|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-482 |
1.90e-151 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 443.74 E-value: 1.90e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQET---------- 75
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsIPKGLRIGYLPQEPpldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 --------------------ASYSFADQTPAE--------------------KKLLEKWRVPVRDFQQ----LSGGEKLK 111
Cdd:COG0488 81 tvldgdaelraleaeleeleAKLAEPDEDLERlaelqeefealggweaearaEEILSGLGFPEEDLDRpvseLSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 112 ARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKF 191
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 192 REKKRLTQQREYEKQQKMVERIEAQMNelaswskkahdqstkkegfkeyhRVKAK-RTDAQIKSKQKRLEKeLEkaKAEP 270
Cdd:COG0488 241 RAERLEQEAAAYAKQQKKIAKEEEFIR-----------------------RFRAKaRKAKQAQSRIKALEK-LE--REEP 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 271 VKPEYTVHFSIDTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV 349
Cdd:COG0488 295 PRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPdSGTVKL 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 SPSANIGYLTQEVFDLPLEQTP-EELFDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVL 428
Cdd:COG0488 375 GETVKIGYFDQHQEELDPDKTVlDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 429 ILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGID 482
Cdd:COG0488 455 LLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-468 |
2.69e-72 |
|
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: 240.22 E-value: 2.69e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQ-DIKMTMVEQETA--------------------- 76
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLPQEPQldptktvrenveegvaeikda 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 -------SYSFADQTPAEKKLLEK-------------W-------------RVPVRD--FQQLSGGEKLKARLAKGLSVD 121
Cdd:TIGR03719 100 ldrfneiSAKYAEPDADFDKLAAEqaelqeiidaadaWdldsqleiamdalRCPPWDadVTKLSGGERRRVALCRLLLSK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 122 ADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKFREKKRLTQQR 201
Cdd:TIGR03719 180 PDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEK 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 202 EYEKQQKMVERieaqmnELaswskkahdqstkkegfkEYHRVKAKRTDAQIKSKQKRLEKELEKAKAEPVKpeyTVHFSI 281
Cdd:TIGR03719 260 EESARQKTLKR------EL------------------EWVRQSPKGRQAKSKARLARYEELLSQEFQKRNE---TAEIYI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 282 DTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWVSPSANIGYLTQ 360
Cdd:TIGR03719 313 PPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDsGTIEIGETVKLAYVDQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EVFDLPLEQTP-EELFD--------NETYKARGHVQSlmrhLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILD 431
Cdd:TIGR03719 393 SRDALDPNKTVwEEISGgldiiklgKREIPSRAYVGR----FNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468
|
490 500 510
....*....|....*....|....*....|....*..
gi 1732943882 432 EPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEK 468
Cdd:TIGR03719 469 EPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDR 505
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-481 |
5.18e-71 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 236.33 E-value: 5.18e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 20 FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------LRQD-----------------IKMTMVE 72
Cdd:PRK15064 17 FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsldpnerlgkLRQDqfafeeftvldtvimghTELWEVK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QE-TASYSFADQT--------------------PAEKK---LLEKWRVPVRD----FQQLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK15064 97 QErDRIYALPEMSeedgmkvadlevkfaemdgyTAEARageLLLGVGIPEEQhyglMSEVAPGWKLRVLLAQALFSNPDI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 125 LLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMkfrekKRLTQQReyE 204
Cdd:PRK15064 177 LLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYM-----TAATQAR--E 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 205 KQQKMVERIEAQMNELASW-SKKAHDQStkkegfkeyhrvKAKrtdaQIKSKQKRlekeLEKAKAEPVKPEYTVHFSI-- 281
Cdd:PRK15064 250 RLLADNAKKKAQIAELQSFvSRFSANAS------------KAK----QATSRAKQ----IDKIKLEEVKPSSRQNPFIrf 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 282 DTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSANIGYLTQ 360
Cdd:PRK15064 310 EQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPdSGTVKWSENANIGYYAQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvfdlpleqtPEELFDNET--------YKARGHVQSLMRH-LG---FTASQWTEPIKHMSMGERVKC---KLMayiLEEK 425
Cdd:PRK15064 390 D---------HAYDFENDLtlfdwmsqWRQEGDDEQAVRGtLGrllFSQDDIKKSVKVLSGGEKGRMlfgKLM---MQKP 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGI 481
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGV 513
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-466 |
1.09e-65 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 222.69 E-value: 1.09e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIV-TLTNVSYEV-KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHL-------IHNDLAPAQGQ---ILRQ---- 64
Cdd:PRK11819 2 MAQYIyTMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRImagvdkeFEGEARPAPGIkvgYLPQepql 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 ---------------DIKMTMVEQETASYSFADQTPAEKKLLEK-------------W-------------RVPVRD--F 101
Cdd:PRK11819 82 dpektvrenveegvaEVKAALDRFNEIYAAYAEPDADFDALAAEqgelqeiidaadaWdldsqleiamdalRCPPWDakV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 102 QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 182 KGNYSGYMKFREkKRLTQQ-REYEKQQKMVERieaqmnELaswskkahdqstkkegfkEYHRVKAK-RtdaQIKSKqKRL 259
Cdd:PRK11819 242 EGNYSSWLEQKA-KRLAQEeKQEAARQKALKR------EL------------------EWVRQSPKaR---QAKSK-ARL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 260 EK--ELEkAKAEPVKPEyTVHFSIDTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII 337
Cdd:PRK11819 293 ARyeELL-SEEYQKRNE-TNEIFIPPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 338 LGQETA-EGSVWVSPSANIGYLTQEVFDLPLEQTP-EELFD--------NETYKARGHVQSlmrhLGFTASQWTEPIKHM 407
Cdd:PRK11819 371 TGQEQPdSGTIKIGETVKLAYVDQSRDALDPNKTVwEEISGgldiikvgNREIPSRAYVGR----FNFKGGDQQKKVGVL 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 408 SMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFL 466
Cdd:PRK11819 447 SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFL 505
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-541 |
5.41e-65 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 222.90 E-value: 5.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQ-----ETAS 77
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiYEQDLIVARLQQdpprnVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 78 -YSF--------AD-------------QTPAEKKL--LEK----------WRVPVRDFQ--------------QLSGGEK 109
Cdd:PRK11147 83 vYDFvaegieeqAEylkryhdishlveTDPSEKNLneLAKlqeqldhhnlWQLENRINEvlaqlgldpdaalsSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 110 LKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYM 189
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 190 KfrekkrltqqreyEKQQKMveRIEAQMNELasWSKK-AHDQSTKKEGfkeyhrVKAKRTDAQiksKQKRLEKELEKAKA 268
Cdd:PRK11147 243 L-------------EKEEAL--RVEELQNAE--FDRKlAQEEVWIRQG------IKARRTRNE---GRVRALKALRRERS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 269 EPVKPEYTVHFSIDTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSV 347
Cdd:PRK11147 297 ERREVMGTAKMQVEEASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADsGRI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 348 WVSPSANIGYLTQEVFDLPLEQTPEelfDN-----ETYKARG---HVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMA 419
Cdd:PRK11147 377 HCGTKLEVAYFDQHRAELDPEKTVM---DNlaegkQEVMVNGrprHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAR 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 420 YILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGI------------DKQLND 487
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKigryvggyhdarQQQAQY 533
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 488 VP---TERNEREELRLKLETERQEVLGKLSFmmpndKGYKELDQafneLTKRIKELD 541
Cdd:PRK11147 534 LAlkqPAVKKKEEAAAPKAETVKRSSKKLSY-----KLQRELEQ----LPQLLEDLE 581
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-482 |
8.48e-63 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 216.96 E-value: 8.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQETAsysfADQTPA-------------- 86
Cdd:PRK10636 19 NATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYtFPGNWQLAWVNQETP----ALPQPAleyvidgdreyrql 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 87 EKKL---------------------LEKWRV--------------------PVRDFqqlSGGEKLKARLAKGLSVDADLL 125
Cdd:PRK10636 95 EAQLhdanerndghaiatihgkldaIDAWTIrsraasllhglgfsneqlerPVSDF---SGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 126 LLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMKFREKKRLTQQREYEK 205
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 206 QQKMVerieaqmnelaswskkAHDQSTkkegfkeYHRVKAKRTDA-QIKSKQKRLEKELEKAKAEPVKPeytVHFSIDTS 284
Cdd:PRK10636 252 QQERV----------------AHLQSY-------IDRFRAKATKAkQAQSRIKMLERMELIAPAHVDNP---FHFSFRAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 285 KKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSPSANIGYLTQEVF 363
Cdd:PRK10636 306 ESLPNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGElAPVSGEIGLAKGIKLGYFAQHQL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 364 D-LPLEQTPEE----LFDNETYkarghvQSLMRHL---GFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:PRK10636 386 EfLRADESPLQhlarLAPQELE------QKLRDYLggfGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1732943882 436 HLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGID 482
Cdd:PRK10636 460 HLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
294-513 |
7.09e-58 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 201.06 E-value: 7.09e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 294 VQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSANIGYLTQEVFDLP------ 366
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGLRIGYLPQEPPLDDdltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 367 ------------------LEQTP--------------EELFDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVK 414
Cdd:COG0488 81 tvldgdaelraleaeleeLEAKLaepdedlerlaelqEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 415 CKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVIsDNGidkQLNDVP----- 489
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILEL-DRG---KLTLYPgnysa 236
|
250 260
....*....|....*....|....*.
gi 1732943882 490 --TERNEREELRLKLETERQEVLGKL 513
Cdd:COG0488 237 ylEQRAERLEQEAAAYAKQQKKIAKE 262
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
292-480 |
2.25e-56 |
|
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: 185.34 E-value: 2.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSANIGYLTQevfdlpleqt 370
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPdEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 peelfdnetykarghvqslmrhlgftasqwtepikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS 450
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 451 QYGGTLLAVSHDRYFLEKTTNSKLVISDNG 480
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-177 |
6.41e-54 |
|
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: 178.80 E-value: 6.41e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-QDIKMtmveqetaSYsfadq 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWgSTVKI--------GY----- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 84 tpaekkllekwrvpvrdFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFL 163
Cdd:cd03221 68 -----------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFL 130
|
170
....*....|....
gi 1732943882 164 DEAATKIWSLEDQT 177
Cdd:cd03221 131 DQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-190 |
1.13e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 178.72 E-value: 1.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-QDIKMTMVEQETASYSf 80
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVKIGYFDQHQEELD- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ADQTPAE------------------KKLL---EKWRVPVRDfqqLSGGEKlkAR--LAKGLSVDADLLLLDEPTNHLDES 137
Cdd:COG0488 392 PDKTVLDelrdgapggteqevrgylGRFLfsgDDAFKPVGV---LSGGEK--ARlaLAKLLLSPPNVLLLDEPTNHLDIE 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 138 SLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:COG0488 467 TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
98-478 |
7.87e-46 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 171.20 E-value: 7.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 98 VRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQT 177
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 178 LIEFKGNYSGYMKFREKKRLTQQREYEKQQKmverieaqmnelaswsKKAHDQStkkegFKEYHRVKAKRTdAQIKSKQK 257
Cdd:PLN03073 419 LVTYKGDYDTFERTREEQLKNQQKAFESNER----------------SRSHMQA-----FIDKFRYNAKRA-SLVQSRIK 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 258 RLEKeLEKAKAEPVKPEYTVHFSIdTSKKTGKRFLEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKI 336
Cdd:PLN03073 477 ALDR-LGHVDAVVNDPDYKFEFPT-PDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKL 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 337 ILGQ-ETAEGSVWVSPSANIGYLTQEVFD-LPLEQTPeELFDNETY------KARGHVQSlmrhLGFTASQWTEPIKHMS 408
Cdd:PLN03073 555 ISGElQPSSGTVFRSAKVRMAVFSQHHVDgLDLSSNP-LLYMMRCFpgvpeqKLRAHLGS----FGVTGNLALQPMYTLS 629
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 409 MGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:PLN03073 630 GGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSE 699
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
292-467 |
1.06e-35 |
|
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: 132.22 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPsAGEVLWngepirdareDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EVfDLPLEQTPEELFD-----NETYKARGHVQSLMRHLGFtASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:COG4133 83 AD-GLKPELTVRENLRfwaalYGLRADREAIDEALEAVGL-AGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 436 HLDLPSREQLEETLSQY---GGTLLAVSHDRYFLE 467
Cdd:COG4133 161 ALDAAGVALLAELIAAHlarGGAVLLTTHQPLELA 195
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-462 |
1.73e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 133.49 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTN--VSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQI------LRQDI------ 66
Cdd:COG1123 1 MTPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPHGGRIsgevllDGRDLlelsea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 ----KMTMVEQETAS----YSFADQ----------TPAE-----KKLLEKWRVPVRDFQ---QLSGGEKLKARLAKGLSV 120
Cdd:COG1123 80 lrgrRIGMVFQDPMTqlnpVTVGDQiaealenlglSRAEararvLELLEAVGLERRLDRyphQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 121 DADLLLLDEPTNHLDESS---LQFLIQQLKSYRG-TVILVSHDRYFLDEAATKIWSLEDQTLIEfkgnysgymkfrekkr 196
Cdd:COG1123 160 DPDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRIVE---------------- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 197 ltqqreyekqQKMVERIEAQMNELAswskkahdqstkkegfkeyhrvkakrtdAQIKSKQKRLEKELEKAKAEPVkpeyt 276
Cdd:COG1123 224 ----------DGPPEEILAAPQALA----------------------------AVPRLGAARGRAAPAAAAAEPL----- 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 277 vhfsidtskktgkrfLEVQNITKAF-----GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV- 349
Cdd:COG1123 261 ---------------LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGlLRPTSGSILFd 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 -------SPSA------NIGYLTQE----------VFDL---PLEQ----TPEElfdnetykARGHVQSLMRHLGFTASQ 399
Cdd:COG1123 326 gkdltklSRRSlrelrrRVQMVFQDpysslnprmtVGDIiaePLRLhgllSRAE--------RRERVAELLERVGLPPDL 397
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 400 WTEPIKHMSMGE--RVkckLMAYIL-EEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:COG1123 398 ADRYPHELSGGQrqRV---AIARALaLEPKLLILDEPTSALDVSVQAQILNLLrdlqRELGLTYLFISHD 464
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-179 |
3.58e-33 |
|
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: 124.47 E-value: 3.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIKmTMVEQETASY-SFAD 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldGKDLA-SLSPKELARKiAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 QtpaekkLLEKWRVPV---RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKSYRG-TVIL 155
Cdd:cd03214 80 Q------ALELLGLAHladRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahQIELLELLRRLARERGkTVVM 153
|
170 180
....*....|....*....|....*..
gi 1732943882 156 VSHDryfLDEA---ATKIWSLEDQTLI 179
Cdd:cd03214 154 VLHD---LNLAaryADRVILLKDGRIV 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-167 |
1.90e-31 |
|
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: 122.07 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RQDI--KMTMV 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgrdlaslsRRELarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 72 EQET-----------------------ASYSFADQTPAEKKL----LEKWRVpvRDFQQLSGGEKLKARLAKGLSVDADL 124
Cdd:COG1120 81 PQEPpapfgltvrelvalgryphlglfGRPSAEDREAVEEALertgLEHLAD--RPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 125 LLLDEPTNHLDESSlQF----LIQQLKSYRG-TVILVSHDryfLDEAA 167
Cdd:COG1120 159 LLLDEPTSHLDLAH-QLevleLLRRLARERGrTVVMVLHD---LNLAA 202
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
292-480 |
6.07e-31 |
|
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: 118.27 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVlgkdikkepeEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvFDLPLEQTPEELFDnetykarghvqslmrhlgftasqwtepikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLP 440
Cdd:cd03230 81 E-PSLYENLTVRENLK------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 441 SREQLEETLSQY---GGTLLAVSHDRYFLEKTTNsKLVISDNG 480
Cdd:cd03230 130 SRREFWELLRELkkeGKTILLSSHILEEAERLCD-RVAILNNG 171
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-175 |
7.24e-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: 117.35 E-value: 7.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIkmtmveqetasysfadqtP 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK------------------D 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 86 AEKKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSHDRYF 162
Cdd:cd00267 63 IAKLPLEELRRRIGYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPEL 142
|
170
....*....|...
gi 1732943882 163 LDEAATKIWSLED 175
Cdd:cd00267 143 AELAADRVIVLKD 155
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
292-462 |
9.25e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.78 E-value: 9.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVlgedvardpaEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvFDLPLEQTPEE-------LFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILDEP 433
Cdd:COG1131 81 E-PALYPDLTVREnlrffarLYGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 434 TNHLDLPSREQLEETLSQY---GGTLLAVSHD 462
Cdd:COG1131 159 TSGLDPEARRELWELLRELaaeGKTVLLSTHY 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-190 |
9.33e-30 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 122.69 E-value: 9.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlrqdiKMTmveqETASYSFADQT 84
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWS----ENANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 PAE-----KKLLE---KWRVPVRDFQQ---------------------LSGGEKLKARLAKGLSVDADLLLLDEPTNHLD 135
Cdd:PRK15064 391 HAYdfendLTLFDwmsQWRQEGDDEQAvrgtlgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 136 ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:PRK15064 471 MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLR 525
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-175 |
1.47e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 115.68 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL-----RQDIKMT-------MVE 72
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRAL-ADLdPPTSGEIYldgkpLSAMPPPewrrqvaYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETA------------SYSFADQTPAE---KKLLEKWRVPV----RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:COG4619 81 QEPAlwggtvrdnlpfPFQLRERKFDReraLELLERLGLPPdildKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 134 LDESSLQFLIQQLKSYR----GTVILVSHDRYFLDEAATKIWSLED 175
Cdd:COG4619 161 LDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
295-508 |
1.75e-29 |
|
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: 122.35 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 295 QNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSANIGYLTQE--------VFD 364
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDfNGEARPQPGIKVGYLPQEpqldptktVRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 LPLEQTPE--ELFD--NETYKA--------------RGHVQSLMRHLGF--TASQ------------WTEPIKHMSMGER 412
Cdd:TIGR03719 88 NVEEGVAEikDALDrfNEISAKyaepdadfdklaaeQAELQEIIDAADAwdLDSQleiamdalrcppWDADVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 413 VKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVIsDNGidkqlNDVPTER 492
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILEL-DRG-----RGIPWEG 241
|
250 260
....*....|....*....|.
gi 1732943882 493 N-----EREELRLKLEtERQE 508
Cdd:TIGR03719 242 NysswlEQKQKRLEQE-EKEE 261
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
292-462 |
2.16e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV------SPSANIGYLTQ-EVF 363
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLfgkpprRARRRIGYVPQrAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 364 D--LPLeqTPEE-----------LFDNETYKARGHVQSLMRHLGFTAsQWTEPIKHMSMGE--RVkckLMAYIL-EEKDV 427
Cdd:COG1121 87 DwdFPI--TVRDvvlmgrygrrgLFRRPSRADREAVDEALERVGLED-LADRPIGELSGGQqqRV---LLARALaQDPDL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 428 LILDEPTNHLDLPSREQLEETLS---QYGGTLLAVSHD 462
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHD 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-197 |
4.91e-29 |
|
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: 120.81 E-value: 4.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLT-------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQetasy 78
Cdd:TIGR03719 318 LGDKVIEAENLTkafgdklLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeIGETVKLAYVDQ----- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 sFADQTPAEKKLLE------------KWRVPVR-----------DFQ----QLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:TIGR03719 393 -SRDALDPNKTVWEeisggldiiklgKREIPSRayvgrfnfkgsDQQkkvgQLSGGERNRVHLAKTLKSGGNVLLLDEPT 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 132 NHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE-FKGNYSGYMKFReKKRL 197
Cdd:TIGR03719 472 NDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDSHVEwFEGNFSEYEEDK-KRRL 537
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
307-435 |
1.55e-28 |
|
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: 110.82 E-value: 1.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 307 FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV-----------SPSANIGYLTQEVFDLPlEQTPEE- 373
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLdgqdltdderkSLRKEIGYVFQDPQLFP-RLTVREn 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 374 ------LFDNETYKARGHVQSLMRHLG---FTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:pfam00005 80 lrlgllLKGLSKREKDARAEEALEKLGlgdLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-166 |
3.47e-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: 110.57 E-value: 3.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTmveqetasysfadQT 84
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-------------KE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 PAEKK-----LLEKWRVP----VRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR---GT 152
Cdd:cd03230 68 PEEVKrrigyLPEEPSLYenltVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKT 147
|
170
....*....|....
