 498
Cdd:cd03231 157 DKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
330-517 |
6.25e-21 |
|
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: 91.79 E-value: 6.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE--------------YGHGCKIGYFA 395
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidgedisglseaelYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QE---HDTLdlnaTVLENL-----QHVA--PELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVL 465
Cdd:cd03261 84 QSgalFDSL----TVFENVafplrEHTRlsEEEIREIVLEKLEAVGLRGAEDLYPAE-LSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 466 LLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAI-ADRIAVLYDG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
330-499 |
7.11e-21 |
|
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: 91.58 E-value: 7.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG----HGC----------KIGYFA 395
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqdiTGLsekelyelrrRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEhdtldlNA-----TVLENL-----QHvaPELDNTQARSI----LGSFLFSGDDAMKPAHvLSGGEKTRLALAtlvtsR 461
Cdd:COG1127 89 QG------GAlfdslTVFENVafplrEH--TDLSEAEIRELvlekLELVGLPGAADKMPSE-LSGGMRKRVALA-----R 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 462 A-----NVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHD 499
Cdd:COG1127 155 AlaldpEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHD 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-499 |
8.39e-21 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.03 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 27 KGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKvrvsgklgylpqdtHASDPT-------------QTALdRMMSARDIAT 93
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGD--------------YEEEPSwdevlkrfrgtelQNYF-KKLYNGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 I-----INRIRKAEKEMTDpdpDVMTKAmnrydkamqdfDKAGgyaAQSEAISMatsLGLpQEVMEQQLGTLSGGQRRRI 168
Cdd:PRK13409 163 VhkpqyVDLIPKVFKGKVR---ELLKKV-----------DERG---KLDEVVER---LGL-ENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 169 ELARILFSDADTLILDEPTNHLD-------ADSIewlRGYLK-KYeggFLVISHSTELLDEVVNKVwHLdaqlgqidMYS 240
Cdd:PRK13409 222 AIAAALLRDADFYFFDEPTSYLDirqrlnvARLI---RELAEgKY---VLVVEHDLAVLDYLADNV-HI--------AYG 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 241 LSwKAYlhqrvvdeerrrrerevaekkaerlmkqGIRLHAKASKA---------VAAQNMMRRAEKllentseaqkaekv 311
Cdd:PRK13409 287 EP-GAY----------------------------GVVSKPKGVRVgineylkgyLPEENMRIRPEP-------------- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 312 adIRFPEPAP----CGRTPIMAKDISKAYG--SNIVFAGvnlAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY 385
Cdd:PRK13409 324 --IEFEERPPrdesERETLVEYPDLTKKLGdfSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 386 ghGCKIGYFAQEHDTlDLNATVLENLQHVAPELDNtqarsilgSFLFSgdDAMKPAHV----------LSGGEKTRLALA 455
Cdd:PRK13409 399 --ELKISYKPQYIKP-DYDGTVEDLLRSITDDLGS--------SYYKS--EIIKPLQLerlldknvkdLSGGELQRVAIA 465
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489925987 456 TLVTSRANVLLLDEPTNNLDPASREEILKAIAKY----EGAIVLVTHD 499
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeerEATALVVDHD 513
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
327-497 |
8.83e-21 |
|
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: 91.59 E-value: 8.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHG--------------CKI 391
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 GYFAQEHDTLDlNATVLENLQHVAPELDNTqARSILGsfLFSGDD----------------AMKPAHVLSGGEKTRLALA 455
Cdd:TIGR02315 82 GMIFQHYNLIE-RLTVLENVLHGRLGYKPT-WRSLLG--RFSEEDkeralsalervgladkAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 456 TLVTSRANVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVLVT 497
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKqvmDYLKRINKEDGITVIIN 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-220 |
9.52e-21 |
|
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: 91.40 E-value: 9.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGA----RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK------------- 64
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRpvtrrrrkafrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 65 LGYLPQDTHAS-DPTQTaldrmmsardIATIIN---RIrkaekemtdpdpdvmtkamnrydkamqdfdkAGGYAAQSEAI 140
Cdd:COG1124 81 VQMVFQDPYASlHPRHT----------VDRILAeplRI-------------------------------HGLPDREERIA 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 141 SMATSLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHST 216
Cdd:COG1124 120 ELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDL 199
|
....
gi 489925987 217 ELLD 220
Cdd:COG1124 200 AVVA 203
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-239 |
1.13e-20 |
|
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: 95.49 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 12 IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDPT 78
Cdd:TIGR01842 328 GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdretfgkHIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 qtaldrmmsardIATIINRIRKaekemtDPDPDVMTKAMnrydkamqdfdKAGGYaaqSEAIsmatsLGLPQ---EVMEQ 155
Cdd:TIGR01842 408 ------------VAENIARFGE------NADPEKIIEAA-----------KLAGV---HELI-----LRLPDgydTVIGP 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 156 QLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR---GYLKKYEGGFLVISHSTELLdEVVNKVwhLDAQ 232
Cdd:TIGR01842 451 GGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALAnaiKALKARGITVVVITHRPSLL-GCVDKI--LVLQ 527
|
....*..
gi 489925987 233 LGQIDMY 239
Cdd:TIGR01842 528 DGRIARF 534
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
329-525 |
1.34e-20 |
|
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: 90.68 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH--------------GckIGYF 394
Cdd:cd03218 3 AENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGqditklpmhkrarlG--IGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHdTLDLNATVLENLQHVAP--ELDNTQARSILGSFL--FSGDD-AMKPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:cd03218 81 PQEA-SIFRKLTVEENILAVLEirGLSKKEREEKLEELLeeFHITHlRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 470 PTNNLDPASREEILKAIA--KYEGAIVLVThDEGAVEALN-PERVLLMPDGD-------EDLWNDS 525
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKilKDRGIGVLIT-DHNVRETLSiTDRAYIIYEGKvlaegtpEEIAANE 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-186 |
2.05e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 90.47 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LG 66
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEdithlpmhkrarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQDthASdptqtaLDRMMSARD-IATIInrirkaekEMTDPDPDvmtKAMNRYDKAMQDFDkaggyaaqseaIS-MAT 144
Cdd:COG1137 82 YLPQE--AS------IFRKLTVEDnILAVL--------ELRKLSKK---EREERLEELLEEFG-----------IThLRK 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 145 SLGLpqevmeqqlgTLSGGQRRRIELARILFSDADTLILDEP 186
Cdd:COG1137 132 SKAY----------SLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-247 |
2.26e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 94.19 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVS--GKLGYLPQDtHASDpt 78
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQD-HAYD-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 qtaldrmmsardiatiinrirkAEKEMTdpdpdvMTKAMNRYDKAMQDfdkaggyaaqSEAI-SMATSLGLPQEVMEQQL 157
Cdd:PRK15064 395 ----------------------FENDLT------LFDWMSQWRQEGDD----------EQAVrGTLGRLLFSQDDIKKSV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAQlGQID 237
Cdd:PRK15064 437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD-GVVD 515
|
250
....*....|
gi 489925987 238 mYSLSWKAYL 247
Cdd:PRK15064 516 -FSGTYEEYL 524
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
330-517 |
3.23e-20 |
|
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: 89.56 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGC---------------K 390
Cdd:cd03258 5 KNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTdltllsgkelrkarrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQEHDTLDlNATVLEN------LQHVAPELDNTQARSILgSFLFSGDDA-MKPAHvLSGGEKTRLALATLVTSRAN 463
Cdd:cd03258 84 IGMIFQHFNLLS-SRTVFENvalpleIAGVPKAEIEERVLELL-ELVGLEDKAdAYPAQ-LSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 464 VLLLDEPTNNLDPASREEILKAIAKYEG----AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRI-CDRVAVMEKG 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
327-517 |
4.28e-20 |
|
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: 89.32 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HGCKIGYFAQe 397
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 HDTLDLNATVLENL------QHVAPELDNTQAR----SILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLL 467
Cdd:cd03296 82 HYALFRHMTVFDNVafglrvKPRSERPPEAEIRakvhELLKLVQLDWLADRYPAQ-LSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 468 DEPTNNLDPASREEILKAIAKYEGAI----VLVTHDEGavEALN-PERVLLMPDG 517
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQE--EALEvADRVVVMNKG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
327-517 |
5.25e-20 |
|
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: 87.27 E-value: 5.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYG--SNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH-----------GCKIGY 393
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGadisqwdpnelGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQEhDTLdLNATVLENlqhvapeldntqarsilgsflfsgddamkpahVLSGGEKTRLALATLVTSRANVLLLDEPTNN 473
Cdd:cd03246 81 LPQD-DEL-FSGSIAEN--------------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 474 LDPASREEILKAIA---KYEGAIVLVTHDEGAVEALnpERVLLMPDG 517
Cdd:cd03246 127 LDVEGERALNQAIAalkAAGATRIVIAHRPETLASA--DRILVLEDG 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
330-496 |
6.62e-20 |
|
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: 88.26 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGckIGYFA 395
Cdd:cd03224 4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherarAG--IGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHDTLDlNATVLENLQHVAPELDNTQARSILGSF--LFSGDDAMK--PAHVLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:cd03224 82 EGRRIFP-ELTVEENLLLGAYARRRAKRKARLERVyeLFPRLKERRkqLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180
....*....|....*....|....*...
gi 489925987 472 NNLDPASREEILKAIAKY--EG-AIVLV 496
Cdd:cd03224 161 EGLAPKIVEEIFEAIRELrdEGvTILLV 188
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
321-498 |
7.18e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 7.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 321 PCGRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgC----------- 389
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL---Cgepvpsrarha 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 --KIGYFAQeHDTLDLNATVLENLQHVAPE--LDNTQARSILGSFL-FSGDDAMKPAHV--LSGGEKTRLALATLVTSRA 462
Cdd:PRK13537 79 rqRVGVVPQ-FDNLDPDFTVRENLLVFGRYfgLSAAAARALVPPLLeFAKLENKADAKVgeLSGGMKRRLTLARALVNDP 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 463 NVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVLVTH 498
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHlmwERLRSLLARGKTILLTTH 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-218 |
7.37e-20 |
|
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: 88.32 E-value: 7.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGL----EIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------- 64
Cdd:cd03255 1 IELKNLsktyGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 65 ---LGYLPQDTHASdPTQTALDRMMsardIATIINRIRKAEKEMtdpdpdvmtkamnrydkamqdfdkaggyaaqsEAIS 141
Cdd:cd03255 81 rrhIGFVFQSFNLL-PDLTALENVE----LPLLLAGVPKKERRE--------------------------------RAEE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 142 MATSLGLPqEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGYLKKYEGGFLVISHSTE 217
Cdd:cd03255 124 LLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPE 202
|
.
gi 489925987 218 L 218
Cdd:cd03255 203 L 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-191 |
8.68e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGY 67
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQDTHASDPtqtaldrmMSARDIAtiinrirkaekemtdpdpdvmtkAMNRYDKamqdfdkaGGYAAQSEAismatslg 147
Cdd:PRK13548 81 LPQHSSLSFP--------FTVEEVV-----------------------AMGRAPH--------GLSRAEDDA-------- 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 148 LPQEVMEQ---------QLGTLSGGQRRRIELARIL--FSDAD----TLILDEPTNHLD 191
Cdd:PRK13548 114 LVAAALAQvdlahlagrDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALD 172
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
343-517 |
9.67e-20 |
|
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: 88.03 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 343 AGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK----------IGYFAQehDTLDLNATVLENL 411
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGYVPQ--DVTLFYGTLRDNI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 QHVAPELDNtqaRSILGSFLFSGDDAMKPAH-------------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:cd03245 99 TLGAPLADD---ERILRAAELAGVTDFVNKHpngldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 479 REEILKAIAKYEG--AIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:cd03245 176 EERLKERLRQLLGdkTLIIITHRPSLLDLVD--RIIVMDSG 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-236 |
1.35e-19 |
|
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: 87.65 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTH----------- 73
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTlfygtlrdnit 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 74 -----ASDptqtalDRMMSARDIATIINRIRKaekemtdpDPDvmtkamnrydkamqdfdkaggyaaqseaismatslGL 148
Cdd:cd03245 100 lgaplADD------ERILRAAELAGVTDFVNK--------HPN-----------------------------------GL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 149 PQEVMEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDeVVNKV 226
Cdd:cd03245 131 DLQIGERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLD-LVDRI 208
|
250
....*....|
gi 489925987 227 WHLDAqlGQI 236
Cdd:cd03245 209 IVMDS--GRI 216
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-222 |
1.59e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 91.72 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRV--SGKLGYLPQDTHASDPTQT 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgeTVKLAYVDQSRDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDRMMSARDIATIINRirkaekemtdpdpDVMTKAmnrYDKAmqdFDKAGGyaaqseaismatslglpqevmEQQ--LG 158
Cdd:PRK11819 405 VWEEISGGLDIIKVGNR-------------EIPSRA---YVGR---FNFKGG---------------------DQQkkVG 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEV 222
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI 508
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
324-517 |
1.62e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.39 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 324 RTPIMA-KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGCKIGYFAQEHDtlD 402
Cdd:PRK09452 11 LSPLVElRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGQDITHVPAENR--H 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 LNA-----------TVLEN------LQHVAPELDNTQARSILGSFLFSGDDAMKPaHVLSGGEKTRLALATLVTSRANVL 465
Cdd:PRK09452 88 VNTvfqsyalfphmTVFENvafglrMQKTPAAEITPRVMEALRMVQLEEFAQRKP-HQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 466 LLDEPTNNLDPASREEI---LKAIAKYEG-AIVLVTHDEGavEALN-PERVLLMPDG 517
Cdd:PRK09452 167 LLDESLSALDYKLRKQMqneLKALQRKLGiTFVFVTHDQE--EALTmSDRIVVMRDG 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
327-517 |
2.03e-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: 85.83 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI--VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhgckigyfaqEHDTLDLN 404
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD----------GVPVSDLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 ATvLENLQHV---APELDNTQARSILGSflfsgddamkpahVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:cd03247 71 KA-LSSLISVlnqRPYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 482 ILKAIAKY--EGAIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:cd03247 137 LLSLIFEVlkDKTLIWITHHLTGIEHMD--KILFLENG 172
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
329-514 |
2.13e-19 |
|
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: 87.49 E-value: 2.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaQEHDTLDL----- 403
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF----------DGEDITGLpphei 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 ----------------NATVLENLQhVAPELDNT-----------------QARSILGsFLFSGDDAMKPAHVLSGGEKT 450
Cdd:cd03219 73 arlgigrtfqiprlfpELTVLENVM-VAAQARTGsglllararreereareRAEELLE-RVGLADLADRPAGELSYGQQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 451 RLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEALNpERVLLM 514
Cdd:cd03219 151 RLEIARALATDPKLLLLDEPAAGLNPEETEELaelIRELRERGITVLLVEHDMDVVMSLA-DRVTVL 216
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
325-518 |
4.41e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 325 TPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGyfAQEHDTLDLN 404
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--AREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 ATVLENLQHVapeLDN----------TQARSILGSFLFSGDDAMKPAhVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:PRK11247 89 DARLLPWKKV---IDNvglglkgqwrDAALQALAAVGLADRANEWPA-ALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 475 DPASREEILKAIA----KYEGAIVLVTHDEGAVEALnPERVLLMPDGD 518
Cdd:PRK11247 165 DALTRIEMQDLIEslwqQHGFTVLLVTHDVSEAVAM-ADRVLLIEEGK 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-191 |
4.77e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 86.71 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGYLP 69
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRplaawspwelarrRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 70 QDTHASDPtqtaldrmMSARDIAtiinrirkaekemtdpdpdvmtkAMNRYdkamqdfdKAGGYAAQSEAIsmatslglP 149
Cdd:COG4559 82 QHSSLAFP--------FTVEEVV-----------------------ALGRA--------PHGSSAAQDRQI--------V 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 150 QEVMEQ-QLG--------TLSGGQRRRIELARIL-------FSDADTLILDEPTNHLD 191
Cdd:COG4559 115 REALALvGLAhlagrsyqTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALD 172
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
327-497 |
5.94e-19 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 86.24 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGckIG 392
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlpmhkrarLG--IG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 393 YFAQEHDTL-DLnaTVLENLQHVAP--ELDNTQARSILGSFL--FS-GDDAMKPAHVLSGGEKTRL----ALATlvtsRA 462
Cdd:COG1137 82 YLPQEASIFrKL--TVEDNILAVLElrKLSKKEREERLEELLeeFGiTHLRKSKAYSLSGGERRRVeiarALAT----NP 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 463 NVLLLDEPTNNLDPASREEILKAIA--KYEGAIVLVT 497
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRhlKERGIGVLIT 192
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
329-517 |
9.62e-19 |
|
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: 85.40 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HG---CKIGYFAQ 396
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmHErarLGIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EhDTLDLNATVLENLQHV---APELDNTQARSILGSFL--FS-GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEP 470
Cdd:TIGR04406 84 E-ASIFRKLTVEENIMAVleiRKDLDRAEREERLEALLeeFQiSHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 471 TNNLDPASREEILKAIA--KYEGAIVLVThDEGAVEALN-PERVLLMPDG 517
Cdd:TIGR04406 163 FAGVDPIAVGDIKKIIKhlKERGIGVLIT-DHNVRETLDiCDRAYIISDG 211
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-226 |
1.24e-18 |
|
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: 84.64 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK---------LGYLPQDth 73
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldiaarnrIGYLPEE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 74 asdptqTALDRMMSARDIATIINRIrkaekemtdpdpdvmtKAMNRYDkamqdfdkaggyaAQSEAISMATSLGLpQEVM 153
Cdd:cd03269 79 ------RGLYPKMKVIDQLVYLAQL----------------KGLKKEE-------------ARRRIDEWLERLEL-SEYA 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 154 EQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY-EGGFLVI--SHSTELLDEVVNKV 226
Cdd:cd03269 123 NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELaRAGKTVIlsTHQMELVEELCDRV 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-239 |
1.54e-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: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASDPTQTALD--RM------MSAR 89
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPELTGREniYLngrllgLSRK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 90 DIATIINRIrkaekemtdpdpdvmtkamnrydkamQDFdkaggyaaqSEaismatsLGlpqEVMEQQLGTLSGGQRRRIE 169
Cdd:cd03220 118 EIDEKIDEI--------------------------IEF---------SE-------LG---DFIDLPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 170 LARILFSDADTLILDEPTNHLDAD----SIEWLRGYLKKYEGGFLViSHSTELLDEVVNKVWHLDAqlGQIDMY 239
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGKTVILV-SHDPSSIKRLCDRALVLEK--GKIRFD 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
13-216 |
1.56e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.68 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHasdptq 79
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTF------ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 taldrMMSardiATIINRIRKAEKEMTDpdpDVMTKAmnrydkamqdfdkaggyAAQSEAISMATSL--GLPQEVMEQql 157
Cdd:COG1132 425 -----LFS----GTIRENIRYGRPDATD---EEVEEA-----------------AKAAQAHEFIEALpdGYDTVVGER-- 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 158 G-TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISH--ST 216
Cdd:COG1132 474 GvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAHrlST 537
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-205 |
1.68e-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: 84.69 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 21 TNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVsgkLGYLPQDthasdptqtalDRMMSARDIATIInrirk 100
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV---AGLVPWK-----------RRKKFLRRIGVVF----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 101 AEKEMTDPD-PDVMTKAMNRydkAMQDFDKAgGYAAQSEAISMATSLGlpqEVMEQQLGTLSGGQRRRIELARILFSDAD 179
Cdd:cd03267 101 GQKTQLWWDlPVIDSFYLLA---AIYDLPPA-RFKKRLDELSELLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180
....*....|....*....|....*.
gi 489925987 180 TLILDEPTNHLDADSIEWLRGYLKKY 205
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEY 199
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-517 |
1.86e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.45 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC-----------KIGYFAQEHDTLDLNATV----- 407
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQVGMVFQNPDNQFVGATVqddva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 --LENLQ----HVAPELDNTQARSILGSFLfsgddAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:PRK13635 105 fgLENIGvpreEMVERVDQALRQVGMEDFL-----NREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRRE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 482 ILKAI--AKYEGAI-VL-VTHDegAVEALNPERVLLMPDG 517
Cdd:PRK13635 179 VLETVrqLKEQKGItVLsITHD--LDEAAQADRVIVMNKG 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
327-517 |
1.94e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQE--------- 397
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrravlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 -HDTLDLNATVLE-----------NLQHVAPELDNTQARSILGSFlfsgddAMKPAHVLSGGEKTRLALA------TLVT 459
Cdd:PRK13548 83 qHSSLSFPFTVEEvvamgraphglSRAEDDALVAAALAQVDLAHL------AGRDYPQLSGGEQQRVQLArvlaqlWEPD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 460 SRANVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVL-VTHDegaveaLN-----PERVLLMPDG 517
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHhvlRLARQLAHERGLAVIvVLHD------LNlaaryADRIVLLHQG 217
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
334-517 |
1.97e-18 |
|
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: 85.90 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 334 KAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGC---------KIGYFAQEHdTLDL 403
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARvAGYDVvreprkvrrSIGIVPQYA-SVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 NATVLENLQHVA-----PElDNTQARSILGSFLFS-GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPA 477
Cdd:TIGR01188 80 DLTGRENLEMMGrlyglPK-DEAEERAEELLELFElGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 478 SREEILKAIAKYEGA---IVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:TIGR01188 159 TRRAIWDYIRALKEEgvtILLTTHYMEEADKLC-DRIAIIDHG 200
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
329-517 |
2.18e-18 |
|
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: 82.48 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIgYFAQEHDTLDLN-ATV 407
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV-DGKEV-SFASPRDARRAGiAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 lenlqhvapeldntqarsilgsflfsgddamkpaHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA 487
Cdd:cd03216 81 ----------------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIR 126
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 488 --KYEG-AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03216 127 rlRAQGvAVIFISHRLDEVFEIA-DRVTVLRDG 158
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-222 |
2.38e-18 |
|
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: 82.09 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPTQtal 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------EVSFASPRD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 drmmsARD--IATIinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaismatslglPQevmeqqlgtL 160
Cdd:cd03216 72 -----ARRagIAMV------------------------------------------------------YQ---------L 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLK--KYEG-GFLVISHStelLDEV 222
Cdd:cd03216 84 SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRrlRAQGvAVIFISHR---LDEV 145
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-218 |
2.91e-18 |
|
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: 83.34 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-----------LGYLPQD 71
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRdvtgvpperrnIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 72 tHASDPTQTALDRM-----MSARDIATIINRIRKAEKEMTDPDPdvmtkaMNRYdkamqdfdkaggyaaqseaismatsl 146
Cdd:cd03259 81 -YALFPHLTVAENIafglkLRGVPKAEIRARVRELLELVGLEGL------LNRY-------------------------- 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 147 glPQEvmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGGFLVISHSTEL 218
Cdd:cd03259 128 --PHE--------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqrELGITTIYVTHDQ 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
327-517 |
3.15e-18 |
|
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: 84.02 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGH-------------- 387
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlAGQdlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 388 GCKIGY-FAQEH--DTLdlnaTVLENlqhVA-P-ELDN-----TQARSILgsflfsgdDAMKPAH-------VLSGGEKT 450
Cdd:COG4181 89 ARHVGFvFQSFQllPTL----TALEN---VMlPlELAGrrdarARARALL--------ERVGLGHrldhypaQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 451 RLALATLVTSRANVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDEGAveALNPERVLLMPDG 517
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHDPAL--AARCDRVLRLRAG 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
330-517 |
3.17e-18 |
|
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: 84.27 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN-IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------KIGYFAQ 396
Cdd:cd03295 4 ENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFID-GEdireqdpvelrrKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 E-----HDTLDLNATVLENLQHVAPELDNTQARSILGSF-LFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEP 470
Cdd:cd03295 83 QiglfpHMTVEENIALVPKLLKWPKEKIRERADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 471 TNNLDPASREEILKAIAKYEGA----IVLVTHDegAVEALN-PERVLLMPDG 517
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQElgktIVFVTHD--IDEAFRlADRIAIMKNG 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-236 |
3.23e-18 |
|
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: 84.03 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTAl 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG------EDITGLPPHEIA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 dRM--------------MSARDiatiiNrirkaekemtdpdpdVMTKAMNRYDKAMQDFDKAGGYAAQSE-AISMATSLG 147
Cdd:cd03219 74 -RLgigrtfqiprlfpeLTVLE-----N---------------VMVAAQARTGSGLLLARARREEREARErAEELLERVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 LpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT---NHLDADSI-EWLRGyLKKYEGGFLVISHSTELLDEVV 223
Cdd:cd03219 133 L-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELaELIRE-LRERGITVLLVEHDMDVVMSLA 210
|
250
....*....|...
gi 489925987 224 NKVWHLDAqlGQI 236
Cdd:cd03219 211 DRVTVLDQ--GRV 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
327-517 |
3.33e-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: 84.81 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFA-----GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------ 389
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEkkaldDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTID-GRditakkkkklkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 ---KIGYFAQ--EHDTLDlnATVLE-------NLQHVAPELDNtQARSILGsfLFSGDDAMK---PAHvLSGGEKTRLAL 454
Cdd:TIGR04521 80 lrkKVGLVFQfpEHQLFE--ETVYKdiafgpkNLGLSEEEAEE-RVKEALE--LVGLDEEYLersPFE-LSGGQMRRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 455 ATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY---EG-AIVLVTHDEGAVeALNPERVLLMPDG 517
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkeKGlTVILVTHSMEDV-AEYADRVIVMHKG 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
327-517 |
3.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.75 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSN------IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV--------EYGHGCKI- 391
Cdd:PRK13633 5 IKCKNVSYKYESNeestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsDEENLWDIr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 ---GYFAQEHDTlDLNATVLENLQHVAPELDNTQARSILGSFlfsgDDAMK----------PAHVLSGGEKTRLALATLV 458
Cdd:PRK13633 85 nkaGMVFQNPDN-QIVATIVEEDVAFGPENLGIPPEEIRERV----DESLKkvgmyeyrrhAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 459 TSRANVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTH-DEGAVEAlnpERVLLMPDG 517
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIkelnKKYGITIILITHyMEEAVEA---DRIIVMDSG 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-230 |
3.40e-18 |
|
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: 83.08 E-value: 3.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDptqtaldrmmsardiatiinRIRKA 101
Cdd:cd03226 20 SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK------PIKAKE--------------------RRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 EKEMTDPDPDVMTKAMnrYDKAMQDFDKAGGYAAQSEAIsMATsLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTL 181
Cdd:cd03226 74 GYVMQDVDYQLFTDSV--REELLLGLKELDAGNEQAETV-LKD-LDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 182 ILDEPTNHLDA---DSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLD 230
Cdd:cd03226 149 IFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-220 |
3.58e-18 |
|
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: 83.86 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYLPQ 70
Cdd:TIGR04406 4 AENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQdithlpmherarlgIGYLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DthASdptqtaLDRMMSARDIATIINRIRKaekemtDPDPDVMTKamnRYDKAMQDFDkaggyaaqseaISmatslglpq 150
Cdd:TIGR04406 84 E--AS------IFRKLTVEENIMAVLEIRK------DLDRAEREE---RLEALLEEFQ-----------IS--------- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 151 EVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS---IEWLRGYLKKYEGGFLVISHST-ELLD 220
Cdd:TIGR04406 127 HLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAvgdIKKIIKHLKERGIGVLITDHNVrETLD 200
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
2-222 |
4.80e-18 |
|
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: 83.50 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqDTHASDPTQtA 81
Cdd:TIGR03864 1 ALEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAG-------HDLRRAPRA-A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 LDRMMSARDIATIinrirkaekemtdpDPDVMTKAMNRYDKAMQDFDKAGGYAAQSEAIsmaTSLGLpQEVMEQQLGTLS 161
Cdd:TIGR03864 73 LARLGVVFQQPTL--------------DLDLSVRQNLRYHAALHGLSRAEARARIAELL---ARLGL-AERADDKVRELN 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKyeggfLVISHS------TELLDEV 222
Cdd:TIGR03864 135 GGHRRRVEIARALLHRPALLLLDEPTVGLDPASRAAITAHVRA-----LARDQGlsvlwaTHLVDEI 196
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
330-501 |
4.90e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 83.60 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTG-------SVEYGHG--CKIG-----YFA 395
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVNDPKVdeRLIRqeagmVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHdtLDLNATVLENLQ----HV---APELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLLD 468
Cdd:PRK09493 85 QFY--LFPHLTALENVMfgplRVrgaSKEEAEKQARELLAKVGLAERAHHYPSE-LSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 489925987 469 EPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEG 501
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLaeEGmTMVIVTHEIG 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-499 |
5.08e-18 |
|
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: 87.15 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 27 KGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKV-----------RVSGK-LG-YLpqdthasdptqtaldrmmsaRDIAT 93
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTeLQdYF--------------------KKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 iiNRIRKAEK-EMTDPDPDVMT----KAMNRYDkamqDFDKAGGYAAQseaismatsLGLpQEVMEQQLGTLSGGQRRRI 168
Cdd:COG1245 158 --GEIKVAHKpQYVDLIPKVFKgtvrELLEKVD----ERGKLDELAEK---------LGL-ENILDRDISELSGGELQRV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 169 ELARILFSDADTLILDEPTNHLD-------ADSIewlRGYLK--KYeggFLVISHSTELLD---EVVNKVWHLDAQLGQI 236
Cdd:COG1245 222 AIAAALLRDADFYFFDEPSSYLDiyqrlnvARLI---RELAEegKY---VLVVEHDLAILDylaDYVHILYGEPGVYGVV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 237 -DMYS--------LswKAYLhqrvvdeerrrrerevaekKAE--RLMKQGIRLHAKASKAVAaqnmmrRAEKLLEntsea 305
Cdd:COG1245 296 sKPKSvrvginqyL--DGYL-------------------PEEnvRIRDEPIEFEVHAPRREK------EEETLVE----- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 306 qkaekvadirFPepapcgrtpimakDISKAYGsnivfaGVNLAIDKGS----RVV-ILGYNGAGKTTTLRLLAHIEEPDT 380
Cdd:COG1245 344 ----------YP-------------DLTKSYG------GFSLEVEGGEiregEVLgIVGPNGIGKTTFAKILAGVLKPDE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 381 GSVEYghGCKIGYFAQ--EHDTldlNATVLENL-QHVAPELDNTQARSILGSFLfsGDDAM--KPAHVLSGGEKTRLALA 455
Cdd:COG1245 395 GEVDE--DLKISYKPQyiSPDY---DGTVEEFLrSANTDDFGSSYYKTEIIKPL--GLEKLldKNVKDLSGGELQRVAIA 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 489925987 456 TLVTSRANVLLLDEPTNNLDPASREEILKAIAKY----EGAIVLVTHD 499
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHD 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-219 |
5.34e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 87.15 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG--KLGYLPQDthasdptQTALDRMmsarD 90
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgiKLGYFAQH-------QLEFLRA----D 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATIINRIRKAEKEMtdpdpdvmtkamnryDKAMQDFdkAGGYAAQSEAISMATslglpqevmeqqlGTLSGGQRRRIEL 170
Cdd:PRK10636 392 ESPLQHLARLAPQEL---------------EQKLRDY--LGGFGFQGDKVTEET-------------RRFSGGEKARLVL 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 171 ARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELL 219
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLL 490
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
5.41e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 85.20 E-value: 5.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL------------GYL 68
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerrvGFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQdtHAsdptqtALDRMMSARD-IATIInRIRKAEKEmtdpdpDVMTKAMnRYDKAMQDFDKAGGYAAQseaismatslg 147
Cdd:COG1118 81 FQ--HY------ALFPHMTVAEnIAFGL-RVRPPSKA------EIRARVE-ELLELVQLEGLADRYPSQ----------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 lpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDA---DSIE-WLRGYLKKYEGGFLVISHSTE----LL 219
Cdd:COG1118 134 ------------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQEealeLA 201
|
....
gi 489925987 220 DEVV 223
Cdd:COG1118 202 DRVV 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
341-517 |
8.05e-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: 82.58 E-value: 8.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEyGHGcKIGYFAQEHDTLDLNATVLENLQHVAPEL-- 418
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-VRG-RVSSLLGLGGGFNPELTGRENIYLNGRLLgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 419 DNTQARSILGSFL-FS--GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREeilKAIAKYE----- 490
Cdd:cd03220 115 SRKEIDEKIDEIIeFSelGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE---KCQRRLRellkq 191
|
170 180
....*....|....*....|....*...
gi 489925987 491 -GAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03220 192 gKTVILVSHDPSSIKRLC-DRALVLEKG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-186 |
8.17e-18 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 82.59 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYL 68
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQdthasdptQTALDRMMSARDiatiinRIRKAEKEMTDPDpdvmTKAMNRYDKAMQDFDKAggyaaqseaiSMATSLGL 148
Cdd:cd03218 81 PQ--------EASIFRKLTVEE------NILAVLEIRGLSK----KEREEKLEELLEEFHIT----------HLRKSKAS 132
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 149 pqevmeqqlgTLSGGQRRRIELARILFSDADTLILDEP 186
Cdd:cd03218 133 ----------SLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
31-226 |
1.24e-17 |
|
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: 81.47 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 31 IGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQD--THASDPTQTALDRMMSARDIATiin 96
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQEfgVYPNFTVREFLDYIAWLKGIPS--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 riRKAEKEMtdpdpDVMTKAMNRYDKAmqdfdkaggyaaqseaismatslglpqevmEQQLGTLSGGQRRRIELARILFS 176
Cdd:cd03264 105 --KEVKARV-----DEVLELVNLGDRA------------------------------KKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 177 DADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVI--SHSTELLDEVVNKV 226
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQV 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
330-496 |
1.47e-17 |
|
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: 81.11 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----EYGH--------GCKIgyfaq 396
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgkSYQKniealrriGALI----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLDLNATVLENLQHVA--PELDNTQARSILGSFLFSgDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:cd03268 79 EAPGFYPNLTARENLRLLArlLGIRKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180
....*....|....*....|....