gi 1732943882 153 VILVSHDryfLDEA 166
Cdd:cd03230 148 ILLSSHI---LEEA 158
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-275 |
6.38e-28 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 118.13 E-value: 6.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlRQDIKMtmveqETASYsfaDQTPA 86
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCGTKL-----EVAYF---DQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 87 ----EKKLLE-----KWRVPV-----------RDF-----------QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD 135
Cdd:PRK11147 393 eldpEKTVMDnlaegKQEVMVngrprhvlgylQDFlfhpkramtpvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 136 ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLI-EFKGnysGYMKFRekkrltQQRE--YEKQQKMVER 212
Cdd:PRK11147 473 VETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNGKIgRYVG---GYHDAR------QQQAqyLALKQPAVKK 543
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 213 IEAQMNELASWSKKahdqSTKKEGFKEyhrvkaKRTDAQIKSKQKRLEKELEKAKAEPVKPEY 275
Cdd:PRK11147 544 KEEAAAPKAETVKR----SSKKLSYKL------QRELEQLPQLLEDLEAEIEALQAQVADADF 596
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
292-499 |
8.74e-28 |
|
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: 111.49 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIdgedvrkeprEARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvFDLPLEQTPEE-------LFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILDEP 433
Cdd:COG4555 82 E-RGLYDRLTVREniryfaeLYGLFDEELKKRIEELIELLGLEEFL-DRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 434 TNHLDLPSREQLEETLSQY---GGTLLAVSHDRYFLEKTTNsKLVISDNG--IDKQLNDVPTERNEREELR 499
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCD-RVVILHKGkvVAQGSLDELREEIGEENLE 229
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-159 |
2.61e-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: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETA---- 76
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGyvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SYSFADQTP-----------------------AEKKLLEKW--RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLL 126
Cdd:COG1121 83 RAEVDWDFPitvrdvvlmgrygrrglfrrpsrADREAVDEAleRVGLEDLAdrpigELSGGQQQRVLLARALAQDPDLLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 127 LDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:COG1121 163 LDEPFAGVDaatEEALYELLRELRREGKTILVVTHD 198
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
292-462 |
2.89e-27 |
|
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: 110.52 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--------SPSA---NIGYLT 359
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGlLKPSSGEVLLdgrdlaslSRRElarRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QE---VFDLpleqTPEEL-----------FDNETYKARGHVQSLMRHLGfTASQWTEPIKHMSMGERVKCKL-MAyILEE 424
Cdd:COG1120 82 QEppaPFGL----TVRELvalgryphlglFGRPSAEDREAVEEALERTG-LEHLADRPVDELSGGERQRVLIaRA-LAQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 425 KDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLarerGRTVVMVLHD 197
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
291-461 |
4.35e-27 |
|
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: 109.79 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII--------------LGQETAEGSVW-VSPsaNI 355
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlFGERRGGEDVWeLRK--RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQEVF-DLPLEQTPEE-----------LFDNETYKARGHVQSLMRHLGFT--ASQwtePIKHMSMGERVKC----KL 417
Cdd:COG1119 81 GLVSPALQlRFPRDETVLDvvlsgffdsigLYREPTDEQRERARELLELLGLAhlADR---PFGTLSQGEQRRVliarAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 418 MAyileEKDVLILDEPTNHLDLPSREQLEETLSQYGG----TLLAVSH 461
Cdd:COG1119 158 VK----DPELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-175 |
5.46e-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: 108.32 E-value: 5.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLT--VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK--------------- 67
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLvdGKDLTklslkelrrkvglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 --------MTMVEQETAsysFA------DQTPAEKKLLE----------KWRVPvrdfQQLSGGEKLKARLAKGLSVDAD 123
Cdd:cd03225 82 qnpddqffGPTVEEEVA---FGlenlglPEEEIEERVEEalelvgleglRDRSP----FTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 124 LLLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-197 |
6.42e-27 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 114.45 E-value: 6.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLT-------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQetasy 78
Cdd:PRK11819 320 LGDKVIEAENLSksfgdrlLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIkIGETVKLAYVDQ----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 sFADQTPAEKKLLE------------KWRVPVRDF----------QQ-----LSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:PRK11819 395 -SRDALDPNKTVWEeisggldiikvgNREIPSRAYvgrfnfkggdQQkkvgvLSGGERNRLHLAKTLKQGGNVLLLDEPT 473
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 132 NHLDESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE-FKGNYSGYMKFReKKRL 197
Cdd:PRK11819 474 NDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSQVEwFEGNFQEYEEDK-KRRL 539
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
293-478 |
1.06e-26 |
|
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: 105.79 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSPsanigyltQEVFDLPLEQtp 371
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDG--------KDIAKLPLEE-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 372 eelfdnetykarghvqsLMRHLGFtasqwtepIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:cd00267 71 -----------------LRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 452 Y---GGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:cd00267 126 LaeeGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-175 |
3.84e-26 |
|
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: 105.64 E-value: 3.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETAS---YS-- 79
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRrlaYLgh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 ----FADQTPAE------------------KKLLEKW------RVPVRdfqQLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:COG4133 83 adglKPELTVREnlrfwaalyglradreaiDEALEAVglaglaDLPVR---QLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 132 NHLDESSLQFLIQQLKSYR---GTVILVSHDRyfLDEAATKIWSLED 175
Cdd:COG4133 160 TALDAAGVALLAELIAAHLargGAVLLTTHQP--LELAAARVLDLGD 204
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
293-462 |
3.85e-26 |
|
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: 104.82 E-value: 3.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWvspsanigyltqeVFDLPLEQTP 371
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGlLKPSSGEIL-------------LDGKDLASLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 372 EElfdnETYKARGHVQSLMRHLGfTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:cd03214 68 PK----ELARKIAYVPQALELLG-LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170
....*....|....*
gi 1732943882 452 Y----GGTLLAVSHD 462
Cdd:cd03214 143 LarerGKTVVMVLHD 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-159 |
2.86e-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: 103.38 E-value: 2.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-------FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTM-------VEQ-ETAS 77
Cdd:cd03235 1 EVEDLTVsygghpvLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKerkrigyVPQrRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 78 YSF-----------------------------ADQTPAEKKLLEKWRvpvRDFQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:cd03235 81 RDFpisvrdvvlmglyghkglfrrlskadkakVDEALERVGLSELAD---RQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 129 EPTNHLD---ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:cd03235 158 EPFAGVDpktQEDIYELLRELRREGMTILVVTHD 191
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
293-462 |
3.61e-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: 103.38 E-value: 3.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSP------SANIGYLTQ--EV- 362
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGkplekeRKRIGYVPQrrSId 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 FDLPLeqTPEELfdnetykarghVQS-LMRHLGF----TASQWTE----------------PIKHMSMGERvKCKLMAYI 421
Cdd:cd03235 81 RDFPI--SVRDV-----------VLMgLYGHKGLfrrlSKADKAKvdealervglseladrQIGELSGGQQ-QRVLLARA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 422 L-EEKDVLILDEPTNHLDLPSREQLEETLSQ---YGGTLLAVSHD 462
Cdd:cd03235 147 LvQDPDLLLLDEPFAGVDPKTQEDIYELLRElrrEGMTILVVTHD 191
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-168 |
6.53e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 101.49 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETasysfadqt 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 paeKKLLEKWRVPVRDFQ-------------QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKS 148
Cdd:cd03229 72 ---PPLRRRIGMVFQDFAlfphltvlenialGLSGGQQQRVALARALAMDPDVLLLDEPTSALDpitRREVRALLKSLQA 148
|
170 180
....*....|....*....|.
gi 1732943882 149 YRG-TVILVSHDryfLDEAAT 168
Cdd:cd03229 149 QLGiTVVLVTHD---LDEAAR 166
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-180 |
6.88e-25 |
|
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: 103.40 E-value: 6.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI-----------KMTMVEQE 74
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEdvrkeprearrQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASYSF----------------ADQTPAEK-----KLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:COG4555 83 RGLYDRltvreniryfaelyglFDEELKKRieeliELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 134 LD-ESSLQF--LIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG4555 163 LDvMARRLLreILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVA 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
10-300 |
1.02e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 108.33 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 10 VSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-LRQDIKMTMVEQETASYSFADQTP--- 85
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRADESPlqh 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 86 ----AEKKLLEKWRVPVRDF-----------QQLSGGEKlkARLAKGLSV--DADLLLLDEPTNHLDESSLQFLIQQLKS 148
Cdd:PRK10636 398 larlAPQELEQKLRDYLGGFgfqgdkvteetRRFSGGEK--ARLVLALIVwqRPNLLLLDEPTNHLDLDMRQALTEALID 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 149 YRGTVILVSHDRYFLDEAATKIWSLEDQTLIEFKGNYSGYmkfrekkrltqqreyekQQKMVeriEAQMNELASWSKKAH 228
Cdd:PRK10636 476 FEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY-----------------QQWLS---DVQKQENQTDEAPKE 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 229 DQSTKKEGFKEYHRVKAK-RTDAQIKSKQ-KRLEKELEKAKAEPVKPEYTVHFS--IDTSKKTG-KRFLEVQNITKA 300
Cdd:PRK10636 536 NNANSAQARKDQKRREAElRTQTQPLRKEiARLEKEMEKLNAQLAQAEEKLGDSelYDQSRKAElTACLQQQASAKS 612
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
5-175 |
8.32e-24 |
|
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: 98.22 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTM 70
Cdd:cd03228 1 IEFKNVSfsYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILidGVDLRdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETasYSFADqtpaekkllekwrvPVRDfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR 150
Cdd:cd03228 81 VPQDP--FLFSG--------------TIRE-NILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
|
170 180
....*....|....*....|....*..
gi 1732943882 151 G--TVILVSHdRYFLDEAATKIWSLED 175
Cdd:cd03228 144 KgkTVIVIAH-RLSTIRDADRIIVLDD 169
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-180 |
1.68e-23 |
|
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: 104.08 E-value: 1.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQdiKM 68
Cdd:COG4987 334 LELEDVSfrYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdlrdldeddLRR--RI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVEQETASYS--------FADQTPAEKKL--------LEKWrvpVRDF------------QQLSGGEKlkARL--AKGL 118
Cdd:COG4987 412 AVVPQRPHLFDttlrenlrLARPDATDEELwaalervgLGDW---LAALpdgldtwlgeggRRLSGGER--RRLalARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 119 SVDADLLLLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLADLLEALAgrTVLLITHRLAGL-ERMDRILVLEDGRIVE 549
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
293-478 |
2.27e-23 |
|
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: 97.92 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAF--GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSP-----------SANIGYL 358
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVLVDGkdltklslkelRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQ-------------EV-FDLPLEQTPEElfdnetyKARGHVQSLMRHLGFtASQWTEPIKHMSMGERVKCKLMAYILEE 424
Cdd:cd03225 81 FQnpddqffgptveeEVaFGLENLGLPEE-------EIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 425 KDVLILDEPTNHLDLPSREQLEE---TLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLEllkKLKAEGKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-166 |
5.04e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 97.83 E-value: 5.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RQDIK--MTMVEQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ETASYSF---------------ADQTPAEKK---------LLEKWRVPVRdfqQLSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:COG1131 81 EPALYPDltvrenlrffarlygLPRKEARERidellelfgLTDAADRKVG---TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 130 PTNHLD-ESSLQF--LIQQLKSYRGTVILVSHDryfLDEA 166
Cdd:COG1131 158 PTSGLDpEARRELweLLRELAAEGKTVLLSTHY---LEEA 194
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
292-478 |
9.29e-23 |
|
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: 97.02 E-value: 9.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPSA---NIGYL 358
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVdgkditkkNLRElrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFDLPLEQT--------PEEL-FDNETYKARghVQSLMRHLGFTAsQWTEPIKHMSMGERvkcKL--MAYILE-EKD 426
Cdd:COG1122 81 FQNPDDQLFAPTveedvafgPENLgLPREEIRER--VEEALELVGLEH-LADRPPHELSGGQK---QRvaIAGVLAmEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 427 VLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDD 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-179 |
1.05e-22 |
|
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: 96.63 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKD-LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDIKM- 68
Cdd:COG1122 1 IELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVlvdgkditkknlreLRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 ----------TMVEQETAsysFA----DQTPAE-----KKLLEkwRVPVRDF-----QQLSGGEKLKARLAKGLSVDADL 124
Cdd:COG1122 81 fqnpddqlfaPTVEEDVA---FGpenlGLPREEirervEEALE--LVGLEHLadrppHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 125 LLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
292-480 |
2.16e-22 |
|
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: 95.36 E-value: 2.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV---------SPSANIGYLtqe 361
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFdgksyqkniEALRRIGAL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 vFDLPleqtpeELFDNET------YKARGH------VQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLI 429
Cdd:cd03268 78 -IEAP------GFYPNLTarenlrLLARLLgirkkrIDEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 430 LDEPTNHLDLPSREQLEET---LSQYGGTLLAVSHDRYFLEKTTnSKLVISDNG 480
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVA-DRIGIINKG 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
9-159 |
6.11e-22 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 94.49 E-value: 6.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVF--KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--QDI-------------KMTMV 71
Cdd:cd03257 8 SVSFPTGGGSVKalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFdgKDLlklsrrlrkirrkEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 72 EQ-----------------ETASYSFADQTPAEKK---LLEKWRVP-VRDF-----QQLSGGEKLKARLAKGLSVDADLL 125
Cdd:cd03257 88 FQdpmsslnprmtigeqiaEPLRIHGKLSKKEARKeavLLLLVGVGlPEEVlnrypHELSGGQRQRVAIARALALNPKLL 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 126 LLDEPTNHLDeSSLQF----LIQQLKSYRG-TVILVSHD 159
Cdd:cd03257 168 IADEPTSALD-VSVQAqildLLKKLQEELGlTLLFITHD 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
277-477 |
6.14e-22 |
|
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: 94.71 E-value: 6.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 277 VHFSIDTSKKTGKRFLEVQNITK-AFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG--QETaEGSVWVS--- 350
Cdd:cd03267 6 LSKSYRVYSKEPGLIGSLKSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGllQPT-SGEVRVAglv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 351 PS-------ANIGYL----TQEVFDLPLEQTPE---ELFDNETYKARGHVQSLMRHLGFTASQWTePIKHMSMGERVKCK 416
Cdd:cd03267 85 PWkrrkkflRRIGVVfgqkTQLWWDLPVIDSFYllaAIYDLPPARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 417 LMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHDRYFLEKTTNSKLVIS 477
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-166 |
9.45e-22 |
|
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: 93.69 E-value: 9.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKD--LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQDIKMTMVEQ 73
Cdd:cd03293 1 LEVRNVSktYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ETA-------------SYSFADQTPAEKK-----LLEKwrVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:cd03293 81 QDAllpwltvldnvalGLELQGVPKAEAReraeeLLEL--VGLSGFenaypHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 131 TNHLDE---SSLQ-FLIQQLKSYRGTVILVSHDryfLDEA 166
Cdd:cd03293 159 FSALDAltrEQLQeELLDIWRETGKTVLLVTHD---IDEA 195
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
4-166 |
1.39e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.39 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVS--YEVK--DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQDIKMTMVE 72
Cdd:COG1116 7 ALELRGVSkrFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETASY-------------SFADQTPAEKK-----LLEkwRVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:COG1116 87 QEPALLpwltvldnvalglELRGVPKAERRerareLLE--LVGLAGFedaypHQLSGGMRQRVAIARALANDPEVLLMDE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 130 PTNHLDE---SSLQFLIQQL-KSYRGTVILVSHDryfLDEA 166
Cdd:COG1116 165 PFGALDAltrERLQDELLRLwQETGKTVLFVTHD---VDEA 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-179 |
2.31e-21 |
|
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: 92.58 E-value: 2.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--QDIKMTMVEQETASYSFad 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgRDVTGVPPERRNIGMVF-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 QTPA--------------------------EKKLLEKWRVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:cd03259 79 QDYAlfphltvaeniafglklrgvpkaeirARVRELLELVGLEGLLnryphELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 132 NHLDESSLQFLIQQLKSYRG----TVILVSHDryfLDEAatkiWSLEDQTLI 179
Cdd:cd03259 159 SALDAKLREELREELKELQRelgiTTIYVTHD---QEEA----LALADRIAV 203
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
292-480 |
5.88e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.50 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF--GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPS---ANIGY 357
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPtSGSVLLdgtdirqlDPAdlrRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVFdlpleqtpeeLF-----DNETYK---------------------ARGHVQSLMRHLGftasqwtEPIKHMSMGE 411
Cdd:cd03245 83 VPQDVT----------LFygtlrDNITLGapladderilraaelagvtdfVNKHPNGLDLQIG-------ERGRGLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 412 RVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHDRYFLEKTtnSKLVISDNG 480
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLV--DRIIVMDSG 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-466 |
6.57e-21 |
|
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: 96.02 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAPAQGQIL-------------------- 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 -----------------------RQDIK---MTMVEQETASYsfADQT--------------PAEK------KLLEKWRV 96
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklRRRIRkriAIMLQRTFALY--GDDTvldnvlealeeigyEGKEavgravDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 97 PVRDF---QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQF----LIQQLKSYRGTVILVSHDRYFLDEAATK 169
Cdd:TIGR03269 159 SHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 170 -IWsLEDQTLIEfKGNYSgymkfrekkrltqqreyekqqkmvERIEAQMnelaswskkahdqstkkEGFKEYhrvkakrt 248
Cdd:TIGR03269 239 aIW-LENGEIKE-EGTPD------------------------EVVAVFM-----------------EGVSEV-------- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 249 daqikSKQKRLEKELEKAKAEPVKPEYtvhFSIDtskktgkrflevQNITKAfgertlFKNTNFTIQHGEKVAIIGPNGS 328
Cdd:TIGR03269 268 -----EKECEVEVGEPIIKVRNVSKRY---ISVD------------RGVVKA------VDNVSLEVKEGEIFGIVGTSGA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 329 GKTTLLKIILG-QETAEGSVWV------------------SPSANIGYLTQEvFDLPLEQT-------------PEELfd 376
Cdd:TIGR03269 322 GKTTLSKIIAGvLEPTSGEVNVrvgdewvdmtkpgpdgrgRAKRYIGILHQE-YDLYPHRTvldnlteaiglelPDEL-- 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 377 netykARGHVQSLMRHLGFTASQWTEPIK----HMSMGERVKCKLMAYILEEKDVLILDEPTNHLD-----------LPS 441
Cdd:TIGR03269 399 -----ARMKAVITLKMVGFDEEKAEEILDkypdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkvdvthsiLKA 473
|
570 580
....*....|....*....|....*
gi 1732943882 442 REQLEEtlsqyggTLLAVSHDRYFL 466
Cdd:TIGR03269 474 REEMEQ-------TFIIVSHDMDFV 491
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
292-478 |
6.81e-21 |
|
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: 89.94 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSpsaNIGYLTQEVFDLPLEQT 370
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILID---GEDLTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 PEELFDNetykarghvQSLMRHLgfTASQ-WTEPikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL 449
Cdd:cd03229 78 IGMVFQD---------FALFPHL--TVLEnIALG---LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALL 143
|
170 180 190
....*....|....*....|....*....|...