gi 489925987 475 DPASREEILKAIAKY--EGAIVLV 496
Cdd:cd03268 158 DPDGIKELRELILSLrdQGITVLI 181
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-222 |
1.71e-17 |
|
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: 80.98 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPqdthasdptQTALdrMMSardiATIIN 96
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVS---------QEPW--IQN----GTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 RIrkaekemtdpdpdVMTKAMN--RYDKAM------QDFDKaggyaaqseaismatslgLPQ----EVMEQqlG-TLSGG 163
Cdd:cd03250 85 NI-------------LFGKPFDeeRYEKVIkacalePDLEI------------------LPDgdltEIGEK--GiNLSGG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLDADSIEWL-----RGYLKKYEGGFLViSHSTELLDEV 222
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLNNKTRILV-THQLQLLPHA 194
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
13-215 |
1.80e-17 |
|
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: 85.49 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDptq 79
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFD--- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 taldrmmsardiATIINRIRKAEKEMTDPDpdvMTKAMNRydkamqdfdkaggyaAQSEAISMATSLGLpQEVMEQQLGT 159
Cdd:TIGR02868 423 ------------TTVRENLRLARPDATDEE---LWAALER---------------VGLADWLRALPDGL-DTVLGEGGAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDAD-SIEWLRGYLKKYEG-GFLVISHS 215
Cdd:TIGR02868 472 LSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-191 |
2.36e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 84.12 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTH------- 73
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG------DDVEalsaraa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 74 ----ASDPTQTALDRMMSARdiaTIINRIRKAEK----EMTDPDPDVMTKAMNRYDKAMqdfdkaggYAAQSeaismats 145
Cdd:PRK09536 76 srrvASVPQDTSLSFEFDVR---QVVEMGRTPHRsrfdTWTETDRAAVERAMERTGVAQ--------FADRP-------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 146 lglpqevmeqqLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK09536 137 -----------VTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
344-498 |
2.38e-17 |
|
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: 80.29 E-value: 2.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLA--HIEEPDTGSVEY-GH-------GCKIGYfAQEHDTLDLNATVLENLQH 413
Cdd:cd03213 27 NVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLInGRpldkrsfRKIIGY-VPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 414 VApeldntQARSIlgsflfsgddamkpahvlSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE---EILKAIAKYE 490
Cdd:cd03213 106 AA------KLRGL------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALqvmSLLRRLADTG 161
|
....*...
gi 489925987 491 GAIVLVTH 498
Cdd:cd03213 162 RTIICSIH 169
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
329-506 |
2.60e-17 |
|
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: 81.62 E-value: 2.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaQEHDTLDLNA--- 405
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF----------DGRDITGLPPhri 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 406 ------------------TVLENLQhVApeLDNTQARSILGSFLFS-----------------------GDDAMKPAHVL 444
Cdd:COG0411 77 arlgiartfqnprlfpelTVLENVL-VA--AHARLGRGLLAALLRLprarreereareraeellervglADRADEPAGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 445 SGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAIAKYEG-AIVLVTHDEGAVEAL 506
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELaelIRRLRDERGiTILLIEHDMDLVMGL 219
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
327-499 |
2.73e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.72 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH------------------- 387
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 388 GCKIGYFAQEHDtLDLNATVLENL-------QHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTS 460
Cdd:PRK11264 84 RQHVGFVFQNFN-LFPHRTVLENIiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRR-LSGGQQQRVAIARALAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 461 RANVLLLDEPTNNLDPASREEIL---KAIAKYEGAIVLVTHD 499
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLntiRQLAQEKRTMVIVTHE 203
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-204 |
3.00e-17 |
|
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: 81.23 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQT 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ---------ALDRMMSARDIATIINRIRKAEKEmtdPDPDVMTKAMNRYDKAMQDFDKAGGYAAQseaismatslglpqe 151
Cdd:cd03296 75 nvgfvfqhyALFRHMTVFDNVAFGLRVKPRSER---PPEAEIRAKVHELLKLVQLDWLADRYPAQ--------------- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 152 vmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:cd03296 137 --------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR 181
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-223 |
3.07e-17 |
|
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: 80.59 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------LGYLPQDtHASDPTQTALDR 84
Cdd:cd03293 15 GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEpvtgpgpdRGYVFQQ-DALLPWLTVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMSARDIAtiinRIRKAEkemtdpdpdvmtkamnRYDKAMQDFDKAG--GYAAQseaismatslgLPQEvmeqqlgtLSG 162
Cdd:cd03293 94 VALGLELQ----GVPKAE----------------ARERAEELLELVGlsGFENA-----------YPHQ--------LSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLDA----DSIEWLRGYLKKYEGGFLVISHStelLDEVV 223
Cdd:cd03293 135 GMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD---IDEAV 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
344-517 |
3.32e-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: 80.84 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG----------HGCKIGY-FAQEH---------DTLDL 403
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAglvpwkrrkkFLRRIGVvFGQKTqlwwdlpviDSFYL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 NATVL--------ENLQHVAPELDntqarsiLGSFLFSgddamkPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD 475
Cdd:cd03267 119 LAAIYdlpparfkKRLDELSELLD-------LEELLDT------PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 476 PASREEILKAI----AKYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03267 186 VVAQENIRNFLkeynRERGTTVLLTSHYMKDIEAL-ARRVLVIDKG 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-226 |
3.65e-17 |
|
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: 80.49 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQ 70
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DthasdptqTALDRMMSARDIATIINRIRKAEKEmtdpdpdvmtKAMNRYDKAMQDFDkaggyaaqseaismatsLGlpq 150
Cdd:cd03265 81 D--------LSVDDELTGWENLYIHARLYGVPGA----------ERRERIDELLDFVG-----------------LL--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 151 EVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGF----LVISHSTELLDEVVNKV 226
Cdd:cd03265 123 EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFgmtiLLTTHYMEEAEQLCDRV 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
337-498 |
4.21e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 337 GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGY----FAQE-----HdtldLNA-- 405
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLW-QGEPIRRqrdeYHQDllylgH----QPGik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 406 ---TVLENL---QHVAPELDNTQARSILGSFLFSG-DDAmkPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:PRK13538 87 telTALENLrfyQRLHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQG 164
|
170 180
....*....|....*....|...
gi 489925987 479 ---REEILKAIAKYEGAIVLVTH 498
Cdd:PRK13538 165 varLEALLAQHAEQGGMVILTTH 187
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-219 |
4.42e-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: 78.80 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIG--ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGY 67
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGAdisqwdpnelgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQDthasdptqtalDRMMSardiATIINRIrkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqseaismatslg 147
Cdd:cd03246 81 LPQD-----------DELFS----GSIAENI------------------------------------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 148 lpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR---GYLKKYEGGFLVISHSTELL 219
Cdd:cd03246 97 ------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNqaiAALKAAGATRIVIAHRPETL 159
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
330-498 |
4.42e-17 |
|
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: 80.14 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC------KIGYFAQEHDTLD 402
Cdd:TIGR03740 4 KNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFdGHPWtrkdlhKIGSLIESPPLYE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 lNATVLENLQHVAP--ELDNTQARSILgSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE 480
Cdd:TIGR03740 84 -NLTARENLKVHTTllGLPDSRIDEVL-NIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDPIGIQ 161
|
170 180
....*....|....*....|.
gi 489925987 481 EILKAIAKYEG---AIVLVTH 498
Cdd:TIGR03740 162 ELRELIRSFPEqgiTVILSSH 182
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
327-517 |
4.76e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY-GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC-------------KI 391
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsGHDItrlknrevpflrrQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 GYFAQEHDTLdLNATVLENLQH---VAPELDNTQARSILGSFLFSG--DDAMKPAHVLSGGEKTRLALATLVTSRANVLL 466
Cdd:PRK10908 82 GMIFQDHHLL-MDRTVYDNVAIpliIAGASGDDIRRRVSAALDKVGllDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489925987 467 LDEPTNNLDPASREEILKAIAKYE--GAIVLV-THDEGAVEALNpERVLLMPDG 517
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNrvGVTVLMaTHDIGLISRRS-YRMLTLSDG 213
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
13-227 |
4.82e-17 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 84.53 E-value: 4.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTH---ASDPTQTALDRMMSAR 89
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhvdGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 90 diatiinrirkaekemtdpdPDVMTKAMNrydkamqdfdkaggyaaqseaiSMATSLGLPQEVMEQQLGTLSGGQRRRIE 169
Cdd:PLN03073 600 --------------------PGVPEQKLR----------------------AHLGSFGVTGNLALQPMYTLSGGQKSRVA 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 170 LARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVW 227
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELW 695
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
327-517 |
5.86e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 80.18 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAgvNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGCKIGYFA----------Q 396
Cdd:COG3840 2 LRLDDLTYRYGDFPLRF--DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN-GQDLTALPpaerpvsmlfQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 E-----------------HDTLDLNATVLENLQHVApeldntqARSILGSFLfsgddAMKPAHvLSGGEKTRLALA-TLV 458
Cdd:COG3840 79 EnnlfphltvaqniglglRPGLKLTAEQRAQVEQAL-------ERVGLAGLL-----DRLPGQ-LSGGQRQRVALArCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 459 TSRaNVLLLDEPTNNLDPASREEIL---KAIAKYEGAIVL-VTHDEGAVEALNPeRVLLMPDG 517
Cdd:COG3840 146 RKR-PILLLDEPFSALDPALRQEMLdlvDELCRERGLTVLmVTHDPEDAARIAD-RVLLVADG 206
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-214 |
6.27e-17 |
|
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: 80.47 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQ- 79
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG------RDITGLPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 ------------------TALDRMMSARDIATiinrirkaekemtdpdPDVMTKAMNRYDKAMQDFDkaggyAAQSEAIS 141
Cdd:COG0411 77 arlgiartfqnprlfpelTVLENVLVAAHARL----------------GRGLLAALLRLPRARREER-----EARERAEE 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 142 MATSLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT---NHLDADSI-EWLRGyLKKYEG-GFLVISH 214
Cdd:COG0411 136 LLERVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELaELIRR-LRDERGiTILLIEH 211
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-191 |
7.04e-17 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 80.10 E-value: 7.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQ-IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQ 79
Cdd:COG3638 1 PMLELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQ-----------DVTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 TALDRMMSAR-DIATI------INRIRkaekemtdpdpdVMT-------------KAM-NRYDKAmqdfDKAGGYAAQSE 138
Cdd:COG3638 70 LRGRALRRLRrRIGMIfqqfnlVPRLS------------VLTnvlagrlgrtstwRSLlGLFPPE----DRERALEALER 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 139 aismatsLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG3638 134 -------VGL-ADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
327-517 |
7.62e-17 |
|
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: 79.33 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEyghgckIGYFAQEHDTLD 402
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAT------VDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 LNA---------------TVLENLQHVAP----ELDNTQAR-SILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRA 462
Cdd:cd03266 76 ARRrlgfvsdstglydrlTARENLEYFAGlyglKGDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 463 NVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLraLGkCILFSTHIMQEVERL-CDRVVVLHRG 212
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
341-512 |
7.89e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.62 E-value: 7.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLL--AHIEEPDTGSVEYghgckigyfaqEHDTLDLNATVLEnlqHVAPEL 418
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDV-----------PDNQFGREASLID---AIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 419 DNTQARSILGS------FLFsgddaMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAK---- 488
Cdd:COG2401 111 DFKDAVELLNAvglsdaVLW-----LRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKlarr 185
|
170 180
....*....|....*....|....
gi 489925987 489 YEGAIVLVTHDEGAVEALNPERVL 512
Cdd:COG2401 186 AGITLVVATHHYDVIDDLQPDLLI 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
331-517 |
9.59e-17 |
|
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: 79.69 E-value: 9.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 331 DISKAYGsNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGCKI----------GYFAQEHdT 400
Cdd:cd03299 5 NLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGKDItnlppekrdiSYVPQNY-A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLNATVLENL------QHVAPELDNTQARSILGSFLFSGDDAMKPAhVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:cd03299 82 LFPHMTVYKNIayglkkRKVDKKEIERKVLEIAEMLGIDHLLNRKPE-TLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 475 DPAS----REEILKAIAKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03299 161 DVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALA-DKVAIMLNG 206
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-194 |
1.03e-16 |
|
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: 79.45 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 14 ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPtqTALDRMMS-ARDIA 92
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG------HDLALADP--AWLRRQVGvVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIINRIRKAEKEMTDPDPDvmtkamnrydkaMQDFDKAGGYAAQSEAIsMATSLGLPQEVMEQQLGtLSGGQRRRIELAR 172
Cdd:cd03252 86 VLFNRSIRDNIALADPGMS------------MERVIEAAKLAGAHDFI-SELPEGYDTIVGEQGAG-LSGGQRQRIAIAR 151
|
170 180
....*....|....*....|..
gi 489925987 173 ILFSDADTLILDEPTNHLDADS 194
Cdd:cd03252 152 ALIHNPRILIFDEATSALDYES 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-239 |
1.18e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.36 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK------LGylpqdthasdptqTALDRMMSARD----I 91
Cdd:COG1134 46 SFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsalleLG-------------AGFHPELTGREniylN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ATIINRIRKAEKEMTDpdpDVmtkamnrydkamQDFdkaggyaaqSEaismatsLGlpqEVMEQQLGTLSGGQRrrielA 171
Cdd:COG1134 113 GRLLGLSRKEIDEKFD---EI------------VEF---------AE-------LG---DFIDQPVKTYSSGMR-----A 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 172 RILFS-----DADTLILDEPTNHLDAD----SIEWLRGYLKKyEGGFLVISHSTELLDEVVNKVWHLDAqlGQIDMY 239
Cdd:COG1134 154 RLAFAvatavDPDILLVDEVLAVGDAAfqkkCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEK--GRLVMD 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-212 |
1.25e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 78.31 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPT---- 78
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG------EPIRRQRDEyhqd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 ------QTALDRMMSARDIATIINRIRKaekemtDPDPDVMTKAMnrydkamqdfdkaggyaaqsEAISMATSLGLPqev 152
Cdd:PRK13538 76 llylghQPGIKTELTALENLRFYQRLHG------PGDDEALWEAL--------------------AQVGLAGFEDVP--- 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 153 meqqLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY-EGGFLVI 212
Cdd:PRK13538 127 ----VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHaEQGGMVI 183
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-215 |
1.42e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQdtHASDPT-- 78
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD--VAEACHyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 --QTALDRMMSARDIATIINRIRKAEkemtDPDPDvmtkamnrydkamqdfdkaggyaaqsEAIsmaTSLGLpQEVMEQQ 156
Cdd:PRK13539 79 ghRNAMKPALTVAENLEFWAAFLGGE----ELDIA--------------------------AAL---EAVGL-APLAHLP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 157 LGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWL----RGYLKKyeGGFLVIS-HS 215
Cdd:PRK13539 125 FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFaeliRAHLAQ--GGIVIAAtHI 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
327-517 |
1.45e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.29 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCKIGYFAQEHDTLDL-- 403
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIaGNHFDFSKTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 -------------NATVLENL-------QHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRAN 463
Cdd:PRK11124 83 nvgmvfqqynlwpHLTVQQNLieapcrvLGLSKDQALARAEKLLERLRLKPYADRFPLH-LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 464 VLLLDEPTNNLDPASREEILKAIAKY-EGAI--VLVTHdEGAVEALNPERVLLMPDG 517
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELaETGItqVIVTH-EVEVARKTASRVVYMENG 217
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
3-202 |
1.62e-16 |
|
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: 78.17 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylPQDTHASDPTQT-- 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT----PLAEQRDEPHENil 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ------ALDRMMSARDIATIINRIRKAEkemtDPDPDVMTKAMNRYDKAmqdfdkaggyaaqseaismatslGLPqevme 154
Cdd:TIGR01189 77 ylghlpGLKPELSALENLHFWAAIHGGA----QRTIEDALAAVGLTGFE-----------------------DLP----- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 155 qqLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYL 202
Cdd:TIGR01189 125 --AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
330-518 |
1.91e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.92 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTG------------SVEYGHGCKI--GYFA 395
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGqifidgedvthrSIQQRDICMVfqSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHDTLDLNATVLENLQHVAPELDNTQARSILGSFLFSGddaMKPAHV--LSGGEKTRLALATLVTSRANVLLLDEPTNN 473
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAG---FEDRYVdqISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 474 LDP----ASREEILKAIAKYEGAIVLVTHDEGAVEALNPErVLLMPDGD 518
Cdd:PRK11432 167 LDAnlrrSMREKIRELQQQFNITSLYVTHDQSEAFAVSDT-VIVMNKGK 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
344-517 |
2.12e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 79.39 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-------------EYGHgcKIGYFAQEHDTLDLNATV--- 407
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwDIRH--KIGMVFQNPDNQFVGATVedd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 ----LEN--LQHVAPELDNTQARSILGSFLFSGDDamkPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:PRK13650 103 vafgLENkgIPHEEMKERVNEALELVGMQDFKERE---PAR-LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 482 ILKAIAK----YEGAIVLVTHDEGAVeALNpERVLLMPDG 517
Cdd:PRK13650 179 LIKTIKGirddYQMTVISITHDLDEV-ALS-DRVLVMKNG 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-226 |
2.40e-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 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: 79.42 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 14 ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQtaldrmmsardiat 93
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG------RDITAKKKKK-------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 iINRIRK--------AEK---EMTDPDpDVMTKAMNrydkamQDFDKAGGYAAQSEAISMatsLGLPQEVMEQQLGTLSG 162
Cdd:TIGR04521 77 -LKDLRKkvglvfqfPEHqlfEETVYK-DIAFGPKN------LGLSEEEAEERVKEALEL---VGLDEEYLERSPFELSG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGGFLVI--SHSTELLDEVVNKV 226
Cdd:TIGR04521 146 GQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVIlvTHSMEDVAEYADRV 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
330-488 |
2.61e-16 |
|
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: 78.43 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYG-SNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK----------IGYFAQe 397
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIRevtldslrraIGVVPQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 hDTLDLNATVLENLQHVAPELDNTQARsilgsflfsgdDAMKPAHV---------------------LSGGEKTRLALAT 456
Cdd:cd03253 83 -DTVLFNDTIGYNIRYGRPDATDEEVI-----------EAAKAAQIhdkimrfpdgydtivgerglkLSGGEKQRVAIAR 150
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 457 LVTSRANVLLLDEPTNNLDPASREEILKAIAK 488
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRD 182
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
332-524 |
2.74e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 332 ISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGC----------KIGYFAQeHDTL 401
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-HGTdvsrlhardrKVGFVFQ-HYAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENL-------------------QHVAPELDNTQARSILGSFlfsgddamkPAHvLSGGEKTRLALATLVTSRA 462
Cdd:PRK10851 86 FRHMTVFDNIafgltvlprrerpnaaaikAKVTQLLEMVQLAHLADRY---------PAQ-LSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 463 NVLLLDEPTNNLDPASREEILKAIAKYEGAI----VLVTHD-EGAVEALNpeRVLLMPDGD-------EDLWND 524
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELkftsVFVTHDqEEAMEVAD--RVVVMSQGNieqagtpDQVWRE 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-199 |
2.77e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgYLPQdthasdptqta 81
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGE--PVPS----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 ldRMMSARDIATIInrirkaeKEMTDPDPDVMTKamnrydKAMQDFDKAGGYAAQSEAISMATSLGLP--QEVMEQQLGT 159
Cdd:PRK13537 74 --RARHARQRVGVV-------PQFDNLDPDFTVR------ENLLVFGRYFGLSAAAARALVPPLLEFAklENKADAKVGE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLD--ADSIEWLR 199
Cdd:PRK13537 139 LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWER 180
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
330-496 |
2.81e-16 |
|
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: 78.10 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGckIGYFA 395
Cdd:COG0410 7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgeditglpphriarLG--IGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHD---TLdlnaTVLENLQhvapeldntqarsiLGSFLFSGDDAMK-------------------PAHVLSGGEKTRLA 453
Cdd:COG0410 85 EGRRifpSL----TVEENLL--------------LGAYARRDRAEVRadlervyelfprlkerrrqRAGTLSGGEQQMLA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 454 LA-TLVtSRANVLLLDEPTNNLDPASREEILKAIA--KYEG-AIVLV 496
Cdd:COG0410 147 IGrALM-SRPKLLLLDEPSLGLAPLIVEEIFEIIRrlNREGvTILLV 192
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-192 |
2.88e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.59 E-value: 2.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQI---------GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK------- 64
Cdd:COG1116 1 MSAAAPALELRGvskrfptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKpvtgpgp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 65 -LGYLPQDtHASDPTQTALDRMMSARDIAtiinRIRKAEkemtdpdpdvmtkamnRYDKAMqdfdkaggyaaqsEAISMa 143
Cdd:COG1116 81 dRGVVFQE-PALLPWLTVLDNVALGLELR----GVPKAE----------------RRERAR-------------ELLEL- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 144 tsLGL-------PQEvmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:COG1116 126 --VGLagfedayPHQ--------LSGGMRQRVAIARALANDPEVLLMDEPFGALDA 171
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
284-498 |
2.91e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 81.75 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 284 KAVAAqnmMRRAEKLLENTSEaqkaekVADIRFPEPAPCGRTPIMAKDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNG 362
Cdd:COG1132 306 RALAS---AERIFELLDEPPE------IPDPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSG 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 363 AGKTTTLRLLAHIEEPDTGSVEYGhGC------------KIGYFAQehDTLDLNATVLENLQHVAPELDNTQARsilgsf 430
Cdd:COG1132 377 SGKSTLVNLLLRFYDPTSGRILID-GVdirdltleslrrQIGVVPQ--DTFLFSGTIRENIRYGRPDATDEEVE------ 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 431 lfsgdDAMKPAHV---------------------LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY 489
Cdd:COG1132 448 -----EAAKAAQAhefiealpdgydtvvgergvnLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL 522
|
250
....*....|.
gi 489925987 490 -EGAIVLV-TH 498
Cdd:COG1132 523 mKGRTTIViAH 533
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
320-498 |
3.45e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 320 APCGRTPIMAKD---ISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY----------G 386
Cdd:PRK13536 32 SIPGSMSTVAIDlagVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 387 HGCKIGYFAQeHDTLDLNATVLENLQhVAPELDNTQARSI------LGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTS 460
Cdd:PRK13536 112 ARARIGVVPQ-FDNLDLEFTVRENLL-VFGRYFGMSTREIeavipsLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 461 RANVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVLVTH 498
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHliwERLRSLLARGKTILLTTH 230
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
329-517 |
3.70e-16 |
|
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: 78.45 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------------HGCKIGY 393
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamsrkelrelRRKKISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQeHDTLDLNATVLEN------LQHVAPELDNTQARSILGSFLFSGDDAMKPaHVLSGGEKTRLALATLVTSRANVLLL 467
Cdd:cd03294 107 VFQ-SFALLPHRTVLENvafgleVQGVPRAEREERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 468 DEPTNNLDPASR----EEILKAIAKYEGAIVLVTHDegAVEALN-PERVLLMPDG 517
Cdd:cd03294 185 DEAFSALDPLIRremqDELLRLQAELQKTIVFITHD--LDEALRlGDRIAIMKDG 237
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
332-516 |
4.13e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 78.20 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 332 ISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY------GHGCKIGYFAQeHDTLDLNA 405
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQ-NEGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 406 TVLEN------LQHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:PRK11248 86 NVQDNvafglqLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 480 EE----ILKAIAKYEGAIVLVTHD-EGAVeALNPERVLLMPD 516
Cdd:PRK11248 165 EQmqtlLLKLWQETGKQVLLITHDiEEAV-FMATELVLLSPG 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-236 |
4.81e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEI-QIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGKVRVSG-------------KLGYL 68
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGielreldpeswrkHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQDTHASDptqtaldrmmsardiATIINRIRKAEKEMTDpdpdvmtkamnryDKAMQDFDKAggYAaqSEAISMATsLGL 148
Cdd:PRK11174 429 GQNPQLPH---------------GTLRDNVLLGNPDASD-------------EQLQQALENA--WV--SEFLPLLP-QGL 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 149 PQEVMEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISHSTELLDEvVNKV 226
Cdd:PRK11174 476 DTPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRqtTLMVTHQLEDLAQ-WDQI 553
|
250
....*....|
gi 489925987 227 WHLDAqlGQI 236
Cdd:PRK11174 554 WVMQD--GQI 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-194 |
5.70e-16 |
|
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: 77.27 E-value: 5.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDptqtaldr 84
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdytlaslrrQIGLVSQDVFLFN-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 mmsardiATIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMQdfdKAGGYaaqseaismatslglpQEVMEQQLGTLSGGQ 164
Cdd:cd03251 90 -------DTVAENIAYGRPGATREEVEEAARAANAHEFIME---LPEGY----------------DTVIGERGVKLSGGQ 143
|
170 180 190
....*....|....*....|....*....|
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
344-517 |
6.08e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 6.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGcKIGYFaqehdtLDLNA------TVLENLQHVApe 417
Cdd:COG1134 44 DVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NG-RVSAL------LELGAgfhpelTGRENIYLNG-- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 418 ldntqarSILGsflFSGDDAMK-----------------PAHVLSGGEKTRLALATLVTSRANVLLLDEptnNL---DPA 477
Cdd:COG1134 114 -------RLLG---LSRKEIDEkfdeivefaelgdfidqPVKTYSSGMRARLAFAVATAVDPDILLVDE---VLavgDAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 478 SRE---EILKAIAKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:COG1134 181 FQKkclARIRELRESGRTVIFVSHSMGAVRRLC-DRAIWLEKG 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-506 |
7.02e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-------YGHGCKIGYFAQEHDtL 401
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldPEDRRRIGYLPEERG-L 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENLQHVApEL---DNTQARSILGSFL--FS-GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD 475
Cdd:COG4152 83 YPKMKVGEQLVYLA-RLkglSKAEAKRRADEWLerLGlGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 476 PASREEILKAI--AKYEGA-IVLVTHDEGAVEAL 506
Cdd:COG4152 162 PVNVELLKDVIreLAAKGTtVIFSSHQMELVEEL 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
344-532 |
7.37e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 7.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----------EYGHGCKIGYFAQEHDTLDLNATVLE--- 409
Cdd:PRK13647 23 GLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaenEKWVRSKVGLVFQDPDDQVFSSTVWDdva 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 ----NLQHVAPELDN--TQARSILGSFLFsgddAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE--- 480
Cdd:PRK13647 103 fgpvNMGLDKDEVERrvEEALKAVRMWDF----RDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQEtlm 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 481 EILKAIAKYEGAIVLVTHD-EGAVE------ALNPERVLlmPDGDEDLWNDSylDLVAE 532
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDvDLAAEwadqviVLKEGRVL--AEGDKSLLTDE--DIVEQ 233
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
3-191 |
7.65e-16 |
|
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: 77.55 E-value: 7.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLP 69
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGvdlhglsrrararRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 70 QDTHASDPtqtaldrmMSARDiATIINRIRKAEKEMTDPDPDVMTkamnrydkamqdfdkAGGYAAQSEAISMATslglp 149
Cdd:TIGR03873 82 QDSDTAVP--------LTVRD-VVALGRIPHRSLWAGDSPHDAAV---------------VDRALARTELSHLAD----- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 150 qevmeQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:TIGR03873 133 -----RDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
327-517 |
8.87e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 8.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY-GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-------YGHGC------KIG 392
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 393 YFAQEHDTLDLNATVLE-------NLQHVAPELDNtQARSILGSFLFSGDDAmKPAHVLSGGEKTRLALATLVTSRANVL 465
Cdd:PRK13639 82 IVFQNPDDQLFAPTVEEdvafgplNLGLSKEEVEK-RVKEALKAVGMEGFEN-KPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 466 LLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEGAVeALNPERVLLMPDG 517
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLnkEGiTIIISTHDVDLV-PVYADKVYVMSDG 213
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
307-517 |
1.07e-15 |
|
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: 79.70 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 307 KAEKVADIRFPEPAPCGRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG 386
Cdd:TIGR01842 299 ANYPSRDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 387 -----------HGCKIGYFAQEHDTLDlnATVLENlqhVAPELDNTQARSILGSFLFSG------------DDAMKPAHV 443
Cdd:TIGR01842 379 gadlkqwdretFGKHIGYLPQDVELFP--GTVAEN---IARFGENADPEKIIEAAKLAGvhelilrlpdgyDTVIGPGGA 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 444 -LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI--AKYEGAIVLV-THDEGAVEALNpeRVLLMPDG 517
Cdd:TIGR01842 454 tLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIkaLKARGITVVViTHRPSLLGCVD--KILVLQDG 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-236 |
1.15e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 77.15 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 16 TLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQT-ALDR--MMSARDIA 92
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRG------QDLYQLDRKQRrAFRRdvQLVFQDSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIINRIRKAEKEMTDPdpdvmTKAMNRYDKAMQdfdkaggyaaQSEAISMATSLGLPQEVMEQQLGTLSGGQRRRIELAR 172
Cdd:TIGR02769 99 SAVNPRMTVRQIIGEP-----LRHLTSLDESEQ----------KARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 173 ILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQI 236
Cdd:TIGR02769 164 ALAVKPKLIVLDEAVSNLDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQI 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
344-517 |
1.21e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.20 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-----HGCK--------IGYFAQEHDTLDLNATVLE- 409
Cdd:PRK13636 24 GININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpidYSRKglmklresVGMVFQDPDNQLFSASVYQd 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 ------NLQ----HVAPELDNTQARSILGSFlfsgddAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:PRK13636 104 vsfgavNLKlpedEVRKRVDNALKRTGIEHL------KDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 480 EEI---LKAIAKYEG-AIVLVTHDEGAVeALNPERVLLMPDG 517
Cdd:PRK13636 178 SEImklLVEMQKELGlTIIIATHDIDIV-PLYCDNVFVMKEG 218
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-511 |
1.23e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 76.69 E-value: 1.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGCKIGYFaQEHD-------------TLDLNATVLEN 410
Cdd:COG4674 28 DLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFG-GTDLTGL-DEHEiarlgigrkfqkpTVFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 411 LqhvapELDNTQARSILGSFLFS------------------GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTN 472
Cdd:COG4674 106 L-----ELALKGDRGVFASLFARltaeerdrieevletiglTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 473 NLDPASRE---EILKAIAKyEGAIVLVTHDEGAVEALNpERV 511
Cdd:COG4674 181 GMTDAETErtaELLKSLAG-KHSVVVVEHDMEFVRQIA-RKV 220
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-204 |
1.28e-15 |
|
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: 76.45 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGA-RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----------------KL 65
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 66 GYLPQDtHASDPTQTALDRMMSAR-----DIATIINRIRKAEKEmtdpdpdvmtkamnrydkamqdfdkaggyaaqsEAI 140
Cdd:cd03256 81 GMIFQQ-FNLIERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQ---------------------------------RAL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 141 SMATSLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:cd03256 127 AALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKR 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-497 |
1.54e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.29 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPTQt 80
Cdd:COG1129 3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE------PVRFRSPRD- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 aldrmmsARD--IATI---INRIrkaekemtdPDpdvMTKA----MNRYDKAMQDFDKAggyAAQSEAISMATSLGLPQE 151
Cdd:COG1129 76 -------AQAagIAIIhqeLNLV---------PN---LSVAenifLGREPRRGGLIDWR---AMRRRARELLARLGLDID 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 152 VmEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWL----RGyLKKyEG-GFLVISHStelLDEVvnkv 226
Cdd:COG1129 134 P-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLfriiRR-LKA-QGvAIIYISHR---LDEV---- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 227 whldaqlgqidmYSLswkaylhqrvvdeerrrrerevaekkAERL--MKQGirlhakasKAVaaqnmmrrAEKLLENTSE 304
Cdd:COG1129 204 ------------FEI--------------------------ADRVtvLRDG--------RLV--------GTGPVAELTE 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 305 AQKAE-----KVADiRFPEPAPCGRTPIM-AKDISKAYgsniVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEP 378
Cdd:COG1129 230 DELVRlmvgrELED-LFPKRAAAPGEVVLeVEGLSVGG----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPA 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 379 DTGSVEYG--------------HGckIGYFAQE--HDTLDLNATVLENLqhVAPELD-------------NTQARSILGS 429
Cdd:COG1129 305 DSGEIRLDgkpvrirsprdairAG--IAYVPEDrkGEGLVLDLSIRENI--TLASLDrlsrgglldrrreRALAEEYIKR 380
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 430 FLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVT 497
Cdd:COG1129 381 LRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELaaEGkAVIVIS 451
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
329-506 |
2.19e-15 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 76.05 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNI----VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH------GCKIGYFAQEH 398
Cdd:COG4525 6 VRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGvpvtgpGADRGVVFQKD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DTLD-LNatVLEN------LQHVAPELDNTQARSILgSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:COG4525 86 ALLPwLN--VLDNvafglrLRGVPKAERRARAEELL-ALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 472 NNLDPASRE---EILKAIAKYEGAIV-LVTHD-EgavEAL 506
Cdd:COG4525 163 GALDALTREqmqELLLDVWQRTGKGVfLITHSvE---EAL 199
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
22-191 |
2.49e-15 |
|
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: 75.23 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK------------LGYLPQDthasDptqtALDRMMSAR 89
Cdd:cd03263 22 SLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarqsLGYCPQF----D----ALFDELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 90 DIATIINRIRKAEKEMtdpdpdvmtkamnrydkamqdfdkaggyaAQSEAISMATSLGLpQEVMEQQLGTLSGGQRRRIE 169
Cdd:cd03263 94 EHLRFYARLKGLPKSE-----------------------------IKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLS 143
|
170 180
....*....|....*....|..
gi 489925987 170 LARILFSDADTLILDEPTNHLD 191
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLD 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
344-518 |
2.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.28 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-----------YGHGCKIGYFAQEHDTLDLNATV----- 407
Cdd:PRK13642 25 GVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgelltaenvWNLRRKIGMVFQNPDNQFVGATVeddva 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 --LENLQHVAPELDNTQARSILGSFLFsgDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKA 485
Cdd:PRK13642 105 fgMENQGIPREEMIKRVDEALLAVNML--DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 486 IA----KYEGAIVLVTHDEGavEALNPERVLLMPDGD 518
Cdd:PRK13642 183 IHeikeKYQLTVLSITHDLD--EAASSDRILVMKAGE 217
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
327-499 |
2.69e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 75.43 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC---------------- 389
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaGHQFdfsqkpsekairllrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 KIGY-FAQEHdtLDLNATVLENLQHvAP--------ELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTS 460
Cdd:COG4161 83 KVGMvFQQYN--LWPHLTVMENLIE-APckvlglskEQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 461 RANVLLLDEPTNNLDP---ASREEILKAIAKYEGAIVLVTHD 499
Cdd:COG4161 159 EPQVLLFDEPTAALDPeitAQVVEIIRELSQTGITQVIVTHE 200
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-223 |
4.31e-15 |
|
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: 74.50 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------LGYLPQ-DTHASDPTQTALDRMMSARdiAT 93
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAspgkgwrhIGYVPQrHEFAWDFPISVAHTVMSGR--TG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 IINRIRKAEKEmtdpdpdvmtkamnrydkamqDFdkaggyAAQSEAISMAtslGLpQEVMEQQLGTLSGGQRRRIELARI 173
Cdd:TIGR03771 79 HIGWLRRPCVA---------------------DF------AAVRDALRRV---GL-TELADRPVGELSGGQRQRVLVARA 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 174 LFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVV 223
Cdd:TIGR03771 128 LATRPSVLLLDEPFTGLDMPTQELLTELFIELAGAGTAILMTTHDLAQAM 177
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
347-517 |
4.53e-15 |
|
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: 74.07 E-value: 4.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 347 LAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGS-----VEYGHGC----KIGYFAQEHDtLDLNATVLENLQ-HVAP 416
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingVDVTAAPpadrPVSMLFQENN-LFAHLTVEQNVGlGLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 417 EL-----DNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALA-TLVTSRAnVLLLDEPTNNLDPASREEILKAIAKY- 489
Cdd:cd03298 98 GLkltaeDRQAIEVALARVGLAGLEKRLPGE-LSGGERQRVALArVLVRDKP-VLLLDEPFAALDPALRAEMLDLVLDLh 175
|
170 180 190
....*....|....*....|....*....|.
gi 489925987 490 ---EGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:cd03298 176 aetKMTVLMVTHQPEDAKRLA-QRVVFLDNG 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-204 |
4.69e-15 |
|
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: 73.38 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQTAL 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGE-----------DLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMMSARDIATIINrirkaekemtdpDPDVMTKaMNRYDKamqdfdkaggyaaqseaismatsLGLPqevmeqqlgtLSG 162
Cdd:cd03229 70 ELPPLRRRIGMVFQ------------DFALFPH-LTVLEN-----------------------IALG----------LSG 103
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:cd03229 104 GQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKS 145
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
344-519 |
5.10e-15 |
|
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: 74.42 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGCKIGYFAQEHDTLDLN------ATVLENL----QH 413
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV-ILEGKQITEPGPDRMVVFQNysllpwLTVRENIalavDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 414 VAPELDNTQARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR----EEILKAI 486
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALvglTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRgnlqEELMQIW 161
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 487 AKYEGAIVLVTHDegAVEALN-PERVLLMPDGDE 519
Cdd:TIGR01184 162 EEHRVTVLMVTHD--VDEALLlSDRVVMLTNGPA 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
327-517 |
5.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 75.17 E-value: 5.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC-----------KIGY 393
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklrkHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQEHDTLDLNATV-------LENlqHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLL 466
Cdd:PRK13648 88 VFQNPDNQFVGSIVkydvafgLEN--HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 467 LDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDegAVEALNPERVLLMPDG 517
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVrkvkSEHNITIISITHD--LSEAMEADHVIVMNKG 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-199 |
8.64e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 8.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYL 68
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQ-DThaSDPTQTALDRM--------MSARDIATIInrirkaekemtdpdPDVMTKAmnRYDKamqdfdKAGGYAAQsea 139
Cdd:PRK13536 120 PQfDN--LDLEFTVRENLlvfgryfgMSTREIEAVI--------------PSLLEFA--RLES------KADARVSD--- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 140 ismatslglpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD--ADSIEWLR 199
Cdd:PRK13536 173 --------------------LSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIWER 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
341-517 |
1.23e-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: 73.24 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHG------CKigyfAQEHDTLDLNAT-------- 406
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlAQ----ASPREILALRRRtigyvsqf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 407 ------------VLENLQH--VAPELDNTQARSILGSF-----LFSgddaMKPAhVLSGGEKTRLALATLVTSRANVLLL 467
Cdd:COG4778 102 lrviprvsaldvVAEPLLErgVDREEARARARELLARLnlperLWD----LPPA-TFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 468 DEPTNNLDPASREEILKAI--AKYEG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:COG4778 177 DEPTASLDAANRAVVVELIeeAKARGtAIIGIFHDEEVREAV-ADRVVDVTPF 228
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
16-192 |
1.23e-14 |
|
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: 71.96 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 16 TLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdPTQTALDRMmsaRDIATII 95
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV------------PVSDLEKAL---SSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 96 NRirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqsEAISMATSLGlpqevmeQQLGT-LSGGQRRRIELARIL 174
Cdd:cd03247 81 NQ----------------------------------------RPYLFDTTLR-------NNLGRrFSGGERQRLALARIL 113
|
170
....*....|....*...
gi 489925987 175 FSDADTLILDEPTNHLDA 192
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDP 131
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
344-517 |
1.33e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.74 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV------------EYGHgcKIGY-FAQE---------HDTL 401
Cdd:COG4586 40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrvlgyvpfkrrkEFAR--RIGVvFGQRsqlwwdlpaIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATV--------LENLQHVAPELDntqarsiLGSFLfsgddaMKPAHVLSGGEKTR--LALATLvtSRANVLLLDEPT 471
Cdd:COG4586 118 RLLKAIyripdaeyKKRLDELVELLD-------LGELL------DTPVRQLSLGQRMRceLAAALL--HRPKILFLDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 472 NNLDPASREEILKAIAKY---EGA-IVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnreRGTtILLTSHDMDDIEALC-DRVIVIDHG 231
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-215 |
1.40e-14 |
|
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: 72.98 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGKVRVSGKLGYLPQDTHASDPTQTAL 82
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNR-LNDLIPGAPDEGEVLLDGKDIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 dRmmsaRDIATIINRirkaekemtdPDPDVMTKAMN-RY-DKAMQDFDKAGGYAAQSEAISMAtslGLPQEVMEQQLGT- 159
Cdd:cd03260 80 -R----RRVGMVFQK----------PNPFPGSIYDNvAYgLRLHGIKLKEELDERVEEALRKA---ALWDEVKDRLHALg 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDADS---IEWLRGYLKKyEGGFLVISHS 215
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHN 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-199 |
1.55e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 74.37 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG---------KLGYLPQDt 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGepldpedrrRIGYLPEE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 73 hasdptqTALDRMMSARDIATIINRIRKaekemtdpdpdvMTKAmnrydkamqdfdkaggyAAQSEAISMATSLGLPqEV 152
Cdd:COG4152 80 -------RGLYPKMKVGEQLVYLARLKG------------LSKA-----------------EAKRRADEWLERLGLG-DR 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 153 MEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR 199
Cdd:COG4152 123 ANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLK 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
23-222 |
1.56e-14 |
|
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: 72.79 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLGYLPQDThasdptqtALDRMMSARD 90
Cdd:cd03266 26 FTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDST--------GLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATIINRIRkaekemtdpdpdvmtkAMNRyDKAMQDFDKaggyaaqseaisMATSLGLpQEVMEQQLGTLSGGQRRRIEL 170
Cdd:cd03266 98 NLEYFAGLY----------------GLKG-DELTARLEE------------LADRLGM-EELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 171 ARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEV 222
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEV 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
345-517 |
2.03e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 73.68 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGS--------VEYGHGC------KIGYFAQEHDTLDLNATV--- 407
Cdd:PRK13640 26 ISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTvwdireKVGIVFQNPDNQFVGATVgdd 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 408 ----LENLQHVAPELDNTQARSILGSFLFSGDDAmKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:PRK13640 106 vafgLENRAVPRPEMIKIVRDVLADVGMLDYIDS-EPAN-LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQIL 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 484 KAIAKYEG----AIVLVTHDEGavEALNPERVLLMPDG 517
Cdd:PRK13640 184 KLIRKLKKknnlTVISITHDID--EANMADQVLVLDDG 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
340-518 |
2.86e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 340 IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKI------GYF--------------AQEHD 399
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVlflpqrPYLplgtlreallypatAEAFS 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLnATVLE--NLQHVAPELDNTQARSilgsflfsgddamkpaHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPA 477
Cdd:COG4178 457 DAEL-REALEavGLGHLAERLDEEADWD----------------QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 478 SREEILKAIAK--YEGAIVLVTHDEgAVEALNPERVLLMPDGD 518
Cdd:COG4178 520 NEAALYQLLREelPGTTVISVGHRS-TLAAFHDRVLELTGDGS 561
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
3-212 |
3.16e-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: 71.37 E-value: 3.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASD----PT 78
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGllylGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 QTALDRMMSARDIATIINRIRKAEKEMTdpdpdvmtkamnrydkAMQDFDKAGgyaaqseaismatslglpqeVMEQQLG 158
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQVEE----------------ALARVGLNG--------------------FEDRPVA 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY-EGGFLVI 212
Cdd:cd03231 125 QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcARGGMVV 179
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-214 |
3.51e-14 |
|
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: 71.87 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHA-SDptqtald 83
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLfSG------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 84 rmmsardiaTIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMQdfdKAGGYaaqseaismatslglpQEVMEQQLGTLSGG 163
Cdd:cd03254 92 ---------TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMK---LPNGY----------------DTVLGENGGNLSQG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISH 214
Cdd:cd03254 144 ERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
325-475 |
3.83e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 325 TPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQE---HDTL 401
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlylDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 DLNATVLENL------QHVAPELDNTQARSILGSflfsgddamkPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD 475
Cdd:PRK09544 83 PLTVNRFLRLrpgtkkEDILPALKRVQAGHLIDA----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-517 |
4.61e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.86 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 309 EKVADIRFPE--PAPCGRTPIMAKDISKAY--GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE 384
Cdd:PRK11160 319 EQKPEVTFPTtsTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 385 YGhGCKIGYFAQehDTLD------------LNATVLENLQHVAPELDNTQARSILG----SFLFSGDDAM--------KP 440
Cdd:PRK11160 399 LN-GQPIADYSE--AALRqaisvvsqrvhlFSATLRDNLLLAAPNASDEALIEVLQqvglEKLLEDDKGLnawlgeggRQ 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 441 ahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EGAIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:PRK11160 476 ---LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQFD--RICVMDNG 549
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-217 |
4.89e-14 |
|
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: 71.17 E-value: 4.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 25 VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-----------------KLGYLPQdthasdptQTALDRMMS 87
Cdd:cd03297 20 DLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrkkinlppqqrKIGLVFQ--------QYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 88 AR-DIATIINRIRKAEKEmtdpdpdvmtkamnrydkamQDFDKaggyaaqseaisMATSLGLpQEVMEQQLGTLSGGQRR 166
Cdd:cd03297 92 VReNLAFGLKRKRNREDR--------------------ISVDE------------LLDLLGL-DHLLNRYPAQLSGGEKQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 167 RIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK----YEGGFLVISHSTE 217
Cdd:cd03297 139 RVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHDLS 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
345-517 |
5.05e-14 |
|
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: 73.60 E-value: 5.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------------HGCKIGYFAQEHdTLDLNATVLE 409
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqdsargiflppHRRRIGYVFQEA-RLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NLQ----HVAPELDNTQARSI-----LGSFLfsgddAMKPAHvLSGGEKTRLALAtlvtsRA-----NVLLLDEPTNNLD 475
Cdd:COG4148 97 NLLygrkRAPRAERRISFDEVvellgIGHLL-----DRRPAT-LSGGERQRVAIG-----RAllsspRLLLMDEPLAALD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 476 PASREEIL----KAIAKYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:COG4148 166 LARKAEILpyleRLRDELDIPILYVSHSLDEVARL-ADHVVLLEQG 210
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-231 |
5.37e-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: 71.31 E-value: 5.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTL--LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVsgklgylpqdTHASDPTqtaldrmmsarD 90
Cdd:COG4778 20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV----------RHDGGWV-----------D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATI----INRIRKAE--------KEMtdpdP-----DVMTKAMNRydkamQDFDKAggyAAQSEAISMATSLGLPQEVM 153
Cdd:COG4778 79 LAQAspreILALRRRTigyvsqflRVI----PrvsalDVVAEPLLE-----RGVDRE---EARARARELLARLNLPERLW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 154 EQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGylKKYEGGFLV-ISHSTELLDEVVNKVWH 228
Cdd:COG4778 147 DLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravvVELIEE--AKARGTAIIgIFHDEEVREAVADRVVD 224
|
...
gi 489925987 229 LDA 231
Cdd:COG4778 225 VTP 227
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
349-499 |
6.59e-14 |
|
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: 71.67 E-value: 6.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 349 IDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQEHdTLDLNATVLENLQHVAPeldntqarsILG 428
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYI-KADYEGTVRDLLSSITK---------DFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 429 SFLFSGDDAMKPAHV----------LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY-----EGAI 493
Cdd:cd03237 91 THPYFKTEIAKPLQIeqildrevpeLSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaenneKTAF 170
|
....*.
gi 489925987 494 VlVTHD 499
Cdd:cd03237 171 V-VEHD 175
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
345-533 |
6.72e-14 |
|
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: 73.22 E-value: 6.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------------HGCKIGYFAQEHdTLDLNATVLE 409
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsrkgiflppEKRRIGYVFQEA-RLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NLQH----VAPELDNTQARSILgSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKA 485
Cdd:TIGR02142 95 NLRYgmkrARPSERRISFERVI-ELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 486 I----AKYEGAIVLVTHDEGAVEALnPERVLLMPDGD-------EDLWNDSYLDLVAEE 533
Cdd:TIGR02142 174 LerlhAEFGIPILYVSHSLQEVLRL-ADRVVVLEDGRvaaagpiAEVWASPDLPWLARE 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-226 |
6.97e-14 |
|
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: 71.29 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 27 KGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-KLGYLPQDTHAsDPTQTALDRMMSARDIATIINRIRKaekEM 105
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKA-DYEGTVRDLLSSITKDFYTHPYFKT---EI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 106 TDPdpdvmtkamnrydkamqdfdkaggyaaqseaismatsLGLPQeVMEQQLGTLSGGQRRRIELARILFSDADTLILDE 185
Cdd:cd03237 100 AKP-------------------------------------LQIEQ-ILDREVPELSGGELQRVAIAACLSKDADIYLLDE 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 186 PTNHLDAD----SIEWLRGYLKKYEGGFLVISHSTELLDEVVNKV 226
Cdd:cd03237 142 PSAYLDVEqrlmASKVIRRFAENNEKTAFVVEHDIIMIDYLADRL 186
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-205 |
7.40e-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: 7.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPT----------NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVsgkLGYLPQDthasdptqtalDR 84
Cdd:COG4586 25 KGLFRREyreveavddiSFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV---LGYVPFK-----------RR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMSARDIATIInrirkAEKEMTDPD-PDVMTKAMNR--YDKAMQDFDKAGGYaaqseaisMATSLGLpQEVMEQQLGTLS 161
Cdd:COG4586 91 KEFARRIGVVF-----GQRSQLWWDlPAIDSFRLLKaiYRIPDAEYKKRLDE--------LVELLDL-GELLDTPVRQLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY 205
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-223 |
7.88e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 7.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL--GYLPQDTHAsDPT-Q 79
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLriGYVPQKLYL-DTTlP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 TALDRMMsardiatiinRIRKAEKemtdpDPDVMtKAMNRYDKAmqdfdkaggyaaqseaismatslglpqEVMEQQLGT 159
Cdd:PRK09544 84 LTVNRFL----------RLRPGTK-----KEDIL-PALKRVQAG---------------------------HLIDAPMQK 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDA-------DSIEWLRGYLkkyEGGFLVISHSTELL----DEVV 223
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqvalyDLIDQLRREL---DCAVLMVSHDLHLVmaktDEVL 192
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-204 |
7.96e-14 |
|
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: 71.18 E-value: 7.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----------------KLGYLPQDtHASD 76
Cdd:TIGR02315 13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGtditklrgkklrklrrRIGMIFQH-YNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 PTQTALDRMMSAR-----DIATIINRIRKAEKEmtdpdpdvmtkamnrydKAMQDFDKAG--GYAAQseaismatslglp 149
Cdd:TIGR02315 92 ERLTVLENVLHGRlgykpTWRSLLGRFSEEDKE-----------------RALSALERVGlaDKAYQ------------- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 150 qevmeqQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:TIGR02315 142 ------RADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKR 190
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-235 |
8.72e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 71.00 E-value: 8.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-----------------KLGYLPQDTHASdPTQ 79
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLL-PDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 TALDRMMsardIATIINRIRKAEkemtdpdpdvmtkamnrydkamqdfdkaggyaAQSEAISMATSLGLPQEVMEQQlGT 159
Cdd:PRK11629 103 TALENVA----MPLLIGKKKPAE--------------------------------INSRALEMLAAVGLEHRANHRP-SE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWLRGYLKKYEG-GFLVISHSTELLDEVVNKVWHLDAQLGQ 235
Cdd:PRK11629 146 LSGGERQRVAIARALVNNPRLVLADEPTGNLDarnADSIFQLLGELNRLQGtAFLVVTHDLQLAKRMSRQLEMRDGRLTA 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
330-499 |
8.86e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.42 E-value: 8.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhG---------------CK 390
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD-GvdltalserelraarRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQeHDTLdLNA-TVLENlqhVA-P-ELDNTQARSI------------LgsflfSGDDAMKPAHvLSGGEKTRL--- 452
Cdd:COG1135 84 IGMIFQ-HFNL-LSSrTVAEN---VAlPlEIAGVPKAEIrkrvaellelvgL-----SDKADAYPSQ-LSGGQKQRVgia 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 453 -ALATlvtsRANVLLLDEPTNNLDPASREEIL---KAI-AKYEGAIVLVTHD 499
Cdd:COG1135 153 rALAN----NPKVLLCDEATSALDPETTRSILdllKDInRELGLTIVLITHE 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-222 |
9.41e-14 |
|
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: 70.83 E-value: 9.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-----------LGYLPQDtHASDPtqtaldRMMSARD 90
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditnlppekrdISYVPQN-YALFP------HMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATIInRIRKAEKEMTDpdpdvmtkamnrydkamqdfdkaggyaaqSEAISMATSLGLpQEVMEQQLGTLSGGQRRRIEL 170
Cdd:cd03299 92 IAYGL-KKRKVDKKEIE-----------------------------RKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAI 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489925987 171 ARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGGFLVIsHSTELLDEV 222
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIrkEFGVTVL-HVTHDFEEA 193
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-199 |
9.49e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.20 E-value: 9.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 6 QGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLP---TAGKVRVSG-----------KLGYLPQD 71
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGrrltalpaeqrRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 72 thasdptqtAL--DRMMSARDIA-TIINRIRKAEkemtdpdpdvmtkamnRYDKAMQDFDKAG--GYAAQSEAismatsl 146
Cdd:COG4136 85 ---------DLlfPHLSVGENLAfALPPTIGRAQ----------------RRARVEQALEEAGlaGFADRDPA------- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 147 glpqevmeqqlgTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR 199
Cdd:COG4136 133 ------------TLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFR 173
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
327-498 |
1.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 71.70 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAG-----VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC------------ 389
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 ---KIGYFAQEHDTLDLNATVLENLQH------VAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTS 460
Cdd:PRK13649 83 irkKVGLVFQFPESQLFEETVLKDVAFgpqnfgVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 461 RANVLLLDEPTNNLDPASREE---ILKAIAKYEGAIVLVTH 498
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKElmtLFKKLHQSGMTIVLVTH 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
327-499 |
1.19e-13 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.15 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH-----------GCKIGYFA 395
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 Q------------EHDTLDLNATVLENLQHvAP----ELDNTQARSILGSFL--FSGDDAMK---PAHvLSGGEKTRLAL 454
Cdd:PRK10619 86 QlrllrtrltmvfQHFNLWSHMTVLENVME-APiqvlGLSKQEARERAVKYLakVGIDERAQgkyPVH-LSGGQQQRVSI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 455 ATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHD 499
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaeEGkTMVVVTHE 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
341-517 |
1.19e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC--------------KIGYFAQEHDTL-DLN 404
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMsklssaakaelrnqKLGFIYQFHHLLpDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 AtvLENLQ------HVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:PRK11629 104 A--LENVAmplligKKKPAEINSRALEMLAAVGLEHRANHRPSE-LSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 479 RE---EILKAIAKYEG-AIVLVTHDEGAVEALNpeRVLLMPDG 517
Cdd:PRK11629 181 ADsifQLLGELNRLQGtAFLVVTHDLQLAKRMS--RQLEMRDG 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
327-517 |
1.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 71.18 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGC----------KIGY 393
Cdd:PRK13632 8 IKVENVSFSYPNSENNAlkNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKiDGITIskenlkeirkKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQEHDTLDLNATV-------LENlQHVAPE-----LDNTQARSILGSFLfsgddaMKPAHVLSGGEKTRLALATLVTSR 461
Cdd:PRK13632 88 IFQNPDNQFIGATVeddiafgLEN-KKVPPKkmkdiIDDLAKKVGMEDYL------DKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 462 ANVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDEGavEALNPERVLLMPDG 517
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdlrKTRKKTLISITHDMD--EAILADKVIVFSEG 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
344-517 |
1.34e-13 |
|
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: 69.48 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIE--EPDTGSVEYghgckigyfaQEHDTLDLNATVlenlqhvapeldnt 421
Cdd:cd03217 18 GVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILF----------KGEDITDLPPEE-------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 422 qaRSILGSFL-------FSGddaMKPAHVL-------SGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA 487
Cdd:cd03217 74 --RARLGIFLafqyppeIPG---VKNADFLryvnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVIN 148
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 488 KY--EG-AIVLVTHDEGAVEALNPERVLLMPDG 517
Cdd:cd03217 149 KLreEGkSVLIITHYQRLLDYIKPDRVHVLYDG 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-226 |
1.44e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.04 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDT---HASDP 77
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------TDVsrlHARDR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 78 ------TQTALDRMMSARD-IA---TIINRIRKaekemtdPDPDVMTKAMNRYDKAMQDFDKAGGYAAQseaismatslg 147
Cdd:PRK10851 75 kvgfvfQHYALFRHMTVFDnIAfglTVLPRRER-------PNAAAIKAKVTQLLEMVQLAHLADRYPAQ----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 lpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLK------KYEGGFlvISHSTELLDE 221
Cdd:PRK10851 137 ------------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRqlheelKFTSVF--VTHDQEEAME 202
|
....*
gi 489925987 222 VVNKV 226
Cdd:PRK10851 203 VADRV 207
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
286-517 |
1.75e-13 |
|
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: 72.86 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 286 VAAQNMMRRAEKLLENTSEAQKaekvadiRFPEPAPCGRtpIMAKDISKAY--GSNIVFAGVNLAIDKGSRVVILGYNGA 363
Cdd:COG4618 299 VSARQAYRRLNELLAAVPAEPE-------RMPLPRPKGR--LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGS 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 364 GKTTTLRLLAHIEEPDTGSVEY-GH----------GCKIGYFAQehDTLDLNATVLENlqhVA--PELDntqARSILgsf 430
Cdd:COG4618 370 GKSTLARLLVGVWPPTAGSVRLdGAdlsqwdreelGRHIGYLPQ--DVELFDGTIAEN---IArfGDAD---PEKVV--- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 431 lfsgdDAMKPAHV---------------------LSGGEKTRLALAtlvtsRA-----NVLLLDEPTNNLDPASREEILK 484
Cdd:COG4618 439 -----AAAKLAGVhemilrlpdgydtrigeggarLSGGQRQRIGLA-----RAlygdpRLVVLDEPNSNLDDEGEAALAA 508
|
250 260 270
....*....|....*....|....*....|....*.
gi 489925987 485 AI--AKYEGAIV-LVTHDEGAVEALNpeRVLLMPDG 517
Cdd:COG4618 509 AIraLKARGATVvVITHRPSLLAAVD--KLLVLRDG 542
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
346-517 |
1.75e-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: 68.33 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 346 NLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQehdtldlnatvlenlqhvAPELDNTQARS 425
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQ------------------RPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 426 ILgsfLFSGDDamkpahVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTHDEgAVEA 505
Cdd:cd03223 83 QL---IYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRP-SLWK 152
|
170
....*....|..
gi 489925987 506 LNPERVLLMPDG 517
Cdd:cd03223 153 FHDRVLDLDGEG 164
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
313-512 |
1.81e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 313 DIRFPEPAPcgrtPIMA-KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK 390
Cdd:PRK13543 1 MIEPLHTAP----PLLAaHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTAT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQEHDTL--------DLNAtvLENLqHVAPELDNTQARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVT 459
Cdd:PRK13543 77 RGDRSRFMAYLghlpglkaDLST--LENL-HFLCGLHGRRAKQMPGSALAIvglAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 460 SRANVLLLDEPTNNLDPAS---REEILKAIAKYEGAIVLVTHdeGAVEALN-PERVL 512
Cdd:PRK13543 154 SPAPLWLLDEPYANLDLEGitlVNRMISAHLRGGGAALVTTH--GAYAAPPvRTRML 208
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-191 |
1.89e-13 |
|
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: 70.02 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPTQTAldrmmsaRDIA 92
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE------DIREQDPVELR-------RKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIINRIrKAEKEMTDPDPDVMTKAMNRYDKAMQDfDKAggyaaqSEAISMatsLGL-PQEVMEQQLGTLSGGQRRRIELA 171
Cdd:cd03295 79 YVIQQI-GLFPHMTVEENIALVPKLLKWPKEKIR-ERA------DELLAL---VGLdPAEFADRYPHELSGGQQQRVGVA 147
|
170 180
....*....|....*....|
gi 489925987 172 RILFSDADTLILDEPTNHLD 191
Cdd:cd03295 148 RALAADPPLLLMDEPFGALD 167
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
317-500 |
1.94e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 317 PEPAPCGR---TPIMA-KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK- 390
Cdd:PRK11607 6 PRPQAKTRkalTPLLEiRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLSh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 -------IGYFAQEHdTLDLNATVLENL-----QHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLV 458
Cdd:PRK11607 86 vppyqrpINMMFQSY-ALFPHMTVEQNIafglkQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 459 TSRANVLLLDEPTNNLDPASRE----EILKAIAKYEGAIVLVTHDE 500
Cdd:PRK11607 165 AKRPKLLLLDEPMGALDKKLRDrmqlEVVDILERVGVTCVMVTHDQ 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
330-506 |
2.00e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 71.60 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH---------GCKIGYFAQEHdT 400
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvppaERGVGMVFQSY-A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 401 LDLNATVLEN------LQHVA-PELDN--TQARSIL--GSFLfsgddAMKPAhVLSGGEKTRLALA-TLVtSRANVLLLD 468
Cdd:PRK11000 86 LYPHLSVAENmsfglkLAGAKkEEINQrvNQVAEVLqlAHLL-----DRKPK-ALSGGQRQRVAIGrTLV-AEPSVFLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 469 EPTNNLDPA----SREEILKAIAKYEGAIVLVTHDEgaVEAL 506
Cdd:PRK11000 159 EPLSNLDAAlrvqMRIEISRLHKRLGRTMIYVTHDQ--VEAM 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-220 |
3.96e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 68.92 E-value: 3.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLE--IQIGARTL--LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------- 63
Cdd:COG1136 4 LLELRNLTksYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslserelarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 64 ---KLGYLPQDTHASdPTQTALDRMMsardIATIINRIRKAEkemtdpdpdvmtkamnrydkamqdfdkaggyaAQSEAI 140
Cdd:COG1136 84 rrrHIGFVFQFFNLL-PELTALENVA----LPLLLAGVSRKE--------------------------------RRERAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 141 SMATSLGLPqEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS----IEWLRGYLKKYEGGFLVISHST 216
Cdd:COG1136 127 ELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP 205
|
....
gi 489925987 217 ELLD 220
Cdd:COG1136 206 ELAA 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-214 |
4.68e-13 |
|
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: 68.68 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----------------KLG 66
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQdthasdptQTAL-DRMMSARDIATIINRIRKAEKEMTDpdpdvmtkamnryDKAMqdfdkaggyaaqsEAISMAts 145
Cdd:cd03261 81 MLFQ--------SGALfDSLTVFENVAFPLREHTRLSEEEIR-------------EIVL-------------EKLEAV-- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 146 lGLPQevMEQQL-GTLSGGQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWL-RGYLKKYEGGFLVISH 214
Cdd:cd03261 125 -GLRG--AEDLYpAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLiRSLKKELGLTSIMVTH 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-223 |
4.82e-13 |
|
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: 71.67 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdtHA-SDPTQTALDRMMS--ARDI 91
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDG---------HDlADYTLASLRRQVAlvSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 A----TIINRIRKAEKEMTDpdpdvmtkaMNRYDKAMQDfdkaggyaAQSEAISMATSLGLPQEVMEQQlGTLSGGQRRR 167
Cdd:TIGR02203 416 VlfndTIANNIAYGRTEQAD---------RAEIERALAA--------AYAQDFVDKLPLGLDTPIGENG-VLLSGGQRQR 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 168 IELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG--FLVISH--ST-ELLDEVV 223
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGrtTLVIAHrlSTiEKADRIV 538
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
347-501 |
4.96e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.52 E-value: 4.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 347 LAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKI---------------------------GYFAQEHD 399
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqdpprnvegtvydfvaegieeqaEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNAT-----VLENLQHVAPELDN-------TQARSILGSFlfsGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLL 467
Cdd:PRK11147 104 ISHLVETdpsekNLNELAKLQEQLDHhnlwqleNRINEVLAQL---GLDPDAALSSLSGGWLRKAALGRALVSNPDVLLL 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 468 DEPTNNLDPAS---REEILKAiakYEGAIVLVTHDEG 501
Cdd:PRK11147 181 DEPTNHLDIETiewLEGFLKT---FQGSIIFISHDRS 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
6-236 |
5.95e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.95 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 6 QGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGYLPQDTHAS--------- 75
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEpLAKLNRAQRKAfrrdiqmvf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 76 -DPTqTALDRMMSARDIatiinrIRKAEKEMTDpdpdvmtkamnrydkamqdFDKAGGYAAQSEaisMATSLGLPQEVME 154
Cdd:PRK10419 96 qDSI-SAVNPRKTVREI------IREPLRHLLS-------------------LDKAERLARASE---MLRAVDLDDSVLD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 155 QQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLD 230
Cdd:PRK10419 147 KRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
|
....*.
gi 489925987 231 AqlGQI 236
Cdd:PRK10419 227 N--GQI 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
330-488 |
7.77e-13 |
|
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: 68.02 E-value: 7.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGS-NIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----------EYGHGCKIGYFAQe 397
Cdd:cd03254 6 ENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidirdisRKSLRSMIGVVLQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 hDTLDLNATVLENLQHVAPELDNT---QARSILGSFLF-----SG-DDAMKP-AHVLSGGEKTRLALATLVTSRANVLLL 467
Cdd:cd03254 85 -DTFLFSGTIMENIRLGRPNATDEeviEAAKEAGAHDFimklpNGyDTVLGEnGGNLSQGERQLLAIARAMLRDPKILIL 163
|
170 180
....*....|....*....|.
gi 489925987 468 DEPTNNLDPASREEILKAIAK 488
Cdd:cd03254 164 DEATSNIDTETEKLIQEALEK 184
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-187 |
7.91e-13 |
|
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: 67.84 E-value: 7.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYL 68
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQDtHASDPTQTALDRMMSARDiatiiNRIRKAEKEmtdpdpdvmtkamnRYDKAMQDFdkaggyaaqseaismatslgl 148
Cdd:cd03224 81 PEG-RRIFPELTVEENLLLGAY-----ARRRAKRKA--------------RLERVYELF--------------------- 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 149 P--QEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT 187
Cdd:cd03224 120 PrlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-236 |
8.00e-13 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 67.77 E-value: 8.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----------------KLGYLPQD----T 72
Cdd:COG2884 13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGqdlsrlkrreipylrrRIGVVFQDfrllP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 73 HasdptQTALDRMMsardIATIInrIRKAEKEMTDPDPDVMTKAmnrydkAMQDFDKAggyaaqseaismatslgLPQEv 152
Cdd:COG2884 93 D-----RTVYENVA----LPLRV--TGKSRKEIRRRVREVLDLV------GLSDKAKA-----------------LPHE- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 153 meqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDAD-SIEWLRgYLKKY-EGG--FLVISHSTELLDEVVNKVWH 228
Cdd:COG2884 138 -------LSGGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIME-LLEEInRRGttVLIATHDLELVDRMPKRVLE 209
|
....*...
gi 489925987 229 LDAqlGQI 236
Cdd:COG2884 210 LED--GRL 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
324-501 |
8.05e-13 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 68.67 E-value: 8.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 324 RTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQEHDTL-- 401
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRV-GGEEIRLKPDRDGELvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 --------------------DLNA--TVLENL----QHV-------APEldntQARSILGSFLFSGDDAMKPAHvLSGGE 448
Cdd:COG4598 85 adrrqlqrirtrlgmvfqsfNLWShmTVLENVieapVHVlgrpkaeAIE----RAEALLAKVGLADKRDAYPAH-LSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 449 KTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEG 501
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLaeEGrTMLVVTHEMG 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
324-498 |
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 489925987 324 RTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTLDL 403
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 ---------------NATVLEN------LQHVAPELDNTQAR---SILGSFLFS--GDDAMKPAHVLSGGEKTRLALATL 457
Cdd:PRK14247 81 rrrvqmvfqipnpipNLSIFENvalglkLNRLVKSKKELQERvrwALEKAQLWDevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 458 VTSRANVLLLDEPTNNLDP---ASREEILKAIAKyEGAIVLVTH 498
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPentAKIESLFLELKK-DMTIVLVTH 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
327-498 |
1.21e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 68.61 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAG-----VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC------------ 389
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 ---KIGYFAQEHDTLDLNATVLENLQhVAPE---LDNTQARSILGSFL----FSGDDAMKPAHVLSGGEKTRLALATLVT 459
Cdd:PRK13643 82 vrkKVGVVFQFPESQLFEETVLKDVA-FGPQnfgIPKEKAEKIAAEKLemvgLADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 460 SRANVLLLDEPTNNLDPASREEILK---AIAKYEGAIVLVTH 498
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQlfeSIHQSGQTVVLVTH 202
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-191 |
1.30e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 25 VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQdthasdptqtaldrmmsardiatiinRIRkaeke 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQ--------------------------YIK----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 105 mtdPDPDVMTKAMNRydKAMQDFDkaGGYAaQSEAISmatSLGLPqEVMEQQLGTLSGGQRRRIELARILFSDADTLILD 184
Cdd:PRK13409 411 ---PDYDGTVEDLLR--SITDDLG--SSYY-KSEIIK---PLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 478
|
....*..