gi 1732943882 450 S----QYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:cd03229 144 KslqaQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-180 |
8.34e-21 |
|
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: 95.98 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEvKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI------------KMTM 70
Cdd:COG4988 337 IELEDVSfsYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrrQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQEtaSYSFA------------DQTPAE-KKLLEkwRVPVRDF-QQLSGGekLKARL---AKGLSV------------- 120
Cdd:COG4988 416 VPQN--PYLFAgtirenlrlgrpDASDEElEAALE--AAGLDEFvAALPDG--LDTPLgegGRGLSGgqaqrlalarall 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 121 -DADLLLLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG4988 490 rDAPLLLLDEPTAHLDAETEAEILQALRRLAKgrTVILITHRLALL-AQADRILVLDDGRIVE 551
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-166 |
9.42e-21 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 89.02 E-value: 9.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKmtmveqetasYSFAdqTPAekkllEKWRVPVRD 100
Cdd:cd03216 17 DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE----------VSFA--SPR-----DARRAGIAM 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 101 FQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD--ESSLQF-LIQQLKSyRG-TVILVSHdryFLDEA 166
Cdd:cd03216 80 VYQLSVGERQMVEIARALARNARLLILDEPTAALTpaEVERLFkVIRRLRA-QGvAVIFISH---RLDEV 145
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
302-476 |
1.03e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 96.01 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 302 GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSA-NIGYLTQEVFDLPL------------- 367
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQpaleyvidgdrey 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 EQTPEELFD-NE------------------TYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVL 428
Cdd:PRK10636 92 RQLEAQLHDaNErndghaiatihgkldaidAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 429 ILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVI 476
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHI 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-175 |
1.93e-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: 89.86 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVF--KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT-MVEQETASY- 78
Cdd:cd03255 1 IELKNLSktYGGGGEKVQalKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISkLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 ---------------------------SFADQTPAEKK-----LLEkwRVPVRDF-----QQLSGGEKLKARLAKGLSVD 121
Cdd:cd03255 81 rrhigfvfqsfnllpdltalenvelplLLAGVPKKERReraeeLLE--RVGLGDRlnhypSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 122 ADLLLLDEPTNHLD-ESSLQF--LIQQLKSYRG-TVILVSHDRyFLDEAATKIWSLED 175
Cdd:cd03255 159 PKIILADEPTGNLDsETGKEVmeLLRELNKEAGtTIVVVTHDP-ELAEYADRIIELRD 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
293-481 |
2.28e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 89.24 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAFGERT-LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSV-----WVSPSA---NIGYLTQEV 362
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKESSGSIllngkPIKAKErrkSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 -FDLPLEQTPEELF--DNETYKARGHVQSLMRHLGFtasqWTEPIKH---MSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:cd03226 81 dYQLFTDSVREELLlgLKELDAGNEQAETVLKDLDL----YALKERHplsLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 437 LDLPSREQLEE---TLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGI 481
Cdd:cd03226 157 LDYKNMERVGElirELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
287-462 |
2.92e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 90.53 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 287 TGKRFLEVQNITKAF----GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV------SPSANI 355
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVLVdgkpvtGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQE--------VFD---LPLEQ---TPEElfdnetykARGHVQSLMRHLGFT--ASQWtePiKHMSMGERVKCKLM- 418
Cdd:COG1116 83 GVVFQEpallpwltVLDnvaLGLELrgvPKAE--------RRERARELLELVGLAgfEDAY--P-HQLSGGMRQRVAIAr 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 419 AYILeEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:COG1116 152 ALAN-DPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-180 |
3.60e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 94.13 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTM 70
Cdd:COG2274 474 IELENVSfrYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidGIDLRqidpaslrrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETASYS--------FADQTPAEKKLLE--KwRVPVRDF----------------QQLSGGEKLKARLAKGLSVDADL 124
Cdd:COG2274 554 VLQDVFLFSgtirenitLGDPDATDEEIIEaaR-LAGLHDFiealpmgydtvvgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 125 LLLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLdEAATKIWSLEDQTLIE 180
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRIVE 689
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-167 |
4.32e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQ-DIKMTMVEQETAsysFADQTPAE-KKLLE--- 92
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVPQRSE---VPDSLPLTvRDLVAmgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 93 -----KWRVPVRD---------------------FQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQL 146
Cdd:NF040873 83 warrgLWRRLTRDdraavddalervgladlagrqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALL 162
|
170 180
....*....|....*....|....
gi 1732943882 147 KSYRG---TVILVSHDryfLDEAA 167
Cdd:NF040873 163 AEEHArgaTVVVVTHD---LELVR 183
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
15-177 |
4.39e-20 |
|
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: 89.03 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 15 KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------------RQdikMTMVEQETASY- 78
Cdd:COG4778 22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdggwvdlaqaspRE---ILALRRRTIGYv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 S-------------------FADQTPAE------KKLLEK-------WRVPVRDFqqlSGGEKLKARLAKGLSVDADLLL 126
Cdd:COG4778 99 SqflrviprvsaldvvaeplLERGVDREeararaRELLARlnlperlWDLPPATF---SGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 127 LDEPTNHLDESSLQF---LIQQLKSyRGTVIL-VSHDRYFLDEAATKIWSLEDQT 177
Cdd:COG4778 176 LDEPTASLDAANRAVvveLIEEAKA-RGTAIIgIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
9-158 |
4.72e-20 |
|
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: 87.75 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETASY-SFADQTPA- 86
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLiSVLNQRPYl 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 87 -EKKLLEKWRvpvrdfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESS-LQFLIQQLKSyrGTVILVSH 158
Cdd:cd03247 87 fDTTLRNNLG------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpitERQlLSLIFEVLKD--KTLIWITH 155
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
292-463 |
6.20e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.36 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVwvspsanigyltqevfdlpleqt 370
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPdSGRI----------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 peeLFDNETYKARGHVQS-----------LMRHL--------GFTASQWTEP-IKhmsmgERVKCKLMAYILE------- 423
Cdd:COG1118 60 ---VLNGRDLFTNLPPRErrvgfvfqhyaLFPHMtvaeniafGLRVRPPSKAeIR-----ARVEELLELVQLEgladryp 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 424 -------------------EKDVLILDEPTNHLDLPSREQLE----ETLSQYGGTLLAVSHDR 463
Cdd:COG1118 132 sqlsggqrqrvalaralavEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQ 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-181 |
7.58e-20 |
|
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: 88.88 E-value: 7.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI------------ 66
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdGQDItglsekelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -KMTMVEQETASYS--------------FADQTPAEKK-----LLEkwRVPVRDFQ-----QLSGGEKLKARLAKGLSVD 121
Cdd:COG1127 82 rRIGMLFQGGALFDsltvfenvafplreHTDLSEAEIRelvleKLE--LVGLPGAAdkmpsELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 122 ADLLLLDEPTNHLD-ESSLQF--LIQQL-KSYRGTVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:COG1127 160 PEILLYDEPTAGLDpITSAVIdeLIRELrDELGLTSVVVTHD---LDSAfaiADRVAVLADGKIIAE 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-132 |
7.97e-20 |
|
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: 86.16 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 20 FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT------------MVEQET------------ 75
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdderkslrkeigYVFQDPqlfprltvrenl 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 --ASYSFADQTPAEKKLLEKW-----------RVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTN 132
Cdd:pfam00005 81 rlGLLLKGLSKREKDARAEEAleklglgdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-178 |
1.50e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.12 E-value: 1.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLT--VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILrqdikmtmveqetasysfADQT 84
Cdd:cd03246 3 VENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVR------------------LDGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 PAEKKLLEKWRVPVRDFQQ-------------LSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKS 148
Cdd:cd03246 65 DISQWDPNELGDHVGYLPQddelfsgsiaeniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDvegERALNQAIAALKA 144
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 149 YRGTVILVSHdRYFLDEAATKIWSLEDQTL 178
Cdd:cd03246 145 AGATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
6-167 |
1.56e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 87.50 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTvfKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI--------KMTMVEQET 75
Cdd:COG3840 3 RLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILwnGQDLtalppaerPVSMLFQEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ---ASYSFADQ-----------TPAEKKLLEKW--RVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHL 134
Cdd:COG3840 81 nlfPHLTVAQNiglglrpglklTAEQRAQVEQAleRVGLAGLldrlpGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 135 D----ESSLQFLIQQLKSYRGTVILVSHDryfLDEAA 167
Cdd:COG3840 161 DpalrQEMLDLVDELCRERGLTVLMVTHD---PEDAA 194
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-181 |
1.65e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 87.62 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDL---APAQGQIL--RQDI------------K 67
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrlNDLipgAPDEGEVLldGKDIydldvdvlelrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVEQETA----------SYSFADQTPAEKKLLEKwRVPVR--------------DFQQLSGGEKLKARLAKGLSVDAD 123
Cdd:cd03260 83 VGMVFQKPNpfpgsiydnvAYGLRLHGIKLKEELDE-RVEEAlrkaalwdevkdrlHALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 124 LLLLDEPTNHLDESS---LQFLIQQLKSyRGTVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:cd03260 162 VLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHN---MQQAarvADRTAFLLNGRLVEF 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
292-462 |
2.03e-19 |
|
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: 87.14 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG----ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVS------PSANIGYLTQ 360
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDgepvtgPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 E--------VFD---LPLEQTpeelfDNETYKARGHVQSLMRHLGFTASQWTEPiKHMS--MGERVkCKLMAYILeEKDV 427
Cdd:cd03293 81 QdallpwltVLDnvaLGLELQ-----GVPKAEARERAEELLELVGLSGFENAYP-HQLSggMRQRV-ALARALAV-DPDV 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 428 LILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
292-461 |
2.45e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 86.57 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG--QETaEGSVWV-------SPSANIGYLTQEV 362
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiiLPD-SGEVLFdgkpldiAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 FDLPLEQTPE------ELFDNETYKARGHVQSLMRHLGFTAsQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:cd03269 80 GLYPKMKVIDqlvylaQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180
....*....|....*....|....*...
gi 1732943882 437 LDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:cd03269 159 LDPVNVELLKDVIRELaraGKTVILSTH 186
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
5-159 |
4.13e-19 |
|
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: 87.18 E-value: 4.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RQDIKMTMVE 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrrARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETAS------------------YSFADQTPAEKKLLEKWRVPV-------RDFQQLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:TIGR03873 82 QDSDTavpltvrdvvalgriphrSLWAGDSPHDAAVVDRALARTelshladRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 128 DEPTNHLDESSlQF----LIQQLKSYRGTVILVSHD 159
Cdd:TIGR03873 162 DEPTNHLDVRA-QLetlaLVRELAATGVTVVAALHD 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-159 |
5.44e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 86.75 E-value: 5.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---------------------LRQDI 66
Cdd:PRK13548 6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngrpladwspaelarrravLPQHS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 KMTM---VEQ--ETASYSFADQTPAEKKLLEKW--RVPV-----RDFQQLSGGEKLKARLAKGL----SVDAD--LLLLD 128
Cdd:PRK13548 86 SLSFpftVEEvvAMGRAPHGLSRAEDDALVAAAlaQVDLahlagRDYPQLSGGEQQRVQLARVLaqlwEPDGPprWLLLD 165
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 129 EPTNHLD----ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK13548 166 EPTSALDlahqHHVLRLARQLAHERGLAVIVVLHD 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-175 |
5.73e-19 |
|
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: 85.39 E-value: 5.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------RQDIKMT-MVEQET 75
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpikaKERRKSIgYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ASYSF-----------ADQTPAEK-------KLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES 137
Cdd:cd03226 81 DYQLFtdsvreelllgLKELDAGNeqaetvlKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 138 SLQF---LIQQLKSYRGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03226 161 NMERvgeLIRELAAQGKAVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-180 |
6.95e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 6.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVK-DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RQDI-----K 67
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsrlkRREIpylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVeqetasysFADQtpaekKLLEKWRV-------------PVRDFQ---------------------QLSGGEKLKAR 113
Cdd:COG2884 81 IGVV--------FQDF-----RLLPDRTVyenvalplrvtgkSRKEIRrrvrevldlvglsdkakalphELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 114 LAKGLSVDADLLLLDEPTNHLD-ESSLQF--LIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDpETSWEImeLLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-164 |
8.58e-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: 85.33 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSY-----EVKDLtvfKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTM--------- 70
Cdd:cd03245 3 IEFRNVSFsypnqEIPAL---DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQldpadlrrn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 ---VEQE------------TASYSFADqtpaEKKLLEKWRVP-VRDF----------------QQLSGGEKLKARLAKGL 118
Cdd:cd03245 80 igyVPQDvtlfygtlrdniTLGAPLAD----DERILRAAELAgVTDFvnkhpngldlqigergRGLSGGQRQAVALARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 119 SVDADLLLLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLD 164
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLD 203
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-181 |
8.99e-19 |
|
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: 85.63 E-value: 8.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI-------------KMT 69
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 MVEQETA---SYSFAD----------QTPAE---KKLLEKW-RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:cd03261 81 MLFQSGAlfdSLTVFEnvafplrehtRLSEEeirEIVLEKLeAVGLRGAEdlypaELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 128 DEPTNHLDE-SSLQF--LIQQLK-SYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:cd03261 161 DEPTAGLDPiASGVIddLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
18-190 |
1.00e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 89.92 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQ-DIKMTMVEQETASYSFADQTP----------- 85
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSaKVRMAVFSQHHVDGLDLSSNPllymmrcfpgv 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 86 AEKKL---LEKWRV----PVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSH 158
Cdd:PLN03073 603 PEQKLrahLGSFGVtgnlALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSH 682
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 159 DRYFLDEAATKIWSLEDQTLIEFKGNYSGYMK 190
Cdd:PLN03073 683 DEHLISGSVDELWVVSEGKVTPFHGTFHDYKK 714
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
292-461 |
1.03e-18 |
|
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: 83.59 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERT--LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV--------SPSA---NIGY 357
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLyDPTSGEILIdgvdlrdlDLESlrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVFdlpleqtpeeLFDnetykarghvQSLMRHLgftasqwtepikhMSMGERvkcKLMAY---ILEEKDVLILDEPT 434
Cdd:cd03228 81 VPQDPF----------LFS----------GTIRENI-------------LSGGQR---QRIAIaraLLRDPPILILDEAT 124
|
170 180
....*....|....*....|....*....
gi 1732943882 435 NHLDLPSREQLEETLSQYGG--TLLAVSH 461
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-159 |
1.05e-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: 85.18 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI------------------------KMTM 70
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLfdGEDItglppheiarlgigrtfqiprlfpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VE--------QETASYSFADQTPAEKKLLEK-----WRV---PVRDFQ--QLSGGEKLKARLAKGLSVDADLLLLDEPT- 131
Cdd:cd03219 93 LEnvmvaaqaRTGSGLLLARARREEREARERaeellERVglaDLADRPagELSYGQQRRLEIARALATDPKLLLLDEPAa 172
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 132 --NHLDESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:cd03219 173 glNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-180 |
1.12e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.10 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKD----LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIKmTMVEQE 74
Cdd:COG1136 1 MSPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLidGQDIS-SLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASY----------------------------SFADQTPAE-----KKLLEkwRVPVRDF-----QQLSGGEKLKARLAK 116
Cdd:COG1136 80 LARLrrrhigfvfqffnllpeltalenvalplLLAGVSRKErreraRELLE--RVGLGDRldhrpSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 117 GLSVDADLLLLDEPTNHLD-ESSLQF--LIQQL-KSYRGTVILVSHDRyFLDEAATKIWSLEDQTLIE 180
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDsKTGEEVleLLRELnRELGTTIVMVTHDP-ELAARADRVIRLRDGRIVS 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
292-463 |
1.40e-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: 84.49 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEILidgrdvtgVPPERrNIGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFD---LPLEqtpEELFDNETYKARghVQSLMRHLGFTAsQWTEPIKHMSMGERVKCKLMAYILEEKDVLIL 430
Cdd:cd03259 81 yalfphltVAEniaFGLK---LRGVPKAEIRAR--VRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 431 DEPTNHLDLPSREQLEETLS----QYGGTLLAVSHDR 463
Cdd:cd03259 155 DEPLSALDAKLREELREELKelqrELGITTIYVTHDQ 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
300-462 |
1.75e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 300 AFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSPSANIGYLTQ--EVFD-LPLeqTPEELF 375
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVRRAGGARVAYVPQrsEVPDsLPL--TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 376 DNETYKARGHVQSLMRHLGFTASQWTE----------PIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQL 445
Cdd:NF040873 79 AMGRWARRGLWRRLTRDDRAAVDDALErvgladlagrQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|
gi 1732943882 446 EETLSQY---GGTLLAVSHD 462
Cdd:NF040873 159 IALLAEEharGATVVVVTHD 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
292-470 |
1.95e-18 |
|
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: 84.08 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG----ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPSA----- 353
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVRVdgtdisklSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 --NIGYLTQE--------VFD---LPLEQTPEElfdNETYKARGHvqSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAY 420
Cdd:cd03255 81 rrHIGFVFQSfnllpdltALEnveLPLLLAGVP---KKERRERAE--ELLERVGLGDRL-NHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHDRYFLEKTT 470
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETGKEVMELLrelnKEAGTTIVVVTHDPELAEYAD 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
293-462 |
2.36e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.91 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAF-----------GERTLF----------KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG--QETAeGSVWV 349
Cdd:COG4586 3 EVENLSKTYrvyekepglkgALKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGilVPTS-GEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 ---SPS-------ANIGYL----TQEVFDLPLEQTpEELF------DNETYKARghVQSLMRHLGFtASQWTEPIKHMSM 409
Cdd:COG4586 82 lgyVPFkrrkefaRRIGVVfgqrSQLWWDLPAIDS-FRLLkaiyriPDAEYKKR--LDELVELLDL-GELLDTPVRQLSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 410 GERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrerGTTILLTSHD 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-167 |
2.72e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI------------KMTMVE 72
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETA-SYSF-----------------ADQTPAEKKLLEKW--RVPV-----RDFQQLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:PRK09536 84 QDTSlSFEFdvrqvvemgrtphrsrfDTWTETDRAAVERAmeRTGVaqfadRPVTSLSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 128 DEPTNHLDessLQFLIQQLKSYR------GTVILVSHDryfLDEAA 167
Cdd:PRK09536 164 DEPTASLD---INHQVRTLELVRrlvddgKTAVAAIHD---LDLAA 203
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
9-173 |
2.86e-18 |
|
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: 87.73 E-value: 2.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDlTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQET--ASYSFADQTP- 85
Cdd:TIGR02857 328 SVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrDQIAWVPQHPf 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 86 ------AEKKLLEK------------WRVPVRDFQQ----------------LSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:TIGR02857 407 lfagtiAENIRLARpdasdaeirealERAGLDEFVAalpqgldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 132 NHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLdEAATKIWSL 173
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
292-462 |
3.77e-18 |
|
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: 87.97 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERT--LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPSA---NIGY 357
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPtSGRILIdgidlrqiDPASlrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVFdlpleqtpeeLF-----DNETYKARG----HVQSLMRHLGFtasqwTEPIKHMSMGervkcklMAYILEEK--- 425
Cdd:COG2274 554 VLQDVF----------LFsgtirENITLGDPDatdeEIIEAARLAGL-----HDFIEALPMG-------YDTVVGEGgsn 611
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 426 -------------------DVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHD 462
Cdd:COG2274 612 lsggqrqrlaiarallrnpRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
23-179 |
5.06e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 5.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQILRQDIKMT------------MVEQET--------------- 75
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARM-AGLLPGQGEILLNGRPLSdwsaaelarhraYLSQQQsppfampvfqylalh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ----ASYSFADQTPAE-------KKLLEkwrvpvRDFQQLSGGEKLKARLAK-------GLSVDADLLLLDEPTNHLD-- 135
Cdd:COG4138 94 qpagASSEAVEQLLAQlaealglEDKLS------RPLTQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDva 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 136 -ESSLQFLIQQLKSYRGTVILVSHD-----RYfldeaATKIWSLEDQTLI 179
Cdd:COG4138 168 qQAALDRLLRELCQQGITVVMSSHDlnhtlRH-----ADRVWLLKQGKLV 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-164 |
5.21e-18 |
|
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: 82.57 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLI--HNDLAPAQGQIL--RQDIK-MTMVEQETASYSF 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILfkGEDITdLPPEERARLGIFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ADQTPAEkkllekwrVP---VRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRG- 151
Cdd:cd03217 82 AFQYPPE--------IPgvkNADFlryvnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREe 153
|
170
....*....|....*
gi 1732943882 152 --TVILVSHDRYFLD 164
Cdd:cd03217 154 gkSVLIITHYQRLLD 168
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
292-349 |
1.03e-17 |
|
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: 82.72 E-value: 1.03e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV 349
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILV 64
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
292-462 |
1.71e-17 |
|
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: 81.40 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLF--KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVS----------PSANIGYL 358
Cdd:cd03263 1 LQIRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINgysirtdrkaARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQevFD-LPLEQTPEELFdnETY-KARGH--------VQSLMRHLGFTaSQWTEPIKHMSMGErvKCKL---MAyILEEK 425
Cdd:cd03263 81 PQ--FDaLFDELTVREHL--RFYaRLKGLpkseikeeVELLLRVLGLT-DKANKRARTLSGGM--KRKLslaIA-LIGGP 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHD 462
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
292-462 |
2.36e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 81.24 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG----ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPSA----- 353
Cdd:COG1136 5 LELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVLIdgqdisslSERElarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 --NIGY----------LTqeVFD---LPLeqtpeeLFDNETYK-ARGHVQSLMRHLG------FTASQwtepikhMSMGE 411
Cdd:COG1136 85 rrHIGFvfqffnllpeLT--ALEnvaLPL------LLAGVSRKeRRERARELLERVGlgdrldHRPSQ-------LSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 412 R---------VKcklmayileEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:COG1136 150 QqrvaiaralVN---------RPKLILADEPTGNLDSKTGEEVLELLrelnRELGTTIVMVTHD 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-175 |
3.26e-17 |
|
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: 80.27 E-value: 3.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL---------RQDI-----KMT 69
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTIIidglkltddKKNInelrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 MVEQetaSYS-FADQT------------------PAEK---KLLEKwrVPVRDFQ-----QLSGGEKLKARLAKGLSVDA 122
Cdd:cd03262 80 MVFQ---QFNlFPHLTvlenitlapikvkgmskaEAEEralELLEK--VGLADKAdaypaQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 123 DLLLLDEPTNHLD----ESSLQfLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:cd03262 155 KVMLFDEPTSALDpelvGEVLD-VMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-159 |
3.27e-17 |
|
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: 81.39 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVK--DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT------------MVEQE 74
Cdd:COG1124 8 SVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrrrrkafrrrvqMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 -TAS-----------------YSFADQTPAEKKLLEK--------WRVPvrdfQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:COG1124 88 pYASlhprhtvdrilaeplriHGLPDREERIAELLEQvglppsflDRYP----HQLSGGQRQRVAIARALILEPELLLLD 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 129 EPTNHLDeSSLQF----LIQQLKSYRG-TVILVSHD 159
Cdd:COG1124 164 EPTSALD-VSVQAeilnLLKDLREERGlTYLFVSHD 198
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-158 |
3.34e-17 |
|
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: 81.28 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 3 EIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----------QDIK---- 67
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrggedvWELRkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 ---MTMVEQ-----------ETASYS----FADQTPAEKKLLEKW--RVPV-----RDFQQLSGGEKLKARLAKGLSVDA 122
Cdd:COG1119 82 lvsPALQLRfprdetvldvvLSGFFDsiglYREPTDEQRERARELleLLGLahladRPFGTLSQGEQRRVLIARALVKDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 123 DLLLLDEPTNHLDESSLQFLIQQLKSYRG----TVILVSH 158
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAegapTLVLVTH 201
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
292-468 |
3.43e-17 |
|
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: 84.43 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF--GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV-----------SPSANIGY 357
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPqSGSITLggvdlrdldedDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQE--VFDLPLEQ---------TPEELfdnetYKA----------RGHVQSLMRHLGFTASQwtepikhMSMGE----- 411
Cdd:COG4987 414 VPQRphLFDTTLREnlrlarpdaTDEEL-----WAAlervglgdwlAALPDGLDTWLGEGGRR-------LSGGErrrla 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 412 --RVkcklmayILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSHDRYFLEK 468
Cdd:COG4987 482 laRA-------LLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGLER 535
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
296-466 |
4.42e-17 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 84.17 E-value: 4.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 296 NITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSPSANIGYLTQE--------VFD-- 364
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDlEPSAGNVSLDPNERLGKLRQDqfafeeftVLDtv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 -------------------LPlEQTPE------EL------FDNETYKARGhvQSLMRHLGFTASQWTEPIKHMSMGERV 413
Cdd:PRK15064 86 imghtelwevkqerdriyaLP-EMSEEdgmkvaDLevkfaeMDGYTAEARA--GELLLGVGIPEEQHYGLMSEVAPGWKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 414 KCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSHDRYFL 466
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFL 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
292-462 |
7.45e-17 |
|
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: 79.85 E-value: 7.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWV--------SPSA------NIG 356
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIdgedisglSEAElyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 357 YLTQE--------VFD---LPLEQTpEELFDNETykaRGHVQSLMRHLGFTASQWTEPIKhMS--MGERVkcKLMAYILE 423
Cdd:cd03261 81 MLFQSgalfdsltVFEnvaFPLREH-TRLSEEEI---REIVLEKLEAVGLRGAEDLYPAE-LSggMKKRV--ALARALAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 424 EKDVLILDEPTNHLDlPSR----EQLEETLSQ-YGGTLLAVSHD 462
Cdd:cd03261 154 DPELLLYDEPTAGLD-PIAsgviDDLIRSLKKeLGLTSIMVTHD 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
292-462 |
8.11e-17 |
|
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: 79.47 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLF----KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSP--------------S 352
Cdd:cd03257 2 LEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGlLKPTSGSIIFDGkdllklsrrlrkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 353 ANIGYLTQE----------VFDLpLEQTPEELFDNETYKARGHVQSL-MRHLGFTASQWTEPIKHMSMGE--RVkCKLMA 419
Cdd:cd03257 82 KEIQMVFQDpmsslnprmtIGEQ-IAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQrqRV-AIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 420 YILEEKdVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:cd03257 160 LALNPK-LLIADEPTSALDVSVQAQILDLLkklqEELGLTLLFITHD 205
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-159 |
8.14e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.16 E-value: 8.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---------------------LRQDI 66
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVrlngrplaawspwelarrravLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 KMTM---VEQ------ETASYSFADQTPAEKKLLEkwRVPV-----RDFQQLSGGEKLKARLAKGL-----SVDAD--LL 125
Cdd:COG4559 85 SLAFpftVEEvvalgrAPHGSSAAQDRQIVREALA--LVGLahlagRSYQTLSGGEQQRVQLARVLaqlwePVDGGprWL 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 126 LLDEPTNHLD----ESSLQfLIQQLKSYRGTVILVSHD 159
Cdd:COG4559 163 FLDEPTSALDlahqHAVLR-LARQLARRGGGVVAVLHD 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-159 |
9.24e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQD-IKMTMVEQE----- 74
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGkLRIGYVPQKlyldt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 ----TASYSF--------ADQTPAEKK-----LLEKwrvpvrDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-- 135
Cdd:PRK09544 81 tlplTVNRFLrlrpgtkkEDILPALKRvqaghLIDA------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDvn 154
|
170 180
....*....|....*....|....*.