gi 489925987 185 EPTNHLD 191
Cdd:PRK13409 479 EPSAHLD 485
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
5-214 |
1.33e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 67.18 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdPTQTAlDR 84
Cdd:PRK13543 14 AHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK------------TATRG-DR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 mmsARDIATIinrirkaeKEMTDPDPDVMTKAMNRYDKAMQdfdkagGYAAQ---SEAISMATSLGLPQEVMEQqlgtLS 161
Cdd:PRK13543 81 ---SRFMAYL--------GHLPGLKADLSTLENLHFLCGLH------GRRAKqmpGSALAIVGLAGYEDTLVRQ----LS 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY---EGGFLVISH 214
Cdd:PRK13543 140 AGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-220 |
1.47e-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: 67.05 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRmmsaRDIATIINR 97
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG------QDVSDLRGRAIPYLR----RKIGVVFQD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRkaekemtdpdpdvMTKAMNRYDK---AMQDFDKAGGYAAqsEAISMATSL-GLPQEVMEQQLGtLSGGQRRRIELARI 173
Cdd:cd03292 87 FR-------------LLPDRNVYENvafALEVTGVPPREIR--KRVPAALELvGLSHKHRALPAE-LSGGEQQRVAIARA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 174 LFSDADTLILDEPTNHLDADSIEWLRGYLKKYE--GGFLVIS-HSTELLD 220
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkaGTTVVVAtHAKELVD 200
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
23-196 |
1.48e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 68.60 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGYLP---------------QDTHAS-DPTQTaldrm 85
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQdITGLSgrelrplrrrmqmvfQDPYASlNPRMT----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 msardIATIInrirkAEkemtdpdpdvmtkamnrydkAMQDFDKAGGYAAQSEAISMATSLGLPQEVMEQQLGTLSGGQR 165
Cdd:COG4608 114 -----VGDII-----AE--------------------PLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQR 163
|
170 180 190
....*....|....*....|....*....|.
gi 489925987 166 RRIELARILFSDADTLILDEPTNHLDAdSIE 196
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALDV-SIQ 193
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-226 |
1.60e-12 |
|
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: 67.31 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQD-THASDPTQT 80
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDG------QDiTGLSEKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDR---M----------MSARDiatiiN---RIRkaekEMTDpdpdvMTKAMnRYDKAMqdfdkaggyaaqsEAISMat 144
Cdd:COG1127 79 ELRRrigMlfqggalfdsLTVFE-----NvafPLR----EHTD-----LSEAE-IRELVL-------------EKLEL-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 145 sLGLPQevMEQQL-GTLSGGQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWL-RGYLKKYEGGFLVISHSTELL 219
Cdd:COG1127 129 -VGLPG--AADKMpSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELiRELRDELGLTSVVVTHDLDSA 205
|
....*..
gi 489925987 220 DEVVNKV 226
Cdd:COG1127 206 FAIADRV 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
325-499 |
1.61e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 325 TPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHdtldln 404
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 ATVLENL--QHVAPELDNTQ-----ARSILGSFL--FSGDD------AMKPAHV----------LSGGEKTRLALATLVT 459
Cdd:PRK11231 75 ARRLALLpqHHLTPEGITVRelvayGRSPWLSLWgrLSAEDnarvnqAMEQTRInhladrrltdLSGGQRQRAFLAMVLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 460 SRANVLLLDEPTNNLDPASREEILKAIAKYEGA---IVLVTHD 499
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQgktVVTVLHD 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-191 |
1.68e-12 |
|
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: 70.32 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQdthasdptqtaLDRMMSARDIATIIN 96
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ-----------TSWIMPGTIKDNIIF 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 RIRkaekemtdpdpdvmtkamnrYDKAMqdfdkaggYAAQSEAISMATSLGLPQEVMEQQLG----TLSGGQRRRIELAR 172
Cdd:TIGR01271 510 GLS--------------------YDEYR--------YTSVIKACQLEEDIALFPEKDKTVLGeggiTLSGGQRARISLAR 561
|
170
....*....|....*....
gi 489925987 173 ILFSDADTLILDEPTNHLD 191
Cdd:TIGR01271 562 AVYKDADLYLLDSPFTHLD 580
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
327-498 |
1.76e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 68.67 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhGC------------- 389
Cdd:PRK11153 2 IELKNISKVFpqGGRTIHAlnNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVD-GQdltalsekelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 --KIGYFAQeHDTLDLNATVLENlqhVA-P-ELDNTQARSI------LGSFLFSGDDAMK-PAHvLSGGEKTRLALATLV 458
Cdd:PRK11153 81 rrQIGMIFQ-HFNLLSSRTVFDN---VAlPlELAGTPKAEIkarvteLLELVGLSDKADRyPAQ-LSGGQKQRVAIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 459 TSRANVLLLDEPTNNLDPASREEILKAIAK----YEGAIVLVTH 498
Cdd:PRK11153 156 ASNPKVLLCDEATSALDPATTRSILELLKDinreLGLTIVLITH 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-517 |
1.96e-12 |
|
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: 66.34 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 333 SKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEygHGCKIGYFAQE--HdtldLNATVLEN 410
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--VPGSIAYVSQEpwI----QNGTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 411 LQHVAPeLDNTQARSILGSFLFSGDDAMKPAH----------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE 480
Cdd:cd03250 86 ILFGKP-FDEERYEKVIKACALEPDLEILPDGdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 481 EI----LKAIAKYEGAIVLVTHdegAVEALNP-ERVLLMPDG 517
Cdd:cd03250 165 HIfencILGLLLNNKTRILVTH---QLQLLPHaDQIVVLDNG 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-229 |
2.04e-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: 66.01 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDM--LPTAGKVRVSGKlgylpqdthasdptqt 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGE---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 aldrmmsarDIatiinrirkaekemtdpdpdvmtKAMNRYDKAmqdfdKAG-GYAAQS-EAISMATSLGLPQEVMEqqlg 158
Cdd:cd03217 65 ---------DI-----------------------TDLPPEERA-----RLGiFLAFQYpPEIPGVKNADFLRYVNE---- 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR---GYLKKYEGGFLVISHSTELLDEVVNKVWHL 229
Cdd:cd03217 104 GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIKPDRVHV 177
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
289-517 |
2.36e-12 |
|
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: 70.04 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 289 QNMMRRAEKLLENTSEAQKAEKVADIRFPEPAPcGRTP-IMAKDISK---AYGSNIVfAGVNLAIDKGSRVVILGYNGAG 364
Cdd:TIGR01257 891 ERALEKTEPLTEEMEDPEHPEGINDSFFERELP-GLVPgVCVKNLVKifePSGRPAV-DRLNITFYENQITAFLGHNGAG 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 365 KTTTLRLLAHIEEPDTGSVEYGhGCKIGY----------FAQEHDTLDLNATVLENLQHVAPELDNTQARSILGSFLFSG 434
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVG-GKDIETnldavrqslgMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLE 1047
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 435 DDAM-----KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGA--IVLVTHDEGAVEALN 507
Cdd:TIGR01257 1048 DTGLhhkrnEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGrtIIMSTHHMDEADLLG 1127
|
250
....*....|
gi 489925987 508 pERVLLMPDG 517
Cdd:TIGR01257 1128 -DRIAIISQG 1136
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-226 |
2.66e-12 |
|
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: 66.45 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthasdptqtaldrmmsaRDIATIINR-IRK 100
Cdd:cd03258 25 SLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDG-------------------------TDLTLLSGKeLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 101 AEKEMTdpdpdvM-----------TKAMN--------RYDKAMQDF------------DKAGGYAAQseaismatslglp 149
Cdd:cd03258 80 ARRRIG------MifqhfnllssrTVFENvalpleiaGVPKAEIEErvlellelvgleDKADAYPAQ------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 150 qevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDA---DSI-EWLRGYLKKYEGGFLVISHSTELLDEVVNK 225
Cdd:cd03258 141 ----------LSGGQKQRVGIARALANNPKVLLCDEATSALDPettQSIlALLRDINRELGLTIVLITHEMEVVKRICDR 210
|
.
gi 489925987 226 V 226
Cdd:cd03258 211 V 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
329-500 |
2.95e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGckIGYF 394
Cdd:COG1129 7 MRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvrfrsprdaqaAG--IAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEhdtLDL--NATVLENL-----QHVAPELD----NTQARSILGSFLFSgDDAMKPAHVLSGGEKTRLALATLVTSRAN 463
Cdd:COG1129 85 HQE---LNLvpNLSVAENIflgrePRRGGLIDwramRRRARELLARLGLD-IDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 464 VLLLDEPTNNLDPASREEILKAIA--KYEG-AIVLVTH--DE 500
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRrlKAQGvAIIYISHrlDE 202
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-192 |
3.11e-12 |
|
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: 65.65 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG--DMLPTAGKVRVSGK----------LGYLPQDTHASdPTQT 80
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRpldkrsfrkiIGYVPQDDILH-PTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDRMMsardiatiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggYAAqseaismatslglpqevmeqQLGTL 160
Cdd:cd03213 99 VRETLM----------------------------------------------FAA--------------------KLRGL 112
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
345-517 |
3.30e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 66.99 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGC--------------KIGYFAQ--EH----DTLDLN 404
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-IIDGVditdkkvklsdirkKVGLVFQypEYqlfeETIEKD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 -ATVLENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:PRK13637 105 iAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEIL 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 484 KAIA----KYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:PRK13637 185 NKIKelhkEYNMTIILVSHSMEDVAKL-ADRIIVMNKG 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-187 |
3.68e-12 |
|
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: 66.16 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LG 66
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQdthasdptqtalDRM----MSARD---IATIINRIRKAEKEmtdpdpdvmtkamnRYDKAMQDFdkaggyaaqsea 139
Cdd:COG0410 82 YVPE------------GRRifpsLTVEEnllLGAYARRDRAEVRA--------------DLERVYELF------------ 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 140 ismatslglP--QEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT 187
Cdd:COG0410 124 ---------PrlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
327-517 |
4.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.03 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFA---GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-----GHGCKIGYFAQ 396
Cdd:PRK13651 3 IKVKNIVKIFnkKLPTELKaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 EHDTLDLNATVLENLQHVapeldnTQARSILG------------------------SFLFSGDDAMKPAHV--------- 443
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKI------KEIRRRVGvvfqfaeyqlfeqtiekdiifgpvSMGVSKEEAKKRAAKyielvglde 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 444 ---------LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHD-EGAVEALNpeR 510
Cdd:PRK13651 157 sylqrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnkQGkTIILVTHDlDNVLEWTK--R 234
|
....*..
gi 489925987 511 VLLMPDG 517
Cdd:PRK13651 235 TIFFKDG 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
326-506 |
4.29e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 326 PIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGH-----------GCKIGYF 394
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGddvealsaraaSRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEhDTLDLNATVLENLqhvapELDNTQARSILGSFLFSGDDAM--------------KPAHVLSGGEKTRLALATLVTS 460
Cdd:PRK09536 83 PQD-TSLSFEFDVRQVV-----EMGRTPHRSRFDTWTETDRAAVeramertgvaqfadRPVTSLSGGERQRVLLARALAQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 461 RANVLLLDEPTNNLDpasreeILKAIAKYEGAIVLVTHDEGAVEAL 506
Cdd:PRK09536 157 ATPVLLLDEPTASLD------INHQVRTLELVRRLVDDGKTAVAAI 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
345-517 |
4.38e-12 |
|
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: 65.71 E-value: 4.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV--------EYGHGC---KIGYFAQehDTLDLNATVLENLQH 413
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdvrDYTLASlrrQIGLVSQ--DVFLFNDTVAENIAY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 414 VAPELDNTQARsilgsflfsgdDAMKPAHV---------------------LSGGEKTRLALATLVTSRANVLLLDEPTN 472
Cdd:cd03251 99 GRPGATREEVE-----------EAARAANAhefimelpegydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 473 NLDPASREEILKAIAK-YEGAIVLV-THDEGAVEalNPERVLLMPDG 517
Cdd:cd03251 168 ALDTESERLVQAALERlMKNRTTFViAHRLSTIE--NADRIVVLEDG 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-220 |
4.58e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-------------LGY 67
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKpismlssrqlarrLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQdtHASDPTQTALDRMMS-ARD-IATIINRirkaekeMTDPDPDVMTKAMnrydkamqdfdkaggyaAQSEAISMAts 145
Cdd:PRK11231 81 LPQ--HHLTPEGITVRELVAyGRSpWLSLWGR-------LSAEDNARVNQAM-----------------EQTRINHLA-- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 146 lglpqevmEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDadsiewlrgylkkyeggflvISHSTELLD 220
Cdd:PRK11231 133 --------DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD--------------------INHQVELMR 179
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-193 |
4.75e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLgylpqdthASDPTQTALDRMM---SAR-DI--ATII 95
Cdd:PRK11160 360 SLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP--------IADYSEAALRQAIsvvSQRvHLfsATLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 96 NRIRKAEKEMTDpdpDVMTKAMNR--YDKAMQDFDkaggyaaqseaismatslGLpqevmEQQLG----TLSGGQRRRIE 169
Cdd:PRK11160 432 DNLLLAAPNASD---EALIEVLQQvgLEKLLEDDK------------------GL-----NAWLGeggrQLSGGEQRRLG 485
|
170 180
....*....|....*....|....
gi 489925987 170 LARILFSDADTLILDEPTNHLDAD 193
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAE 509
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
276-498 |
5.03e-12 |
|
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: 68.61 E-value: 5.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 276 IRLHAKASKAVAAQNmmRRAEKLLENTSEAQKAEKVADIRFpepapcgRTPIMAKDISKAYGSNI-VFAGVNLAIDKGSR 354
Cdd:TIGR01193 432 INLQPKLQAARVANN--RLNEVYLVDSEFINKKKRTELNNL-------NGDIVINDVSYSYGYGSnILSDISLTIKMNSK 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 355 VVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC-----------KIGYFAQEHDTLDlnATVLENLQHVAPEldNTQA 423
Cdd:TIGR01193 503 TTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqFINYLPQEPYIFS--GSILENLLLGAKE--NVSQ 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 424 RSILGSFLFS-------------GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAK-Y 489
Cdd:TIGR01193 579 DEIWAACEIAeikddienmplgyQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNlQ 658
|
....*....
gi 489925987 490 EGAIVLVTH 498
Cdd:TIGR01193 659 DKTIIFVAH 667
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-214 |
5.38e-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: 67.00 E-value: 5.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGkvRVSGKLGYLPQD-THASDptqtalDRMMSAR--DIATIinri 98
Cdd:COG0444 25 SFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPG--ITSGEILFDGEDlLKLSE------KELRKIRgrEIQMI---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 99 rkaekeMTDP----DPdVMT---------KAMNRYDKAmqdfdkaggyAAQSEAISMATSLGL--PQEVMEQ---QLgtl 160
Cdd:COG0444 92 ------FQDPmtslNP-VMTvgdqiaeplRIHGGLSKA----------EARERAIELLERVGLpdPERRLDRyphEL--- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISH 214
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITH 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
15-230 |
5.39e-12 |
|
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: 65.21 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFH----VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTAL------DR 84
Cdd:cd03298 7 RFSYGEQPMHfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING------VDVTAAPPADRPVsmlfqeNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMSARDIATIINRIRKAEKEMTDPDPDVMTKAMNRydkamqdfdkaggyaaqseaismatsLGLpQEVMEQQLGTLSGGQ 164
Cdd:cd03298 81 LFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALAR--------------------------VGL-AGLEKRLPGELSGGE 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLD 230
Cdd:cd03298 134 RQRVALARVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
330-486 |
5.75e-12 |
|
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: 65.64 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGS---NIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK----------IGYFA 395
Cdd:cd03249 4 KNVSFRYPSrpdVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEhDTLdLNATVLENLQHVAPELDNTQARSILG-----SFLFS---GDDAMKPAH--VLSGGEKTRLALATLVTSRANVL 465
Cdd:cd03249 84 QE-PVL-FDGTIAENIRYGKPDATDEEVEEAAKkanihDFIMSlpdGYDTLVGERgsQLSGGQKQRIAIARALLRNPKIL 161
|
170 180
....*....|....*....|.
gi 489925987 466 LLDEPTNNLDPASREEILKAI 486
Cdd:cd03249 162 LLDEATSALDAESEKLVQEAL 182
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
17-191 |
6.57e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 66.03 E-value: 6.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQdthasdptqtaLDRMMSARDIATIIN 96
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQ-----------FSWIMPGTIKENIIF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 RIRKAEKemtdpdpdvmtkamnRYDKAMQdfdkaggyAAQ-SEAISmatslGLPQE---VMEQQLGTLSGGQRRRIELAR 172
Cdd:cd03291 121 GVSYDEY---------------RYKSVVK--------ACQlEEDIT-----KFPEKdntVLGEGGITLSGGQRARISLAR 172
|
170
....*....|....*....
gi 489925987 173 ILFSDADTLILDEPTNHLD 191
Cdd:cd03291 173 AVYKDADLYLLDSPFGYLD 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-518 |
9.17e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.35 E-value: 9.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKvrvsgklgylpqdtHASDPTQTALdrmMSARDIATIINR 97
Cdd:PRK10938 19 LQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--------------RQSQFSHITR---LSFEQLQKLVSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 I-RKAEKEMTDPDPDvmtkamnrydkamqDFdkagGYAAqSEAISMATSLGLPQEVMEQQLGT----------LSGGQRR 166
Cdd:PRK10938 82 EwQRNNTDMLSPGED--------------DT----GRTT-AEIIQDEVKDPARCEQLAQQFGItalldrrfkyLSTGETR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 167 RIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKyeggflvISHSTELLDEVVNKVWHLDAQLGQIdmyslswkAY 246
Cdd:PRK10938 143 KTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFDEIPDFVQFA--------GV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 247 LhqrvvdeerrrrerevaekkAER-LMKQGIRlHAKASKAVAAQnmMRRAEKLlENTSEAQKAEKVADIRFPEPAPcgrt 325
Cdd:PRK10938 208 L--------------------ADCtLAETGER-EEILQQALVAQ--LAHSEQL-EGVQLPEPDEPSARHALPANEP---- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 326 PIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLA-----------------------------HIe 376
Cdd:PRK10938 260 RIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndltlfgrrrgsgetiwdikkHI- 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 377 epdtGSV------EYGHGCKI------GYFaqehDTLDLNATVLENLQHVApeldnTQARSILGsflFSGDDAMKPAHVL 444
Cdd:PRK10938 339 ----GYVssslhlDYRVSTSVrnvilsGFF----DSIGIYQAVSDRQQKLA-----QQWLDILG---IDKRTADAPFHSL 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 445 SGGEKtRLALATlvtsRANV-----LLLDEPTNNLDPASRE------EILkaIAKYEGAIVLVTH-DEGAVEALNpERVL 512
Cdd:PRK10938 403 SWGQQ-RLALIV----RALVkhptlLILDEPLQGLDPLNRQlvrrfvDVL--ISEGETQLLFVSHhAEDAPACIT-HRLE 474
|
....*.
gi 489925987 513 LMPDGD 518
Cdd:PRK10938 475 FVPDGD 480
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-204 |
1.06e-11 |
|
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: 64.20 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL--GYLPQDTHASDPTQT-ALDRMMSAR 89
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtDLPPKDRDIAMVFQNyALYPHMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 90 D-IATIInRIRKAEKEMTDpdpdvmtkamnrydkamqdfdkaggyaaqSEAISMATSLGLpQEVMEQQLGTLSGGQRRRI 168
Cdd:cd03301 91 DnIAFGL-KLRKVPKDEID-----------------------------ERVREVAELLQI-EHLLDRKPKQLSGGQRQRV 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 489925987 169 ELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:cd03301 140 ALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKR 175
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
327-517 |
1.15e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.91 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------HGCK---IGYF 394
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplHARArrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHDTL------DLNATVLENLQHVAPELDNTQARSILGSFLFSG-DDAMKPAhvLSGGEKTRLALATLVTSRANVLLL 467
Cdd:PRK10895 84 PQEASIFrrlsvyDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHlRDSMGQS--LSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 468 DEPTNNLDPASREEILKAIA--KYEGAIVLVThDEGAVEALNP-ERVLLMPDG 517
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEhlRDSGLGVLIT-DHNVRETLAVcERAYIVSQG 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-222 |
1.26e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 65.49 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRvsgklgYLPQDTHasdpTQTALDRMMSARDIATI--- 94
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE------WIFKDEK----NKKKTKEKEKVLEKLVIqkt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 95 -------INRIRK--------AEKEMTDP--DPDVMTKAMNrydkamQDFDKAGGYAAQSEAISMatsLGLPQEVMEQQL 157
Cdd:PRK13651 93 rfkkikkIKEIRRrvgvvfqfAEYQLFEQtiEKDIIFGPVS------MGVSKEEAKKRAAKYIEL---VGLDESYLQRSP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLD-ADSIEWLRGYLKKYEGGFLVIShSTELLDEV 222
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQGKTIIL-VTHDLDNV 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
327-498 |
1.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 65.43 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAG-----VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGC------------ 389
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralydVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 390 ---KIGYFAQ--EHDTLDlnATVLEN-----LQHVAPELDNTQ-ARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLV 458
Cdd:PRK13634 83 lrkKVGIVFQfpEHQLFE--ETVEKDicfgpMNFGVSEEDAKQkAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 459 TSRANVLLLDEPTNNLDPASREEILKAIAKY--EG--AIVLVTH 498
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKglTTVLVTH 204
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
345-517 |
1.46e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.19 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-----HGCK----------IGYFAQEHDTLDLNATVLE 409
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDdititHKTKdkyirpvrkrIGMVFQFPESQLFEDTVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NL----QHVAPELDNTQARS--ILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:PRK13646 106 EIifgpKNFKMNLDEVKNYAhrLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 484 KAIAKYE----GAIVLVTHDEGAVeALNPERVLLMPDG 517
Cdd:PRK13646 186 RLLKSLQtdenKTIILVSHDMNEV-ARYADEVIVMKEG 222
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
346-484 |
1.61e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 346 NLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---HGCK------IGYFAQE-----------------HD 399
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdHTTTppsrrpVSMLFQEnnlfshltvaqniglglNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVApeldntqARSILGSFLfsgddAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:PRK10771 99 GLKLNAAQREKLHAIA-------RQMGIEDLL-----ARLPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
....*
gi 489925987 480 EEILK 484
Cdd:PRK10771 166 QEMLT 170
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-204 |
2.53e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-----------LGYLPQ 70
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 DThasdptqtALDRMMSARDiatiiN-----RIRKAEKEmtdpdpdvmtkamNRYDKAMqdfdkaggyaaqsEAISMats 145
Cdd:COG3842 85 DY--------ALFPHLTVAE-----NvafglRMRGVPKA-------------EIRARVA-------------ELLEL--- 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 146 LGLPQevMEQQL-GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:COG3842 123 VGLEG--LADRYpHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR 180
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-191 |
2.56e-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: 63.79 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDptqta 81
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrrAIGVVPQDTVLFN----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 ldrmmsardiATIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMQDFDkagGYAAQseaismatslglpqeVMEQQLgTLS 161
Cdd:cd03253 89 ----------DTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPD---GYDTI---------------VGERGL-KLS 139
|
170 180 190
....*....|....*....|....*....|
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:cd03253 140 GGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
327-499 |
2.88e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.95 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG----HGCKIGYFA------- 395
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvATTPSRELAkrlailr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QE-HDTLDLnaTV-----------------LENLQHVAPELDNTQARSILGSFLfsgDDamkpahvLSGGEKTRLALATL 457
Cdd:COG4604 82 QEnHINSRL--TVrelvafgrfpyskgrltAEDREIIDEAIAYLDLEDLADRYL---DE-------LSGGQRQRAFIAMV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 458 VTSRANVLLLDEPTNNLDPA-SRE--EILKAIAKYEG-AIVLVTHD 499
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKhSVQmmKLLRRLADELGkTVVIVLHD 195
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-236 |
2.93e-11 |
|
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: 62.93 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLgyLPQDTHASD------ 76
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK--LTDDKKNINelrqkv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 ----------PTQTALDRMMSArdiatiinrIRKAEKEmtdPDPDVMTKAMnRYDKAMQDFDKAGGYAAQseaismatsl 146
Cdd:cd03262 79 gmvfqqfnlfPHLTVLENITLA---------PIKVKGM---SKAEAEERAL-ELLEKVGLADKADAYPAQ---------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 147 glpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDAdsiEWLRGYLK-----KYEG-GFLVISHSTELLD 220
Cdd:cd03262 136 -------------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDP---ELVGEVLDvmkdlAEEGmTMVVVTHEMGFAR 199
|
250
....*....|....*.
gi 489925987 221 EVVNKVWHLDAqlGQI 236
Cdd:cd03262 200 EVADRVIFMDD--GRI 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-192 |
4.28e-11 |
|
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: 62.84 E-value: 4.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGAR----TLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGYLPQDTHA-- 74
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQdLFALDEDARArl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 75 -SD------------PTQTALDrmmsardiatiinrirkaekemtdpdpDVMTKAmnrydkamqdfDKAGGYAAQSEAIS 141
Cdd:COG4181 88 rARhvgfvfqsfqllPTLTALE---------------------------NVMLPL-----------ELAGRRDARARARA 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 142 MATSLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:COG4181 130 LLERVGL-GHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDA 179
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
327-499 |
4.61e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV---------EYGHGCK--IGYF 394
Cdd:PRK13652 4 IETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVlirgepitkENIREVRkfVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHDTLDLNATVLENLQHVAPEL---DNTQARSILGSFLFSGDDAM--KPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:PRK13652 84 FQNPDDQIFSPTVEQDIAFGPINLgldEETVAHRVSSALHMLGLEELrdRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 470 PTNNLDPASREEILKAI----AKYEGAIVLVTHD 499
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQ 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
344-517 |
4.62e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.28 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPD---TGSVEY-GHGCKIGY--------FAQEHDTLDLNATVLENL 411
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYnGIPYKEFAekypgeiiYVSEEDVHFPTLTVRETL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 QHVApeldntqarSILGSFLFSGddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI---AK 488
Cdd:cd03233 105 DFAL---------RCKGNEFVRG---------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIrtmAD 166
|
170 180 190
....*....|....*....|....*....|
gi 489925987 489 YEGAIVLVTHDEGAVEALNP-ERVLLMPDG 517
Cdd:cd03233 167 VLKTTTFVSLYQASDEIYDLfDKVLVLYEG 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
330-498 |
5.26e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.05 E-value: 5.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG--------------HGckIGYFA 395
Cdd:COG3845 9 RGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirsprdaiaLG--IGMVH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QeH----DTLdlnaTVLENL-----QHVAPELDNTQARSILGSflFSGD-----DAMKPAHVLSGGEKTRL----ALATl 457
Cdd:COG3845 87 Q-HfmlvPNL----TVAENIvlglePTKGGRLDRKAARARIRE--LSERygldvDPDAKVEDLSVGEQQRVeilkALYR- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 458 vtsRANVLLLDEPTNNLDPASREE---ILKAIAKyEG-AIVLVTH 498
Cdd:COG3845 159 ---GARILILDEPTAVLTPQEADElfeILRRLAA-EGkSIIFITH 199
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
15-191 |
5.39e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 5.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDPtqta 81
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsskafarKVAYLPQQLPAAEG---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 ldrmMSARDIATI--------INRIRKAEKEMTDpdpdvmtkamnrydkamqdfdkaggyaaqsEAISMATSLGLPQEVM 153
Cdd:PRK10575 100 ----MTVRELVAIgrypwhgaLGRFGAADREKVE------------------------------EAISLVGLKPLAHRLV 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 154 EqqlgTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10575 146 D----SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-191 |
5.83e-11 |
|
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: 65.15 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIG-ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL-------------GYL 68
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSlkdidrhtlrqfiNYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQDTHASDptQTALDRM-MSARDIATIinrirkaekemtdpdpdvmtkamnrydkamQDFDKAGGYAAQSEAISmATSLG 147
Cdd:TIGR01193 554 PQEPYIFS--GSILENLlLGAKENVSQ------------------------------DEIWAACEIAEIKDDIE-NMPLG 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 148 LPQEVMEQQlGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:TIGR01193 601 YQTELSEEG-SSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
356-507 |
5.94e-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: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 356 VILGYNGAGKTTTLR--LLAHIEEPDTGSVEYGHGCKIgyfAQEHDTL---DLNATVLENLQHVApeldnTQARSILGSF 430
Cdd:cd03240 26 LIVGQNGAGKTTIIEalKYALTGELPPNSKGGAHDPKL---IREGEVRaqvKLAFENANGKKYTI-----TRSLAILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 431 LF-----SGDDAMKPAHVLSGGEKT------RLALATLVTSRANVLLLDEPTNNLDPASRE----EILKAIAKYEG-AIV 494
Cdd:cd03240 98 IFchqgeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaEIIEERKSQKNfQLI 177
|
170
....*....|...
gi 489925987 495 LVTHDEGAVEALN 507
Cdd:cd03240 178 VITHDEELVDAAD 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-498 |
5.95e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 62.94 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLL---------AHIE-----------EPDTGSVEYG 386
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrllelneeARVEgevrlfgrniySPDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 387 HgcKIGYFAQ-----EHDTLDLNATV---LENLQHVAPELDNTQARSILGSFLFsgdDAMK------PAHvLSGGEKTRL 452
Cdd:PRK14267 85 R--EVGMVFQypnpfPHLTIYDNVAIgvkLNGLVKSKKELDERVEWALKKAALW---DEVKdrlndyPSN-LSGGQRQRL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 453 ALATLVTSRANVLLLDEPTNNLDPASR---EEILKAIaKYEGAIVLVTH 498
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTakiEELLFEL-KKEYTIVLVTH 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-517 |
6.14e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 62.80 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGS-----NIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----------EYGHGCKIGY 393
Cdd:COG1101 5 KNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIlidgkdvtklpEYKRAKYIGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 FAQehDTLDLNA---TVLENLQ---------HVAPELDNTQAR------SILGSFLfsgDDAMK-PAHVLSGGEKTRLAL 454
Cdd:COG1101 85 VFQ--DPMMGTApsmTIEENLAlayrrgkrrGLRRGLTKKRRElfrellATLGLGL---ENRLDtKVGLLSGGQRQALSL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 455 --ATLVTSRanVLLLDEPTNNLDPASREEIL----KAIAKYEGAIVLVTHD-EGAVEALNpeRVLLMPDG 517
Cdd:COG1101 160 lmATLTKPK--LLLLDEHTAALDPKTAALVLelteKIVEENNLTTLMVTHNmEQALDYGN--RLIMMHEG 225
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-224 |
6.25e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 63.21 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 14 ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSgklgylpqdthasdptqtalDRMMSARDIAT 93
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--------------------DIVVSSTSKQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 IINRIRKAEKEMTD-PDPDVMTKAMNRyDKAM--QDF--DKAGGYAAQSEAISMatsLGLPQEVMEQQLGTLSGGQRRRI 168
Cdd:PRK13643 78 EIKPVRKKVGVVFQfPESQLFEETVLK-DVAFgpQNFgiPKEKAEKIAAEKLEM---VGLADEFWEKSPFELSGGQMRRV 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 169 ELARILFSDADTLILDEPTNHLDADS-IEWLRGYLKKYEGGFLVIShSTELLDEVVN 224
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFESIHQSGQTVVL-VTHLMDDVAD 209
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
5-229 |
8.13e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDML--PTAGKVRVSGKLGYLPQDTHASDPTQTAL 82
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTggGAPRGARVTGDVTLNGEPLAAIDAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMM-----------SARDIaTIINRIRKAEKemtdpdpdvmTKAMNRYDkamqdfdkaGGYAAQSEAISMATSLglpqe 151
Cdd:PRK13547 84 LRAVlpqaaqpafafSAREI-VLLGRYPHARR----------AGALTHRD---------GEIAWQALALAGATAL----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 152 vMEQQLGTLSGGQRRRIELARIL---------FSDADTLILDEPTNHLDadsiewlrgylkkyeggflvISHSTELLDEV 222
Cdd:PRK13547 139 -VGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALD--------------------LAHQHRLLDTV 197
|
....*....