gi 1732943882 136 -ESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK09544 155 gQVALYDLIDQLRRELDcAVLMVSHD 180
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-181 |
1.03e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 79.74 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYeVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------------ 62
Cdd:COG1134 24 LKELLLRRRRTR-REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEvngrvsallelgagfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 ---RQDIKMT-----MVEQETASY-----SFADqtpaekklLEKW-RVPVRDFqqlSGGekLKARLAKGLS--VDADLLL 126
Cdd:COG1134 103 ltgRENIYLNgrllgLSRKEIDEKfdeivEFAE--------LGDFiDQPVKTY---SSG--MRARLAFAVAtaVDPDILL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 127 LDEPTNHLDES----SLQFlIQQLKSYRGTVILVSHDRYFLDEAATK-IWsLEDQTLIEF 181
Cdd:COG1134 170 VDEVLAVGDAAfqkkCLAR-IRELRESGRTVIFVSHSMGAVRRLCDRaIW-LEKGRLVMD 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
9-164 |
1.05e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 79.23 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDL--APAQGQIlrqDIKMTMVEQETasySFADQTPA 86
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---DVPDNQFGREA---SLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 87 EKKLLEK--------------WRvpvRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFL---IQQL-KS 148
Cdd:COG2401 109 KGDFKDAvellnavglsdavlWL---RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVarnLQKLaRR 185
|
170
....*....|....*.
gi 1732943882 149 YRGTVILVSHDRYFLD 164
Cdd:COG2401 186 AGITLVVATHHYDVID 201
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
292-468 |
1.14e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.94 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPSA------NI 355
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVngqdlsrlKRREipylrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQE--------VFD---LPLEQTPeelFDNETYKARghVQSLMRHLGFTASQWTEPIkHMSMGE--RVkckLMAY-I 421
Cdd:COG2884 82 GVVFQDfrllpdrtVYEnvaLPLRVTG---KSRKEIRRR--VREVLDLVGLSDKAKALPH-ELSGGEqqRV---AIARaL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 422 LEEKDVLILDEPTNHLDlP--SRE--QLEETLSQYGGTLLAVSHDRYFLEK 468
Cdd:COG2884 153 VNRPELLLADEPTGNLD-PetSWEimELLEEINRRGTTVLIATHDLELVDR 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-180 |
1.19e-16 |
|
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: 79.16 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKD----LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL--RQDI---------- 66
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-NGLeRPTSGSVLvdGTDLtllsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 ---KMTMVEQ------------------ETASYSFADQTPAEKKLLEkwRVPVRDFQ-----QLSGGEKLKARLAKGLSV 120
Cdd:cd03258 80 arrRIGMIFQhfnllssrtvfenvalplEIAGVPKAEIEERVLELLE--LVGLEDKAdaypaQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 121 DADLLLLDEPTNHLD----ESSLQfLIQQLKSYRG-TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03258 158 NPKVLLCDEATSALDpettQSILA-LLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEVVE 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
13-159 |
1.59e-16 |
|
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: 79.31 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-F------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI----------------- 66
Cdd:COG0411 6 EVRGLTKrFgglvavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILfdGRDItglpphriarlgiartf 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -------KMTMVE------QETASYSFAD---QTPAEKK-----------------LLEKWRVPVRDfqqLSGGEKLKAR 113
Cdd:COG0411 86 qnprlfpELTVLEnvlvaaHARLGRGLLAallRLPRARReereareraeellervgLADRADEPAGN---LSYGQQRRLE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 114 LAKGLSVDADLLLLDEPT---NHLDESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:COG0411 163 IARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHD 212
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-462 |
2.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.77 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV-------SPSANIGYLtqevf 363
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWdgepldpEDRRRIGYL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 364 dlpleqtPEE--LFDNET------YKARGH----------VQSLMRHLGFtASQWTEPIKHMSMGERVKCKLMAYILEEK 425
Cdd:COG4152 77 -------PEErgLYPKMKvgeqlvYLARLKglskaeakrrADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSHD 462
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELaakGTTVIFSSHQ 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
292-467 |
2.17e-16 |
|
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: 77.57 E-value: 2.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ---ETAEGSVWvspsanigYLTQEVFDLPLE 368
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkyEVTEGEIL--------FKGEDITDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 369 -----------QTPEELfdnetykaRG-HVQSLMRHL--GFtasqwtepikhmSMGERVKCKLMAYILEEKDVLILDEPT 434
Cdd:cd03217 73 erarlgiflafQYPPEI--------PGvKNADFLRYVneGF------------SGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 435 NHLDLPSREQLEETLSQY---GGTLLAVSHDRYFLE 467
Cdd:cd03217 133 SGLDIDALRLVAEVINKLreeGKSVLIITHYQRLLD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
292-461 |
2.19e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPS----ANIGYL 358
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPdSGEILIdgkpvrirSPRdaiaLGIGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE--VFD---------LPLEQTPEELFDNEtyKARGHVQSLMRHLGFTASqWTEPIKHMSMGER-----VKCklmayIL 422
Cdd:COG3845 86 HQHfmLVPnltvaenivLGLEPTKGGRLDRK--AARARIRELSERYGLDVD-PDAKVEDLSVGEQqrveiLKA-----LY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 423 EEKDVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLaaeGKSIIFITH 199
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-159 |
2.72e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.59 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ---------------------ILR 63
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEvlvdgldvattpsrelakrlaILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 64 QDIKMTM---VEQETA----SYSFADQTPAEKKLLEKW--RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:COG4604 82 QENHINSrltVRELVAfgrfPYSKGRLTAEDREIIDEAiaYLDLEDLAdryldELSGGQRQRAFIAMVLAQDTDYVLLDE 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 130 PTNHLDES-SLQfLIQQLKSY---RG-TVILVSHD 159
Cdd:COG4604 162 PLNNLDMKhSVQ-MMKLLRRLadeLGkTVVIVLHD 195
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
292-461 |
2.79e-16 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 76.31 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSpsanigylTQEV-FDLPLEq 369
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVD--------GKEVsFASPRD- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 370 tpeelfdnetykarghvqslMRHLG-FTASQwtepikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:cd03216 72 --------------------ARRAGiAMVYQ-------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170
....*....|....*.
gi 1732943882 449 ---LSQYGGTLLAVSH 461
Cdd:cd03216 125 irrLRAQGVAVIFISH 140
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
292-462 |
2.90e-16 |
|
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: 78.15 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTILfggedatdVPVQErNVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFD---LPLEQTPEELFDNETyKARGHVQSLMR--HLGFTASQWTEpikHMSMGERVKCKLMAYILEEKDVL 428
Cdd:cd03296 83 yalfrhmtVFDnvaFGLRVKPRSERPPEA-EIRAKVHELLKlvQLDWLADRYPA---QLSGGQRQRVALARALAVEPKVL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 429 ILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLhdelHVTTVFVTHD 196
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-194 |
4.51e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.02 E-value: 4.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTM 70
Cdd:PRK11160 339 LTLNNVSftYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlnGQPIAdyseaalrqaISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETASYS--------FADQTPAEKKL--------LEK----------W-----RvpvrdfqQLSGGEKLKARLAKGLS 119
Cdd:PRK11160 419 VSQRVHLFSatlrdnllLAAPNASDEALievlqqvgLEKlleddkglnaWlgeggR-------QLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 120 VDADLLLLDEPTNHLD---ESSLQFLIQQLKSYRgTVILVSHDRYFLdEAATKIWSLEDQTLIEfKGNYS-------GYM 189
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDaetERQILELLAEHAQNK-TVLMITHRLTGL-EQFDRICVMDNGQIIE-QGTHQellaqqgRYY 568
|
....*
gi 1732943882 190 KFREK 194
Cdd:PRK11160 569 QLKQR 573
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-161 |
6.54e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.75 E-value: 6.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIKMTMVEQETASYSFA 81
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 DQ---TP---AEKKLLEKWRVP-----------------------------VRDFQQLSGGEKLKARLAKGLSVDADLLL 126
Cdd:PRK11231 82 PQhhlTPegiTVRELVAYGRSPwlslwgrlsaednarvnqameqtrinhlaDRRLTDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 127 LDEPTNHLDES---SLQFLIQQLKSYRGTVILVSHD-----RY 161
Cdd:PRK11231 162 LDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
292-462 |
6.55e-16 |
|
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: 77.09 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGER----TLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSP--------------- 351
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPtSGTVRLAGqdlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 352 SANIGYLTQEvFDL-P----LE--QTPEELFDNETYKAR----------GHvqsLMRHLgftasqwtePiKHMSMGE--R 412
Cdd:COG4181 89 ARHVGFVFQS-FQLlPtltaLEnvMLPLELAGRRDARARarallervglGH---RLDHY---------P-AQLSGGEqqR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 413 VkcklM---AYILEEKdVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:COG4181 155 V----AlarAFATEPA-ILFADEPTGNLDAATGEQIIDLLfelnRERGTTLVLVTHD 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-467 |
6.76e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 27 VQQGDIIGIIGKNGAGKSTLLHLIHNDLAP------------------------------AQGQIlRQDIKMTMVEQetA 76
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEI-KVVHKPQYVDL--I 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SYSF----------ADQTPAEKKLLEKWRV-PV--RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQ 140
Cdd:PRK13409 173 PKVFkgkvrellkkVDERGKLDEVVERLGLeNIldRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqRLNVA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 141 FLIQQLKSYRgTVILVSHDRYFLDeaatkiwSLEDQTLIEFkGNYSGYMKFREKKrltqqreyekqqkmverieaqmnel 220
Cdd:PRK13409 253 RLIRELAEGK-YVLVVEHDLAVLD-------YLADNVHIAY-GEPGAYGVVSKPK------------------------- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 221 aswskkahdqSTKkEGFKEYhrvkakrtdaqikskqkrLEKELekaKAEPVK-PEYTVHFSI--DTSKKTGKRFLEVQNI 297
Cdd:PRK13409 299 ----------GVR-VGINEY------------------LKGYL---PEENMRiRPEPIEFEErpPRDESERETLVEYPDL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 298 TKAFGERTLFKNTNfTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSvwVSPSANIGYLTQEV---FDLP----LEQ 369
Cdd:PRK13409 347 TKKLGDFSLEVEGG-EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdEGE--VDPELKISYKPQYIkpdYDGTvedlLRS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 370 TPEElFDNETYKarghvQSLMRHLGFtasqwtEPI-----KHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQ 444
Cdd:PRK13409 424 ITDD-LGSSYYK-----SEIIKPLQL------ERLldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
490 500
....*....|....*....|....*..
gi 1732943882 445 LEETLSQY----GGTLLAVSHDRYFLE 467
Cdd:PRK13409 492 VAKAIRRIaeerEATALVVDHDIYMID 518
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
292-461 |
7.50e-16 |
|
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: 75.33 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG--ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--------SPSA---NIGY 357
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGlLRPTSGRVRLdgadisqwDPNElgdHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVfdlpleqtpeELFDNetykarghvqSLMrhlgftasqwtEPIkhMSMGERVKCKLMAYILEEKDVLILDEPTNHL 437
Cdd:cd03246 81 LPQDD----------ELFSG----------SIA-----------ENI--LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 1732943882 438 DLPSREQLEETLSQ---YGGTLLAVSH 461
Cdd:cd03246 128 DVEGERALNQAIAAlkaAGATRIVIAH 154
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-167 |
7.92e-16 |
|
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: 80.33 E-value: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYE-----VKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------- 61
Cdd:COG1123 260 LLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 LRQDI-------------KMTmVEQETA----SYSFADQTPAEKK---LLEKWRVPVRDFQ----QLSGGEKLKARLAKG 117
Cdd:COG1123 340 LRRRVqmvfqdpysslnpRMT-VGDIIAeplrLHGLLSRAERRERvaeLLERVGLPPDLADryphELSGGQRQRVAIARA 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 118 LSVDADLLLLDEPTNHLDESS----LQfLIQQLKSYRG-TVILVSHD----RYFLDEAA 167
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVqaqiLN-LLRDLQRELGlTYLFISHDlavvRYIADRVA 476
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
292-485 |
9.37e-16 |
|
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: 76.14 E-value: 9.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW--------VSPSA-NIGYLTQE 361
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPtSGRIYiggrdvtdLPPKDrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFD---LPLEQtpeELFDNETYKARghVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEKDVLIL 430
Cdd:cd03301 81 yalyphmtVYDniaFGLKL---RKVPKDEIDER--VREVAELLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 431 DEPTNHLDLPSREQLEETLS----QYGGTLLAVSHDRyfLEKTT-NSKLVISDNGIDKQL 485
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKrlqqRLGTTTIYVTHDQ--VEAMTmADRIAVMNDGQIQQI 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
292-462 |
1.20e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSP-----------SANIGYLT 359
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGehiqhyaskevARRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QEVfDLPLEQTPEELFDNETY-----------KARGHVQSLMRHLGFTaSQWTEPIKHMSMGERVKCKLMAYILEEKDVL 428
Cdd:PRK10253 88 QNA-TTPGDITVQELVARGRYphqplftrwrkEDEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 429 ILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnrekGYTLAAVLHD 203
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-159 |
1.50e-15 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------------------RQDIKMTM- 70
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTvrgrvssllglgggfnpeltgRENIYLNGr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 -----------VEQETASYS----FADQtpaekkllekwrvPVRdfqQLSGGekLKARLAKGLS--VDADLLLLDEPTNH 133
Cdd:cd03220 111 llglsrkeideKIDEIIEFSelgdFIDL-------------PVK---TYSSG--MKARLAFAIAtaLEPDILLIDEVLAV 172
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 134 LDESslqF------LIQQLKSYRGTVILVSHD 159
Cdd:cd03220 173 GDAA---FqekcqrRLRELLKQGKTVILVSHD 201
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
288-452 |
1.60e-15 |
|
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: 75.77 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 288 GKRFLEVQNITKafgERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ----ETAEGSVWVSPSA--------NI 355
Cdd:cd03234 7 WDVGLKAKNWNK---YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRveggGTTSGQILFNGQPrkpdqfqkCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQEVFDLP---LEQT---------PEELfdNETYKARGHVQSLMRHLGFTasqwtePIKHM-----SMGERVKCKLM 418
Cdd:cd03234 84 AYVRQDDILLPgltVRETltytailrlPRKS--SDAIRKKRVEDVLLRDLALT------RIGGNlvkgiSGGERRRVSIA 155
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 419 AYILEEKDVLILDEPTNHLDLPSREQLEETLSQY 452
Cdd:cd03234 156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-466 |
1.80e-15 |
|
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: 79.44 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 28 QQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ---------ILR-------QD-------------IKMTMVEQetASY 78
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdeVLKrfrgtelQDyfkklangeikvaHKPQYVDL--IPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 SF----------ADQTPAEKKLLEKWRV-PV--RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES---SLQFL 142
Cdd:COG1245 175 VFkgtvrellekVDERGKLDELAEKLGLeNIldRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYqrlNVARL 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 143 IQQLKSYRGTVILVSHDRYFLDeaatkiwSLEDQTLIeFKGNYSGYmkfrekKRLTQQReyekqqkmverieaqmnelas 222
Cdd:COG1245 255 IRELAEEGKYVLVVEHDLAILD-------YLADYVHI-LYGEPGVY------GVVSKPK--------------------- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 223 wskkahdqSTKK------EGFKEYHRVKakrtdaqIKSKQKRLE-KELEKAKAEPVKPEYTvhfsidtskktgkrflevq 295
Cdd:COG1245 300 --------SVRVginqylDGYLPEENVR-------IRDEPIEFEvHAPRREKEEETLVEYP------------------- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 296 NITKAFGERTLFKNTNfTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSvwVSPSANIGYLTQEV---FDLP----L 367
Cdd:COG1245 346 DLTKSYGGFSLEVEGG-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPdEGE--VDEDLKISYKPQYIspdYDGTveefL 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 EQTPEELFDNETYKARghvqsLMRHLGFtasqwtEPI-----KHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSR 442
Cdd:COG1245 423 RSANTDDFGSSYYKTE-----IIKPLGL------EKLldknvKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
490 500
....*....|....*....|....*...