gi 489925987 223 --VNKVWHL 229
Cdd:PRK13547 198 rrLARDWNL 206
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-191 |
8.33e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 62.41 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQTal 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL-----------DVATT-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 drmmSARDIATIINRIRKaekemtdpDPDVMTK-------AMNRY----------DKAMQDfdkaggyaaqsEAISmatS 145
Cdd:COG4604 69 ----PSRELAKRLAILRQ--------ENHINSRltvrelvAFGRFpyskgrltaeDREIID-----------EAIA---Y 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 146 LGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG4604 123 LDL-EDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD 167
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-226 |
8.98e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.76 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 14 ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthaSDPTqtalDRMMSARDI-- 91
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG-----------VDIT----DKKVKLSDIrk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ---------------ATIINRIRKAEKEMTDPDPDVMtkamNRYDKAMQdfdkaggyaaqseaismatSLGLPQEVM-EQ 155
Cdd:PRK13637 84 kvglvfqypeyqlfeETIEKDIAFGPINLGLSEEEIE----NRVKRAMN-------------------IVGLDYEDYkDK 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 156 QLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDA----DSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKV 226
Cdd:PRK13637 141 SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVAKLADRI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
9.74e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 62.73 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQD-------THASDP 77
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseetvwdvrrQVGMVFQNpdnqfvgATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 78 TQTALDRMMSARDiaTIINRIRKAEKEMtdpdpdvmtkamnrydkAMQDFdkaggyaaqseaismatslglpqevMEQQL 157
Cdd:PRK13635 103 VAFGLENIGVPRE--EMVERVDQALRQV-----------------GMEDF-------------------------LNREP 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRgYLKKyEGGFLVIShSTELLDEV 222
Cdd:PRK13635 139 HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVR-QLKE-QKGITVLS-ITHDLDEA 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
324-497 |
1.01e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.34 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 324 RTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGS---VEY-GHGCK--------- 390
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELlGRTVQregrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 ------IGYFAQEHDTLDlNATVLEN---------------LQHVAPELDNT--QARSILGSFLFsgddAMKPAHVLSGG 447
Cdd:PRK09984 82 rksranTGYIFQQFNLVN-RLSVLENvligalgstpfwrtcFSWFTREQKQRalQALTRVGMVHF----AHQRVSTLSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 448 EKTRLALATLVTSRANVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVLVT 497
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARivmDTLRDINQNDGITVVVT 209
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-219 |
1.20e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 62.31 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdTHASDPTqtaldRMMSARDIATIINR 97
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--------IDTGDFS-----KLQGIRKLVGIVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 I-------RKAEKEMT-DPDPDVM--TKAMNRYDKAMQDFdKAGGYAAQSeaismatslglPQevmeqqlgTLSGGQRRR 167
Cdd:PRK13644 85 NpetqfvgRTVEEDLAfGPENLCLppIEIRKRVDRALAEI-GLEKYRHRS-----------PK--------TLSGGQGQC 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 168 IELARILFSDADTLILDEPTNHLDADS-IEWLRGYLKKYEGG--FLVISHSTELL 219
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGktIVYITHNLEEL 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-517 |
1.21e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG------------KLG-YL- 68
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcarltpakahQLGiYLv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 69 PQDTHASdPTQTALDrmmsarDIATIINRIRKAEKEMTDpdpdvMTKAMN-RYDKAMQdfdkaggyaaqseaismATSLg 147
Cdd:PRK15439 92 PQEPLLF-PNLSVKE------NILFGLPKRQASMQKMKQ-----LLAALGcQLDLDSS-----------------AGSL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 lpqEVMEQQLgtlsggqrrrIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHStelLDEVvn 224
Cdd:PRK15439 142 ---EVADRQI----------VEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlaQGvGIVFISHK---LPEI-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 225 kvWHLDAQLGqidmyslswkaylhqrvvdeerrrrerevaekkaerLMKQG-IRLHAKA---SKAVAAQNMMRRAEKLle 300
Cdd:PRK15439 204 --RQLADRIS------------------------------------VMRDGtIALSGKTadlSTDDIIQAITPAAREK-- 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 301 NTSEAQKAekvadirFPEPAPCGRT-----PIMAKDISKAYGsnivFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHI 375
Cdd:PRK15439 244 SLSASQKL-------WLELPGNRRQqaagaPVLTVEDLTGEG----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 376 EEPDTGSVEYGhGCKIG-------------YFAQEHDT--LDLNATVLEN---LQHVAPE--LDNTQARSILGSFL---- 431
Cdd:PRK15439 313 RPARGGRIMLN-GKEINalstaqrlarglvYLPEDRQSsgLYLDAPLAWNvcaLTHNRRGfwIKPARENAVLERYRraln 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 432 --FSGDDamKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAIAKYEGAIVLVTHDEGAVEAL 506
Cdd:PRK15439 392 ikFNHAE--QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIyqlIRSIAAQNVAVLFISSDLEEIEQM 469
|
570
....*....|.
gi 489925987 507 NpERVLLMPDG 517
Cdd:PRK15439 470 A-DRVLVMHQG 479
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
336-499 |
1.21e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 62.33 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 336 YGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYfaQEHDTLDLN---ATVLEN-- 410
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW-QGKPLDY--SKRGLLALRqqvATVFQDpe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 411 LQHVAPELDNTQARSI--LG----SFLFSGDDAM----------KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:PRK13638 88 QQIFYTDIDSDIAFSLrnLGvpeaEITRRVDEALtlvdaqhfrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180
....*....|....*....|....*...
gi 489925987 475 DPASREE---ILKAIAKYEGAIVLVTHD 499
Cdd:PRK13638 168 DPAGRTQmiaIIRRIVAQGNHVIISSHD 195
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-223 |
1.23e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgYLPQDTHASDPTQTAL---------Drmmsa 88
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH--DLRDYTLASLRNQVALvsqnvhlfnD----- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 89 rdiaTIINRIRKAEKEmtdpdpdvmtkamnRYDKAmqDFDKAGGYAAQSEAIsmatslglpqEVMEQQLGT--------L 160
Cdd:PRK11176 432 ----TIANNIAYARTE--------------QYSRE--QIEEAARMAYAMDFI----------NKMDNGLDTvigengvlL 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADS---IEWLRGYLKKyEGGFLVISH--ST-ELLDEVV 223
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESeraIQAALDELQK-NRTSLVIAHrlSTiEKADEIL 549
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
329-517 |
1.30e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 1.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAY---------GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQE-- 397
Cdd:PRK10419 6 VSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRAqr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 -----------HDTL-------DLNATVLENLQHVApELDNT----QARSILGSFLFSGDDAMKPAHVLSGGEKTRLALA 455
Cdd:PRK10419 85 kafrrdiqmvfQDSIsavnprkTVREIIREPLRHLL-SLDKAerlaRASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 456 TLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEG----AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfgtACLFITHDLRLVERF-CQRVMVMDNG 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-237 |
1.40e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGYLPQDTH---ASD 76
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEdISTLKPEIYrqqVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 PTQTALDRMMSARDIATIINRIRKAEkemtdPDPDVMTKAMNRYdkamqdfdkaggyaaqseaismatslGLPQEVMEQQ 156
Cdd:PRK10247 86 CAQTPTLFGDTVYDNLIFPWQIRNQQ-----PDPAIFLDDLERF--------------------------ALPDTILTKN 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 157 LGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSI----EWLRGYLKKYEGGFLVISHSTellDEV--VNKVWHLD 230
Cdd:PRK10247 135 IAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDK---DEInhADKVITLQ 211
|
....*..
gi 489925987 231 AQLGQID 237
Cdd:PRK10247 212 PHAGEMQ 218
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
357-505 |
1.43e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQEHDT-------LDLNATVLENLQHVApELDNTQARSILGS 429
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNINNIAKPYCTyighnlgLKLEMTVFENLKFWS-EIYNSAETLYAAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 430 FLFSGDDAM-KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI--LKAIAKYEGAIVLV-THDEGAVEA 505
Cdd:PRK13541 109 HYFKLHDLLdEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLnnLIVMKANSGGIVLLsSHLESSIKS 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-198 |
1.53e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.39 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylPQdthasdptqtaldRMMSARD-----IATIinr 97
Cdd:PRK11288 25 FDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ----EM-------------RFASTTAalaagVAII--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 irkaEKEM-TDPDpdvMTKAMNRYdkaMQDFDKAGGYAAQSEAISMATS----LGL---PQevmeQQLGTLSGGQRRRIE 169
Cdd:PRK11288 85 ----YQELhLVPE---MTVAENLY---LGQLPHKGGIVNRRLLNYEAREqlehLGVdidPD----TPLKYLSIGQRQMVE 150
|
170 180
....*....|....*....|....*....
gi 489925987 170 LARILFSDADTLILDEPTNHLDADSIEWL 198
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSLSAREIEQL 179
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
324-499 |
1.61e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 324 RTPIMA-KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC----------KI 391
Cdd:PRK10247 4 NSPLLQlQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 GYFAQehdTLDL-NATVLENL------QHVAPELDNTQARsiLGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANV 464
Cdd:PRK10247 84 SYCAQ---TPTLfGDTVYDNLifpwqiRNQQPDPAIFLDD--LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 465 LLLDEPTNNLDPASREEILKAIAKY----EGAIVLVTHD 499
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHD 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-214 |
1.75e-10 |
|
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: 63.16 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGKVRVSGK-LGYLP---------------QDTHASdptqtaLDRM 85
Cdd:COG4172 306 SLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdLDGLSrralrplrrrmqvvfQDPFGS------LSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 MSARDIAT---IINRIRKAEKEMTDpdpdvmtkamnRYDKAMQDfdkaggyaaqseaismatsLGLPQEVMEQQLGTLSG 162
Cdd:COG4172 379 MTVGQIIAeglRVHGPGLSAAERRA-----------RVAEALEE-------------------VGLDPAARHRYPHEFSG 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISH 214
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILDLLRDLQREHGLAYLFISH 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
336-500 |
1.77e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.73 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 336 YGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-------------GHGCKIGYFAQEHDTLD 402
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqsikkdlctyqKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 LNATVLENLQHVAPELDNTQARSI--LGSFLfsgddaMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE 480
Cdd:PRK13540 91 LRENCLYDIHFSPGAVGITELCRLfsLEHLI------DYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|...
gi 489925987 481 EILKAIAKYE---GAIVLVTHDE 500
Cdd:PRK13540 165 TIITKIQEHRakgGAVLLTSHQD 187
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
330-505 |
1.94e-10 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.57 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPD---TGSVEY-GHGC--------KIGYFAQE 397
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLnGRRLtalpaeqrRIGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 hDTLDLNATVLENLQHVAPELDNTQAR---------SI-LGSFlFSGDdamkPAhVLSGGEKTRLALATLVTSRANVLLL 467
Cdd:COG4136 85 -DLLFPHLSVGENLAFALPPTIGRAQRrarveqaleEAgLAGF-ADRD----PA-TLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 468 DEPTNNLDPASREEI----LKAIAKYEGAIVLVTHDEGAVEA 505
Cdd:COG4136 158 DEPFSKLDAALRAQFrefvFEQIRQRGIPALLVTHDEEDAPA 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-204 |
2.01e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 62.40 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MA-IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL-GYLPqdthasdpt 78
Cdd:COG3839 1 MAsLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDvTDLP--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 qtALDR---M----------MSARDiatiiN-----RIRKAEKEmtdpdpdvmtkamnRYDKAMQDfdkaggyaaqseai 140
Cdd:COG3839 72 --PKDRniaMvfqsyalyphMTVYE-----NiafplKLRKVPKA--------------EIDRRVRE-------------- 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 141 sMATSLGLpqevmEQQL----GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:COG3839 117 -AAELLGL-----EDLLdrkpKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKR 178
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
327-498 |
2.07e-10 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 61.21 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLL---------AHIEepdtGSVEYgHGCKIgYfaqe 397
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndlipgARVE----GEILL-DGEDI-Y---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 398 HDTLDLNA-----------------TVLEN------LQHVAP--ELDNTQARSILGSFLFS--GDDAMKPAHVLSGGEKT 450
Cdd:COG1117 82 DPDVDVVElrrrvgmvfqkpnpfpkSIYDNvayglrLHGIKSksELDEIVEESLRKAALWDevKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 451 RLALAtlvtsRA-----NVLLLDEPTNNLDPASR---EEILKAIAK-YegAIVLVTH 498
Cdd:COG1117 162 RLCIA-----RAlavepEVLLMDEPTSALDPISTakiEELILELKKdY--TIVIVTH 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-199 |
2.81e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQTALDRMMsaRDIATIINR 97
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK-----------DITDWQTAKIM--REAVAIVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRKAEKEMTDPDPDVMtkamnrydkamqdfdkaGGYAAQSEA----ISMATSLgLP--QEVMEQQLGTLSGGQRRRIELA 171
Cdd:PRK11614 88 GRRVFSRMTVEENLAM-----------------GGFFAERDQfqerIKWVYEL-FPrlHERRIQRAGTMSGGEQQMLAIG 149
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 172 RILFSDADTLILDEPTNHLDA-------DSIEWLR 199
Cdd:PRK11614 150 RALMSQPRLLLLDEPSLGLAPiiiqqifDTIEQLR 184
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
344-497 |
3.06e-10 |
|
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: 60.36 E-value: 3.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEpdTGSVEYGH----GCK---------IGYFAQeHDTLDLNATVLEN 410
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQilfnGQPrkpdqfqkcVAYVRQ-DDILLPGLTVRET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 411 LQHVA----PELDNTQARSILGSFLFSGDDAMKP-AHV----LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:cd03234 102 LTYTAilrlPRKSSDAIRKKRVEDVLLRDLALTRiGGNlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170
....*....|....*...
gi 489925987 482 ILKAIAKY--EGAIVLVT 497
Cdd:cd03234 182 LVSTLSQLarRNRIVILT 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
341-500 |
3.31e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC--------------KIGYFAQEHDTL-DLN 404
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLhqmdeearaklrakHVGFVFQSFMLIpTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 AtvLENLQHVA---PELDN---TQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:PRK10584 105 A--LENVELPAllrGESSRqsrNGAKALLEQLGLGKRLDHLPAQ-LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*.
gi 489925987 479 REEILKAI----AKYEGAIVLVTHDE 500
Cdd:PRK10584 182 GDKIADLLfslnREHGTTLILVTHDL 207
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
330-517 |
3.35e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 62.82 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSN----IVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSveyghgckigYFAQEHDTLDLNA 405
Cdd:PRK10535 8 KDIRRSYPSGeeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGT----------YRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 406 TVLENLQ-----------HVAPELDNTQ-------------------ARSILGSfLFSGDDAMKPAHVLSGGEKTRLALA 455
Cdd:PRK10535 78 DALAQLRrehfgfifqryHLLSHLTAAQnvevpavyaglerkqrllrAQELLQR-LGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 456 TLVTSRANVLLLDEPTNNLDPASREE---ILKAIAKYEGAIVLVTHD-EGAVEAlnpERVLLMPDG 517
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEvmaILHQLRDRGHTVIIVTHDpQVAAQA---ERVIEIRDG 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-217 |
3.41e-10 |
|
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: 63.11 E-value: 3.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 25 VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK------------LGYLPQdthasdptQTALDRMMSARDIA 92
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltnisdvhqnMGYCPQ--------FDAIDDLLTGREHL 2033
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIINRIRKAEKEmtdpdpdvmtkamnrydkamqDFDKAGGYAAQSEAISMATslglpqevmEQQLGTLSGGQRRRIELAR 172
Cdd:TIGR01257 2034 YLYARLRGVPAE---------------------EIEKVANWSIQSLGLSLYA---------DRLAGTYSGGNKRKLSTAI 2083
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 173 ILFSDADTLILDEPTNHLD--ADSIEW--LRGYLKKyEGGFLVISHSTE 217
Cdd:TIGR01257 2084 ALIGCPPLVLLDEPTTGMDpqARRMLWntIVSIIRE-GRAVVLTSHSME 2131
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-230 |
3.94e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 61.00 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthaSDPTQTALDRMMSARDIATIINRIRKA 101
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGY----------HITPETGNKNLKKLRKKVSLVFQFPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 EKEMTDPDPDVMTKAMNRydkamqdfdKAGGYAAQSEAISMATSLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTL 181
Cdd:PRK13641 97 QLFENTVLKDVEFGPKNF---------GFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 182 ILDEPTNHLDADSIEWLRGYLKKYE-GGFLVI--SHSTELLDEVVNKVWHLD 230
Cdd:PRK13641 168 CLDEPAAGLDPEGRKEMMQLFKDYQkAGHTVIlvTHNMDDVAEYADDVLVLE 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
18-194 |
3.99e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTR----VITGDMLPTAgKVRVSGKL----GYLPQDTHASDPTQTALDRMMSar 89
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTvqreGRLARDIRKSRANTGYIFQQFN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 90 diatIINRIRKAEkemtdpdpDVMTKAMNR---YDKAMQDFDKAggyaAQSEAISMATSLGLPQeVMEQQLGTLSGGQRR 166
Cdd:PRK09984 97 ----LVNRLSVLE--------NVLIGALGStpfWRTCFSWFTRE----QKQRALQALTRVGMVH-FAHQRVSTLSGGQQQ 159
|
170 180
....*....|....*....|....*...
gi 489925987 167 RIELARILFSDADTLILDEPTNHLDADS 194
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPES 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
330-498 |
4.09e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 62.43 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGS---NIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV--------EYGHGC---KIGYFA 395
Cdd:TIGR00958 482 QDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVlldgvplvQYDHHYlhrQVALVG 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEhdTLDLNATVLENlqhVAPELDNTQARSILGSFLFSG--DDAMKPAH-----------VLSGGEKTRLALATLVTSRA 462
Cdd:TIGR00958 562 QE--PVLFSGSVREN---IAYGLTDTPDEEIMAAAKAANahDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKP 636
|
170 180 190
....*....|....*....|....*....|....*.
gi 489925987 463 NVLLLDEPTNNLDPASREEILKAIAKYEGAIVLVTH 498
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
18-206 |
4.81e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.56 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-KLGYLPQDTHasdptqtaldrmmsardiatiIN 96
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKY---------------------IR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 RIRK--------AEKEMTDpdpDVMTKAMNRYDKAMQ-DFDKAGGYAAQseaisMATSLGLPQEVMEQQLGTLSGGQRRR 167
Cdd:PRK13646 82 PVRKrigmvfqfPESQLFE---DTVEREIIFGPKNFKmNLDEVKNYAHR-----LLMDLGFSRDVMSQSPFQMSGGQMRK 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 168 IELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYE 206
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQ 192
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
345-517 |
4.94e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----EYGHGCK-------IGYFAQEHDTLDLNATVLENLQ 412
Cdd:PRK13644 21 INLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsgiDTGDFSKlqgirklVGIVFQNPETQFVGRTVEEDLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 413 hVAPE---LDNTQARSILGSFLFS---GDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI 486
Cdd:PRK13644 101 -FGPEnlcLPPIEIRKRVDRALAEiglEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERI 179
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 487 AKYE---GAIVLVTHDegaVEALN-PERVLLMPDG 517
Cdd:PRK13644 180 KKLHekgKTIVYITHN---LEELHdADRIIVMDRG 211
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-192 |
5.07e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.90 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTT----LTRVITgdmlPTAGKVRVSGklgylpQDThaSDPTQTAL------ 82
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTlinlLQRVFD----PQSGRILIDG------TDI--RTVTRASLrrniav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 ---DRMMSARDIAtiiNRIRKAEKEMTDPDpdvMTKAMNRydkamqdfdkaggyAAQSEAIsMATSLGLPQEVMEQQlGT 159
Cdd:PRK13657 414 vfqDAGLFNRSIE---DNIRVGRPDATDEE---MRAAAER--------------AQAHDFI-ERKPDGYDTVVGERG-RQ 471
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-222 |
5.22e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.58 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYLPQdtHASD-PTQTALDR-M 85
Cdd:COG3845 25 SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvrirsprdaialgIGMVHQ--HFMLvPNLTVAENiV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 MSARDIATIINRIRKAEKEMTDpdpdvmtkAMNRYdkamqdfdkaggyaaqseaismatslGL---PQEVMEQqlgtLSG 162
Cdd:COG3845 103 LGLEPTKGGRLDRKAARARIRE--------LSERY--------------------------GLdvdPDAKVED----LSV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVISHStelLDEV 222
Cdd:COG3845 145 GEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLaaEGkSIIFITHK---LREV 204
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-203 |
5.54e-10 |
|
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: 59.56 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPTQT-- 80
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK------DITNLPPHKRpv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 -------ALDRMMS-ARDIATIInRIRKAEKemtdpdpdvmtKAMNRYDKAMQDFDKAGGYAAQSeaismatslglPQEv 152
Cdd:cd03300 75 ntvfqnyALFPHLTvFENIAFGL-RLKKLPK-----------AEIKERVAEALDLVQLEGYANRK-----------PSQ- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 153 meqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLK 203
Cdd:cd03300 131 -------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELK 174
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
345-499 |
5.63e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 5.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC--------------KIGYFAQEHDTLDLNATVLE 409
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NLQH------VAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:PRK13641 106 DVEFgpknfgFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170
....*....|....*....
gi 489925987 484 KAIAKYEGA---IVLVTHD 499
Cdd:PRK13641 186 QLFKDYQKAghtVILVTHN 204
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-220 |
5.93e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDML--PTAGKVRVsgklgylPQDTHASDpt 78
Cdd:COG2401 29 IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDV-------PDNQFGRE-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 qtaldrmmsardiATIINRIRKaekemtDPDPDVMTKAMNRydkamqdfdkaggyAAQSEAISMatsLGLPQEvmeqqlg 158
Cdd:COG2401 100 -------------ASLIDAIGR------KGDFKDAVELLNA--------------VGLSDAVLW---LRRFKE------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 159 tLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEW----LRGYLKKYEGGFLVISHSTELLD 220
Cdd:COG2401 137 -LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARRAGITLVVATHHYDVID 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-220 |
5.93e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.91 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKV--------------RVSGKLGYLPQ 70
Cdd:PRK10895 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 71 dthasdptQTALDRMMSARDIATIINRIRKAEKEMTDPDpdvmtkamnRYDKAMQDFDKAggyaaqseaiSMATSLGlpq 150
Cdd:PRK10895 86 --------EASIFRRLSVYDNLMAVLQIRDDLSAEQRED---------RANELMEEFHIE----------HLRDSMG--- 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 151 evmeqqlGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS---IEWLRGYLKKYEGGFLVISHST-ELLD 220
Cdd:PRK10895 136 -------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITDHNVrETLA 202
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
279-517 |
6.71e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 6.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 279 HAKAsKAV-AAQNMMrraeKLLENTSEAQKAEKVadirfpEPAPCGRTPIMAKD--ISKAYGSniVFAG-VNLAIDKGSR 354
Cdd:PRK11174 312 HAKA-QAVgAAESLV----TFLETPLAHPQQGEK------ELASNDPVTIEAEDleILSPDGK--TLAGpLNFTLPAGQR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 355 VVILGYNGAGKTTTLR-LLAHIeePDTGSVeyghgcKIGyfAQEHDTLDLN-----------------ATVLENLQHVAP 416
Cdd:PRK11174 379 IALVGPSGAGKTSLLNaLLGFL--PYQGSL------KIN--GIELRELDPEswrkhlswvgqnpqlphGTLRDNVLLGNP 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 417 ELDNTQARSIL-----GSFLFS---------GDDAMKpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI 482
Cdd:PRK11174 449 DASDEQLQQALenawvSEFLPLlpqgldtpiGDQAAG----LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
250 260 270
....*....|....*....|....*....|....*...
gi 489925987 483 LKAIAKYEGA--IVLVTHDegaVEAL-NPERVLLMPDG 517
Cdd:PRK11174 525 MQALNAASRRqtTLMVTHQ---LEDLaQWDQIWVMQDG 559
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
8-226 |
7.04e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.60 E-value: 7.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 8 LEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDT----HASDPTQTald 83
Cdd:PRK10619 11 LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlKVADKNQL--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 84 RMMSARdiATIINRIRKAEKEMTDPDpDVMTKAMNRYDKAMQDfdkaggyaAQSEAISMATSLGLPQEVMEQQLGTLSGG 163
Cdd:PRK10619 88 RLLRTR--LTMVFQHFNLWSHMTVLE-NVMEAPIQVLGLSKQE--------ARERAVKYLAKVGIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLDADSI-EWLRGYLKKYEGG--FLVISHSTELLDEVVNKV 226
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVgEVLRIMQQLAEEGktMVVVTHEMGFARHVSSHV 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-191 |
8.55e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.48 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdmL--PTAGKVRVSGklgylpQDTHASDPTQTALDRmmsaRD 90
Cdd:COG1135 16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL--LerPTSGSVLVDG------VDLTALSERELRAAR----RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATI---------------------INRIRKAEkemtdpdpdvmtkamnRYDKAMQ--DF----DKAGGYAAQseaisma 143
Cdd:COG1135 84 IGMIfqhfnllssrtvaenvalpleIAGVPKAE----------------IRKRVAEllELvglsDKADAYPSQ------- 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 144 tslglpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG1135 141 ----------------LSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-229 |
8.68e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 32 GLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGY-------LPQD--THASDPTQ----TALDRmmsarDIATIINR 97
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpLDYskrgllaLRQQvaTVFQDPEQqifyTDIDS-----DIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRKAEKEMTdpdpdvmtkamNRYDKAMQDFDKaggyaaqseaismatslglpQEVMEQQLGTLSGGQRRRIELARILFSD 177
Cdd:PRK13638 106 LGVPEAEIT-----------RRVDEALTLVDA--------------------QHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 178 ADTLILDEPTNHLDADSIEWLRGYLKKY--EGGFLVI-SHSTELLDEVVNKVWHL 229
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIsSHDIDLIYEISDAVYVL 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
13-217 |
9.09e-10 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 59.49 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL--------GYLPQDtHASDPTQTALDR 84
Cdd:COG4525 18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPvtgpgadrGVVFQK-DALLPWLNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMsardIATIINRIRKAEkemtdpdpdvmtkamnRYDKAMQdfdkaggyaaqseaisMATSLGLpQEVMEQQLGTLSGGQ 164
Cdd:COG4525 97 VA----FGLRLRGVPKAE----------------RRARAEE----------------LLALVGL-ADFARRRIWQLSGGM 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYL----KKYEGGFLVISHSTE 217
Cdd:COG4525 140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLITHSVE 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-517 |
9.12e-10 |
|
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: 57.83 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG------------HGCKIGYFAQE--HDTLDLNAT 406
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgkpvtrrsprdaIRAGIAYVPEDrkREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 407 VLENLqhvapeldntqarsILGSFLfsgddamkpahvlSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI 486
Cdd:cd03215 95 VAENI--------------ALSSLL-------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 487 AKY--EG-AIVLVTHDegavealNPE------RVLLMPDG 517
Cdd:cd03215 148 RELadAGkAVLLISSE-------LDEllglcdRILVMYEG 180
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-230 |
9.15e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 59.82 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQI-GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptQTA 81
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE--------------PIT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 LDRMMSARDIATIInrirkaekeMTDPDPDVMTKAMNR---YDKAMQDFDKAGGYAAQSEAISMatsLGLpQEVMEQQLG 158
Cdd:PRK13652 70 KENIREVRKFVGLV---------FQNPDDQIFSPTVEQdiaFGPINLGLDEETVAHRVSSALHM---LGL-EELRDRVPH 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYegGFLVI--SHSTELLDEVVNKVWHLD 230
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvKELIDFLNDLPETY--GMTVIfsTHQLDLVPEMADYIYVMD 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-227 |
9.17e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 59.71 E-value: 9.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdPTQTALDRMMSARDIATIInrIRKA 101
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE------------PIKYDKKSLLEVRKTVGIV--FQNP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 EKEMTDP--DPDVMTKAMNrydkamqdfdkaggyaaqseaismatsLGLPQEVMEQQLGT-----------------LSG 162
Cdd:PRK13639 88 DDQLFAPtvEEDVAFGPLN---------------------------LGLSKEEVEKRVKEalkavgmegfenkpphhLSG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWLRGYLKKyEGGFLVIS-HSTELLDEVVNKVW 227
Cdd:PRK13639 141 GQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNK-EGITIIIStHDVDLVPVYADKVY 208
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-229 |
9.33e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.42 E-value: 9.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptQTALDRMMSARDIATIIN 96
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQ--------------SIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 RirkaekemTDPDPDVMTKamnryDKAMQDFDKAGGYAAQSEAISMaTSLGlpqEVMEQQLGTLSGGQRRRIELARILFS 176
Cdd:PRK13540 82 R--------SGINPYLTLR-----ENCLYDIHFSPGAVGITELCRL-FSLE---HLIDYPCGLLSSGQKRQVALLRLWMS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 177 DADTLILDEPTNHLDADSIEWLRGYLKKYE---GGFLVISHSTELLDEVVNKVWHL 229
Cdd:PRK13540 145 KAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQDLPLNKADYEEYHL 200
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-236 |
1.03e-09 |
|
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: 59.02 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQTALDRM-----------MSARD 90
Cdd:TIGR01184 5 NLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----------QITEPGPDRMvvfqnysllpwLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 -IATIINRIrkaekemtdpdpdvmtkamnrydkaMQDFDKAGGYAAQSEAISMatsLGLpQEVMEQQLGTLSGGQRRRIE 169
Cdd:TIGR01184 74 nIALAVDRV-------------------------LPDLSKSERRAIVEEHIAL---VGL-TEAADKRPGQLSGGMKQRVA 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 170 LARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EGGF--LVISHSTE----LLDEVVNKVWHLDAQLGQI 236
Cdd:TIGR01184 125 IARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIweEHRVtvLMVTHDVDeallLSDRVVMLTNGPAANIGQI 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-214 |
1.49e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.18 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdpTQTAL 82
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI-------------NYNKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMMSARDIATIINRIRKAEKEMTDPDPDVMTKAMNRydKAMQ----DFDKAggyaaQSEAISMATSLGLPQEvMEQQLG 158
Cdd:PRK09700 73 DHKLAAQLGIGIIYQELSVIDELTVLENLYIGRHLTK--KVCGvniiDWREM-----RVRAAMMLLRVGLKVD-LDEKVA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 159 TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWL---RGYLKKYEGGFLVISH 214
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISH 203
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
22-191 |
1.63e-09 |
|
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: 57.95 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRMMSARDIatiINRIRKA 101
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND------QSHTGLAPYQRPVSMLFQENNL---FAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 EKEMTDPDPDVMTKAMNrydkamqdfdkaggyaaQSEAISMATSLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTL 181
Cdd:TIGR01277 89 QNIGLGLHPGLKLNAEQ-----------------QEKVVDAAQQVGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPIL 150
|
170
....*....|
gi 489925987 182 ILDEPTNHLD 191
Cdd:TIGR01277 151 LLDEPFSALD 160
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-499 |
1.90e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 58.51 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGhgcKIGYFAQE--HDTLDLN 404
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEG---RVEFFNQNiyERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 -----------------ATVLENLQ--------HVAPELDNTQARSILGSFLFS--GDDAMKPAHVLSGGEKTRLALATL 457
Cdd:PRK14258 85 rlrrqvsmvhpkpnlfpMSVYDNVAygvkivgwRPKLEIDDIVESALKDADLWDeiKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 458 VTSRANVLLLDEPTNNLDPASREEILKAIA----KYEGAIVLVTHD 499
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQslrlRSELTMVIVSHN 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-218 |
1.93e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 58.46 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK-LGYLPQDTHAsdptqta 81
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhIEGLPGHQIA------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 ldRMMSARDIATIinrirKAEKEMTdpdpdVMTK---AMNRYDKA--MQDFDKAGGY-AAQSEAISMATS----LGLpQE 151
Cdd:PRK11300 79 --RMGVVRTFQHV-----RLFREMT-----VIENllvAQHQQLKTglFSGLLKTPAFrRAESEALDRAATwlerVGL-LE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 152 VMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT---NHLDADSIEWLRGYLKKYEG-GFLVISHSTEL 218
Cdd:PRK11300 146 HANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHDMKL 216
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-517 |
2.22e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 25 VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRvsgklgYLPQDTHASDP--TQTAldrmmsarDIATI---INRIR 99
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIL------YLGKEVTFNGPksSQEA--------GIGIIhqeLNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 100 K---AE-----KEMTDPdpdvmtkaMNRYD-KAMqdfdkaggYAaqsEAISMATSLGLPQEvMEQQLGTLSGGQRRRIEL 170
Cdd:PRK10762 93 QltiAEniflgREFVNR--------FGRIDwKKM--------YA---EADKLLARLNLRFS-SDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 171 ARILFSDADTLILDEPTNHLDADSIEWLRGYLK--KYEG-GFLVISHSTELLDEVVNKVWHL-DAQ-LGQIDMYSLswka 245
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRelKSQGrGIVYISHRLKEIFEICDDVTVFrDGQfIAEREVADL---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 246 ylhqrvvdeerrrrerevaekKAERLMKqgirlhakaskavaaqnMM--RRAEKllentseaqkaekvadiRFPEPA-PC 322
Cdd:PRK10762 229 ---------------------TEDSLIE-----------------MMvgRKLED-----------------QYPRLDkAP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 323 GRTPIMAKDISkayGSNIvfAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE-YGHGCK----------- 390
Cdd:PRK10762 254 GEVRLKVDNLS---GPGV--NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTlDGHEVVtrspqdglang 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 391 IGYFAQE--HDTLDLNATVLEN--------LQHVAPELDNTQARSILGSF--LF-----SGDdamKPAHVLSGGEKTRLA 453
Cdd:PRK10762 329 IVYISEDrkRDGLVLGMSVKENmsltalryFSRAGGSLKHADEQQAVSDFirLFniktpSME---QAIGLLSGGNQQKVA 405
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 454 LATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG-AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaEGlSIILVSSEMPEVLGMS-DRILVMHEG 471
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-192 |
2.25e-09 |
|
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: 60.34 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDthasdptqtaldrmmsardiATIINr 97
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQ--------------------AWIQN- 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 irkaekemtdpdpDVMTKAMnRYDKAMQDfdkaGGYAAQSEAISMATSL-----GLPQEVMEQQLgTLSGGQRRRIELAR 172
Cdd:TIGR00957 713 -------------DSLRENI-LFGKALNE----KYYQQVLEACALLPDLeilpsGDRTEIGEKGV-NLSGGQKQRVSLAR 773
|
170 180
....*....|....*....|
gi 489925987 173 ILFSDADTLILDEPTNHLDA 192
Cdd:TIGR00957 774 AVYSNADIYLFDDPLSAVDA 793
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
327-517 |
2.32e-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: 57.42 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNI--VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaqehDTLDLN 404
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-------------DGIDIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 ATVLENLQHVA------PELDNTQARSILGSF-LFSGDDAMKPAHV------LSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:cd03369 74 TIPLEDLRSSLtiipqdPTLFSGTIRSNLDPFdEYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 472 NNLDPASREEILKAIAK-YEGA-IVLVTHDEGAVeaLNPERVLLMPDG 517
Cdd:cd03369 154 ASIDYATDALIQKTIREeFTNStILTIAHRLRTI--IDYDKILVMDAG 199
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
3-191 |
2.80e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLP 69
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 70 QDthASDPTQTALDRMMSARDIA--TIINRIRKAekemtdpDPDVMTKAMnrydkamqdfdkaggyaaQSEAISmatslg 147
Cdd:PRK10253 88 QN--ATTPGDITVQELVARGRYPhqPLFTRWRKE-------DEEAVTKAM------------------QATGIT------ 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 148 lpqEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10253 135 ---HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
327-517 |
2.85e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV-----EYGH-------GCKIGYF 394
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinniNYNKldhklaaQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEHDTLDlNATVLENL---QHVA------PELDNTQARSILGSFLFSGD---DAMKPAHVLSGGEKTRLALATLVTSRA 462
Cdd:PRK09700 86 YQELSVID-ELTVLENLyigRHLTkkvcgvNIIDWREMRVRAAMMLLRVGlkvDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 463 NVLLLDEPTNNLDPASREE---ILKAIAKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYlflIMNQLRKEGTAIVYISHKLAEIRRIC-DRYTVMKDG 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
16-191 |
2.96e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 16 TLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK----------LGYLPQDTHA--SDPTQTAlD 83
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQSEEVdwSFPVLVE-D 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 84 RMMSARDIATIINRIRKAEkemtdpDPDVMTKAMNRYDkaMQDFdkaggyaaqseaismatslglpqevMEQQLGTLSGG 163
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKR------DRQIVTAALARVD--MVEF-------------------------RHRQIGELSGG 146
|
170 180
....*....|....*....|....*...
gi 489925987 164 QRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK15056 147 QKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-224 |
2.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSgklgylpqdthasdptqtalDRMMSARDIATIINRIRK- 100
Cdd:PRK13649 27 NLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVD--------------------DTLITSTSKNKDIKQIRKk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 101 -------AEKEMTDpdpDVMTKamnryDKAM--QDFDkaggyAAQSEAISMA----TSLGLPQEVMEQQLGTLSGGQRRR 167
Cdd:PRK13649 87 vglvfqfPESQLFE---ETVLK-----DVAFgpQNFG-----VSQEEAEALAreklALVGISESLFEKNPFELSGGQMRR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 168 IELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELLDEVVN 224
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVAN 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
326-498 |
3.11e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 3.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 326 PIM-AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEE--PD---TGSVEY-GHGCkigyFAQEH 398
Cdd:PRK14239 4 PILqVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYnGHNI----YSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DTLDLNA--------------TVLENL-----------QHVapeLDNTQARSILGSFLFS--GDDAMKPAHVLSGGEKTR 451
Cdd:PRK14239 80 DTVDLRKeigmvfqqpnpfpmSIYENVvyglrlkgikdKQV---LDEAVEKSLKGASIWDevKDRLHDSALGLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489925987 452 LALATLVTSRANVLLLDEPTNNLDPASR---EEILKAIaKYEGAIVLVTH 498
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAgkiEETLLGL-KDDYTMLLVTR 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-191 |
3.60e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.25 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPtQTALdrmmsARDIAtIINR 97
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGH------EVVTRSP-QDGL-----ANGIV-YISE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRKAEKEMTDpdpdvMTKAMNRYDKAMQDFDKAGG---YAAQSEAIS---MATSLGLPQevMEQQLGTLSGGQRRRIELA 171
Cdd:PRK10762 335 DRKRDGLVLG-----MSVKENMSLTALRYFSRAGGslkHADEQQAVSdfiRLFNIKTPS--MEQAIGLLSGGNQQKVAIA 407
|
170 180
....*....|....*....|
gi 489925987 172 RILFSDADTLILDEPTNHLD 191
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVD 427
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
341-517 |
4.11e-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: 58.96 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV--------EYGHGCKIGYFAQ-EHDTLDLNATVLENL 411
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdlaDYTLASLRRQVALvSQDVVLFNDTIANNI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 QHVAP-ELDNTQARSIL-GSFLFSGDDAM---------KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE 480
Cdd:TIGR02203 427 AYGRTeQADRAEIERALaAAYAQDFVDKLplgldtpigENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESER 506
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 481 EILKAIAK-YEGAIVLV-THDEGAVEalNPERVLLMPDG 517
Cdd:TIGR02203 507 LVQAALERlMQGRTTLViAHRLSTIE--KADRIVVMDDG 543
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-191 |
4.85e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASD---- 76
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAirll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 --------------PTQTALDRMMSARdiatiiNRIRKAEKEmtdpdpdvmtkamnrydkamqdfdkaggyAAQSEAISM 142
Cdd:COG4161 81 rqkvgmvfqqynlwPHLTVMENLIEAP------CKVLGLSKE-----------------------------QAREKAMKL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489925987 143 ATSLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG4161 126 LARLRL-TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
32-221 |
5.04e-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: 59.26 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 32 GLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptqtaldrmmsarDIATIINRIRKAEKEMtdPDPD 111
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK-------------------------DIETNLDAVRQSLGMC--PQHN 1012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 112 VMTKAMNRYDKaMQDFDKAGGYA---AQSEAISMATSLGLPQEVMEQQlGTLSGGQRRRIELARILFSDADTLILDEPTN 188
Cdd:TIGR01257 1013 ILFHHLTVAEH-ILFYAQLKGRSweeAQLEMEAMLEDTGLHHKRNEEA-QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTS 1090
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 189 HLDADSIEWLRGYLKKYEGGFLVIShSTELLDE 221
Cdd:TIGR01257 1091 GVDPYSRRSIWDLLLKYRSGRTIIM-STHHMDE 1122
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-192 |
5.94e-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: 5.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLP----TAGKVRVSGK----------LGYLPQDthasdptqt 80
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISG-RVEgggtTSGQILFNGQprkpdqfqkcVAYVRQD--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 alDRMMS---ARDIATIINRIRKAEKeMTDPDPDVMTKAMNRYDKAMQDfdkAGGYaaqseaismatslglpqeVMEQql 157
Cdd:cd03234 90 --DILLPgltVRETLTYTAILRLPRK-SSDAIRKKRVEDVLLRDLALTR---IGGN------------------LVKG-- 143
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 158 gtLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:cd03234 144 --ISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-214 |
6.48e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 6.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgYLPQDTHASDPTQTAL----DRMMSARDIATIINR 97
Cdd:TIGR00958 501 TFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV--PLVQYDHHYLHRQVALvgqePVLFSGSVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRKAEKEMtdpdpdVMTKAMnrydkamqdfdkaggyAAQSEAISMATSLGLPQEVMEQqlGT-LSGGQRRRIELARILFS 176
Cdd:TIGR00958 579 LTDTPDEE------IMAAAK----------------AANAHDFIMEFPNGYDTEVGEK--GSqLSGGQKQRIAIARALVR 634
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 177 DADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISH 214
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
11-191 |
6.97e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 56.48 E-value: 6.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 11 QIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGKVRVSGKLgyLPQdthasdptqtaldrmMSARD 90
Cdd:PRK03695 5 DVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQP--LEA---------------WSAAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IAtiinrIRKAEKEMTDPDPDVMTK----AMNRYDKAMQDfdkaggyAAQSEAISMATSLGLpQEVMEQQLGTLSGGQRR 166
Cdd:PRK03695 67 LA-----RHRAYLSQQQTPPFAMPVfqylTLHQPDKTRTE-------AVASALNEVAEALGL-DDKLGRSVNQLSGGEWQ 133
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 167 RIELA-------RILFSDADTLILDEPTNHLD 191
Cdd:PRK03695 134 RVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-220 |
7.45e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 58.28 E-value: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGA-RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdmLPTAGkvrvSGKLG-------------- 66
Cdd:COG4178 362 ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--LWPYG----SGRIArpagarvlflpqrp 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQDThasdptqtaLDRMMSardiatiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggYAAQSEAISMATSl 146
Cdd:COG4178 436 YLPLGT---------LREALL---------------------------------------------YPATAEAFSDAEL- 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 147 glpQEVMEQ-QLG--------------TLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK--YEGGF 209
Cdd:COG4178 461 ---REALEAvGLGhlaerldeeadwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTV 537
|
250
....*....|.
gi 489925987 210 LVISHSTELLD 220
Cdd:COG4178 538 ISVGHRSTLAA 548
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
153-228 |
7.53e-09 |
|
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: 55.69 E-value: 7.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 153 MEQQLGTLSGGQRR------RIELARILFSDADTLILDEPTNHLDADSIEW-----LRGYLKKYEGGFLVISHSTELLDe 221
Cdd:cd03240 109 LLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeiIEERKSQKNFQLIVITHDEELVD- 187
|
....*..
gi 489925987 222 VVNKVWH 228
Cdd:cd03240 188 AADHIYR 194
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
330-517 |
8.91e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.54 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GH------GCKIgyfAQ------ 396
Cdd:PRK11300 9 SGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQhieglpGHQI---ARmgvvrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 -EHDTLDLNATVLENL---QHvapeldnTQARSILGSFLF-------SGDDAM-----------------KPAHVLSGGE 448
Cdd:PRK11300 86 fQHVRLFREMTVIENLlvaQH-------QQLKTGLFSGLLktpafrrAESEALdraatwlervgllehanRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 449 KTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAK----YEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElrneHNVTVLLIEHDMKLVMGIS-DRIYVVNQG 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
341-517 |
9.54e-09 |
|
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: 56.35 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY---------GHGCK-------------IGYFAQEH 398
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqdlyqldRKQRRafrrdvqlvfqdsPSAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DTLDLNATVLENLQHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD--- 475
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDmvl 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 476 PASREEILKAIAKYEG-AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:TIGR02769 186 QAVILELLRKLQQAFGtAYLFITHDLRLVQSFC-QRVAVMDKG 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-187 |
9.56e-09 |
|
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: 55.99 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 4 EAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYLP 69
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEditklppheraragIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 70 QDthasdptqtaldRMmsardiatIINRIRKAEKEMTdpdpdvmtkamnrydkamqdfdkagGYAAQSEAismatSLGLP 149
Cdd:TIGR03410 82 QG------------RE--------IFPRLTVEENLLT-------------------------GLAALPRR-----SRKIP 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 150 QEVME-----QQL-----GTLSGGQRRRIELARILFSDADTLILDEPT 187
Cdd:TIGR03410 112 DEIYElfpvlKEMlgrrgGDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
3-219 |
1.04e-08 |
|
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: 54.47 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGA-RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdmLPTAGKVRVS----GKLGYLPQDThasdp 77
Cdd:cd03223 1 IELENLSLATPDgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--LWPWGSGRIGmpegEDLLFLPQRP----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 78 tqtaldrmmsardiatiinrirkaekemtdpdpdvmtkamnrydkamqdfdkaggYaaqseaismatslgLPQEVMEQQL 157
Cdd:cd03223 74 -------------------------------------------------------Y--------------LPLGTLREQL 84
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 158 -----GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELL 219
Cdd:cd03223 85 iypwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGHRPSLW 151
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
344-517 |
1.18e-08 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 55.73 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEepdtgSVEYGHGcKIGYfaQEHDTLDLN------------------- 404
Cdd:TIGR01978 18 GVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHP-----SYEVTSG-TILF--KGQDLLELEpderaraglflafqypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 405 --ATVLENLQHVA---------PELDNTQARSILGSFLFSGDdaMKPAHV-------LSGGEKTRLALATLVTSRANVLL 466
Cdd:TIGR01978 90 pgVSNLEFLRSALnarrsargeEPLDLLDFEKLLKEKLALLD--MDEEFLnrsvnegFSGGEKKRNEILQMALLEPKLAI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489925987 467 LDEPTNNLDPASREEILKAIAKY---EGAIVLVTHDEGAVEALNPERVLLMPDG 517
Cdd:TIGR01978 168 LDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHVLLDG 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
323-497 |
1.62e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 323 GRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTlRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTLD 402
Cdd:NF000106 10 ARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 LNATVL----------ENLQHVAPELD------NTQARSILGSFLFSgDDAMKPAHVLSGGEKTRLALATLVTSRANVLL 466
Cdd:NF000106 89 *HRPVR*grresfsgrENLYMIGR*LDlsrkdaRARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLY 167
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 467 LDEPTNNLDPASREEILKAIAKY--EGAIVLVT 497
Cdd:NF000106 168 LDEPTTGLDPRTRNEVWDEVRSMvrDGATVLLT 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
23-191 |
1.97e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.13 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRmmsaRDIATI-------I 95
Cdd:PRK11308 36 FTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG------QDLLKADPEAQKLLR----QKIQIVfqnpygsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 96 NRIRKAEKEMTDPdPDVMTK--AMNRYDKAMQdfdkaggyaaqseaisMATSLGLPQEVMEQQLGTLSGGQRRRIELARI 173
Cdd:PRK11308 106 NPRKKVGQILEEP-LLINTSlsAAERREKALA----------------MMAKVGLRPEHYDRYPHMFSGGQRQRIAIARA 168
|
170
....*....|....*...
gi 489925987 174 LFSDADTLILDEPTNHLD 191
Cdd:PRK11308 169 LMLDPDVVVADEPVSALD 186
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
12-191 |
2.08e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 54.88 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 12 IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----------------KLGYLPQDTHas 75
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrevpflrrQIGMIFQDHH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 76 dptqTALDRmmSARDIATIINRIRKAEKEmtdpdpDVMTKAMNRYDKaMQDFDKAGGYAAQseaismatslglpqevmeq 155
Cdd:PRK10908 90 ----LLMDR--TVYDNVAIPLIIAGASGD------DIRRRVSAALDK-VGLLDKAKNFPIQ------------------- 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 489925987 156 qlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10908 138 ----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
345-517 |
2.17e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEePDTGSV--------EYGHgCKI----GYFAQEHDTLdLNATVLENLQ 412
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIqfagqpleAWSA-AELarhrAYLSQQQTPP-FAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 413 -HVAPELDNTQARSILG---SFLFSGDDAMKPAHVLSGGE--KTRLALATL-VTSRAN----VLLLDEPTNNLDPASR-- 479
Cdd:PRK03695 92 lHQPDKTRTEAVASALNevaEALGLDDKLGRSVNQLSGGEwqRVRLAAVVLqVWPDINpagqLLLLDEPMNSLDVAQQaa 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 480 -EEILKAIAKYEGAIVLVTHDegaveaLN-----PERVLLMPDG 517
Cdd:PRK03695 172 lDRLLSELCQQGIAVVMSSHD------LNhtlrhADRVWLLKQG 209
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
341-517 |
2.38e-08 |
|
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: 54.80 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC----------KIGYFAQEHdtLDLNATVLE 409
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLaladpawlrrQVGVVLQEN--VLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NLQHVAPELDN---TQARSILGSFLF-----SGDDAM--KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:cd03252 95 NIALADPGMSMervIEAAKLAGAHDFiselpEGYDTIvgEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 480 EEI---LKAIAKYEGAIVlVTHDEGAVEalNPERVLLMPDG 517
Cdd:cd03252 175 HAImrnMHDICAGRTVII-IAHRLSTVK--NADRIIVMEKG 212
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-224 |
2.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 55.48 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthasdptqtaldrmMSARDIATIINRIRKA 101
Cdd:PRK13633 30 NLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG----------------------LDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 EKEMTDPDpdvmtkamNRYDKAMQDFDKAGGyaaqseaismATSLGLPQEVMEQQLGT-----------------LSGGQ 164
Cdd:PRK13633 88 GMVFQNPD--------NQIVATIVEEDVAFG----------PENLGIPPEEIRERVDEslkkvgmyeyrrhaphlLSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLDA----DSIEWLRGYLKKYEGGFLVISHsteLLDEVVN 224
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPsgrrEVVNTIKELNKKYGITIILITH---YMEEAVE 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
22-191 |
2.60e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 56.00 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRMMSA----------RDI 91
Cdd:PRK11607 39 SLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDG------VDLSHVPPYQRPINMMFQSyalfphmtveQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ATIINRIRKAEKEMTDPDPDVMTKAMnrydkaMQDFDKAGgyaaqseaismatslglPQEvmeqqlgtLSGGQRRRIELA 171
Cdd:PRK11607 113 AFGLKQDKLPKAEIASRVNEMLGLVH------MQEFAKRK-----------------PHQ--------LSGGQRQRVALA 161
|
170 180
....*....|....*....|
gi 489925987 172 RILFSDADTLILDEPTNHLD 191
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALD 181
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
444-517 |
2.61e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 2.61e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 444 LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAK----YEGAIVLVTHDEGAVEALNPErVLLMPDG 517
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnkeYKKRIIMVTHNMDQVLRIADE-VIVMHEG 227
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
335-488 |
2.72e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.99 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 335 AYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGCKIGYFAQEH-----DTLDLNATVLE 409
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEvarriGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 NL-------------QHVAPELDNTQARSILGSFLFSG--DDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:PRK10253 95 DItvqelvargryphQPLFTRWRKEDEEAVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170
....*....|....
gi 489925987 475 DPASREEILKAIAK 488
Cdd:PRK10253 175 DISHQIDLLELLSE 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-506 |
2.89e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTtLTRVITGDMLPTAGKVRVSGKLGYLPQDT-HASDPTQtaldRMMSARDIAT 93
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKS-VTALSILRLLPSPPVVYPSGDIRFHGESLlHASEQTL----RGVRGNKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 I-------INRIRKAEKEMTDpdpdVMT--KAMNRYdkamqdfdkaggyAAQSEAISMATSLGLPQEvmEQQLG----TL 160
Cdd:PRK15134 97 IfqepmvsLNPLHTLEKQLYE----VLSlhRGMRRE-------------AARGEILNCLDRVGIRQA--AKRLTdyphQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVwhldaqlgqi 236
Cdd:PRK15134 158 SGGERQRVMIAMALLTRPELLIADEPTTALDvsvqAQILQLLRELQQELNMGLLFITHNLSIVRKLADRV---------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 237 dmyslswkaylhqrvvdeerrrrerevaekkaeRLMKQGIRLHAKASKAVAAQNMMRRAEKLLEntseaqkAEKVADirf 316
Cdd:PRK15134 228 ---------------------------------AVMQNGRCVEQNRAATLFSAPTHPYTQKLLN-------SEPSGD--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 317 PEPAPCGRTPIM-AKDISKAY-----------GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTT----LRLLAhieepDT 380
Cdd:PRK15134 265 PVPLPEPASPLLdVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLIN-----SQ 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 381 GSVEYG----------------HGCKIgYFAQEHDTLDLNATVL----ENLQHVAPELDNTQ--ARSILGSFLFSGDDAM 438
Cdd:PRK15134 340 GEIWFDgqplhnlnrrqllpvrHRIQV-VFQDPNSSLNPRLNVLqiieEGLRVHQPTLSAAQreQQVIAVMEEVGLDPET 418
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 439 K---PAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAI-AKYEGAIVLVTHDEGAVEAL 506
Cdd:PRK15134 419 RhryPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQIlalLKSLqQKHQLAYLFISHDLHVVRAL 492
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
327-499 |
2.89e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.73 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAYGSniVFAGVNLA-IDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYfaqehdtldlna 405
Cdd:cd03222 1 QLYPDCVKRYGV--FFLLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVY------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 406 tvlenlqhvapeldntqarsilgsflfsgddamKPAHV-LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILK 484
Cdd:cd03222 66 ---------------------------------KPQYIdLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAAR 112
|
170
....*....|....*....
gi 489925987 485 AIAKY----EGAIVLVTHD 499
Cdd:cd03222 113 AIRRLseegKKTALVVEHD 131
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-191 |
3.22e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.18 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 10 IQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDM-------LPTAGKVRVSG--------KLGYLPQDTHa 74
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpqgysndLTLFGRRRGSGetiwdikkHIGYVSSSLH- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 75 sdptqtaldrmMSARDIATIINRIrkaekemtdpdpdvmtkaMNRYdkamqdFDKAGGYAAQSEAISMATS-----LGLP 149
Cdd:PRK10938 347 -----------LDYRVSTSVRNVI------------------LSGF------FDSIGIYQAVSDRQQKLAQqwldiLGID 391
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489925987 150 QEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10938 392 KRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-191 |
3.23e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASD---- 76
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTPSDKAirel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 --------------PTQTALDRMMSARdiatiiNRIRKAEKEmtdpdpdvmtKAMNRYDKAMQDF---DKAGGYAAQsea 139
Cdd:PRK11124 81 rrnvgmvfqqynlwPHLTVQQNLIEAP------CRVLGLSKD----------QALARAEKLLERLrlkPYADRFPLH--- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 140 ismatslglpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK11124 142 --------------------LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
329-499 |
3.25e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 54.79 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 329 AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLL---------AHIEepdtGSVEYgHGCKIgyFAQEHD 399
Cdd:PRK14243 13 TENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndlipgFRVE----GKVTF-HGKNL--YAPDVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 400 TLDLNATVLENLQHVAP--------------------ELDNTQARSILGSFLFS--GDDAMKPAHVLSGGEKTRLALATL 457
Cdd:PRK14243 86 PVEVRRRIGMVFQKPNPfpksiydniaygaringykgDMDELVERSLRQAALWDevKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489925987 458 VTSRANVLLLDEPTNNLDPASR---EEILKAIaKYEGAIVLVTHD 499
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTlriEELMHEL-KEQYTIIIVTHN 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-222 |
3.27e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLgylpqdthasdptqtaldrmMSARDIATIINR 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL--------------------LTEENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IrkaekEMTDPDPDvmtkamNRYDKAMQDFDKAGG-------YAAQSEAISMATSLGLPQEVMEQQLGTLSGGQRRRIEL 170
Cdd:PRK13650 83 I-----GMVFQNPD------NQFVGATVEDDVAFGlenkgipHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 171 ARILFSDADTLILDEPTNHLDA----DSIEWLRGYLKKYEGGFLVISHStelLDEV 222
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPegrlELIKTIKGIRDDYQMTVISITHD---LDEV 204
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-191 |
4.75e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.82 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQtaldRMMS-------------- 87
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSR----RPVSmlfqennlfshltv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 88 ARDIATIIN---RIRKAEKEmtdpdpdvmtkamnrydkAMQDfdkaggyaaqseaisMATSLGLpQEVMEQQLGTLSGGQ 164
Cdd:PRK10771 89 AQNIGLGLNpglKLNAAQRE------------------KLHA---------------IARQMGI-EDLLARLPGQLSGGQ 134
|
170 180
....*....|....*....|....*..
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10771 135 RQRVALARCLVREQPILLLDEPFSALD 161
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
325-517 |
4.97e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.16 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 325 TPIM-AKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY--GHGCKIGYFA------ 395
Cdd:PRK11701 4 QPLLsVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmRDGQLRDLYAlseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 -----------QEH--DTL-----------------------DLNATVLENLQHVapELDntQARSilgsflfsgDDAmk 439
Cdd:PRK11701 84 rrllrtewgfvHQHprDGLrmqvsaggnigerlmavgarhygDIRATAGDWLERV--EID--AARI---------DDL-- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 440 PAhVLSGGEKTRLALA-TLVTsRANVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDEgAVEALNPERVLLM 514
Cdd:PRK11701 149 PT-TFSGGMQQRLQIArNLVT-HPRLVFMDEPTGGLDVSVQARLLDLLrglvRELGLAVVIVTHDL-AVARLLAHRLLVM 225
|
...
gi 489925987 515 PDG 517
Cdd:PRK11701 226 KQG 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-192 |
5.19e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 6 QGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRV-SGKLGYLPQDThasdptqtaldR 84
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAgTAPLAEAREDT-----------R 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MM--SARDI--ATIINRIRKAEKEmtdpdpdvmtkamNRYDKAMQDFDkaggyaaqseaismatSLGLPQEVMEQQlGTL 160
Cdd:PRK11247 85 LMfqDARLLpwKKVIDNVGLGLKG-------------QWRDAALQALA----------------AVGLADRANEWP-AAL 134
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:PRK11247 135 SGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-192 |
5.20e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.90 E-value: 5.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTA-GKVRVSGKLGYLPQdthasdptqtaldrmmsardI 91
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGTVAYVPQ--------------------V 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ATIINRIRKAEKEMTDP-DPDvmtkamnRYDKAM------QDFDKAGGyaaqseaismatslGLPQEVMEQQLgTLSGGQ 164
Cdd:PLN03130 688 SWIFNATVRDNILFGSPfDPE-------RYERAIdvtalqHDLDLLPG--------------GDLTEIGERGV-NISGGQ 745
|
170 180
....*....|....*....|....*...
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:PLN03130 746 KQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-214 |
5.99e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.10 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 12 IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTT----LTRVItgdmlptagkvRVSGKLGYLPQDTHASDPTQtaldrMMS 87
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----------NSQGEIWFDGQPLHNLNRRQ-----LLP 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 88 ARdiatiinriRKAEKEMTDPDpdvmtKAMNRYDKAMQDFdkAGGY--------AAQSEA--ISMATSLGLPQEVMEQQL 157
Cdd:PRK15134 360 VR---------HRIQVVFQDPN-----SSLNPRLNVLQII--EEGLrvhqptlsAAQREQqvIAVMEEVGLDPETRHRYP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISH 214
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISH 484
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-191 |
6.25e-08 |
|
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: 53.27 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLT----RVITgdmlPTAGKVRVSGklgylpqdthasdptqtaldrmmsaRDIAT 93
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLVE----LSSGSILIDG-------------------------VDISK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 94 I-INRIRKAekeMT----DP-----------DPDvmtkamNRYD-----KAMQDfdkaggyaAQSEAISMATSLGLPQEV 152
Cdd:cd03244 71 IgLHDLRSR---ISiipqDPvlfsgtirsnlDPF------GEYSdeelwQALER--------VGLKEFVESLPGGLDTVV 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 153 MEQQLGtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:cd03244 134 EEGGEN-LSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
328-499 |
6.48e-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: 53.91 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 328 MAKDISKAYGSNiVFAGVNLAIDKGSRVV-ILGYNGAGKTTTLRLLA---------HIEEPD-TGSVEYGHGCKI-GYFA 395
Cdd:cd03236 2 LEDEPVHRYGPN-SFKLHRLPVPREGQVLgLVGPNGIGKSTALKILAgklkpnlgkFDDPPDwDEILDEFRGSELqNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 396 QEHDTlDLNATVleNLQHVapELDNTQARSILGSFLFSGD---------DAMKPAHV-------LSGGEKTRLALATLVT 459
Cdd:cd03236 81 KLLEG-DVKVIV--KPQYV--DLIPKAVKGKVGELLKKKDergkldelvDQLELRHVldrnidqLSGGELQRVAIAAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 460 SRANVLLLDEPTNNLDPASR---EEILKAIAKYEGAIVLVTHD 499
Cdd:cd03236 156 RDADFYFFDEPSSYLDIKQRlnaARLIRELAEDDNYVLVVEHD 198
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
341-485 |
6.58e-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: 54.09 E-value: 6.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEygHGCKIGYFAQEhdTLDLNATVLENLQhVAPELDN 420
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQF--SWIMPGTIKENII-FGVSYDE 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 421 TQARSILGSFLFSGDDAMKPAH----------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKA 485
Cdd:cd03291 127 YRYKSVVKACQLEEDITKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
357-506 |
6.65e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.79 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGYFAQEHDTL------DLNATVLENLQHV----------APELDN 420
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgycpqfDAIDDLLTGREHLylyarlrgvpAEEIEK 2049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 421 TQARSI--LGSFLFsgddAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASRE---EILKAIAKYEGAIVL 495
Cdd:TIGR01257 2050 VANWSIqsLGLSLY----ADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRmlwNTIVSIIREGRAVVL 2125
|
170
....*....|.
gi 489925987 496 VTHDEGAVEAL 506
Cdd:TIGR01257 2126 TSHSMEECEAL 2136
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
128-226 |
8.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.86 E-value: 8.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 128 DKAGGYAAQSEAISMATslgLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDA----DSIEWLRGYLK 203
Cdd:PRK13645 122 NKQEAYKKVPELLKLVQ---LPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPkgeeDFINLFERLNK 198
|
90 100
....*....|....*....|...
gi 489925987 204 KYEGGFLVISHSTELLDEVVNKV 226
Cdd:PRK13645 199 EYKKRIIMVTHNMDQVLRIADEV 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
14-194 |
9.71e-08 |
|
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: 52.86 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 14 ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLgyLPQDTHASDPTQTAL---DRMMSARD 90
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP--ISQYEHKYLHSKVSLvgqEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IATIInrirkAEKEMTDPDPDVMTKAmnrydkamqdfDKAGGYAAQSEaismaTSLGLPQEVMEQQlGTLSGGQRRRIEL 170
Cdd:cd03248 104 LQDNI-----AYGLQSCSFECVKEAA-----------QKAHAHSFISE-----LASGYDTEVGEKG-SQLSGGQKQRVAI 161
|
170 180
....*....|....*....|....
gi 489925987 171 ARILFSDADTLILDEPTNHLDADS 194
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAES 185
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
344-488 |
1.12e-07 |
|
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: 54.44 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGCK----------IGYFAQehDTLDLNATVLENLQ 412
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIdGQDIRdvtqaslraaIGIVPQ--DTVLFNDTIAYNIA 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 413 HVAPelDNTQARSIlgsflfsgdDAMKPAHV---------------------LSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:COG5265 454 YGRP--DASEEEVE---------AAARAAQIhdfieslpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEAT 522
|
170
....*....|....*..
gi 489925987 472 NNLDPASREEILKAIAK 488
Cdd:COG5265 523 SALDSRTERAIQAALRE 539
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
346-518 |
1.20e-07 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 53.88 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 346 NLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQ---------------EHDTLDLNATVLEN 410
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLI-DGVDIAKISDaelrevrrkkiamvfQSFALMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 411 ------LQHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR----E 480
Cdd:PRK10070 127 tafgmeLAGINAEERREKALDALRQVGLENYAHSYPDE-LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtemqD 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 481 EILKAIAKYEGAIVLVTHDEGAVEALNpERVLLMPDGD 518
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIG-DRIAIMQNGE 242
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
330-499 |
1.70e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.85 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIG-------YFAQEHDTL- 401
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-DGENIPamsrsrlYTVRKRMSMl 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 402 --------DLNatVLENL-------QHVAPELDNTQARSILGSFLFSGDDAMKPAHvLSGGEKTRLALATLVTSRANVLL 466
Cdd:PRK11831 90 fqsgalftDMN--VFDNVayplrehTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSE-LSGGMARRAALARAIALEPDLIM 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 467 LDEPTNNLDPASREEILKAIAKYEGAI----VLVTHD 499
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHD 203
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
351-512 |
1.71e-07 |
|
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: 50.83 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 351 KGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaqehdtldlnatvlenlqhVAPELDNTQARSILGSF 430
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY----------------------------IDGEDILEEVLDQLLLI 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 431 LFSGDDAMkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGA---------IVLVTHDEG 501
Cdd:smart00382 53 IVGGKKAS-----GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLllkseknltVILTTNDEK 127
|
170
....*....|.
gi 489925987 502 AVEALNPERVL 512
Cdd:smart00382 128 DLGPALLRRRF 138
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
33-249 |
1.71e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 53.32 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 33 LVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-KLG-YLPQDTHASDPTQTALDRMMSARDIATIINRIRKAEKEMTDPDP 110
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiYIGdKKNNHELITNPYSKKIKNFKELRRRVSMVFQFPEYQLFKDTIEK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 111 DVMTKAMNRYDKAMQDFDKAGGYAAQseaismatsLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHL 190
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKFYLNK---------MGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 191 D-ADSIEWLRGYL--KKYEGGFLVISHSTELLDEVVNKVWHLDAqlGQIDMYSLSWKAYLHQ 249
Cdd:PRK13631 208 DpKGEHEMMQLILdaKANNKTVFVITHTMEHVLEVADEVIVMDK--GKILKTGTPYEIFTDQ 267
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-214 |
1.86e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 52.22 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITgDMLPTAGKVRVSGKLGYLPQDTHASDptqtal 82
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFN-RLIELYPEARVSGEVYLDGQDIFKMD------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 drMMSARDIATIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMQDFDKAGGYAAQSEAI--SMATSLGLPQevmeqqlGTL 160
Cdd:PRK14247 77 --VIELRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLwdEVKDRLDAPA-------GKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADS---IEWLRGYLKKyEGGFLVISH 214
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-194 |
1.87e-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: 52.16 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDptqtaldr 84
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGvdirdlnlrwlrsQIGLVSQEPVLFD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 mmsardiATIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMqdfDKAGGYaaqseaismatslglpQEVMEQQLGTLSGGQ 164
Cdd:cd03249 91 -------GTIAENIRYGKPDATDEEVEEAAKKANIHDFIM---SLPDGY----------------DTLVGERGSQLSGGQ 144
|
170 180 190
....*....|....*....|....*....|
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:cd03249 145 KQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-215 |
1.95e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.54 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG--DMLPTA---GKVRVSGKLGYLPQdthaSD 76
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNIYSPD----VD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 77 PTQTaldrmmsaRDIATIINRIRKAEKEMTDPDPDVMTKAMNRYDKAMQDFDKAGGYAAQSEAismatslgLPQEV---M 153
Cdd:PRK14267 80 PIEV--------RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEWALKKAA--------LWDEVkdrL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 154 EQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWLRGYLKKyEGGFLVISHS 215
Cdd:PRK14267 144 NDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHS 207
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
327-532 |
2.49e-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: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTL----RLLA-----HIEEPDTGSVEYGHGCK-IGYF 394
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLStegeiQIDGVSWNSVTLQTWRKaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEhdTLDLNATVLENL----QHVAPEL----DNTQARSILGSFLFSGDDAMKPA-HVLSGGEKTRLALATLVTSRANVL 465
Cdd:TIGR01271 1298 PQK--VFIFSGTFRKNLdpyeQWSDEEIwkvaEEVGLKSVIEQFPDKLDFVLVDGgYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 466 LLDEPTNNLDPASReEILKAIAKYEGAIVLVTHDEGAVEALNPERVLLMPDGDEDLWNDSYLDLVAE 532
Cdd:TIGR01271 1376 LLDEPSAHLDPVTL-QIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-191 |
2.63e-07 |
|
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: 52.26 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQ-TALDR----M------- 85
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDG------QDIAAMSRKElRELRRkkisMvfqsfal 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 ---MSARDIATIINRIRKAEKEmtdpdpdvmtkamNRYDKAMQDFDKAG--GYAAQseaismatslgLPQEvmeqqlgtL 160
Cdd:cd03294 114 lphRTVLENVAFGLEVQGVPRA-------------EREERAAEALELVGleGWEHK-----------YPDE--------L 161
|
170 180 190
....*....|....*....|....*....|.