gi 1732943882 443 EQLEETLSQY----GGTLLAVSHDRYFL 466
Cdd:COG1245 492 LAVAKAIRRFaenrGKTAMVVDHDIYLI 519
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
292-462 |
1.98e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 1.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVwvspsanigyltqEVFDLPLEQ- 369
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEV-------------RLNGRPLADw 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 370 TPEEL--------------FD---------------NETYKARGHVQSLMR-----HLGftasqwTEPIKHMSMGE---- 411
Cdd:PRK13548 70 SPAELarrravlpqhsslsFPftveevvamgraphgLSRAEDDALVAAALAqvdlaHLA------GRDYPQLSGGEqqrv 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 412 ---RVKCKLMAYILEEKdVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:PRK13548 144 qlaRVLAQLWEPDGPPR-WLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
292-462 |
2.27e-15 |
|
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: 75.29 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII------LGQETAEGSVWVSPSaNIGYLTQEVFDL 365
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlIPGAPDEGEVLLDGK-DIYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 366 PLE-----QTPEEL----FDNETYKARGHVQSLMRHLGFTASqwtEPIKHMSMGERVKCKLMAYILE------------- 423
Cdd:cd03260 80 RRRvgmvfQKPNPFpgsiYDNVAYGLRLHGIKLKEELDERVE---EALRKAALWDEVKDRLHALGLSggqqqrlclaral 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 424 --EKDVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHD 462
Cdd:cd03260 157 anEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-164 |
2.45e-15 |
|
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: 78.67 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFK-NVNA-SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG------------QILRQDIK 67
Cdd:COG1245 336 KEEETLVEYPDLTKSYGGFSlEVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGevdedlkisykpQYISPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTmVEQ--ETASYSFADQTPAE---------KKLLEKwrvPVRDfqqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD- 135
Cdd:COG1245 416 GT-VEEflRSANTDDFGSSYYKteiikplglEKLLDK---NVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDv 488
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 136 ESSLQF--LIQQL-KSYRGTVILVSHDRYFLD 164
Cdd:COG1245 489 EQRLAVakAIRRFaENRGKTAMVVDHDIYLID 520
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-159 |
2.80e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 75.98 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDikmtMVEQETASYSFADQT- 84
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA----QPLESWSSKAFARKVa 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 -------PAE----KKLLEKWRVP---------VRDFQQ--------------------LSGGEKLKARLAKGLSVDADL 124
Cdd:PRK10575 89 ylpqqlpAAEgmtvRELVAIGRYPwhgalgrfgAADREKveeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK10575 169 LLLDEPTSALDiahQVDVLALVHRLSQERGlTVIAVLHD 207
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
276-476 |
2.83e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 276 TVHFSIDTskktgKRFLEVQNITKAFG------ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETaegsvwv 349
Cdd:COG2401 14 TKVYSSVL-----DLSERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 spsaniGYLTQEVFDLPLEQTPEELFDNETYKARGHVQSLMRHLGF----TASQWTEPIKHMSMGERVKCKLMAYILEEK 425
Cdd:COG2401 82 ------GTPVAGCVDVPDNQFGREASLIDAIGRKGDFKDAVELLNAvglsDAVLWLRRFKELSTGQKFRFRLALLLAERP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLS----QYGGTLLAVSHdRYFLEKTTNSKLVI 476
Cdd:COG2401 156 KLLVIDEFCSHLDRQTAKRVARNLQklarRAGITLVVATH-HYDVIDDLQPDLLI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
291-481 |
2.84e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV------SPSAN-----IGYL 358
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTlTPTAGTVLVagddveALSARaasrrVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEV---FDLPLEQTPE-------ELFDNETYKARGHVQSLMRHLGfTASQWTEPIKHMSMGERVKCKLMAYILEEKDVL 428
Cdd:PRK09536 83 PQDTslsFEFDVRQVVEmgrtphrSRFDTWTETDRAAVERAMERTG-VAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 429 ILDEPTNHLDLPSREQ---LEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGI 481
Cdd:PRK09536 162 LLDEPTASLDINHQVRtleLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-159 |
2.87e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.45 E-value: 2.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------LRQDIKMTMVEQETASY- 78
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwkrrkkFLRRIGVVFGQKTQLWWd 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 -----SFA------DQTPAEKK--------LLEKWRV---PVRdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD- 135
Cdd:cd03267 110 lpvidSFYllaaiyDLPPARFKkrldelseLLDLEELldtPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDv 186
|
170 180
....*....|....*....|....*..
gi 1732943882 136 ---ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:cd03267 187 vaqENIRNFLKEYNRERGTTVLLTSHY 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
292-463 |
2.92e-15 |
|
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: 78.48 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV--------SPSA---NIGYL 358
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFvDPTEGSIAVngvpladaDADSwrdQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFDLP-----------LEQTPEELFD-------NETYKARGhvQSLMRHLGFTASQwtepikhMSMGERVKCKLMAY 420
Cdd:TIGR02857 402 PQHPFLFAgtiaenirlarPDASDAEIREaleraglDEFVAALP--QGLDTPIGEGGAG-------LSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSHDR 463
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRL 517
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
292-461 |
3.11e-15 |
|
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: 74.12 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKA------FGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ---ETAEGSVWV--------SPSAN 354
Cdd:cd03213 4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtgLGVSGEVLIngrpldkrSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 355 IGYLTQEVFDLPlEQTPEElfdnetykarghvqSLMrhlgFTASqwtepIKHMSMGERVKCKLMAYILEEKDVLILDEPT 434
Cdd:cd03213 84 IGYVPQDDILHP-TLTVRE--------------TLM----FAAK-----LRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 435 NHLDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLadtGRTIICSIH 169
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
291-463 |
4.81e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.68 E-value: 4.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW--------VSPSA-NIGYLTQ 360
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRILldgrdvtgLPPEKrNVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 E--------VFD---LPLEQtpeELFDNETYKARghVQSLMRHLGFTA------SQwtepikhMSMGE--RVkcKL---M 418
Cdd:COG3842 85 DyalfphltVAEnvaFGLRM---RGVPKAEIRAR--VAELLELVGLEGladrypHQ-------LSGGQqqRV--ALaraL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732943882 419 AYileEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHDR 463
Cdd:COG3842 151 AP---EPRVLLLDEPLSALDAKLREEMREELRRLqrelGITFIYVTHDQ 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-172 |
5.58e-15 |
|
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: 72.41 E-value: 5.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 29 QGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDikmtmveqetasysfADQTPAEKKLLEKWRVPVRDFQQLSGGE 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID---------------GEDILEEVLDQLLLIIVGGKKASGSGEL 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 109 KLKARLAKGLSVDADLLLLDEPTNHLDESS---------LQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWS 172
Cdd:smart00382 66 RLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
255-499 |
5.67e-15 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 77.98 E-value: 5.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 255 KQKRLEKELEKAKAEPVK---PEYTVHFSIDTSKKTGKRfLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKT 331
Cdd:PLN03073 139 RQREVQYQAHVAEMEAAKagmPGVYVNHDGNGGGPAIKD-IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKT 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 332 TLLKI---------------------ILGQETA-------------------------------EGSVWVSPSANIGYLT 359
Cdd:PLN03073 218 TFLRYmamhaidgipkncqilhveqeVVGDDTTalqcvlntdiertqlleeeaqlvaqqrelefETETGKGKGANKDGVD 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QEVFDLPLEQTPEELFDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDL 439
Cdd:PLN03073 298 KDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 440 PSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGIDKQLNDVPT-ERNEREELR 499
Cdd:PLN03073 378 HAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTfERTREEQLK 438
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-166 |
6.37e-15 |
|
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: 74.99 E-value: 6.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI--------------KMTMVEQ----------- 73
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidGQDIaamsrkelrelrrkKISMVFQsfallphrtvl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ETASYSFADQTPAEKKLLEKW-----RVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-----ESS 138
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAaealeLVGLEGWehkypDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirrEMQ 200
|
170 180
....*....|....*....|....*...
gi 1732943882 139 LQFLIQQLKSYRgTVILVSHDryfLDEA 166
Cdd:cd03294 201 DELLRLQAELQK-TIVFITHD---LDEA 224
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
292-461 |
6.74e-15 |
|
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: 73.30 E-value: 6.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSPSA----------NIGYLTQ 360
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGlSPPLAGRVLLNGGPldfqrdsiarGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 evfdLPLEQTPEELFDNETYKARGH----VQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:cd03231 81 ----APGIKTTLSVLENLRFWHADHsdeqVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*...
gi 1732943882 437 LDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:cd03231 156 LDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-179 |
7.09e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQILRQDIKMT-------------MVEQETASY----------S 79
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEawsaaelarhrayLSQQQTPPFampvfqyltlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 FADQTPAEK------------KLLEKWRVPVrdfQQLSGGEKLKARLA-------KGLSVDADLLLLDEPTNHLD---ES 137
Cdd:PRK03695 94 QPDKTRTEAvasalnevaealGLDDKLGRSV---NQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDvaqQA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 138 SLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK03695 171 ALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
292-462 |
9.25e-15 |
|
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: 73.87 E-value: 9.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGE-RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK-------------IILGQETAEgsvwVSPSA---N 354
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKminrlieptsgeiFIDGEDIRE----QDPVElrrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 355 IGYLTQEVFDLP-------------LEQTPEElfdnetyKARGHVQSLMRHLGFTASQWTEPIKH-MSMGERVKCKLMAY 420
Cdd:cd03295 77 IGYVIQQIGLFPhmtveenialvpkLLKWPKE-------KIRERADELLALVGLDPAEFADRYPHeLSGGQQQRVGVARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
292-461 |
9.53e-15 |
|
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: 72.35 E-value: 9.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGE--RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSP----------SANIGYL 358
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPqQGEITLDGvpvsdlekalSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFdlpleqtpeeLFDNetykarghvqSLMRHLGftasqwtepiKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLD 438
Cdd:cd03247 81 NQRPY----------LFDT----------TLRNNLG----------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
|
170 180
....*....|....*....|....*
gi 1732943882 439 LPSREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03247 131 PITERQLLSLIFEVlkDKTLIWITH 155
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
292-453 |
1.03e-14 |
|
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: 73.00 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGeKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV---SPSAN-------IGYLTQ 360
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATlTPPSSGTIRIdgqDVLKQpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvFDLPLEQTPEELFDnetY----------KARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLIL 430
Cdd:cd03264 80 E-FGVYPNFTVREFLD---YiawlkgipskEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180
....*....|....*....|...
gi 1732943882 431 DEPTNHLDLPSREQLEETLSQYG 453
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELG 177
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-159 |
1.10e-14 |
|
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: 76.63 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 3 EIVTLTNVSYEVKDLT--------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQE 74
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSagypgappVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 ----TASYS------FA------------DQTPAE-KKLLEKWRV--PVRDF------------QQLSGGEKLKARLAKG 117
Cdd:TIGR02868 406 evrrRVSVCaqdahlFDttvrenlrlarpDATDEElWAALERVGLadWLRALpdgldtvlgeggARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 118 LSVDADLLLLDEPTNHLD-ESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDaETADELLEDLLAALSGrTVVLITHH 529
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
292-349 |
1.31e-14 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 73.49 E-value: 1.31e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV 349
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTITV 60
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-183 |
1.44e-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: 73.14 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 15 KDLTVF--KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETASYSFADQTPA------ 86
Cdd:cd03299 8 KDWKEFklKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQNYAlfphmt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 87 ---------EKKLLEKWRVPV----------------RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQF 141
Cdd:cd03299 88 vykniayglKKRKVDKKEIERkvleiaemlgidhllnRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 142 LIQQLK----SYRGTVILVSHDryfLDEAatkiWSLEDQTLIEFKG 183
Cdd:cd03299 168 LREELKkirkEFGVTVLHVTHD---FEEA----WALADKVAIMLNG 206
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
13-165 |
1.50e-14 |
|
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: 72.08 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV---FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTmveqeTASYSFADQ-----T 84
Cdd:cd03215 6 EVRGLSVkgaVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT-----RRSPRDAIRagiayV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 PAEKK---LLEKWrvPVRD----FQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR---GTVI 154
Cdd:cd03215 81 PEDRKregLVLDL--SVAEnialSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVL 158
|
170
....*....|.
gi 1732943882 155 LVSHDryfLDE 165
Cdd:cd03215 159 LISSE---LDE 166
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-158 |
1.59e-14 |
|
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: 72.70 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RQDI-----------K 67
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiaaRNRIgylpeerglypK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVEQETASYSFADQTPAE-KKLLEKW--RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSL 139
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEaRRRIDEWleRLELSEYAnkrveELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV 164
|
170 180
....*....|....*....|..
gi 1732943882 140 QFL---IQQLKSYRGTVILVSH 158
Cdd:cd03269 165 ELLkdvIRELARAGKTVILSTH 186
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-166 |
1.90e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.75 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhndlA----PAQGQIL--RQDI-------- 66
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI----AgfetPDSGRILldGRDVtglppekr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 KMTMVEQetaSY----------------SFADQTPAEKK-----LLEkwRVPVRDF-----QQLSGGEKLKARLAKGLSV 120
Cdd:COG3842 78 NVGMVFQ---DYalfphltvaenvafglRMRGVPKAEIRarvaeLLE--LVGLEGLadrypHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 121 DADLLLLDEPTNHLDES---SLQFLIQQL-KSYRGTVILVSHDRyflDEA 166
Cdd:COG3842 153 EPRVLLLDEPLSALDAKlreEMREELRRLqRELGITFIYVTHDQ---EEA 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-180 |
1.99e-14 |
|
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: 72.25 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT-----------MVEQ 73
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniealrrigaLIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 E------TA-------------SYSFADQTPAEKKLLEKWRVPVRDFqqlSGGekLKARLAKGLSV--DADLLLLDEPTN 132
Cdd:cd03268 81 PgfypnlTArenlrllarllgiRKKRIDEVLDVVGLKDSAKKKVKGF---SLG--MKQRLGIALALlgNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 133 HLDE---SSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03268 156 GLDPdgiKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIE 206
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
292-479 |
2.27e-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: 72.33 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQnITKAFGERTLfkNTNFTIQhGEKVAIIGPNGSGKTTLLKIILGQETAE-------GSVWVSPSAN---------I 355
Cdd:cd03297 2 LCVD-IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDggtivlnGTVLFDSRKKinlppqqrkI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQEVfdlpleqtpeELF------DNETYKARGHVQSLMR-------------HLGFtasqwtEPIKHMSMGERVKCK 416
Cdd:cd03297 78 GLVFQQY----------ALFphlnvrENLAFGLKRKRNREDRisvdelldllgldHLLN------RYPAQLSGGEKQRVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 417 LMAYILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDN 479
Cdd:cd03297 142 LARALAAQPELLLLDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
304-480 |
2.61e-14 |
|
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: 70.65 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 304 RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGqetaegsVWVSPSANIGYLTQE-VFDLPleQTPeelfdnetYKA 382
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-------LWPWGSGRIGMPEGEdLLFLP--QRP--------YLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 383 RGhvqSLMRHLGFTasqWTepiKHMSMGERvkcKLMAY---ILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAV 459
Cdd:cd03223 77 LG---TLREQLIYP---WD---DVLSGGEQ---QRLAFarlLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
170 180
....*....|....*....|.
gi 1732943882 460 SHdRYFLEKTTNSKLVISDNG 480
Cdd:cd03223 145 GH-RPSLWKFHDRVLDLDGEG 164
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-156 |
3.56e-14 |
|
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: 72.19 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI-KMTM----------------------VE 72
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILldGQDItKLPMhkrarlgigylpqeasifrkltVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 Q------ETASYSFADQTPAEKKLLEKWRV-PVRDFQ--QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE---SSLQ 140
Cdd:cd03218 94 EnilavlEIRGLSKKEREEKLEELLEEFHItHLRKSKasSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPiavQDIQ 173
|
170
....*....|....*.
gi 1732943882 141 FLIQQLKSyRGTVILV 156
Cdd:cd03218 174 KIIKILKD-RGIGVLI 188
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
292-347 |
4.14e-14 |
|
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: 72.08 E-value: 4.14e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSV 347
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPtSGSV 57
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-160 |
4.48e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 71.67 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKE---IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQET-- 75
Cdd:PRK10247 1 MQEnspLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 --ASYS------FAD--------------QTPAEKKL---LEKWRVPVRDFQQ----LSGGEKLKARLAKGLSVDADLLL 126
Cdd:PRK10247 81 qqVSYCaqtptlFGDtvydnlifpwqirnQQPDPAIFlddLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 127 LDEPTNHLDESSLQF---LIQQLKSYRGTVIL-VSHDR 160
Cdd:PRK10247 161 LDEITSALDESNKHNvneIIHRYVREQNIAVLwVTHDK 198
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
292-462 |
5.34e-14 |
|
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: 74.41 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV-----------SPSANIGYL 358
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFlPPYSGSILIngvdlsdldpaSWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE--VFDLPLEQ---------TPEELFD--NETYkARGHVQSLMR----HLGFTASQwtepikhMSMGE-------RVk 414
Cdd:COG4988 417 PQNpyLFAGTIREnlrlgrpdaSDEELEAalEAAG-LDEFVAALPDgldtPLGEGGRG-------LSGGQaqrlalaRA- 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 415 cklmayILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSHD 462
Cdd:COG4988 488 ------LLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
276-480 |
6.49e-14 |
|
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: 71.02 E-value: 6.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 276 TVHFSIDTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--SPS 352
Cdd:cd03220 7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPDSGTVTVrgRVS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 353 ANIGYLTQevFDlpLEQTPEElfdNETYKAR--GHVQSLMR-HLGFTAsQWTE-------PIKHMSMGERVKCKLMAYIL 422
Cdd:cd03220 87 SLLGLGGG--FN--PELTGRE---NIYLNGRllGLSRKEIDeKIDEII-EFSElgdfidlPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 423 EEKDVLILDEPT----NHLDLPSREQLEETLSQyGGTLLAVSHDRYFLEKTTNSKLVIsDNG 480
Cdd:cd03220 159 LEPDILLIDEVLavgdAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVL-EKG 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-167 |
6.73e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.97 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLT--VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQ 64
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 DIKM------------------------------TMVE------QETASYSFADQTPAekkllekwrvpvrdfqQLSGGE 108
Cdd:PRK13635 82 QVGMvfqnpdnqfvgatvqddvafglenigvpreEMVErvdqalRQVGMEDFLNREPH----------------RLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 109 KLKARLAKGLSVDADLLLLDEPTNHLDESSLQFL---IQQLKSYRG-TVILVSHDryfLDEAA 167
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVletVRQLKEQKGiTVLSITHD---LDEAA 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
292-461 |
7.43e-14 |
|
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: 70.47 E-value: 7.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-----------QETAEGSVWVSPSANIGYLTQ 360
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGllrpdsgevrwNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EVfDLPLEQTPEElfdNETYKARGH------VQSLMRHLGFTASQWTePIKHMSMGERVKCKLMAYILEEKDVLILDEPT 434
Cdd:TIGR01189 81 LP-GLKPELSALE---NLHFWAAIHggaqrtIEDALAAVGLTGFEDL-PAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 435 NHLDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:TIGR01189 156 TALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-480 |
7.82e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 7.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWVS----PS------ANIGYLTQ 360
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCgepvPSrarharQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 evfdlpleqtpeelFDN--ETYKARGHVQSLMRHLGFTASQWTE-----------------PIKHMSMGERVKCKLMAYI 421
Cdd:PRK13537 88 --------------FDNldPDFTVRENLLVFGRYFGLSAAAARAlvppllefaklenkadaKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 422 LEEKDVLILDEPTNHLDLPSR----EQLEETLSQyGGTLLAVSHdryFLEKTTN--SKLVISDNG 480
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARhlmwERLRSLLAR-GKTILLTTH---FMEEAERlcDRLCVIEEG 214
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
292-461 |
9.19e-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: 70.47 E-value: 9.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG-ERTLF---KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQetaegsvwVSPSAniGYLTQEVFDlpL 367
Cdd:cd03266 2 ITADALTKRFRdVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL--------LEPDA--GFATVDGFD--V 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 EQTPEE-------LFDNE------------TYKARGH----------VQSLMRHLGFTASQwTEPIKHMSMGERVKCKLM 418
Cdd:cd03266 70 VKEPAEarrrlgfVSDSTglydrltarenlEYFAGLYglkgdeltarLEELADRLGMEELL-DRRVGGFSTGMRQKVAIA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 419 AYILEEKDVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLralGKCILFSTH 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-434 |
1.04e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RQDIKM--TMVEQETASysFADQTPAE 87
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILldgepvrfrspRDAQAAgiAIIHQELNL--VPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 -----------------------KKLLEKW------RVPVRDfqqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES- 137
Cdd:COG1129 99 niflgreprrgglidwramrrraRELLARLgldidpDTPVGD---LSVAQQQLVEIARALSRDARVLILDEPTASLTERe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 138 --SLQFLIQQLKSyRG-TVILVSHdryFLDEaatkIWSLEDQTLIeFK-GNYSGYMKFRE--KKRLTqqreyekqQKMVE 211
Cdd:COG1129 176 veRLFRIIRRLKA-QGvAIIYISH---RLDE----VFEIADRVTV-LRdGRLVGTGPVAEltEDELV--------RLMVG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 212 RieaqmnELASwskkahdqstkkegfkEYHRVKAkrtdaqikskqkrlekelekAKAEPVkpeytvhfsidtskktgkrf 291
Cdd:COG1129 239 R------ELED----------------LFPKRAA--------------------APGEVV-------------------- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKafgeRTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SPS----ANIGYL 358
Cdd:COG1129 257 LEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAdSGEIRLdgkpvrirSPRdairAGIAYV 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE------VFDLPLEqtpeelfDNETY---------------KARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKC-- 415
Cdd:COG1129 333 PEDrkgeglVLDLSIR-------ENITLasldrlsrgglldrrRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVvl 405
|
490 500
....*....|....*....|
gi 1732943882 416 -KLMAyilEEKDVLILDEPT 434
Cdd:COG1129 406 aKWLA---TDPKVLILDEPT 422
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
294-474 |
1.09e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 294 VQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSPSANIGYLTQEVF---DLPLEQ 369
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLvAPDEGVIKRNGKLRIGYVPQKLYldtTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 370 TPEELFDNETYKA-------RGHVQSLMRHlgftasqwtePIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSR 442
Cdd:PRK09544 87 NRFLRLRPGTKKEdilpalkRVQAGHLIDA----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 443 EQLEETLSQYGGTL----LAVSHDRYFLEKTTNSKL 474
Cdd:PRK09544 157 VALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVL 192
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
30-166 |
1.12e-13 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 70.02 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 30 GDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------------RQDIKMTMVEQETA-----------SYSFAD 82
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdsrkkinlpPQQRKIGLVFQQYAlfphlnvrenlAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 QTPAEKKLLEKWRVPV--------RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS----LQFLIQQLKSYR 150
Cdd:cd03297 103 KRNREDRISVDELLDLlgldhllnRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLPELKQIKKNLN 182
|
170
....*....|....*.