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:cd03294 162 SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
336-499 |
2.69e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 336 YGSNiVFAGVNLAIDKGSRVV-ILGYNGAGKTTTLRLLA---------HIEEPDTGSV-EYGHGCKIG-YFAqehDTLDL 403
Cdd:PRK13409 83 YGVN-GFKLYGLPIPKEGKVTgILGPNGIGKTTAVKILSgelipnlgdYEEEPSWDEVlKRFRGTELQnYFK---KLYNG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 NATVLENLQHV--APE---------LDNTQARSILGSFL--FSGDDAM-KPAHVLSGGEKTRLALATLVTSRANVLLLDE 469
Cdd:PRK13409 159 EIKVVHKPQYVdlIPKvfkgkvrelLKKVDERGKLDEVVerLGLENILdRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190
....*....|....*....|....*....|..
gi 489925987 470 PTNNLDPASREEILKAIAKY-EGAIVLVT-HD 499
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELaEGKYVLVVeHD 270
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
435-523 |
3.30e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.59 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 435 DDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA--KYEGAIVLVTHdegavealNPERVL 512
Cdd:PRK14246 145 DRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSH--------NPQQVA 216
|
90
....*....|.
gi 489925987 513 LMPDGDEDLWN 523
Cdd:PRK14246 217 RVADYVAFLYN 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-221 |
3.53e-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: 53.38 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITgDMLPTAGKVRVSG-------------KLGYLPQDTHASDPT- 78
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGvswnsvtlqtwrkAFGVIPQKVFIFSGTf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 QTALD--RMMSARDIATIINRIrkAEKEMTDPDPDvmtkamnRYDKAMQDfdkaGGYaaqseaismatslglpqevmeqq 156
Cdd:TIGR01271 1309 RKNLDpyEQWSDEEIWKVAEEV--GLKSVIEQFPD-------KLDFVLVD----GGY----------------------- 1352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 157 lgTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVI--SHSTELLDE 221
Cdd:TIGR01271 1353 --VLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIlsEHRVEALLE 1417
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-193 |
3.54e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTqtalDRMMSARDIA 92
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE-----------DVT----HRSIQQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIInrirkaEKEMTDPDpdvMTKAMN-RYDKAMQDFDKAGGYAAQSEAISMATSLGLPQEVMEQqlgtLSGGQRRRIELA 171
Cdd:PRK11432 82 MVF------QSYALFPH---MSLGENvGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQ----ISGGQQQRVALA 148
|
170 180
....*....|....*....|..
gi 489925987 172 RILFSDADTLILDEPTNHLDAD 193
Cdd:PRK11432 149 RALILKPKVLLFDEPLSNLDAN 170
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-191 |
3.57e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.92 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-------------KLGYLPQDTHASDPTQTALDrmmsa 88
Cdd:PRK13632 29 SFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiskenlkeirkKIGIIFQNPDNQFIGATVED----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 89 rDIATIINRIRKAEKEMTDPDPDVMTKAmnrydkAMQDF-DKAggyaaqseaismatslglPQEvmeqqlgtLSGGQRRR 167
Cdd:PRK13632 104 -DIAFGLENKKVPPKKMKDIIDDLAKKV------GMEDYlDKE------------------PQN--------LSGGQKQR 150
|
170 180
....*....|....*....|....
gi 489925987 168 IELARILFSDADTLILDEPTNHLD 191
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLD 174
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
33-222 |
4.31e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 51.93 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 33 LVGRNGAGKTTLTRVITGdMLPTAGKVRVSGKLGYLPQDTHASDPT---------QTALDRMMSARDIATIINRIRKAEK 103
Cdd:COG3593 28 LVGENNSGKSSILEALRL-LLGPSSSRKFDEEDFYLGDDPDLPEIEieltfgsllSRLLRLLLKEEDKEELEEALEELNE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 104 EMtDPDPDVMTKAMNRYDKAMQDFDKAGGYAAQSEAISMATSLGL----PQEVMEQQLGTlsgGQRRRI------ELARI 173
Cdd:COG3593 107 EL-KEALKALNELLSEYLKELLDGLDLELELSLDELEDLLKSLSLriedGKELPLDRLGS---GFQRLIllallsALAEL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 174 LFSDADTLIL-DEPTNHLDADSIEWLRGYLKKYEGG---FLVISHSTELLDEV 222
Cdd:COG3593 183 KRAPANPILLiEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEV 235
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
18-191 |
4.36e-07 |
|
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: 50.79 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLgylPQDTHASDPTQTALDRMMSARDIATIINR 97
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN---ESEPSFEATRSRNRYSVAYAAQKPWLLNA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 irKAEKEMTDPDPdvmtkamnrydkamqdFDKAGgYAAQSEAISMATSLGLPQEVMEQQLG----TLSGGQRRRIELARI 173
Cdd:cd03290 94 --TVEENITFGSP----------------FNKQR-YKAVTDACSLQPDIDLLPFGDQTEIGergiNLSGGQRQRICVARA 154
|
170
....*....|....*...
gi 489925987 174 LFSDADTLILDEPTNHLD 191
Cdd:cd03290 155 LYQNTNIVFLDDPFSALD 172
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
327-517 |
5.00e-07 |
|
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: 51.39 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 327 IMAKDISKAY--GSNIVFAGVNLAIDKGSRVVILGYNGAGKTTT----LRLLA-----HIEEPDTGSVEYGHGCK-IGYF 394
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNtegdiQIDGVSWNSVPLQKWRKaFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 395 AQEhdTLDLNATVLENL----QHVAPEL----DNTQARSILGSFLFSGDDAMKPA-HVLSGGEKTRLALATLVTSRANVL 465
Cdd:cd03289 83 PQK--VFIFSGTFRKNLdpygKWSDEEIwkvaEEVGLKSVIEQFPGQLDFVLVDGgCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489925987 466 LLDEPTNNLDPASReEILKAIAKYEGAIVLVTHDEGAVEA-LNPERVLLMPDG 517
Cdd:cd03289 161 LLDEPSAHLDPITY-QVIRKTLKQAFADCTVILSEHRIEAmLECQRFLVIEEN 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-191 |
5.25e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.34 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTA---GKVRVSGKlgYLPQDThasdptqtaldrMMSARDI 91
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGI--TLTAKT------------VWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ATIInrirkaekeMTDPDpdvmtkamNRYDKAMQDFDKAGGYaaQSEAISMATSLGLPQEVMEQ---------QLGTLSG 162
Cdd:PRK13640 86 VGIV---------FQNPD--------NQFVGATVGDDVAFGL--ENRAVPRPEMIKIVRDVLADvgmldyidsEPANLSG 146
|
170 180
....*....|....*....|....*....
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
22-186 |
5.57e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 50.52 E-value: 5.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQtaldRMMS-------------- 87
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG------QDLTALPPAE----RPVSmlfqennlfphltv 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 88 ARDIATIInrirkaekemtdpDPDVmtkamnRYDkamqdfdkaggyAAQSEAIS-MATSLGLpqEVMEQQL-GTLSGGQR 165
Cdd:COG3840 89 AQNIGLGL-------------RPGL------KLT------------AEQRAQVEqALERVGL--AGLLDRLpGQLSGGQR 135
|
170 180
....*....|....*....|.
gi 489925987 166 RRIELARILFSDADTLILDEP 186
Cdd:COG3840 136 QRVALARCLVRKRPILLLDEP 156
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-191 |
6.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.17 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLE--IQIG---ARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSgklgylpqdthas 75
Cdd:PRK13634 1 MDITFQKVEhrYQYKtpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 76 dptqtalDRMMSARDIATIINRIRK--------AEKEMTDP--DPDVMTKAMNRydkAMQDFDkaggyaAQSEAISMATS 145
Cdd:PRK13634 68 -------ERVITAGKKNKKLKPLRKkvgivfqfPEHQLFEEtvEKDICFGPMNF---GVSEED------AKQKAREMIEL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489925987 146 LGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK13634 132 VGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-229 |
7.04e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 50.82 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 8 LEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHAsdptqtaLDRMMS 87
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQ-------IDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 88 ARDIATIINRirkaekemtdPDPdvmTKAMNRYDKAMQDFDKAGGYAAQSEAISMATSL---GLPQEV---MEQQLGTLS 161
Cdd:PRK14246 89 RKEVGMVFQQ----------PNP---FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLrkvGLWKEVydrLNSPASQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLD---ADSIEWLRGYLKKyEGGFLVISHSTELLDEVVNKVWHL 229
Cdd:PRK14246 156 GGQQQRLTIARALALKPKVLLMDEPTSMIDivnSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFL 225
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
444-517 |
7.14e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 51.39 E-value: 7.14e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 444 LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI--AKYEGAIVLV-THDEGAVEALNPErVLLMPDG 517
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldAKANNKTVFViTHTMEHVLEVADE-VIVMDKG 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
3-192 |
7.62e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQiGARTLLHPTNFHVAKGDKIGLVGRNGAGKTtLTRVITGDMLP-----TAGKVRVSGKlGYLPQDthasdp 77
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS-LTCAAALGILPagvrqTAGRVLLDGK-PVAPCA------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 78 tqtaldrmMSARDIATIINRIRKAekemTDPdpdVMTKAmnryDKAMQDFDKAGGYAAQSEAISMATSLGL--PQEVMEQ 155
Cdd:PRK10418 76 --------LRGRKIATIMQNPRSA----FNP---LHTMH----THARETCLALGKPADDATLTAALEAVGLenAARVLKL 136
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 156 QLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:PRK10418 137 YPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
336-499 |
8.38e-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: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 336 YGSNiVFAGVNLAIDKGSRVV-ILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCK--IGYFA----QEH--DTLDLNAT 406
Cdd:COG1245 83 YGEN-GFRLYGLPVPKKGKVTgILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDevLKRFRgtelQDYfkKLANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 407 VLENLQHV--APE---------LDNTQARSILGSF--LFSGDDAM-KPAHVLSGGEKTRLALATLVTSRANVLLLDEPTN 472
Cdd:COG1245 162 VAHKPQYVdlIPKvfkgtvrelLEKVDERGKLDELaeKLGLENILdRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180 190
....*....|....*....|....*....|
gi 489925987 473 NLDPASREEILKAI---AKYEGAIVLVTHD 499
Cdd:COG1245 242 YLDIYQRLNVARLIrelAEEGKYVLVVEHD 271
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-518 |
9.67e-07 |
|
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: 51.22 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPtAGKVRVSGKLGYLPQD-THASDPTQTALdRmmsARDI 91
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILR-LLP-DPAAHPSGSILFDGQDlLGLSERELRRI-R---GNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 92 ATIInrirkaeKE-MTDPDPdVMT------------KAMNRYdkamqdfdkaggyAAQSEAISMATSLGLPQEvmEQQLG 158
Cdd:COG4172 95 AMIF-------QEpMTSLNP-LHTigkqiaevlrlhRGLSGA-------------AARARALELLERVGIPDP--ERRLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 159 T----LSGGQRRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGyLKKYEG-GFLVISHstellD-EVVNKVwh 228
Cdd:COG4172 152 AyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDvtvqAQILDLLKD-LQRELGmALLLITH-----DlGVVRRF-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 229 ldaqlgqidmyslswkaylhqrvvdeerrrrerevaekkAERL--MKQGirlhakaskAVAAQNmmrRAEKLLENTSEA- 305
Cdd:COG4172 224 ---------------------------------------ADRVavMRQG---------EIVEQG---PTAELFAAPQHPy 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 306 -QK---AEKVADirfPEPAPCGRTPIM-AKDISKAY---------GSNIVFA--GVNLAIDKGSRVVILGYNGAGKTTT- 368
Cdd:COG4172 253 tRKllaAEPRGD---PRPVPPDAPPLLeARDLKVWFpikrglfrrTVGHVKAvdGVSLTLRRGETLGLVGESGSGKSTLg 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 369 ---LRLLAHieepdTGSVEYGHgckigyfaQEHDTLD---------------------LN------ATVLENLQHVAPEL 418
Cdd:COG4172 330 lalLRLIPS-----EGEIRFDG--------QDLDGLSrralrplrrrmqvvfqdpfgsLSprmtvgQIIAEGLRVHGPGL 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 419 DNTQ----ARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEI---LKAI-AKYE 490
Cdd:COG4172 397 SAAErrarVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQIldlLRDLqREHG 476
|
570 580
....*....|....*....|....*...
gi 489925987 491 GAIVLVTHDEGAVEALNpERVLLMPDGD 518
Cdd:COG4172 477 LAYLFISHDLAVVRALA-HRVMVMKDGK 503
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-222 |
9.78e-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: 50.88 E-value: 9.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 32 GLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG-----------------KLGYLPQDthasdptqtaldrmmsardiATI 94
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrkgiflppekrRIGYVFQE--------------------ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 95 InrirkaekemtdpdPDVMTKAMNRYdkAMQDFDKAGGYAAQSEAISMatsLGLpQEVMEQQLGTLSGGQRRRIELARIL 174
Cdd:TIGR02142 87 F--------------PHLSVRGNLRY--GMKRARPSERRISFERVIEL---LGI-GHLLGRLPGRLSGGEKQRVAIGRAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 175 FSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGF----LVISHStelLDEV 222
Cdd:TIGR02142 147 LSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFgipiLYVSHS---LQEV 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
341-485 |
9.80e-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: 51.83 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEygHGCKIGYFAQEhdTLDLNATVLENLQhVAPELDN 420
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQT--SWIMPGTIKDNII-FGLSYDE 515
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 421 TQARSILGSFLFSGDDAMKPAH----------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKA 485
Cdd:TIGR01271 516 YRYTSVIKACQLEEDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
352-517 |
1.04e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 352 GSRVVILGYNGAGKTTTLRLLAHIEEPDT---GSVEYgHGCKIGY--------FAQEHDTLDLNATVLENLQHVA----- 415
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLL-NGMPIDAkemraisaYVQQDDLFIPTLTVREHLMFQAhlrmp 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 416 PELDNTQARSILGSFLfsgdDAM---KPAH----------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE- 481
Cdd:TIGR00955 130 RRVTKKEKRERVDEVL----QALglrKCANtrigvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSv 205
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 482 --ILKAIAKYEGAIVLVTHDEGAVEALNPERVLLMPDG 517
Cdd:TIGR00955 206 vqVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEG 243
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-191 |
1.14e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.13 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVsgklGYLPQDTHASDPTQTA 81
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV----GDITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 LDRMMSaRDIATIINRI-----RKA-EKEMTDPdpdVMTKAMNRydkamqdfdkaggyaaqSEAISMATSL----GL--- 148
Cdd:PRK11264 79 LIRQLR-QHVGFVFQNFnlfphRTVlENIIEGP---VIVKGEPK-----------------EEATARARELlakvGLagk 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925987 149 ----PQEvmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK11264 138 etsyPRR--------LSGGQQQRVAIARALAMRPEVILFDEPTSALD 176
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
330-517 |
1.16e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAhieepdtgsveyGHGckiGYFAQEHDTLDLNATVLE 409
Cdd:CHL00131 11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA------------GHP---AYKILEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 nlqhVAPEldntqARSILGSFL--------------------------FSGDDAMKP-----------------AHVL-- 444
Cdd:CHL00131 76 ----LEPE-----ERAHLGIFLafqypieipgvsnadflrlaynskrkFQGLPELDPlefleiineklklvgmdPSFLsr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 445 ------SGGEKTR---LALATLVTSRAnvlLLDEPTNNLDPASREEILKAIAKY---EGAIVLVTHDEGAVEALNPERVL 512
Cdd:CHL00131 147 nvnegfSGGEKKRneiLQMALLDSELA---ILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDYVH 223
|
....*
gi 489925987 513 LMPDG 517
Cdd:CHL00131 224 VMQNG 228
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
283-517 |
1.17e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 283 SKAVAAQNMMRRAEKLLentseaqkaekVADIRFPEPAPCGRTPIMAKDISKAYGS------NIVFAGVNLAIDKGSRVV 356
Cdd:PLN03232 579 SQVVNANVSLQRIEELL-----------LSEERILAQNPPLQPGAPAISIKNGYFSwdsktsKPTLSDINLEIPVGSLVA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLR-LLAHIEEPDTGSVEYgHGcKIGYFAQEhdTLDLNATVLENL---QHVAPE-----LDNTQARSIL 427
Cdd:PLN03232 648 IVGGTGEGKTSLISaMLGELSHAETSSVVI-RG-SVAYVPQV--SWIFNATVRENIlfgSDFESErywraIDVTALQHDL 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 428 GsfLFSGDDAMKPAHV---LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYE---GAIVLVTHDEG 501
Cdd:PLN03232 724 D--LLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElkgKTRVLVTNQLH 801
|
250
....*....|....*.
gi 489925987 502 AVEALnpERVLLMPDG 517
Cdd:PLN03232 802 FLPLM--DRIILVSEG 815
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
330-506 |
1.21e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.88 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHGCKIGY-----------FAQEH 398
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqtakimreavaIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 399 DTLDLNATVLENLQHVAPELDNTQ----ARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNL 474
Cdd:PRK11614 89 RRVFSRMTVEENLAMGGFFAERDQfqerIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 475 DPASREEILKAIAKY--EG-AIVLVthDEGAVEAL 506
Cdd:PRK11614 169 APIIIQQIFDTIEQLreQGmTIFLV--EQNANQAL 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-191 |
1.26e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 51.25 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVsgklgylpqdtHASDPTQTALDRMMSARDIA-- 92
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF-----------HDIPLTKLQLDSWRSRLAVVsq 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 -------TIINRIrkaekemtdpdpdvmtkAMNRYDKAMQDFDKAGGYAAQSEAIsmatsLGLPQ----EVMEQQLgTLS 161
Cdd:PRK10789 397 tpflfsdTVANNI-----------------ALGRPDATQQEIEHVARLASVHDDI-----LRLPQgydtEVGERGV-MLS 453
|
170 180 190
....*....|....*....|....*....|
gi 489925987 162 GGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK10789 454 GGQKQRISIARALLLNAEILILDDALSAVD 483
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-517 |
1.27e-06 |
|
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: 50.98 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGkvrVSGKLGYLPQDTHASDPTQTAL 82
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGT---WDGEIYWSGSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMMSARDIATIINRIRKAEK-----EMTDPDPDVMTKAMNRYDKAMqdfdkaggyaaqseaismATSLGLPQEVMEQQL 157
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENiflgnEITLPGGRMAYNAMYLRAKNL------------------LRELQLDADNVTRPV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 158 GTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGY---LKKYEGGFLVISHSTELLDEVVNKVWHL-DAQ- 232
Cdd:TIGR02633 140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIrDGQh 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 233 LGQIDMYSLSWKAYLHQRVVDEERRRREREVAEKKAERLMKQGIRLHAKASKAVAAQN----MMRRAEKL-LENTSEAQK 307
Cdd:TIGR02633 220 VATKDMSTMSEDDIITMMVGREITSLYPHEPHEIGDVILEARNLTCWDVINPHRKRVDdvsfSLRRGEILgVAGLVGAGR 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 308 AEKVADIRFPEPAPC-GRTPIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIeepdtgsveyg 386
Cdd:TIGR02633 300 TELVQALFGAYPGKFeGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKNITLSVLKSF----------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 387 hgCKIGYF--AQEHDTLDLNATVLEnLQHVAPELdntqarsilgsflfsgddamkPAHVLSGGEKTRLALATLVTSRANV 464
Cdd:TIGR02633 369 --CFKMRIdaAAELQIIGSAIQRLK-VKTASPFL---------------------PIGRLSGGNQQKAVLAKMLLTNPRV 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 465 LLLDEPTNNLDPASREEILK---AIAKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKlinQLAQEGVAIIVVSSELAEVLGLS-DRVLVIGEG 479
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-222 |
1.40e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LGYLPQDTHAsdpTQT 80
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYIPEDRLG---RGL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDrmMSARD--IATIINRIRKAEKEMTDPdpdvmtKAMNRY-DKAMQDFD-KAGGYaaqseaismatslglpqevmEQQ 156
Cdd:COG3845 348 VPD--MSVAEnlILGRYRRPPFSRGGFLDR------KAIRAFaEELIEEFDvRTPGP--------------------DTP 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 157 LGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY--EG-GFLVIShstELLDEV 222
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELrdAGaAVLLIS---EDLDEI 465
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-191 |
1.45e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.71 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVI-------TGDML--------PTAGKVRVSGKLGY 67
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLIvdglkvndPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 68 LPQDTHASdPTQTALDRMMSARdiatiiNRIRKAEKEmtdpdpdvmtkamnrydkamqdfdkaggyAAQSEAISMATSLG 147
Cdd:PRK09493 82 VFQQFYLF-PHLTALENVMFGP------LRVRGASKE-----------------------------EAEKQARELLAKVG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 148 LpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK09493 126 L-AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-187 |
1.47e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 51.28 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptqtA 81
Cdd:NF033858 266 AIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ----------------P 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 LDrmmsARDIATiinRIRkaekemtdpdpdV--MTKAMNRYDK--AMQDFD-----------KAGGYAAQseaisMATSL 146
Cdd:NF033858 330 VD----AGDIAT---RRR------------VgyMSQAFSLYGEltVRQNLElharlfhlpaaEIAARVAE-----MLERF 385
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 147 GLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPT 187
Cdd:NF033858 386 DL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
328-505 |
2.09e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 328 MA----KDISKAYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVE------------------ 384
Cdd:PRK11650 1 MAglklQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWiggrvvnelepadrdiam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 385 -------YGH---------GCKIGYFAQEHdtldlnatVLENLQHVAPELDntqarsiLGSFLfsgddAMKPAHvLSGGE 448
Cdd:PRK11650 81 vfqnyalYPHmsvrenmayGLKIRGMPKAE--------IEERVAEAARILE-------LEPLL-----DRKPRE-LSGGQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489925987 449 KTRLALAtlvtsRA-----NVLLLDEPTNNLDP----ASREEI------LKAIAKYegaivlVTHDEgaVEA 505
Cdd:PRK11650 140 RQRVAMG-----RAivrepAVFLFDEPLSNLDAklrvQMRLEIqrlhrrLKTTSLY------VTHDQ--VEA 198
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-191 |
2.28e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 49.26 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITgDMLPTAGKVRVSGKLGYLPQDTHasdptqta 81
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVEFFNQNIY-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 lDRMMSardiatiINRIRKaEKEMTDPDPDVMtkAMNRYDKAMQDFdKAGGYAAQSE-------AISMATSLGLPQEVME 154
Cdd:PRK14258 78 -ERRVN-------LNRLRR-QVSMVHPKPNLF--PMSVYDNVAYGV-KIVGWRPKLEiddivesALKDADLWDEIKHKIH 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 155 QQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK14258 146 KSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
442-518 |
2.29e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 442 HVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA----KYEGAIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlqkEMSMGVIFITHDMGVVAEI-ADRVLVMYQG 245
|
.
gi 489925987 518 D 518
Cdd:PRK10261 246 E 246
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
335-498 |
2.36e-06 |
|
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: 48.48 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 335 AYGSNI-VFAGVNLAIDKGSRVVILGYNGAGKTTTLrlLAHIEEPDT--GSVEYGHGCKIGYFAQEHDTLD--------- 402
Cdd:cd03290 9 SWGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLL--LAILGEMQTleGKVHWSNKNESEPSFEATRSRNrysvayaaq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 403 ----LNATVLENLQHVAPeLDNTQARSILGSFLFSGDDAMKP----------AHVLSGGEKTRLALATLVTSRANVLLLD 468
Cdd:cd03290 87 kpwlLNATVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 469 EPTNNL-----DPASREEILKAIAKYEGAIVLVTH 498
Cdd:cd03290 166 DPFSALdihlsDHLMQEGILKFLQDDKRTLVLVTH 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
13-191 |
2.46e-06 |
|
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: 50.20 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDThaSDPTQTALDRM--MSARD 90
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG------QDI--RDVTQASLRAAigIVPQD 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 IA----TIINRIRKAEKEMTDPDpdVMTkamnrydkamqdfdkaggyAAQSEAISmATSLGLPQ----EVMEQQLgTLSG 162
Cdd:COG5265 441 TVlfndTIAYNIAYGRPDASEEE--VEA-------------------AARAAQIH-DFIESLPDgydtRVGERGL-KLSG 497
|
170 180
....*....|....*....|....*....
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
23-191 |
2.61e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 48.96 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthasdptqtaldRMMSARDIATIINRIrkae 102
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMG--------------------REVNAENEKWVRSKV---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 103 kEMTDPDPDVMTKAMNRYDkamqdfDKAGGyaaqseaismATSLGLPQEVMEQQLGT-----------------LSGGQR 165
Cdd:PRK13647 82 -GLVFQDPDDQVFSSTVWD------DVAFG----------PVNMGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQK 144
|
170 180
....*....|....*....|....*.
gi 489925987 166 RRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK13647 145 KRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
330-486 |
2.66e-06 |
|
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: 48.64 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNI--VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEY-GHGC----------KIGYFAQ 396
Cdd:cd03244 6 KNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDIskiglhdlrsRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 397 ehDTLDLNATVLENL----QHVAPELDNTQARSILGSFLFSGDDAMkPAHV------LSGGEKTRLALATLVTSRANVLL 466
Cdd:cd03244 86 --DPVLFSGTIRSNLdpfgEYSDEELWQALERVGLKEFVESLPGGL-DTVVeeggenLSVGQRQLLCLARALLRKSKILV 162
|
170 180
....*....|....*....|
gi 489925987 467 LDEPTNNLDPASREEILKAI 486
Cdd:cd03244 163 LDEATASVDPETDALIQKTI 182
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-186 |
2.84e-06 |
|
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: 49.33 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQgLEIQIGARTLlhPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK---------------- 64
Cdd:COG4148 1 MMLEVD-FRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsargiflpphrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 65 -LGYLPQDT----HasdptqtaldrmMSARDiatiinrirkaekemtdpdpdvmtkamN-RYdkAMQDFDKAGGYAAQSE 138
Cdd:COG4148 78 rIGYVFQEArlfpH------------LSVRG---------------------------NlLY--GRKRAPRAERRISFDE 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489925987 139 AISMatsLGLpQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEP 186
Cdd:COG4148 117 VVEL---LGI-GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-194 |
3.19e-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: 48.18 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGAR--TLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasdptqt 80
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 aldrmmsarDIATI-INRIRKAekeMT--DPDPDVMTKA----MNRYDKamqdFDKAGGYAAQSeaismATSLGLpqevm 153
Cdd:cd03369 71 ---------DISTIpLEDLRSS---LTiiPQDPTLFSGTirsnLDPFDE----YSDEEIYGALR-----VSEGGL----- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489925987 154 eqqlgTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:cd03369 125 -----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-217 |
3.22e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 48.54 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------LGYLPQDtH 73
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaeRGVVFQN-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 74 ASDPTQTALDRMMSARDIATIinriRKAEKEMTdpdpdvmtkamnrydkamqdfdkaggyaaqseAISMATSLGLpQEVM 153
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGV----EKMQRLEI--------------------------------AHQMLKKVGL-EGAE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 154 EQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKK--YEGG--FLVISHSTE 217
Cdd:PRK11248 123 KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGkqVLLITHDIE 190
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
344-497 |
3.53e-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: 47.62 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAhiEEPDTGSVE-----YGHGCKIGY-----FAQEHDTLDLNATVLEnlqh 413
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVITgeiliNGRPLDKNFqrstgYVEQQDVHSPNLTVRE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 414 vapeldntqarSILGSFLFSGddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EG 491
Cdd:cd03232 99 -----------ALRFSALLRG---------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLadSG 158
|
....*.
gi 489925987 492 AIVLVT 497
Cdd:cd03232 159 QAILCT 164
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-191 |
3.69e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.24 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 25 VAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRmmsARDIATIINRIrkaeke 104
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVG------QPLHQMDEEARAKLR---AKHVGFVFQSF------ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 105 MTDPD----PDVMTKAMNRYDKAMQdfdkaggyaAQSEAISMATSLGLPQEV--MEQQLgtlSGGQRRRIELARILFSDA 178
Cdd:PRK10584 98 MLIPTlnalENVELPALLRGESSRQ---------SRNGAKALLEQLGLGKRLdhLPAQL---SGGEQQRVALARAFNGRP 165
|
170
....*....|...
gi 489925987 179 DTLILDEPTNHLD 191
Cdd:PRK10584 166 DVLFADEPTGNLD 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
343-486 |
4.00e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 343 AGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQE----------HDTLDLNATVLENLQ 412
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGTDIRTVTRAslrrniavvfQDAGLFNRSIEDNIR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 413 HVAP-----ELDNTQARSILGSFLFSGDDAMKpAHV------LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREE 481
Cdd:PRK13657 431 VGRPdatdeEMRAAAERAQAHDFIERKPDGYD-TVVgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAK 509
|
....*
gi 489925987 482 ILKAI 486
Cdd:PRK13657 510 VKAAL 514
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
357-499 |
4.31e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 48.25 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLRLLAHIEEPDTGSVEyghgckigyfaqehdtldLNATVLENLQHVA------------PELDNTQAR 424
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEIL------------------LDAQPLESWSSKAfarkvaylpqqlPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 425 SI--LGSFLFSG-------------DDA-----MKP-AH----VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASR 479
Cdd:PRK10575 104 ELvaIGRYPWHGalgrfgaadrekvEEAislvgLKPlAHrlvdSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180
....*....|....*....|....
gi 489925987 480 EEILKAI---AKYEGAIVL-VTHD 499
Cdd:PRK10575 184 VDVLALVhrlSQERGLTVIaVLHD 207
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
22-198 |
4.78e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 4.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVS--------------GKLGYLPQDTHA-SDPTQTALD-RM 85
Cdd:PTZ00265 405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlkdinlkwwrSKIGVVSQDPLLfSNSIKNNIKySL 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 86 MSARDIATIINRIRK---AEKEMTDPDPDVMTKAMNRYDKAMQDFDKAGGYAAQ--------SEAISMATSL-------G 147
Cdd:PTZ00265 485 YSLKDLEALSNYYNEdgnDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRknyqtikdSEVVDVSKKVlihdfvsA 564
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 148 LPQEvMEQQLGT----LSGGQRRRIELARILFSDADTLILDEPTNHLDADSiEWL 198
Cdd:PTZ00265 565 LPDK-YETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYL 617
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
11-192 |
5.32e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 11 QIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDthasdptqtaldrmmsard 90
Cdd:PTZ00243 669 ELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQ------------------- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 iATIINRIRKAEKEMTDP-DPDVMTKAMNrydkamqdfdkaggyAAQSEAISMATSLGLPQEVMEQQLgTLSGGQRRRIE 169
Cdd:PTZ00243 730 -AWIMNATVRGNILFFDEeDAARLADAVR---------------VSQLEADLAQLGGGLETEIGEKGV-NLSGGQKARVS 792
|
170 180
....*....|....*....|...
gi 489925987 170 LARILFSDADTLILDEPTNHLDA 192
Cdd:PTZ00243 793 LARAVYANRDVYLLDDPLSALDA 815
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-237 |
6.81e-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: 48.98 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVItGDMLPTAGKVRV---SGKLGYLPQDTHASDPTqtaldrmmsARDiaTIInri 98
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRLTkpaKGKLFYVPQRPYMTLGT---------LRD--QII--- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 99 rkaekemtdpdpdvmtkamnrYDKAMQDFDKAGGYAAQSEAISMATSLG--LPQEV----MEQQLGTLSGGQRRRIELAR 172
Cdd:TIGR00954 537 ---------------------YPDSSEDMKRRGLSDKDLEQILDNVQLThiLEREGgwsaVQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 173 ILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTELldevvnkvWHLDAQLGQID 237
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSHRKSL--------WKYHEYLLYMD 652
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
412-499 |
7.04e-06 |
|
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: 48.15 E-value: 7.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 QHVAPELDNTQARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRAN---VLLLDEPTNNLDPASREEILKAI-- 486
Cdd:pfam13304 205 GIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLke 284
|
90
....*....|....
gi 489925987 487 -AKYEGAIVLVTHD 499
Cdd:pfam13304 285 lSRNGAQLILTTHS 298
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
344-532 |
7.43e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaQEHDTLDLNATVLENL----QHV----- 414
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY----------QGQDLLKADPEAQKLLrqkiQIVfqnpy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 415 --------------APELDNT---------QARSILGSFLFSGDDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:PRK11308 103 gslnprkkvgqileEPLLINTslsaaerreKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 472 NNLDPASREEILKAIA----KYEGAIVLVTHDEGAVEALNPErVLLMpdgdedlwndsYLDLVAE 532
Cdd:PRK11308 183 SALDVSVQAQVLNLMMdlqqELGLSYVFISHDLSVVEHIADE-VMVM-----------YLGRCVE 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-498 |
7.49e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYGHgcKIGYFAQEhdTLDLNATVLENLQHVAPELDNTQAR 424
Cdd:PTZ00243 679 VSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER--SIAYVPQQ--AWIMNATVRGNILFFDEEDAARLAD 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 425 SILGSFLfSGDDAMKPAHV----------LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIakYEGAI- 493
Cdd:PTZ00243 755 AVRVSQL-EADLAQLGGGLeteigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEEC--FLGALa 831
|
....*....
gi 489925987 494 ----VLVTH 498
Cdd:PTZ00243 832 gktrVLATH 840
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-236 |
8.16e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.78 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthasdptqtalDRMMSardiATIINR 97
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG-------------------ELLTA----ENVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 IRKAEKEMTDPDpdvmtkamNRYDKAMQDFDKAGGYAAQ----SEAISMATSLGLPQEVME---QQLGTLSGGQRRRIEL 170
Cdd:PRK13642 80 RRKIGMVFQNPD--------NQFVGATVEDDVAFGMENQgiprEEMIKRVDEALLAVNMLDfktREPARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 171 ARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHStelLDEVVNKVWHLDAQLGQI 236
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAASSDRILVMKAGEI 218
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-191 |
8.41e-06 |
|
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: 47.87 E-value: 8.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 33 LVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqdthasDPTQTALDRmmsaRDIATIInrirkaEKEMTDPDpdv 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE-----------DVTNVPPHL----RHINMVF------QSYALFPH--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 113 MTKAMN-RYDKAMQDFDKAGGYAAQSEAISMATSLGLPQEVMEQqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:TIGR01187 57 MTVEENvAFGLKMRKVPRAEIKPRVLEALRLVQLEEFADRKPHQ----LSGGQQQRVALARALVFKPKILLLDEPLSALD 132
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-191 |
8.51e-06 |
|
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: 47.36 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 28 GDKIGLVGRNGAGKTTLTRVITGDMLPTAGKvrvsgklgylpqdtHASDPtqtaldrmmsarDIATIINRIRKAE----- 102
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------------FDDPP------------DWDEILDEFRGSElqnyf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 103 KEMTDPDPDVMTKAMNrYD--------KAMQDFDKAGGYAAQSEAISmatSLGLPQeVMEQQLGTLSGGQRRRIELARIL 174
Cdd:cd03236 80 TKLLEGDVKVIVKPQY-VDlipkavkgKVGELLKKKDERGKLDELVD---QLELRH-VLDRNIDQLSGGELQRVAIAAAL 154
|
170
....*....|....*..
gi 489925987 175 FSDADTLILDEPTNHLD 191
Cdd:cd03236 155 ARDADFYFFDEPSSYLD 171
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
28-212 |
9.48e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.57 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 28 GDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpQDTHASDPTQTALDRmmsaRDIATIInrirkaekemtd 107
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG------QDVATLDADALAQLR----REHFGFI------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 108 pdpdvmtkaMNRYD-----KAMQDFDKAGGYAA------QSEAISMATSLGLPQEVmEQQLGTLSGGQRRRIELARILFS 176
Cdd:PRK10535 92 ---------FQRYHllshlTAAQNVEVPAVYAGlerkqrLLRAQELLQRLGLEDRV-EYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 489925987 177 DADTLILDEPTNHLDADSIEWLRGYLKKY-EGGFLVI 212
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVI 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-192 |
1.40e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPT-AGKVRVSGKLGYLPQdthasdptqtaldrmmsardIATIIN 96
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVVIRGSVAYVPQ--------------------VSWIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 97 -RIRKAEKEMTDPDPDVMTKAMNRydKAMQ-DFDKAGGYAAQseaismatslglpqEVMEQQLgTLSGGQRRRIELARIL 174
Cdd:PLN03232 693 aTVRENILFGSDFESERYWRAIDV--TALQhDLDLLPGRDLT--------------EIGERGV-NISGGQKQRVSMARAV 755
|
170
....*....|....*...
gi 489925987 175 FSDADTLILDEPTNHLDA 192
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDA 773
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
344-517 |
1.44e-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: 48.02 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 344 GVNLAIDKGSRVVILGYNGAGKTTTLR-LLAHIEEPDTGSVEYGhgcKIGYFAQEhdTLDLNATVLENLQHVAPeLDNTQ 422
Cdd:TIGR00957 656 GITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEGHVHMKG---SVAYVPQQ--AWIQNDSLRENILFGKA-LNEKY 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 423 ARSILGSFLFSGDDAMKPAH----------VLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGA 492
Cdd:TIGR00957 730 YQQVLEACALLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGV 809
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489925987 493 I-----VLVTH--------------DEGAVEALNPERVLLMPDG 517
Cdd:TIGR00957 810 LknktrILVTHgisylpqvdviivmSGGKISEMGSYQELLQRDG 853
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-222 |
1.52e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 47.62 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTA---GKVRVSGKlgylpqdthasdPTQ 79
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGE------------ELQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 TALDRMMSARDIAtIINRIRKAEKEMTDPDPDVMTKAMNRYdkAMQDFDkaggyAAQSEAISMATSLGLPQEVmEQQLGT 159
Cdd:PRK13549 73 ASNIRDTERAGIA-IIHQELALVKELSVLENIFLGNEITPG--GIMDYD-----AMYLRAQKLLAQLKLDINP-ATPVGN 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLK--KYEGGFLV-ISHStelLDEV 222
Cdd:PRK13549 144 LGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRdlKAHGIACIyISHK---LNEV 206
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
22-187 |
1.71e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 46.26 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGklgylpqdthasdptqTALDRMMSARdiatiINRI--- 98
Cdd:COG4674 30 SLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG----------------TDLTGLDEHE-----IARLgig 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 99 RKAEKemtdpdPDV---------MTKAMNRyDKAMQDFDKAGGYAAQSEAI-SMATSLGLpQEVMEQQLGTLSGGQRRRI 168
Cdd:COG4674 89 RKFQK------PTVfeeltvfenLELALKG-DRGVFASLFARLTAEERDRIeEVLETIGL-TDKADRLAGLLSHGQKQWL 160
|
170
....*....|....*....
gi 489925987 169 ELARILFSDADTLILDEPT 187
Cdd:COG4674 161 EIGMLLAQDPKLLLLDEPV 179
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-231 |
1.74e-05 |
|
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: 46.77 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITgDMLPTAGKVRVSGklgylpqdthasdptqtaldrmMSARDIA 92
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG----------------------VSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 tiINRIRKAEkemtdpdpDVMTKAMNRYDKAM-QDFDKAGGYAAQsEAISMATSLGLpQEVMEQQLG-----------TL 160
Cdd:cd03289 72 --LQKWRKAF--------GVIPQKVFIFSGTFrKNLDPYGKWSDE-EIWKVAEEVGL-KSVIEQFPGqldfvlvdggcVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVI--SHSTELLDEVV-------NKVWHLDA 231
Cdd:cd03289 140 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVIlsEHRIEAMLECQrflvieeNKVRQYDS 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-191 |
1.82e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 1 MAIEAQGLEiqigARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK--------------LG 66
Cdd:PRK11288 256 VRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpidirsprdairagIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 67 YLPQDTHASD--PTQTALDRM-MSAR----DIATIINriRKAEKEMTDpdpdvmtkamnRYDKAMqdfdkaggyaaqseA 139
Cdd:PRK11288 332 LCPEDRKAEGiiPVHSVADNInISARrhhlRAGCLIN--NRWEAENAD-----------RFIRSL--------------N 384
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 140 ISMATSlglpqevmEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK11288 385 IKTPSR--------EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-224 |
1.83e-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: 45.50 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 8 LEIQ-IGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylpqDTHASDPtqtaldRMM 86
Cdd:cd03215 5 LEVRgLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGK------PVTRRSP------RDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 87 SARDIATIinrirkaekemtdpdPDvmtkamNRydkamqdfdkaggyaaQSEAI----SMATSLGLPQevmeqqlgTLSG 162
Cdd:cd03215 73 IRAGIAYV---------------PE------DR----------------KREGLvldlSVAENIALSS--------LLSG 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 163 GQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKY-EGGFLVISHSTElLDEVVN 224
Cdd:cd03215 108 GNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELaDAGKAVLLISSE-LDELLG 169
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-517 |
1.97e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.63 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 312 ADIRFPEPApcgrtpIMAKDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGsVEYGHGCKI 391
Cdd:PRK14271 13 ADVDAAAPA------MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 392 G--YFAQEHDTLDLNATVLENLQHVAPE----LDNT----QARSILGSFLFSGDDAMKPAHV----------------LS 445
Cdd:PRK14271 86 GgrSIFNYRDVLEFRRRVGMLFQRPNPFpmsiMDNVlagvRAHKLVPRKEFRGVAQARLTEVglwdavkdrlsdspfrLS 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 446 GGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEG--AIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARIS-DRAALFFDG 238
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-65 |
3.30e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 3.30e-05
10 20 30
....*....|....*....|....*....|....*....
gi 489925987 27 KGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKL 65
Cdd:PRK13546 49 EGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEV 87
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-194 |
3.51e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 3.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 119 RYDKAMQDFDKAGGYAAQSEAISmatslGLPQEvMEQQLG----TLSGGQRRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIE-----SLPNK-YDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
357-525 |
3.65e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.02 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 357 ILGYNGAGKTTTLRLLAHIEEPDTGSVEYG---------------HGCKIGYFAQEHdTLDLNATVLENLQHVAPELDNT 421
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNgrvlfdaekgiclppEKRRIGYVFQDA-RLFPHYKVRGNLRYGMAKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 422 QARSILGsfLFSGDDAMK--PaHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD-PASREEI--LKAIAK-YEGAIVL 495
Cdd:PRK11144 108 QFDKIVA--LLGIEPLLDryP-GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLpyLERLAReINIPILY 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 496 VTH--DEgaVEALnPERVLLMPDGD-------EDLWNDS 525
Cdd:PRK11144 185 VSHslDE--ILRL-ADRVVVLEQGKvkafgplEEVWASS 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
15-192 |
3.73e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.58 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLP---TAGKVRVSGKL----------GYLPQDthasD---PT 78
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPidakemraisAYVQQD----DlfiPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 79 QTALDRMM-SARdiATIINRIRKAEKemtdpdpdvmtkaMNRYDKAMQDFdkaGGYAAQSeaismaTSLGLPQEVMeqql 157
Cdd:TIGR00955 114 LTVREHLMfQAH--LRMPRRVTKKEK-------------RERVDEVLQAL---GLRKCAN------TRIGVPGRVK---- 165
|
170 180 190
....*....|....*....|....*....|....*
gi 489925987 158 gTLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:TIGR00955 166 -GLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-191 |
4.10e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 45.30 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 5 AQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASDP------- 77
Cdd:PRK11701 9 VRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAerrrllr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 78 ------TQTALD--RM-MSARdiATIINRIrkaekemtdpdpdvMTKAMNRYDKAMQdfdKAGGYAAQSEaismatslgL 148
Cdd:PRK11701 89 tewgfvHQHPRDglRMqVSAG--GNIGERL--------------MAVGARHYGDIRA---TAGDWLERVE---------I 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489925987 149 PQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:PRK11701 141 DAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
341-504 |
4.25e-05 |
|
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: 45.15 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 341 VFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSV------------EYGHGcKIGYFAQEhDTLdLNATVL 408
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgkpisqyehKYLHS-KVSLVGQE-PVL-FARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 409 EN----LQHVAPE-LDNTQARSILGSF---LFSG--DDAMKPAHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPAS 478
Cdd:cd03248 106 DNiaygLQSCSFEcVKEAAQKAHAHSFiseLASGydTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190
....*....|....*....|....*....|
gi 489925987 479 REEILKAIakYEG----AIVLVTHDEGAVE 504
Cdd:cd03248 186 EQQVQQAL--YDWperrTVLVIAHRLSTVE 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
438-514 |
4.68e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 45.49 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 438 MKPaHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI----AKYEGAIVLVTHDEGAVEALNpERVLL 513
Cdd:PRK09473 157 MYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLnelkREFNTAIIMITHDLGVVAGIC-DKVLV 234
|
.
gi 489925987 514 M 514
Cdd:PRK09473 235 M 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
33-215 |
4.99e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 45.15 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 33 LVGRNGAGKTTLTRVIT--GDMLPTagkVRVSGKLGYLPQDTHAsdPTQTALDrmmsardiatiinrIRKaEKEMT--DP 108
Cdd:PRK14239 36 LIGPSGSGKSTLLRSINrmNDLNPE---VTITGSIVYNGHNIYS--PRTDTVD--------------LRK-EIGMVfqQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 109 DPDVMTKAMN---------RYDKAMQDfdkaggYAAQSEAISMATSLGLPQEVMEQQLGtLSGGQRRRIELARILFSDAD 179
Cdd:PRK14239 96 NPFPMSIYENvvyglrlkgIKDKQVLD------EAVEKSLKGASIWDEVKDRLHDSALG-LSGGQQQRVCIARVLATSPK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 180 TLILDEPTNHLDADSI----EWLRGYLKKYEggFLVISHS 215
Cdd:PRK14239 169 IILLDEPTSALDPISAgkieETLLGLKDDYT--MLLVTRS 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
404-517 |
5.43e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 404 NATVLENLQHVApeLDNTQArsILGSFLFSgddamkpahvLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEIL 483
Cdd:PRK10418 115 DATLTAALEAVG--LENAAR--VLKLYPFE----------MSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARIL 180
|
90 100 110
....*....|....*....|....*....|....*...
gi 489925987 484 ---KAIAKYEG-AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:PRK10418 181 dllESIVQKRAlGMLLVTHDMGVVARL-ADDVAVMSHG 217
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-191 |
6.34e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 44.79 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVItgDML--PTAGKVRVSGKLGYLPQD----THAS 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCI--NLLetPDSGEIRVGGEEIRLKPDrdgeLVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 76 DPTQtaLDRM----------------MSArdIATIIN------RIRKAEkemtdpdpdVMTKAMNRYDKaMQDFDKAGGY 133
Cdd:COG4598 86 DRRQ--LQRIrtrlgmvfqsfnlwshMTV--LENVIEapvhvlGRPKAE---------AIERAEALLAK-VGLADKRDAY 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489925987 134 AAQseaismatslglpqevmeqqlgtLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:COG4598 152 PAH-----------------------LSGGQQQRAAIARALAMEPEVMLFDEPTSALD 186
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-226 |
6.45e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.12 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 23 FHVAKGDKIGLVGRNGAGKTTLTRVITGdMLPTAGKVrVSGKLGYLPQDTHASDPTQTaldRMMSARDIATIInrirkaE 102
Cdd:PRK11022 28 YSVKQGEVVGIVGESGSGKSVSSLAIMG-LIDYPGRV-MAEKLEFNGQDLQRISEKER---RNLVGAEVAMIF------Q 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 103 KEMTDPDP--DVMTKAMNRYdKAMQDFDKAggyAAQSEAISMATSLGLPQ-----EVMEQQLgtlSGGQRRRIELARILF 175
Cdd:PRK11022 97 DPMTSLNPcyTVGFQIMEAI-KVHQGGNKK---TRRQRAIDLLNQVGIPDpasrlDVYPHQL---SGGMSQRVMIAMAIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 176 SDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKV 226
Cdd:PRK11022 170 CRPKLLIADEPTTALDvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-63 |
7.21e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 45.65 E-value: 7.21e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG 63
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-198 |
8.58e-05 |
|
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: 43.79 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 15 RTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDmlpTAGKVRVSGKLGYlpqDTHASDPTQTALDR---MMSARD- 90
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDIHY---NGIPYKEFAEKYPGeiiYVSEEDv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 91 -IATIINRirkaekemtdpdpdvmtkamnrydkamqdfdkaggyaaqsEAISMATSL-GlpqevmEQQLGTLSGGQRRRI 168
Cdd:cd03233 94 hFPTLTVR----------------------------------------ETLDFALRCkG------NEFVRGISGGERKRV 127
|
170 180 190
....*....|....*....|....*....|.
gi 489925987 169 ELARILFSDADTLILDEPTNHLDADS-IEWL 198
Cdd:cd03233 128 SIAEALVSRASVLCWDNSTRGLDSSTaLEIL 158
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
154-191 |
8.71e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 8.71e-05
10 20 30
....*....|....*....|....*....|....*...
gi 489925987 154 EQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLD 191
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
31-214 |
1.13e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.46 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 31 IGLVGRNGAGKTTLTRVITgdmlpTA--GKVRVSGKLgylPQDTHASDPTQTALDRMMSARDIATIINRIRKAEKEMTDP 108
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIR-----YAlyGKARSRSKL---RSDLINVGSEEASVELEFEHGGKRYRIERRQGEFAEFLEA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 109 DPDVMTKAMNR------YDKAMQDFDKAggYAAQSEAISMATSLGLPQEVMEQQL------GTLSGGQRRRIELARILfs 176
Cdd:COG0419 98 KPSERKEALKRllgleiYEELKERLKEL--EEALESALEELAELQKLKQEILAQLsgldpiETLSGGERLRLALADLL-- 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 489925987 177 dadTLILDepTNHLDADSIEWLRGYLKKYEggflVISH 214
Cdd:COG0419 174 ---SLILD--FGSLDEERLERLLDALEELA----IITH 202
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
345-488 |
1.32e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYghgckigyfaqehDTLDLNATVLENL-QHVAPELDN--- 420
Cdd:PRK11176 362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-------------DGHDLRDYTLASLrNQVALVSQNvhl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 421 ---TQARSILGSF--LFSGDD---AMKPAHV---------------------LSGGEKTRLALATLVTSRANVLLLDEPT 471
Cdd:PRK11176 429 fndTIANNIAYARteQYSREQieeAARMAYAmdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEAT 508
|
170
....*....|....*..
gi 489925987 472 NNLDPASREEILKAIAK 488
Cdd:PRK11176 509 SALDTESERAIQAALDE 525
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
332-500 |
1.40e-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: 42.70 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 332 ISKAYGSNIvfAGVNLAIDKGSRVVILGYNGAGKTTTLRllahieepDTGsveYGHGCKIgyFAQEHDTLDLNATVLenl 411
Cdd:cd03238 3 VSGANVHNL--QNLDVSIPLNVLVVVTGVSGSGKSTLVN--------EGL---YASGKAR--LISFLPKFSRNKLIF--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 412 qhvapeLDNTQARSILG-SFLFSGddamKPAHVLSGGEKTRLALAT--LVTSRANVLLLDEPTNNLDPASREEILKAIAK 488
Cdd:cd03238 65 ------IDQLQFLIDVGlGYLTLG----QKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKG 134
|
170
....*....|....*
gi 489925987 489 Y--EG-AIVLVTHDE 500
Cdd:cd03238 135 LidLGnTVILIEHNL 149
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-514 |
1.47e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTtLTRVITGDMLPTAGKVRVSGKLGYLPQDTHASDPTQTALDRMMSAR--DIATIInrir 99
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKS-VTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVRgaDMAMIF---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 100 kaEKEMTDPDPdVMTKAmNRYDKAMQDFDKAGGYAAQSEAISMATSLGLP--QEVMEQQLGTLSGGQRRRIELARILFSD 177
Cdd:PRK10261 111 --QEPMTSLNP-VFTVG-EQIAESIRLHQGASREEAMVEAKRMLDQVRIPeaQTILSRYPHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 178 ADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVwhldaqlgqIDMYSlswkaylHQRVVD 253
Cdd:PRK10261 187 PAVLIADEPTTALDvtiqAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV---------LVMYQ-------GEAVET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 254 EERRRREREVAEKKAERLMKQGIRLhakasKAVAAQNMMRRAEKLLENTSEAQKAEKVADIRFP-EPA-----PCGRTPI 327
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVPQL-----GAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVVDgEPIlqvrnLVTRFPL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 328 MAKDISKAygSNIVFAGVNLAID--KGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYG-------HGCKIG------ 392
Cdd:PRK10261 326 RSGLLNRV--TREVHAVEKVSFDlwPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlSPGKLQalrrdi 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 393 --YFAQEHDTLDLNATV----LENLQhVAPELDNTQARSILGSFL----FSGDDAMKPAHVLSGGEKTRLALATLVTSRA 462
Cdd:PRK10261 404 qfIFQDPYASLDPRQTVgdsiMEPLR-VHGLLPGKAAAARVAWLLervgLLPEHAWRYPHEFSGGQRQRICIARALALNP 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 463 NVLLLDEPTNNLDPASREEILKAIAKYEG----AIVLVTHDEGAVEALNpERVLLM 514
Cdd:PRK10261 483 KVIIADEAVSALDVSIRGQIINLLLDLQRdfgiAYLFISHDMAVVERIS-HRVAVM 537
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
444-500 |
1.66e-04 |
|
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: 42.35 E-value: 1.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489925987 444 LSGGEKTRLALATLVTS----RANVLLLDEPTNNLDPASREEILKAIAKY--EGAIVLV-THDE 500
Cdd:cd03227 78 LSGGEKELSALALILALaslkPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQVIViTHLP 141
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
153-192 |
1.66e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 43.86 E-value: 1.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489925987 153 MEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDA 192
Cdd:PRK11000 127 LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
20-64 |
2.13e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 43.81 E-value: 2.13e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489925987 20 PTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK 64
Cdd:PRK10522 341 PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK 385
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
440-499 |
2.99e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 42.30 E-value: 2.99e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 440 PAHVLSGGEKTRLALATLVTsranvLLLDepTNNLDPASREEILKAIAkyegAIVLVTHD 499
Cdd:COG0419 155 PIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
444-516 |
3.08e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 3.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 444 LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIA----KYEGAIVLVTHDEGAVEALNPERVLLMPD 516
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITIAHRIASIKRSDKIVVFNNPD 1435
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-194 |
3.09e-04 |
|
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: 43.78 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 17 LLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSG----KLGylpqdthasdptqtaldrMMSARDIA 92
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniaKIG------------------LHDLRFKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 93 TIINRirkaekemtdpDPDVMTKAMNrydkamQDFDKAGGYAaqSEAISMATSL------------GLPQEVMEQQlGTL 160
Cdd:TIGR00957 1363 TIIPQ-----------DPVLFSGSLR------MNLDPFSQYS--DEEVWWALELahlktfvsalpdKLDHECAEGG-ENL 1422
|
170 180 190
....*....|....*....|....*....|....
gi 489925987 161 SGGQRRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-236 |
3.43e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDmlpTAGKVrVSGKLGYLPQDTHASDPTQTAL 82
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH---PAYKI-LEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRMMSARDIATIINRIRKAekemtdpdpDVMTKAMNRYDKAMQ--DFDKAGGYAAQSEAISMatsLGLPQEVMEQQLGT- 159
Cdd:CHL00131 84 LGIFLAFQYPIEIPGVSNA---------DFLRLAYNSKRKFQGlpELDPLEFLEIINEKLKL---VGMDPSFLSRNVNEg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 160 LSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLR---GYLKKYEGGFLVISHSTELLDEVVNKVWHLdAQLGQI 236
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAegiNKLMTSENSIILITHYQRLLDYIKPDYVHV-MQNGKI 230
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-186 |
3.80e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 42.44 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgYLPQDTHASdpTQTAL 82
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE--NIPAMSRSR--LYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 83 DRM-MSARDIA-----TIINRIRKAEKEMTD-PDPDVMTKAMNRYdkamqdfdkaggyaaqsEAISM--ATSLgLPQEvm 153
Cdd:PRK11831 84 KRMsMLFQSGAlftdmNVFDNVAYPLREHTQlPAPLLHSTVMMKL-----------------EAVGLrgAAKL-MPSE-- 143
|
170 180 190
....*....|....*....|....*....|...
gi 489925987 154 eqqlgtLSGGQRRRIELARILFSDADTLILDEP 186
Cdd:PRK11831 144 ------LSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
442-517 |
4.92e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.77 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 442 HVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEG----AIVLVTHDEGAVEALnPERVLLMPDG 517
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnmGLLFITHNLSIVRKL-ADRVAVMQNG 233
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
444-505 |
5.46e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 41.47 E-value: 5.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 444 LSGGEKTRLALATLVTSRANVLL--LDEPTNNLDPASREEILKAIAKYEGA---IVLVTHDEGAVEA 505
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLgntVLVVEHDEDTIRA 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-222 |
6.51e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 3 IEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG--DMLPTAGKVRVSGKlgylpqDTHASDPTQT 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGreDYEVTGGTVEFKGK------DLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 81 ALDRMMSARD-------------IATIINRIRKAEKEmtdpdpdvmtKAMNRYDkaMQDFdkaggyaaQSEAISMatsLG 147
Cdd:PRK09580 76 AGEGIFMAFQypveipgvsnqffLQTALNAVRSYRGQ----------EPLDRFD--FQDL--------MEEKIAL---LK 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 148 LPQEVMEQQLGT-LSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGG---FLVISHSTELLDEV 222
Cdd:PRK09580 133 MPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkrsFIIVTHYQRILDYI 211
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
356-518 |
8.88e-04 |
|
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: 40.72 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 356 VILGYNGAGKTT-----TLRLLAhiEEPDTGSVEYGHGckigYFAQEHDTLDLNATVLENLQ----HVAPELDNTQ-ARS 425
Cdd:cd03279 32 LICGPTGAGKSTildaiTYALYG--KTPRYGRQENLRS----VFAPGEDTAEVSFTFQLGGKkyrvERSRGLDYDQfTRI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 426 IL---GSFlfsgDDAMK-PAHVLSGGEK------TRLALATLVTSRANV----LLLDEPTNNLDPASRE---EILKAIAK 488
Cdd:cd03279 106 VLlpqGEF----DRFLArPVSTLSGGETflaslsLALALSEVLQNRGGArleaLFIDEGFGTLDPEALEavaTALELIRT 181
|
170 180 190
....*....|....*....|....*....|
gi 489925987 489 YEGAIVLVTHDEGAVEALnPERVLLMPDGD 518
Cdd:cd03279 182 ENRMVGVISHVEELKERI-PQRLEVIKTPG 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
146-221 |
1.00e-03 |
|
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: 40.38 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 146 LGLPQEVMEQQLGTLSGGQRRRIELARILFSDAD--TLILDEPTNHLDADSIEWLRGYLKKY--EGG-FLVISHSTELLD 220
Cdd:cd03238 74 VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidLGNtVILIEHNLDVLS 153
|
.
gi 489925987 221 E 221
Cdd:cd03238 154 S 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-194 |
1.09e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.79 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 11 QIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVI---------TGDMLPTAGKV--RVSGKLGYLPQDThasdptq 79
Cdd:PLN03211 77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPtkQILKRTGFVTQDD------- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 80 tALDRMMSARDIATIINRIRkaekemtdpdpdvMTKAMNRYDKAmqdfdkaggyaaqSEAISMATSLGLPQ----EVMEQ 155
Cdd:PLN03211 150 -ILYPHLTVRETLVFCSLLR-------------LPKSLTKQEKI-------------LVAESVISELGLTKcentIIGNS 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 489925987 156 QLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADS 194
Cdd:PLN03211 203 FIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
444-500 |
1.34e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 444 LSGGEKT------RLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEGAI---VLVTHDE 500
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIpqvIIVSHDE 854
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
126-220 |
1.37e-03 |
|
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: 39.65 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 126 DFDKAGGYAAQSEAISMATSLGLpqevmeqqlgtlSGGQRRRIELARIL----FSDADTLILDEPTNHLDADSIEWLRGY 201
Cdd:cd03227 56 SGVKAGCIVAAVSAELIFTRLQL------------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEA 123
|
90 100
....*....|....*....|..
gi 489925987 202 LKKYEGG---FLVISHSTELLD 220
Cdd:cd03227 124 ILEHLVKgaqVIVITHLPELAE 145
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
345-475 |
1.38e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 41.65 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 345 VNLAIDKGSRVVILGYNGAGKTTTLRllAHIEE----PDTGSVEYGhgcKIGYFAQEhdTLDLNATVLENLQHVAPELDN 420
Cdd:PLN03130 636 INLDVPVGSLVAIVGSTGEGKTSLIS--AMLGElpprSDASVVIRG---TVAYVPQV--SWIFNATVRDNILFGSPFDPE 708
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489925987 421 TQARSILGSFLfSGDDAMKPAHVL----------SGGEKTRLALATLVTSRANVLLLDEPTNNLD 475
Cdd:PLN03130 709 RYERAIDVTAL-QHDLDLLPGGDLteigergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-236 |
1.55e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.38 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGK----------------LGYLPQDTHAS-DPTQTALDR 84
Cdd:PRK10261 344 SFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlspgklqalrrdIQFIFQDPYASlDPRQTVGDS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 85 MMSARDIATIINrirkaekemtdpdpdvmtkamnrydkamqdfdkagGYAAQSEAISMATSLGLPQEVMEQQLGTLSGGQ 164
Cdd:PRK10261 424 IMEPLRVHGLLP-----------------------------------GKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQ 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489925987 165 RRRIELARILFSDADTLILDEPTNHLD----ADSIEWLRGYLKKYEGGFLVISHSTELLDEVVNKVWHLdaQLGQI 236
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDvsirGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM--YLGQI 542
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
442-517 |
1.72e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 442 HVLSGGEKTRLALATLVTSRANVLLLDEPTNNLD---PASREEILKAIAKYEG-AIVLVTHDEGAVeALNPERVLLMPDG 517
Cdd:PRK11022 152 HQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDvtiQAQIIELLLELQQKENmALVLITHDLALV-AEAAHKIIVMYAG 230
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
433-513 |
1.77e-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: 41.11 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 433 SGDDAMKPAHVLSGGE------KTRLALATLVTSRANV----LLLDEPTNNLDPASRE---EILKAIAKYEGAIVLVTHD 499
Cdd:TIGR00618 940 AYTGSVRPSATLSGGEtflaslSLALALADLLSTSGGTvldsLFIDEGFGSLDEDSLDraiGILDAIREGSKMIGIISHV 1019
|
90
....*....|....
gi 489925987 500 EGAVEALnPERVLL 513
Cdd:TIGR00618 1020 PEFRERI-PHRILV 1032
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
330-498 |
1.99e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 330 KDISKAYGSNIVFAGVNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVEYgHGCKIGYFAQEHdtldlnatVLE 409
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILF-QGKEIDFKSSKE--------ALE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 410 N-LQHVAPELDNTQARSI-----LGSF----LFSGDDAM------------------KPAHVLSGGEKTRLALATLVTSR 461
Cdd:PRK10982 73 NgISMVHQELNLVLQRSVmdnmwLGRYptkgMFVDQDKMyrdtkaifdeldididprAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489925987 462 ANVLLLDEPTNNLDPASREEILKAIAKYEG---AIVLVTH 498
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKErgcGIVYISH 192
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
444-503 |
2.10e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 40.25 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 444 LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKY--EGAIVLV-THDEGAV 503
Cdd:PRK15056 143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELrdEGKTMLVsTHNLGSV 205
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
30-54 |
2.21e-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: 38.63 E-value: 2.21e-03
10 20
....*....|....*....|....*
gi 489925987 30 KIGLVGRNGAGKTTLTRVITGDMLP 54
Cdd:COG4917 3 RIMLIGRSGAGKTTLTQALNGEELE 27
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-204 |
2.72e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 140 ISMATSLGLPQEVMEQQLGTLSGGQRRRIELARILFSD--ADTLILDEPTNHLDADSIEWLRGYLKK 204
Cdd:PRK00635 457 LSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLHPQDTHKLINVIKK 523
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
144-226 |
2.79e-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: 39.09 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 144 TSLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDAD----SIEWLRGYLKKYEGGFLVISHSTELL 219
Cdd:cd03222 56 DEWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVL 135
|
....*..
gi 489925987 220 DEVVNKV 226
Cdd:cd03222 136 DYLSDRI 142
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-193 |
2.82e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 39.73 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 18 LHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVrvsgklgyLPQDTHASDPTQTALdrmmsARDIATIINr 97
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI--------FYNNQAITDDNFEKL-----RKHIGIVFQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 98 irkaekemtdpDPDvmtkamNRYDKAMQDFDKAGGYaaQSEAISMATSLGLPQEVMEQ---------QLGTLSGGQRRRI 168
Cdd:PRK13648 91 -----------NPD------NQFVGSIVKYDVAFGL--ENHAVPYDEMHRRVSEALKQvdmleradyEPNALSGGQKQRV 151
|
170 180
....*....|....*....|....*
gi 489925987 169 ELARILFSDADTLILDEPTNHLDAD 193
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPD 176
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-212 |
3.31e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.69 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 2 AIEAQGLEIQIGARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITgDMLPTAGKVRVSGklgylpqdthasdptqta 81
Cdd:PRK14271 21 AMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLN-RMNDKVSGYRYSG------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 82 lDRMMSARDIAT---IINRIRKAEKEMTDPDPDVMTkAMNRYDKAMQDFDKAGGYAAQSEAISMATSLGLPQEVMEQQLG 158
Cdd:PRK14271 82 -DVLLGGRSIFNyrdVLEFRRRVGMLFQRPNPFPMS-IMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 159 T---LSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVI 212
Cdd:PRK14271 160 SpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVI 216
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-80 |
3.38e-03 |
|
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: 38.76 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 13 GARTLLHPTNFHVAKGDKIGLVGRNGAGKTTLTRVITG--DMLPTAGKVRVSGKL---------GYLPQ-DTHasDPTQT 80
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPldknfqrstGYVEQqDVH--SPNLT 95
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
444-517 |
3.78e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.91 E-value: 3.78e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 444 LSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAI---AKYEGAIVLVTHDEGAVEALNpERVLLMPDG 517
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLInqlVQQGVAIIVISSELPEVLGLS-DRVLVMHEG 481
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
153-219 |
3.84e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 40.27 E-value: 3.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489925987 153 MEQQLGTLSGGQRR------RIELARILFSDADTLILDEPTNHLDAD---SIEWLRGYLKKYEGGF---LVISHSTELL 219
Cdd:PRK01156 795 MVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDrrtNLKDIIEYSLKDSSDIpqvIMISHHRELL 873
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
316-517 |
4.30e-03 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 39.57 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 316 FPEP-APCGRTPIMAKDISKAYGSNIVFAG-VNLAIDKGSRVVILGYNGAGKTTTLRLLAHIEEPDTGSVeYGHGCKIGY 393
Cdd:PRK10522 311 FPRPqAFPDWQTLELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-LLDGKPVTA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 394 fAQEHDTLDLNATVLENLqHVAPELDNTQARSILGSFLFSGDDAMKPAHV------------LSGGEKTRLALATLVTSR 461
Cdd:PRK10522 390 -EQPEDYRKLFSAVFTDF-HLFDQLLGPEGKPANPALVEKWLERLKMAHKleledgrisnlkLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489925987 462 ANVLLLDEPTNNLDPASREE-------ILKAIAKyegAIVLVTHDEGAVEalNPERVLLMPDG 517
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREfyqvllpLLQEMGK---TIFAISHDDHYFI--HADRLLEMRNG 525
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
160-220 |
4.67e-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: 39.30 E-value: 4.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 160 LSGGQRRRIELARILFSDAD---TLILDEPTNHLDADSIEWLRGYLKKYEGG---FLVISHSTELLD 220
Cdd:pfam13304 237 LSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHSPLLLD 303
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-222 |
4.69e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 22 NFHVAKGDKIGLVGRNGAGKTTLTRVITGDMLPTAGKVRVSGKlgylPQDTHASdptQTALDRMMSArdIATIINRIRKA 101
Cdd:PRK10982 18 NLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK----EIDFKSS---KEALENGISM--VHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 102 ekemtdpdpDVMTKA-MNRYDKAMQDFDKAGGYaaqSEAISMATSLGL---PQEvmeqQLGTLSGGQRRRIELARILFSD 177
Cdd:PRK10982 89 ---------SVMDNMwLGRYPTKGMFVDQDKMY---RDTKAIFDELDIdidPRA----KVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489925987 178 ADTLILDEPTNHLDADSIEWLRGYLKKYEG---GFLVISHSTE----LLDEV 222
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKErgcGIVYISHKMEeifqLCDEI 204
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
441-491 |
5.63e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 5.63e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 489925987 441 AHVLSGGEKTRLALATLVTSRANVLLLDEPTNNLDPASREEILKAIAKYEG 491
Cdd:PTZ00265 577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKG 627
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
138-219 |
7.73e-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: 37.35 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 138 EAISMATSLGLPQEVMEQQLGTLSGGQRRRIELARILFSDADTLILDEPTNHLDADSIEWLRGYLKKYEGGFLVISHSTE 217
Cdd:smart00382 39 EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
..
gi 489925987 218 LL 219
Cdd:smart00382 119 VI 120
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
148-218 |
8.96e-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: 37.63 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925987 148 LPQ----EVMEQQLGTLSGGQRRRIELA-RILFSDA---------DTLILDEPTNHLDADSIEWLRGYLKKYEGGF---L 210
Cdd:cd03279 108 LPQgefdRFLARPVSTLSGGETFLASLSlALALSEVlqnrggarlEALFIDEGFGTLDPEALEAVATALELIRTENrmvG 187
|
....*...
gi 489925987 211 VISHSTEL 218
Cdd:cd03279 188 VISHVEEL 195
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-220 |
9.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.89 E-value: 9.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489925987 154 EQQLGTLSGGQR------RRIELARILFSDADTLILDEPTNHLDADS----IEWLRGYLKKYEgGFLVISHSTELLD 220
Cdd:PRK03918 783 ERPLTFLSGGERialglaFRLALSLYLAGNIPLLILDEPTPFLDEERrrklVDIMERYLRKIP-QVIIVSHDEELKD 858
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