gi 1732943882 151 GTVILVSHDryfLDEA 166
Cdd:cd03297 183 IPVIFVTHD---LSEA 195
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
12-166 |
1.37e-13 |
|
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: 70.23 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 12 YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ--ILRQDIKMTMVE-QETASYS------FAD 82
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTayINGYSIRTDRKAaRQSLGYCpqfdalFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 QTPAEK--------------------------KLLEKWRVPVRDfqqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE 136
Cdd:cd03263 90 LTVREHlrfyarlkglpkseikeevelllrvlGLTDKANKRART---LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190
....*....|....*....|....*....|...
gi 1732943882 137 SSLQF---LIQQLKSYRgTVILVSHDryfLDEA 166
Cdd:cd03263 167 ASRRAiwdLILEVRKGR-SIILTTHS---MDEA 195
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
292-478 |
1.50e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.50 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF----------------------GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW 348
Cdd:COG1134 5 IEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPtSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 349 VSpsaniGYLTQevfdlPLeqtpeEL---FDNE-TykARGHVQSLMRHLGFTASQWTE-----------------PIKHM 407
Cdd:COG1134 85 VN-----GRVSA-----LL-----ELgagFHPElT--GRENIYLNGRLLGLSRKEIDEkfdeivefaelgdfidqPVKTY 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 408 SMGERVkcKL---MAYILEEkDVLILDEPTNHLDLP----SREQLEEtLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:COG1134 148 SSGMRA--RLafaVATAVDP-DILLVDEVLAVGDAAfqkkCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
292-462 |
1.95e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 71.64 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW--------VSPSA-NIGYLTQE 361
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEILiggrdvtdLPPKDrNIAMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFD---LPLEQ--TPEelfdnETYKARghVQSLMRHLGFT------ASQwtepikhMSMGER---------V 413
Cdd:COG3839 84 yalyphmtVYEniaFPLKLrkVPK-----AEIDRR--VREAAELLGLEdlldrkPKQ-------LSGGQRqrvalgralV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 414 KcklmayileEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:COG3839 150 R---------EPKVFLLDEPLSNLDAKLRVEMRAEIKRLhrrlGTTTIYVTHD 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
5-187 |
1.98e-13 |
|
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: 69.12 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVK------DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQ--GQIL-------RQDIK-- 67
Cdd:cd03213 4 LSFRNLTVTVKsspsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLingrpldKRSFRki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVEQETasYSFADQTPAEK-----KLlekwrvpvrdfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFL 142
Cdd:cd03213 84 IGYVPQDD--ILHPTLTVRETlmfaaKL-----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 143 IQQLKSYRG---TVILVSHdryfldEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:cd03213 151 MSLLRRLADtgrTIICSIH------QPSSEIFELFDKLLLLSQGRviYFG 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-158 |
2.00e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.89 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEvKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTM 70
Cdd:COG1132 340 IEFENVSfsYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidGVDIRdltleslrrqIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETA----------SYSFADQTPAE--------------KKLLEKWRVPVRDF-QQLSGGEklKARL--AKGLSVDAD 123
Cdd:COG1132 419 VPQDTFlfsgtireniRYGRPDATDEEveeaakaaqahefiEALPDGYDTVVGERgVNLSGGQ--RQRIaiARALLKDPP 496
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 124 LLLLDEPTNHLD---ESslqfLIQQ-LKSYRG--TVILVSH 158
Cdd:COG1132 497 ILILDEATSALDtetEA----LIQEaLERLMKgrTTIVIAH 533
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
173-279 |
2.20e-13 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 65.67 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 173 LEDQTLIEFKGNYSGYMKFREKKRLTQQREYEKQQKMVERIEAQMNELASWSKKAhdqstkkegfkeyhrvkakrtdAQI 252
Cdd:pfam12848 3 LERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKA----------------------KQA 60
|
90 100
....*....|....*....|....*..
gi 1732943882 253 KSKQKRLEKeLEKAKAePVKPEYTVHF 279
Cdd:pfam12848 61 QSRIKALEK-MERIEK-PERDKPKLRF 85
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-183 |
2.37e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 70.53 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLT---VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------------R 63
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIidgdllteenvwdiR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 64 QDIKMTM-----------VEQETAsYSFADQTPAEKKLLEKWR-----VPVRDFQ-----QLSGGEKLKARLAKGLSVDA 122
Cdd:PRK13650 81 HKIGMVFqnpdnqfvgatVEDDVA-FGLENKGIPHEEMKERVNealelVGMQDFKerepaRLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 123 DLLLLDEPTNHLDESSLQFLIQQLKS----YRGTVILVSHDryfLDEAAtkiwsLEDQTLIEFKG 183
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD---LDEVA-----LSDRVLVMKNG 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-166 |
2.61e-13 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 69.42 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT------MVEQEtaSYSF-------------- 80
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITepgpdrMVVFQ--NYSLlpwltvrenialav 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ----ADQTPAEKKLLEKWRVPVRDFQ--------QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQ-FLIQ 144
Cdd:TIGR01184 80 drvlPDLSKSERRAIVEEHIALVGLTeaadkrpgQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltRGNLQeELMQ 159
|
170 180
....*....|....*....|..
gi 1732943882 145 QLKSYRGTVILVSHDryfLDEA 166
Cdd:TIGR01184 160 IWEEHRVTVLMVTHD---VDEA 178
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
292-347 |
2.81e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.75 E-value: 2.81e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSV 347
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGlLPPAAGTI 59
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-158 |
2.86e-13 |
|
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: 69.06 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT----------MVEQETASYSFAD------------- 82
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaappadrpvsMLFQENNLFAHLTveqnvglglspgl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 -QTPAEKKLLEK--WRVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKSYRG 151
Cdd:cd03298 100 kLTAEDRQAIEValARVGLAGLEkrlpgELSGGERQRVALARVLVRDKPVLLLDEPFAALDpalRAEMLDLVLDLHAETK 179
|
....*...
gi 1732943882 152 -TVILVSH 158
Cdd:cd03298 180 mTVLMVTH 187
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
18-159 |
3.40e-13 |
|
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: 69.52 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRQDIKM-----TMVEQET 75
Cdd:cd03256 15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkalrqLRRQIGMifqqfNLIERLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 A---------SY-----SFADQ-TPAEK----KLLEkwRVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:cd03256 95 VlenvlsgrlGRrstwrSLFGLfPKEEKqralAALE--RVGLLDKayqraDQLSGGQQQRVAIARALMQQPKLILADEPV 172
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 132 NHLD-ESSLQF--LIQQLKSYRG-TVILVSHD 159
Cdd:cd03256 173 ASLDpASSRQVmdLLKRINREEGiTVIVSLHQ 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-164 |
3.98e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.76 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 10 VSYE--VKDLTVFK-NVNAS-VQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG------------QILRQDIKMTmVEQ 73
Cdd:PRK13409 341 VEYPdlTKKLGDFSlEVEGGeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelkisykpQYIKPDYDGT-VED 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ------ETASYSFADQTPAEK----KLLEKwrvPVRDfqqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-ESSLQF- 141
Cdd:PRK13409 420 llrsitDDLGSSYYKSEIIKPlqleRLLDK---NVKD---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLAVa 493
|
170 180
....*....|....*....|....*
gi 1732943882 142 -LIQQL-KSYRGTVILVSHDRYFLD 164
Cdd:PRK13409 494 kAIRRIaEEREATALVVDHDIYMID 518
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
292-462 |
4.71e-13 |
|
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: 68.55 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII--LGQETAeGSVWVSP----------SANIGYLT 359
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLttLLKPTS-GRATVAGhdvvreprevRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QEVfDLPLEQTPEE-------LFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILDE 432
Cdd:cd03265 80 QDL-SVDDELTGWEnlyiharLYGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 433 PTNHLDLPSREQLEETLSQ----YGGTLLAVSHD 462
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKlkeeFGMTILLTTHY 191
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-159 |
4.86e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVS--YEVK--DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL---------------- 62
Cdd:COG1135 1 MIELENLSktFPTKggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI-NLLeRPTSGSVLvdgvdltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 -RQDIkmTMVEQ------------------ETASYSFADQTPAEKKLLE-------KWRVPvrdfQQLSGGEKLKARLAK 116
Cdd:COG1135 80 aRRKI--GMIFQhfnllssrtvaenvalplEIAGVPKAEIRKRVAELLElvglsdkADAYP----SQLSGGQKQRVGIAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 117 GLSVDADLLLLDEPTNHLD----ESSLQfLIQQLKSYRG-TVILVSHD 159
Cdd:COG1135 154 ALANNPKVLLCDEATSALDpettRSILD-LLKDINRELGlTIVLITHE 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-181 |
5.00e-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: 68.87 E-value: 5.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDI--- 66
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdpveLRRKIgyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 --------KMTmVEQETASYSFADQTPAEKK------LLEKWRVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:cd03295 81 iqqiglfpHMT-VEENIALVPKLLKWPKEKIreradeLLALVGLDPAEFadrypHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 128 DEPTNHLD---ESSLQFLIQQLKSYRG-TVILVSHDryfLDEA---ATKIWSLEDQTLIEF 181
Cdd:cd03295 160 DEPFGALDpitRDQLQEEFKRLQQELGkTIVFVTHD---IDEAfrlADRIAIMKNGEIVQV 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
292-462 |
5.51e-13 |
|
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: 68.42 E-value: 5.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVS--PSANIG------------ 356
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPtSGEILLDgkDITNLPphkrpvntvfqn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 357 -----YLTqeVFD-----LPLEQTPEELFDNETYKARGHVQsLMRHLGFTASQwtepikhMSMGERVKCKLMAYILEEKD 426
Cdd:cd03300 81 yalfpHLT--VFEniafgLRLKKLPKAEIKERVAEALDLVQ-LEGYANRKPSQ-------LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 427 VLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLqkelGITFVFVTHD 190
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
292-370 |
6.15e-13 |
|
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: 68.75 E-value: 6.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGE-RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--------------SPSANI 355
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGlVEPTSGSVLIdgtdinklkgkalrQLRRQI 80
|
90
....*....|....*
gi 1732943882 356 GYLTQEvFDLPLEQT 370
Cdd:cd03256 81 GMIFQQ-FNLIERLS 94
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-168 |
6.79e-13 |
|
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: 68.05 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT----------MVEQE 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTdlppkdrdiaMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASY---------SFA----DQTPAE--------KKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:cd03301 81 YALYphmtvydniAFGlklrKVPKDEidervrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 134 LD-------ESSLQFLIQQLKSyrgTVILVSHDRyflDEAAT 168
Cdd:cd03301 161 LDaklrvqmRAELKRLQQRLGT---TTIYVTHDQ---VEAMT 196
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-166 |
7.02e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 7.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--------------RQdIK--- 67
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVlngrdlftnlppreRR-VGfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 --------MTmVEQETAsysFA----DQTPAEKK-----LLEkwRVPVRDF-----QQLSGGEKlkAR--LAKGLSVDAD 123
Cdd:COG1118 82 qhyalfphMT-VAENIA---FGlrvrPPSKAEIRarveeLLE--LVQLEGLadrypSQLSGGQR--QRvaLARALAVEPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 124 LLLLDEPTNHLDeSSL-----QFLIQQLKSYRGTVILVSHDRyflDEA 166
Cdd:COG1118 154 VLLLDEPFGALD-AKVrkelrRWLRRLHDELGGTTVFVTHDQ---EEA 197
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
307-462 |
7.58e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 70.85 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 307 FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVS-----------PSANIGYLTQE--VFDLPL----- 367
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQDahLFDTTVrenlr 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 ----EQTPEELFDnetYKARGHVQSLMRHLGFTASQW-TEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSR 442
Cdd:TIGR02868 431 larpDATDEELWA---ALERVGLADWLRALPDGLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|..
gi 1732943882 443 EQLEETLSQY--GGTLLAVSHD 462
Cdd:TIGR02868 508 DELLEDLLAAlsGRTVVLITHH 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
5-167 |
7.82e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.07 E-value: 7.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVfkNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIKMTMVEQETASYSFAD 82
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTlnGQDHTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 Q----------------------TPAEKKLLEKW--RVPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:PRK10771 80 NnlfshltvaqniglglnpglklNAAQREKLHAIarQMGIEDLlarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 134 LD----ESSLQFLIQQLKSYRGTVILVSHDryfLDEAA 167
Cdd:PRK10771 160 LDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEDAA 194
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
292-464 |
8.25e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII-------LGQETAEGSVWVSPSANigYLTQEVFD 364
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFarlltpqSGTVFLGDKPISMLSSR--QLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 LPLEQ-TPE----------------ELFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDV 427
Cdd:PRK11231 81 LPQHHlTPEgitvrelvaygrspwlSLWGRLSAEDNARVNQAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 428 LILDEPTNHLDLpsREQLE-----ETLSQYGGTLLAVSHD-----RY 464
Cdd:PRK11231 160 VLLDEPTTYLDI--NHQVElmrlmRELNTQGKTVVTVLHDlnqasRY 204
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-187 |
9.63e-13 |
|
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: 67.68 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 15 KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHN---DLAPAQGQIL---RQDIKMTM------VEQ--------- 73
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILfngQPRKPDQFqkcvayVRQddillpglt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 --ETASYS--FADQTPAEKKLLEKwRVPV---RD----------FQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE 136
Cdd:cd03234 98 vrETLTYTaiLRLPRKSSDAIRKK-RVEDvllRDlaltriggnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 137 SSLQFLIQQLKSY--RGTVILVShdryfLDEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:cd03234 177 FTALNLVSTLSQLarRNRIVILT-----IHQPRSDLFRLFDRILLLSSGEivYSG 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-180 |
1.03e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL---------RQDI-----KM 68
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCI-NLLeEPDSGTITvdgedltdsKKDInklrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVEQetaSYS-FADQT--------P----------AEKK---LLEkwRVPVRDFQ-----QLSGGEKLKARLAKGLSVD 121
Cdd:COG1126 80 GMVFQ---QFNlFPHLTvlenvtlaPikvkkmskaeAEERameLLE--RVGLADKAdaypaQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 122 ADLLLLDEPTNHLD-ESS---LQfLIQQLKSyRG-TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:COG1126 155 PKVMLFDEPTSALDpELVgevLD-VMRDLAK-EGmTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
292-465 |
1.08e-12 |
|
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: 67.17 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV------SPSANIGYLTQEV-- 362
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPdSGTIIIdglkltDDKKNINELRQKVgm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 ----FDLPLEQTpeeLFDNETY-----------KARGHVQSLMRHLGFtASQWTEPIKHMSMGERVKCKLMAYILEEKDV 427
Cdd:cd03262 81 vfqqFNLFPHLT---VLENITLapikvkgmskaEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 428 LILDEPTNHLDlPS--REQLE--ETLSQYGGTLLAVSHDRYF 465
Cdd:cd03262 157 MLFDEPTSALD-PElvGEVLDvmKDLAEEGMTMVVVTHEMGF 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-159 |
1.29e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 68.25 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RQDI-----KM 68
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipamsRSRLytvrkRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVEQETAsySFADQTPAEK---KLLEKWRVPVRDFQ---------------------QLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK11831 87 SMLFQSGA--LFTDMNVFDNvayPLREHTQLPAPLLHstvmmkleavglrgaaklmpsELSGGMARRAALARAIALEPDL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 125 LLLDEPTNHLDESS---LQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK11831 165 IMFDEPFVGQDPITmgvLVKLISELNSALGvTCVVVSHD 203
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
292-462 |
1.52e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSA-------NIGYLTQEVFD 364
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAplaeareDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 LPLEQtpeeLFDNETYKARGHVQSLMRH------LGFTASQWTEPikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PRK11247 93 LPWKK----VIDNVGLGLKGQWRDAALQalaavgLADRANEWPAA---LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180
....*....|....*....|....*...
gi 1732943882 439 LPSR---EQLEETL-SQYGGTLLAVSHD 462
Cdd:PRK11247 166 ALTRiemQDLIESLwQQHGFTVLLVTHD 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
292-492 |
1.53e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.43 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEG--------SVwVSPSANIGYLTQE-- 361
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlivdglKV-NDPKVDERLIRQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 -VFD----LP----LEQT---PEELFDNETYKARGHVQSLMRHLGFTASQWTEPiKHMSMGER----------VKCKLMa 419
Cdd:PRK09493 81 mVFQqfylFPhltaLENVmfgPLRVRGASKEEAEKQARELLAKVGLAERAHHYP-SELSGGQQqrvaiaralaVKPKLM- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 420 yileekdvlILDEPTNHLDLPSRE---QLEETLSQYGGTLLAVSHDRYFLEKTTnSKLVISDNG-------IDKQLNDVP 489
Cdd:PRK09493 159 ---------LFDEPTSALDPELRHevlKVMQDLAEEGMTMVIVTHEIGFAEKVA-SRLIFIDKGriaedgdPQVLIKNPP 228
|
...
gi 1732943882 490 TER 492
Cdd:PRK09493 229 SQR 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
292-348 |
1.94e-12 |
|
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: 67.37 E-value: 1.94e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW 348
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPtSGRIL 62
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
13-159 |
1.98e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 66.35 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-------FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAP---AQGQILRQDIKMTM--VEQETASYSF 80
Cdd:COG4136 3 SLENLTItlggrplLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAlpAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ADQ---------------TPAEKKLLEKwRVPV--------------RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:COG4136 83 QDDllfphlsvgenlafaLPPTIGRAQR-RARVeqaleeaglagfadRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 132 NHLD----ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:COG4136 162 SKLDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
13-131 |
2.02e-12 |
|
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: 66.69 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF-------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--QDI----------------- 66
Cdd:cd03224 2 EVENLNAGygksqilFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdgRDItglppheraragigyvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -------KMTmVEQ--ETASYSFADQTPAEK---------KLLEKWRVPVrdfQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:cd03224 82 egrrifpELT-VEEnlLLGAYARRRAKRKARlervyelfpRLKERRKQLA---GTLSGGEQQMLAIARALMSRPKLLLLD 157
|
...
gi 1732943882 129 EPT 131
Cdd:cd03224 158 EPS 160
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-159 |
2.03e-12 |
|
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: 66.69 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKD----LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--LRQDIK---------- 67
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVrlAGQDLFaldedararl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 -----------------MTMVEQ-----ETASYSFADQTPAEkkLLEkwRV---------PvrdfQQLSGGEKLKARLAK 116
Cdd:COG4181 88 rarhvgfvfqsfqllptLTALENvmlplELAGRRDARARARA--LLE--RVglghrldhyP----AQLSGGEQQRVALAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 117 GLSVDADLLLLDEPTNHLDESSLQFLIQ---QLKSYRG-TVILVSHD 159
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQIIDllfELNRERGtTLVLVTHD 206
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
287-463 |
2.86e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 287 TGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV---------------- 349
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIdgedvthrsiqqrdic 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 ------------SPSANIGYltqevfDLPLEQTPEElfdnETYKARGHVQSLMRHLGFtASQWTEPIkhmSMGERVKCKL 417
Cdd:PRK11432 82 mvfqsyalfphmSLGENVGY------GLKMLGVPKE----ERKQRVKEALELVDLAGF-EDRYVDQI---SGGQQQRVAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 418 M-AYILEEKdVLILDEPTNHLDL----PSREQLEETLSQYGGTLLAVSHDR 463
Cdd:PRK11432 148 ArALILKPK-VLLFDEPLSNLDAnlrrSMREKIRELQQQFNITSLYVTHDQ 197
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-180 |
3.10e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 69.37 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEV---KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI--------- 66
Cdd:TIGR00958 475 LEGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLldGVPLvqydhhylh 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -KMTMVEQETASYSFA---------DQTPAEKKLLEKWRVPVRDF----------------QQLSGGEKLKARLAKGLSV 120
Cdd:TIGR00958 555 rQVALVGQEPVLFSGSvreniayglTDTPDEEIMAAAKAANAHDFimefpngydtevgekgSQLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 121 DADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR00958 635 KPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSVVE 693
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
310-462 |
3.13e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 310 TNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVS-------PSANI----GYLTQE---VFDLPLEQ-----T 370
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAgqpleawSAAELarhrAYLSQQqtpPFAMPVFQyltlhQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 PEElfdNETYKARGHVQSLMRHLGFTaSQWTEPIKHMSMGE--RVkcKLMAYILE-------EKDVLILDEPTNHLDLPS 441
Cdd:PRK03695 95 PDK---TRTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEwqRV--RLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....
gi 1732943882 442 R---EQLEETLSQYGGTLLAVSHD 462
Cdd:PRK03695 169 QaalDRLLSELCQQGIAVVMSSHD 192
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-159 |
3.55e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RQDIKMTMveQEt 75
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplaeaREDTRLMF--QD- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 asysfADQTPAEK-------KLLEKWR---------VPVRDFQQ-----LSGGEKLKARLAKGLSVDADLLLLDEPTNHL 134
Cdd:PRK11247 90 -----ARLLPWKKvidnvglGLKGQWRdaalqalaaVGLADRANewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180
....*....|....*....|....*....
gi 1732943882 135 DESS---LQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK11247 165 DALTrieMQDLIESLWQQHGfTVLLVTHD 193
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
311-462 |
3.67e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.40 E-value: 3.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 311 NFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVS-------PSANI----GYLTQE---VFDLPLEQ-----TP 371
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNgrplsdwSAAELarhrAYLSQQqspPFAMPVFQylalhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 372 EELFDNETYKArghVQSLMRHLGFTaSQWTEPIKHMSMGE--RVkcKLMAYILE-------EKDVLILDEPTNHLDLpsR 442
Cdd:COG4138 96 AGASSEAVEQL---LAQLAEALGLE-DKLSRPLTQLSGGEwqRV--RLAAVLLQvwptinpEGQLLLLDEPMNSLDV--A 167
|
170 180
....*....|....*....|....*
gi 1732943882 443 EQ-----LEETLSQYGGTLLAVSHD 462
Cdd:COG4138 168 QQaaldrLLRELCQQGITVVMSSHD 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-184 |
4.09e-12 |
|
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: 66.09 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEvKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTMVEQET 75
Cdd:cd03254 8 VNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidGIDIRdisrkslrsmIGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ASYS--------FADQTPAEKKLLEKWR-VPVRDF----------------QQLSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:cd03254 87 FLFSgtimenirLGRPNATDEEVIEAAKeAGAHDFimklpngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 131 TNHLD---ESSLQFLIQQLKSYRgTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGN 184
Cdd:cd03254 167 TSNIDtetEKLIQEALEKLMKGR-TSIIIAH-RLSTIKNADKILVLDDGKIIE-EGT 220
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
12-170 |
4.65e-12 |
|
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: 64.65 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 12 YEVKDLTV--FKNVNASVQQGDIIGIIGKNGAGKSTLLhlihNDLAPAQGQILRQDIKMTMVEQETAsysFADQTPAEKK 89
Cdd:cd03238 1 LTVSGANVhnLQNLDVSIPLNVLVVVTGVSGSGKSTLV----NEGLYASGKARLISFLPKFSRNKLI---FIDQLQFLID 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 90 LLEKWRVPVRDFQQLSGGEKLKARLAK--GLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSHDRYFLD 164
Cdd:cd03238 74 VGLGYLTLGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDVLS 153
|
....*.
gi 1732943882 165 EAATKI 170
Cdd:cd03238 154 SADWII 159
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
292-363 |
5.46e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.27 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITkaF---GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV--------SPSA---NIG 356
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTSGRILIdgvdirdlTLESlrrQIG 417
|
....*..
gi 1732943882 357 YLTQEVF 363
Cdd:COG1132 418 VVPQDTF 424
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-170 |
5.60e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 65.88 E-value: 5.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQ-GQILRQDIKMT------------- 69
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITsGDLIVDGLKVNdpkvderlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 -MVEQE-------TA------------SYSFADQTPAEKKLLEKWRVPVRDFQ---QLSGGEKLKARLAKGLSVDADLLL 126
Cdd:PRK09493 80 gMVFQQfylfphlTAlenvmfgplrvrGASKEEAEKQARELLAKVGLAERAHHypsELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 127 LDEPTNHLD-ESSLQFL--IQQLKSYRGTVILVSHDRYFLDEAATKI 170
Cdd:PRK09493 160 FDEPTSALDpELRHEVLkvMQDLAEEGMTMVIVTHEIGFAEKVASRL 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
306-381 |
5.72e-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: 64.80 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 306 LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSanIGYLTQE------------VFDLPleqtpe 372
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKlSGSVSVPGS--IAYVSQEpwiqngtireniLFGKP------ 91
|
....*....
gi 1732943882 373 elFDNETYK 381
Cdd:cd03250 92 --FDEERYE 98
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-190 |
5.82e-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: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI----------KMTM 70
Cdd:cd03251 1 VEFKNVTfrYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQET----------ASYSFADQTPAE--------------KKLLEKWRVPVRDF-QQLSGGEKLKARLAKGLSVDADLL 125
Cdd:cd03251 81 VSQDVflfndtvaenIAYGRPGATREEveeaaraanahefiMELPEGYDTVIGERgVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 126 LLDEPTNHLD---ESSLQFLIQQLKSYRgTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGNYSGYMK 190
Cdd:cd03251 161 ILDEATSALDtesERLVQAALERLMKNR-TTFVIAH-RLSTIENADRIVVLEDGKIVE-RGTHEELLA 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
9-171 |
6.61e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 66.04 E-value: 6.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVK--DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT-------MVEQETA--- 76
Cdd:COG4525 10 SVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgadrgVVFQKDAllp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 ----------SYSFADQTPAE-KKLLEKW--RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD--- 135
Cdd:COG4525 90 wlnvldnvafGLRLRGVPKAErRARAEELlaLVGLADFArrriwQLSGGMRQRVGIARALAADPRFLLMDEPFGALDalt 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 136 -ESSLQFLIQQLKSYRGTVILVSHDryfLDEA---ATKIW 171
Cdd:COG4525 170 rEQMQELLLDVWQRTGKGVFLITHS---VEEAlflATRLV 206
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-131 |
6.78e-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: 65.39 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF-------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI----------------- 66
Cdd:COG0410 5 EVENLHAGyggihvlHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRfdGEDItglpphriarlgigyvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -------KMTmVEQ--ETASYSFADQTPAEK----------KLLEKWRVPVRdfqQLSGGEK--LkArLAKGLSVDADLL 125
Cdd:COG0410 85 egrrifpSLT-VEEnlLLGAYARRDRAEVRAdlervyelfpRLKERRRQRAG---TLSGGEQqmL-A-IGRALMSRPKLL 158
|
....*.
gi 1732943882 126 LLDEPT 131
Cdd:COG0410 159 LLDEPS 164
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
313-461 |
7.44e-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: 64.82 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 313 TIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWVSpsaNIGYLTQEVFDLPLEQTPEE--LFDNETYKA------- 382
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQsGRVLIN---GVDVTAAPPADRPVSMLFQEnnLFAHLTVEQnvglgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 383 ---------RGHVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLS--- 450
Cdd:cd03298 97 pglkltaedRQAIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLdlh 175
|
170
....*....|..
gi 1732943882 451 -QYGGTLLAVSH 461
Cdd:cd03298 176 aETKMTVLMVTH 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-185 |
8.01e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.71 E-value: 8.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF--------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPA-QGQILR-QDIKMTMVEQetASY---- 78
Cdd:cd03223 2 ELENLSLAtpdgrvllKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWgSGRIGMpEGEDLLFLPQ--RPYlplg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 SFADQtpaekkLLEKWRvpvrdfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYRGTVILVSH 158
Cdd:cd03223 79 TLREQ------LIYPWD------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH 146
|
170 180
....*....|....*....|....*...
gi 1732943882 159 dRyfldeaaTKIWSLEDQTL-IEFKGNY 185
Cdd:cd03223 147 -R-------PSLWKFHDRVLdLDGEGGW 166
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
292-376 |
8.72e-12 |
|
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: 67.47 E-value: 8.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF--GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSV---------WvSPSA---NIG 356
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGvWPPTAGSVrldgadlsqW-DREElgrHIG 409
|
90 100
....*....|....*....|
gi 1732943882 357 YLTQEVfdlpleqtpeELFD 376
Cdd:COG4618 410 YLPQDV----------ELFD 419
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
18-157 |
9.48e-12 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 65.05 E-value: 9.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI------------------------KMTmV 71
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFldGEDIthlpmhkrarlgigylpqeasifrKLT-V 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 72 EQ------ETASYSFADQTPAEKKLLEKWRV-PVRDF--QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE---SSL 139
Cdd:COG1137 96 EDnilavlELRKLSKKEREERLEELLEEFGItHLRKSkaYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiavADI 175
|
170
....*....|....*...
gi 1732943882 140 QFLIQQLKSyRGTVILVS 157
Cdd:COG1137 176 QKIIRHLKE-RGIGVLIT 192
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-175 |
1.06e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 64.35 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 16 DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRQdiKMTMVEQET--- 75
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIrvngqdvsdlrgraipyLRR--KIGVVFQDFrll 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ------ASYSFADQTPAEKKLLEKWRVP-----------VRDF-QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES 137
Cdd:cd03292 91 pdrnvyENVAFALEVTGVPPREIRKRVPaalelvglshkHRALpAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 138 SLQFLIQQLKSY--RGTVILVS-HDRYFLDEAATKIWSLED 175
Cdd:cd03292 171 TTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALER 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-159 |
1.18e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 65.52 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------RQDI------- 66
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgepldpedRRRIgylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 ----KMTMVEQetASYsFA---DQTPAE-----KKLLEK------WRVPVrdfQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:COG4152 81 glypKMKVGEQ--LVY-LArlkGLSKAEakrraDEWLERlglgdrANKKV---EELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 129 EPTNHLDESSLQFLIQQLKSYR--G-TVILVSHD 159
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAakGtTVIFSSHQ 188
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
21-183 |
1.33e-11 |
|
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: 64.31 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI-----------KMTMVEQETASYS---------- 79
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkepaearrRLGFVSDSTGLYDrltarenley 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 FAD--------QTPAEKKLLEKWR------VPVRDFQQlsgGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQ 145
Cdd:cd03266 102 FAGlyglkgdeLTARLEELADRLGmeelldRRVGGFST---GMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 146 LKSYR--GTVILVSHDRyfLDEAAtkiwSLEDQTLIEFKG 183
Cdd:cd03266 179 IRQLRalGKCILFSTHI--MQEVE----RLCDRVVVLHRG 212
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
291-461 |
1.33e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII--LGQeTAEGSV-WvspsanigyltqevFDLPL 367
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILagLAR-PDAGEVlW--------------QGEPI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 EQTPEELFDNETYkaRGH---VQSLM---RHLGFTASQWTE---------------------PIKHMSMGERVKCKLMAY 420
Cdd:PRK13538 66 RRQRDEYHQDLLY--LGHqpgIKTELtalENLRFYQRLHGPgddealwealaqvglagfedvPVRQLSAGQQRRVALARL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSH 461
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
286-463 |
1.43e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 286 KTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIlgqetaegSVWVSP-SANIGYLTQEVFD 364
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIV--------ASLISPtSGTLLFEGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 LPLE----------QTP----EELFDNET--YKARGH-------VQSLMRhLGFTASQWTEPIKHMSMGERVKCKLMAYI 421
Cdd:PRK10247 74 LKPEiyrqqvsycaQTPtlfgDTVYDNLIfpWQIRNQqpdpaifLDDLER-FALPDTILTKNIAELSGGEKQRISLIRNL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 422 LEEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHDR 463
Cdd:PRK10247 153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYvreqNIAVLWVTHDK 198
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
14-164 |
1.47e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLTVFK-NVNA-SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILrqdikmtmVEQETASYS----FADQTPAE 87
Cdd:cd03237 7 KKTLGEFTlEVEGgSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE--------IELDTVSYKpqyiKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 KKLLEK----------WRVPV-----------RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQL 146
Cdd:cd03237 79 RDLLSSitkdfythpyFKTEIakplqieqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180
....*....|....*....|..
gi 1732943882 147 KSY----RGTVILVSHDRYFLD 164
Cdd:cd03237 159 RRFaennEKTAFVVEHDIIMID 180
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
292-463 |
1.55e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 65.88 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEG----------SVWVSPSANIGYLTQE 361
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSghirfhgtdvSRLHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFD--------LPLEQTPeelfdnETYKARGHVQSL--MRHLGFTASQWTepiKHMSMGERVKCKLMAYILE 423
Cdd:PRK10851 83 yalfrhmtVFDniafgltvLPRRERP------NAAAIKAKVTQLleMVQLAHLADRYP---AQLSGGQKQRVALARALAV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 424 EKDVLILDEPTNHLDLPSREQLEETLSQ----YGGTLLAVSHDR 463
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELRRWLRQlheeLKFTSVFVTHDQ 197
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
292-462 |
1.61e-11 |
|
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: 64.84 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVwVSPSA-------------NIGYL 358
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGT-VDLAGvdlhglsrrararRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEV-FDLPLE--------QTP-EELFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVL 428
Cdd:TIGR03873 81 EQDSdTAVPLTvrdvvalgRIPhRSLWAGDSPHDAAVVDRALARTELSHLA-DRDMSTLSGGERQRVHVARALAQEPKLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 429 ILDEPTNHLDLpsREQLE-----ETLSQYGGTLLAVSHD 462
Cdd:TIGR03873 160 LLDEPTNHLDV--RAQLEtlalvRELAATGVTVVAALHD 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
283-463 |
1.62e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.12 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 283 TSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEgsvwvspSANIGYLTQEV 362
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-------SGRIMLDGQDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 FDLPLEQTP-------------EELFDNETY------------KARGHVQSLMRHLGFTASQwtePIKHMSMGERVKCKL 417
Cdd:PRK09452 79 THVPAENRHvntvfqsyalfphMTVFENVAFglrmqktpaaeiTPRVMEALRMVQLEEFAQR---KPHQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 418 MAYILEEKDVLILDEPTNHLDLPSREQLEETLS----QYGGTLLAVSHDR 463
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLRKQMQNELKalqrKLGITFVFVTHDQ 205
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-158 |
1.78e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 63.67 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETA-SYSFADQTPAEKKLL---E 92
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIArGLLYLGHAPGIKTTLsvlE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 93 KWRVPVRD----------------------FQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR 150
Cdd:cd03231 93 NLRFWHADhsdeqveealarvglngfedrpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHC 172
|
170
....*....|.
gi 1732943882 151 ---GTVILVSH 158
Cdd:cd03231 173 argGMVVLTTH 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-180 |
1.82e-11 |
|
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: 64.04 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVE---------- 72
Cdd:cd03252 1 ITFEHVRfrYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADpawlrrqvgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 --QETASYS--------FADQTPAEKKLLEKWRVP-VRDF----------------QQLSGGEKLKARLAKGLSVDADLL 125
Cdd:cd03252 81 vlQENVLFNrsirdniaLADPGMSMERVIEAAKLAgAHDFiselpegydtivgeqgAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 126 LLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGRIVE 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
292-363 |
1.89e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 64.28 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW-----VSP-------SANIGYL 358
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFldgedITHlpmhkraRLGIGYL 83
|
....*..
gi 1732943882 359 TQE--VF 363
Cdd:COG1137 84 PQEasIF 90
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
293-439 |
2.38e-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: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV-------SPSA----NIGYLTQ 360
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVdgldvatTPSRelakRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 E--------VFDL------PLEQ---TPEelfDNEtykargHVQSLMRHLGFtasqwtEPIKH-----MSMGERvkckLM 418
Cdd:COG4604 83 EnhinsrltVRELvafgrfPYSKgrlTAE---DRE------IIDEAIAYLDL------EDLADryldeLSGGQR----QR 143
|
170 180
....*....|....*....|....*
gi 1732943882 419 AYI----LEEKDVLILDEPTNHLDL 439
Cdd:COG4604 144 AFIamvlAQDTDYVLLDEPLNNLDM 168
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-159 |
2.38e-11 |
|
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: 63.37 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGdIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--QDIKMTMVE---------Q 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgQDVLKQPQKlrrrigylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ETASYS------FAD-----------QTPAE-KKLLEK---WRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTN 132
Cdd:cd03264 80 EFGVYPnftvreFLDyiawlkgipskEVKARvDEVLELvnlGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 133 HLD-ESSLQF--LIQQLKSYRgTVILVSHD 159
Cdd:cd03264 160 GLDpEERIRFrnLLSELGEDR-IVILSTHI 188
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-159 |
2.42e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI------------KMTM 70
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsklqgirKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETASYSFADQT---------------PAE-KKL---------LEKWRvpVRDFQQLSGGEKLKARLAKGLSVDADLL 125
Cdd:PRK13644 81 IVFQNPETQFVGRTveedlafgpenlclpPIEiRKRvdralaeigLEKYR--HRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 126 LLDEPTNHLDESSLQFLIQQLKSYR---GTVILVSHD 159
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHekgKTIVYITHN 195
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-158 |
2.46e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.21 E-value: 2.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEV--KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDL-APAQGQIL----------------- 62
Cdd:PRK11153 2 IELKNISkvFPQggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-NLLeRPTSGRVLvdgqdltalsekelrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 RQDIKM-----------TMVEQ-----ETASYSFADQTPAEKKLLEkwRVPVRDFQ-----QLSGGEKLKARLAKGLSVD 121
Cdd:PRK11153 81 RRQIGMifqhfnllssrTVFDNvalplELAGTPKAEIKARVTELLE--LVGLSDKAdrypaQLSGGQKQRVAIARALASN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 122 ADLLLLDEPTNHLD----ESSLQFLIQQLKSYRGTVILVSH 158
Cdd:PRK11153 159 PKVLLCDEATSALDpattRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-159 |
2.60e-11 |
|
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: 63.80 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT----------MVEQE 74
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITnlpphkrpvnTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASY---------SFADQTPAEKKLLEKWRVPV------------RDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:cd03300 81 YALFphltvfeniAFGLRLKKLPKAEIKERVAEaldlvqlegyanRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 134 LD---ESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:cd03300 161 LDlklRKDMQLELKRLQKELGiTFVFVTHD 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-339 |
2.93e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 27 VQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT---------MVEQE------------------TASYS 79
Cdd:PRK10938 26 LNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlsfeqlqkLVSDEwqrnntdmlspgeddtgrTTAEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 FADQTPAE------------KKLLEkwrvpvRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLK 147
Cdd:PRK10938 106 IQDEVKDParceqlaqqfgiTALLD------RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 148 SYRG---TVILVSHDRYFLDEAATKIWSLEDQTLIEfkgnysgymkfrekkrlTQQREYEKQQKMVerieAQMnelasws 224
Cdd:PRK10938 180 SLHQsgiTLVLVLNRFDEIPDFVQFAGVLADCTLAE-----------------TGEREEILQQALV----AQL------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 225 kkAHDqstkkegfkeyhrvkakrtdaqikskqkrlekelEKAKAEPVkPEyTVHFSIDTSKKTGKRFLEVQNITKAFGER 304
Cdd:PRK10938 232 --AHS----------------------------------EQLEGVQL-PE-PDEPSARHALPANEPRIVLNNGVVSYNDR 273
|
330 340 350
....*....|....*....|....*....|....*
gi 1732943882 305 TLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-159 |
2.93e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.74 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG---------------QILRQD 65
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGrivfdgkditdwqtaKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 66 I-----------KMTMVEQETASYSFADQTPAEKKLLEKWRVPVRDFQQ-------LSGGEKLKARLAKGLSVDADLLLL 127
Cdd:PRK11614 82 VaivpegrrvfsRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERriqragtMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 128 DEPTNHLDESSLQFL---IQQLKSYRGTVILVSHD 159
Cdd:PRK11614 162 DEPSLGLAPIIIQQIfdtIEQLREQGMTIFLVEQN 196
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-166 |
3.01e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 64.44 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------------RQ------ 64
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarhaRQrvgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 -----DIKMTMVE--QETASY---SFADQTPAEKKLLE------KWRVPVRDfqqLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK13537 87 qfdnlDPDFTVREnlLVFGRYfglSAAAARALVPPLLEfaklenKADAKVGE---LSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 129 EPTNHLDESSLQFLIQQLKSY--RG-TVILVSHdryFLDEA 166
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLlaRGkTILLTTH---FMEEA 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
311-465 |
3.36e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 65.59 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 311 NFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVS----PSANIG-------------YLTQEVFDLPLEQTPE 372
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGlYRPESGEILLDgqpvTADNREayrqlfsavfsdfHLFDRLLGLDGEADPA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 373 ElfdnetykarghVQSLMRHLGftasqwtepIKH-------------MSMGERvkcK----LMAYiLEEKDVLILDE--- 432
Cdd:COG4615 432 R------------ARELLERLE---------LDHkvsvedgrfsttdLSQGQR---KrlalLVAL-LEDRPILVFDEwaa 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 433 ---PT------NHLdLPSreqleetLSQYGGTLLAVSHD-RYF 465
Cdd:COG4615 487 dqdPEfrrvfyTEL-LPE-------LKARGKTVIAISHDdRYF 521
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-158 |
3.56e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 63.52 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVF-------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAP---AQGQIL--RQDI 66
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYygdkqalKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmNDLIPgarVEGEILldGEDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 ------------KMTMVEQ----------ETASYSFADQTPAEKKLLEKwRV-----------PVRD-FQQ----LSGGE 108
Cdd:COG1117 81 ydpdvdvvelrrRVGMVFQkpnpfpksiyDNVAYGLRLHGIKSKSELDE-IVeeslrkaalwdEVKDrLKKsalgLSGGQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 109 KLkaRL--AKGLSVDADLLLLDEPTNHLD-ESSLQF--LIQQLKS-YrgTVILVSH 158
Cdd:COG1117 160 QQ--RLciARALAVEPEVLLMDEPTSALDpISTAKIeeLILELKKdY--TIVIVTH 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
17-180 |
3.86e-11 |
|
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: 63.67 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRQDIKMTMVE------- 72
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsfrgqdlyqldrkqrraFRRDVQLVFQDspsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETASYSFA---------DQTPAEKKLLEKWR-VPVRDF------QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD- 135
Cdd:TIGR02769 104 RMTVRQIIGeplrhltslDESEQKARIAELLDmVGLRSEdadklpRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDm 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 136 --ESSLQFLIQQLKSYRGTV-ILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR02769 184 vlQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIVE 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
292-468 |
3.90e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 64.47 E-value: 3.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV----------SPSANIGYLTQ 360
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVlgvpvpararLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 evFD-LPLEQTPEE-------LFDNETYKARGHVQSLMrHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDE 432
Cdd:PRK13536 122 --FDnLDLEFTVREnllvfgrYFGMSTREIEAVIPSLL-EFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 433 PTNHLDLPSR----EQLEETLSQyGGTLLAVSHdryFLEK 468
Cdd:PRK13536 199 PTTGLDPHARhliwERLRSLLAR-GKTILLTTH---FMEE 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
292-433 |
4.11e-11 |
|
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: 62.95 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW-----VSP-------SANIGYL 358
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGKILldgqdITKlpmhkraRLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE--VF-DLPLEQT----PEELFDNETYKARgHVQSLMRHLGFTASQWTEPIkHMSMGERVKCKLMAYILEEKDVLILD 431
Cdd:cd03218 81 PQEasIFrKLTVEENilavLEIRGLSKKEREE-KLEELLEEFHITHLRKSKAS-SLSGGERRRVEIARALATNPKFLLLD 158
|
..
gi 1732943882 432 EP 433
Cdd:cd03218 159 EP 160
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
292-433 |
4.34e-11 |
|
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: 63.06 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWV-------SP-----SANIGYL 358
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDaGKILIdgqdithLPmheraRLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE--VF-DLPLEQTPE---ELFDNETYKARGH-VQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILD 431
Cdd:TIGR04406 82 PQEasIFrKLTVEENIMavlEIRKDLDRAEREErLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 1732943882 432 EP 433
Cdd:TIGR04406 161 EP 162
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
292-478 |
5.38e-11 |
|
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: 62.43 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTL-FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWVSPSA--------------NI 355
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTIRVNGQDvsdlrgraipylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQE--------VFD---LPLEQT---PEElfdnetykARGHVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYI 421
Cdd:cd03292 81 GVVFQDfrllpdrnVYEnvaFALEVTgvpPRE--------IRKRVPAALELVGLSHKHRALP-AELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 422 LEEKDVLILDEPTNHLDLP-SREQLE--ETLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDtTWEIMNllKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-159 |
6.25e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 6.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQDIK----MTMV-EQET-------ASYSF- 80
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfKRRKEfarrIGVVfGQRSqlwwdlpAIDSFr 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ------------ADQTPAE-KKLL---EKWRVPVRdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD----ESSLQ 140
Cdd:COG4586 119 llkaiyripdaeYKKRLDElVELLdlgELLDTPVR---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskEAIRE 195
|
170
....*....|....*....
gi 1732943882 141 FLIQQLKSYRGTVILVSHD 159
Cdd:COG4586 196 FLKEYNRERGTTILLTSHD 214
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
304-480 |
6.59e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.83 E-value: 6.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 304 RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSPSANIGYLTQEVFdLPL----EQ----TPEEL 374
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGlWPYGSGRIARPAGARVLFLPQRPY-LPLgtlrEAllypATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 375 FDNETYKA---RGHVQSLMRHLGFTASqWTepiKHMSMGE-------RVkcklmayILEEKDVLILDEPTNHLDLPSREQ 444
Cdd:COG4178 455 FSDAELREaleAVGLGHLAERLDEEAD-WD---QVLSLGEqqrlafaRL-------LLHKPDWLFLDEATSALDEENEAA 523
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 445 LEETLSQ--YGGTLLAVSHdRYFLEKTTNSKLVISDNG 480
Cdd:COG4178 524 LYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-348 |
7.45e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 62.44 E-value: 7.45e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 292 LEVQNITKAFGErtlFK---NTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVW 348
Cdd:COG4674 11 LYVEDLTVSFDG---FKalnDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKtRPDSGSVL 68
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
291-434 |
7.48e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.27 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV--------SP----SANIGY 357
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLdgepvrfrSPrdaqAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQE------------VFdLPLEQTPEELFD-NETYKArghVQSLMRHLGFTASQWTePIKHMSMGER-----VKcklmA 419
Cdd:COG1129 84 IHQElnlvpnlsvaenIF-LGREPRRGGLIDwRAMRRR---ARELLARLGLDIDPDT-PVGDLSVAQQqlveiAR----A 154
|
170
....*....|....*
gi 1732943882 420 YILEEKdVLILDEPT 434
Cdd:COG1129 155 LSRDAR-VLILDEPT 168
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-167 |
8.26e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.80 E-value: 8.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSY------EVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------- 61
Cdd:PRK13633 1 MNEMIKCKNVSYkyesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 --LRQDIKM-----------TMVEQETAsysFADQT----PAEKKL-----LEkwRVPVRDFQQ-----LSGGEKLKARL 114
Cdd:PRK13633 81 wdIRNKAGMvfqnpdnqivaTIVEEDVA---FGPENlgipPEEIRErvdesLK--KVGMYEYRRhaphlLSGGQKQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 115 AKGLSVDADLLLLDEPTNHLDESSLQFLIQQLK----SYRGTVILVSHdryFLDEAA 167
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKelnkKYGITIILITH---YMEEAV 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-170 |
8.68e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.55 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIvTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhndlA----PAQGQILRQDIKMT------- 69
Cdd:COG3839 1 MASL-ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMI----AgledPTSGEILIGGRDVTdlppkdr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 ---MVEQETASY---------SF----ADQTPAEKK--------------LLEkwRVPvrdfQQLSGGEKLKARLAKGLS 119
Cdd:COG3839 76 niaMVFQSYALYphmtvyeniAFplklRKVPKAEIDrrvreaaellgledLLD--RKP----KQLSGGQRQRVALGRALV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 120 VDADLLLLDEPTNHLD-------ESSLQFLIQQLKSyrgTVILVSHDryfLDEA---ATKI 170
Cdd:COG3839 150 REPKVFLLDEPLSNLDaklrvemRAEIKRLHRRLGT---TTIYVTHD---QVEAmtlADRI 204
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-166 |
8.77e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 63.31 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------------- 61
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvpararlararigvvpq 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 ---------LRQDI-------KMTMVEQETASYSFADQTPAEKKLlekwRVPVRDfqqLSGGEKLKARLAKGLSVDADLL 125
Cdd:PRK13536 122 fdnldleftVRENLlvfgryfGMSTREIEAVIPSLLEFARLESKA----DARVSD---LSGGMKRRLTLARALINDPQLL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 126 LLDEPTNHLDESSLQFLIQQLKSY--RG-TVILVSHdryFLDEA 166
Cdd:PRK13536 195 ILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTH---FMEEA 235
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-174 |
9.01e-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: 61.47 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 35 IIGKNGAGKSTLLHLIHNDL---APAQGQILRQDIKMTMVEQETASYSFADQTPAEKKLlekwrVPVRDFQQ-------- 103
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALtgeLPPNSKGGAHDPKLIREGEVRAQVKLAFENANGKKY-----TITRSLAIlenvifch 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 104 --------------LSGGEKLKA----RLA--KGLSVDADLLLLDEPTNHLDESSL-QFLIQQLKSYRGT----VILVSH 158
Cdd:cd03240 102 qgesnwplldmrgrCSGGEKVLAsliiRLAlaETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQknfqLIVITH 181
|
170
....*....|....*.
gi 1732943882 159 DRYFLDeAATKIWSLE 174
Cdd:cd03240 182 DEELVD-AADHIYRVE 196
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
13-168 |
9.87e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 63.70 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLT-------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RQDIKMTM--- 70
Cdd:PRK11607 21 EIRNLTksfdgqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMldgvdlshvppyQRPINMMFqsy 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 -------VEQETASYSFADQTP-AEKK--------LLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHL 134
Cdd:PRK11607 101 alfphmtVEQNIAFGLKQDKLPkAEIAsrvnemlgLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGAL 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 135 DES---SLQF-LIQQLKSYRGTVILVSHDRyflDEAAT 168
Cdd:PRK11607 181 DKKlrdRMQLeVVDILERVGVTCVMVTHDQ---EEAMT 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-199 |
1.05e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 62.29 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIKM-----------------------TMVEQ 73
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVvnGQTINLvrdkdgqlkvadknqlrllrtrlTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ETASYSF-----------------ADQTPAEKKLLEKWRVPVRDFQQ------LSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:PRK10619 100 HFNLWSHmtvlenvmeapiqvlglSKQEARERAVKYLAKVGIDERAQgkypvhLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 131 TNHLDES---SLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEdQTLIEFKGNYSGYMKFREKKRLTQ 199
Cdd:PRK10619 180 TSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLH-QGKIEEEGAPEQLFGNPQSPRLQQ 250
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
292-462 |
1.15e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.69 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLfkNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--------SPSAN-IGYLTQE 361
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWngqdltalPPAERpVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --VFD-LPLEQ------------TPEElfdnetyKARghVQSLMRHLGFTA------SQwtepikhMSMGERVKCKLMAY 420
Cdd:COG3840 80 nnLFPhLTVAQniglglrpglklTAEQ-------RAQ--VEQALERVGLAGlldrlpGQ-------LSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYGGTLLAVSHD 462
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEmldlVDELCRERGLTVLMVTHD 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-158 |
1.38e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.04 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLT-------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETASYSFADQ-- 83
Cdd:PRK13539 4 EGEDLAcvrggrvLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRna 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 84 -----TPAEKklLEKWR---------------------VPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES 137
Cdd:PRK13539 84 mkpalTVAEN--LEFWAaflggeeldiaaaleavglapLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*
gi 1732943882 138 SlQFLIQQLKSYR----GTVILVSH 158
Cdd:PRK13539 162 A-VALFAELIRAHlaqgGIVIAATH 185
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
292-339 |
1.53e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 1.53e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 292 LEVQNITKAFG-----ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAG 54
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
5-166 |
1.84e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.19 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETASYSFA--D 82
Cdd:PRK10789 316 VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAvvS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 QTP-----------------AEKKLLEK-----------WRVPvRDFQ--------QLSGGEKLKARLAKGLSVDADLLL 126
Cdd:PRK10789 396 QTPflfsdtvannialgrpdATQQEIEHvarlasvhddiLRLP-QGYDtevgergvMLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 127 LDEPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLDEA 166
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQWGEgrTVIISAHRLSALTEA 516
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-199 |
1.91e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 61.72 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVF-----KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT---------- 69
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 ------MVEQETASYSFADQTPAE--------KKLLEKwrVPVRDFQ-----------------QLSGGEKLKARLAKGL 118
Cdd:PRK13646 83 vrkrigMVFQFPESQLFEDTVEREiifgpknfKMNLDE--VKNYAHRllmdlgfsrdvmsqspfQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 119 SVDADLLLLDEPTNHLDESSLQFLIQQLKSYR----GTVILVSHDRYFLDEAATKIWSLEDQTLIEfkgNYSGYMKFREK 194
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHDMNEVARYADEVIVMKEGSIVS---QTSPKELFKDK 237
|
....*
gi 1732943882 195 KRLTQ 199
Cdd:PRK13646 238 KKLAD 242
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
284-463 |
2.02e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 284 SKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETaegsvwvsPSA-NIGYLTQEV 362
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ--------PTAgQIMLDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 FDLPLEQTP-EELFdnETYKARGHVqSLMRHLGFTASQWTEP-------------IKHM-----------SMGERVKCKL 417
Cdd:PRK11607 84 SHVPPYQRPiNMMF--QSYALFPHM-TVEQNIAFGLKQDKLPkaeiasrvnemlgLVHMqefakrkphqlSGGQRQRVAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 418 MAYILEEKDVLILDEPTNHLD--LPSREQLE--ETLSQYGGTLLAVSHDR 463
Cdd:PRK11607 161 ARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
18-157 |
2.03e-10 |
|
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: 61.14 E-value: 2.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI------------------------KMTMV 71
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILidGQDIthlpmherarlgigylpqeasifrKLTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 72 EQETASYSF-ADQTPAEKK-----LLEKWRVP-VRDF--QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE---SSL 139
Cdd:TIGR04406 95 ENIMAVLEIrKDLDRAEREerleaLLEEFQIShLRDNkaMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPiavGDI 174
|
170
....*....|....*...
gi 1732943882 140 QFLIQQLKSyRGTVILVS 157
Cdd:TIGR04406 175 KKIIKHLKE-RGIGVLIT 191
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
5-181 |
2.13e-10 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 63.23 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEV--KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------------- 61
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgrhigy 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 LRQDIKM---TmVEQETAsySFADQTPAekKLLE--KwRVPVRDF----------------QQLSGGEKLKARLAKGLSV 120
Cdd:COG4618 411 LPQDVELfdgT-IAENIA--RFGDADPE--KVVAaaK-LAGVHEMilrlpdgydtrigeggARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 121 DADLLLLDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSHDRYFLdEAATKIWSLEDQTLIEF 181
Cdd:COG4618 485 DPRLVVLDEPNSNLDdegEAALAAAIRALKARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAF 547
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-135 |
2.14e-10 |
|
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: 63.78 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------------LRQDIKMTMVEQETASYS 79
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswimpgtIKDNIIFGLSYDEYRYTS 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 FADQTPAEK---KLLEKWRVPVRDFQ-QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD 135
Cdd:TIGR01271 521 VIKACQLEEdiaLFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
289-462 |
2.16e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.57 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 289 KRFLEVQNITKAF--GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKI-------------ILGQETAEGSVWvSPSA 353
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLlnglllpeagtitVGGMVLSEETVW-DVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 NIGYltqeVFdlpleQTPEELFDNETYK---ARG-------------HVQSLMRHLGFTASQWTEPiKHMSMGERVKCKL 417
Cdd:PRK13635 82 QVGM----VF-----QNPDNQFVGATVQddvAFGlenigvpreemveRVDQALRQVGMEDFLNREP-HRLSGGQKQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732943882 418 MAYILEEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVrqlkEQKGITVLSITHD 200
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-158 |
2.27e-10 |
|
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: 60.06 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKM-TMVEQETASYSFADQTPAE 87
Cdd:TIGR01189 5 NLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 KKLLEKW----------------------RVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQ 140
Cdd:TIGR01189 85 KPELSALenlhfwaaihggaqrtiedalaAVGLTGFEdlpaaQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 1732943882 141 FLIQQLKSY---RGTVILVSH 158
Cdd:TIGR01189 165 LLAGLLRAHlarGGIVLLTTH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
292-461 |
2.38e-10 |
|
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: 60.71 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG-ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV-----------SPSANIGYL 358
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfYDVSSGSILIdgqdirevtldSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQevfDLPL--------------EQTPEELFdnETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEE 424
Cdd:cd03253 81 PQ---DTVLfndtigynirygrpDATDEEVI--EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 425 KDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-166 |
2.58e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK-------------- 67
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSIKkdlctyqkqlcfvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 --------MTMVEQETASYSFADQTPAEKKLLEKWRVP-VRDFQ--QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE 136
Cdd:PRK13540 81 hrsginpyLTLRENCLYDIHFSPGAVGITELCRLFSLEhLIDYPcgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|...
gi 1732943882 137 SSLQFLIQQLKSYR---GTVILVSHDRYFLDEA 166
Cdd:PRK13540 161 LSLLTIITKIQEHRakgGAVLLTSHQDLPLNKA 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
18-179 |
2.58e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.16 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMtmveQETASYSFADQ---------TPAE- 87
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHI----QHYASKEVARRigllaqnatTPGDi 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 -------------KKLLEKWR------------------VPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE 136
Cdd:PRK10253 97 tvqelvargryphQPLFTRWRkedeeavtkamqatgithLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 137 S---SLQFLIQQLKSYRG-TVILVSHDryfLDEA---ATKIWSLEDQTLI 179
Cdd:PRK10253 177 ShqiDLLELLSELNREKGyTLAAVLHD---LNQAcryASHLIALREGKIV 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-159 |
2.63e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETAS----------YSFADQTP--- 85
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAelrnqklgfiYQFHHLLPdft 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 86 ------------------AEKKLLE-------KWRVPVRDfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE---S 137
Cdd:PRK11629 104 alenvamplligkkkpaeINSRALEmlaavglEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaD 182
|
170 180
....*....|....*....|...
gi 1732943882 138 SLQFLIQQLKSYRGTVIL-VSHD 159
Cdd:PRK11629 183 SIFQLLGELNRLQGTAFLvVTHD 205
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-159 |
2.79e-10 |
|
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: 61.61 E-value: 2.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-FK----------NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAP---AQGQIL--RQDI---------- 66
Cdd:COG0444 3 EVRNLKVyFPtrrgvvkavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdGEDLlklsekelrk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 ----KMTMVEQE---------TASYSFAD----QTPAEKK--------LLEkwRV----PVRDFQ----QLSGGEKLKAR 113
Cdd:COG0444 83 irgrEIQMIFQDpmtslnpvmTVGDQIAEplriHGGLSKAeareraieLLE--RVglpdPERRLDryphELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 114 LAKGLSVDADLLLLDEPTNHLDESS----LQfLIQQLKSYRG-TVILVSHD 159
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIqaqiLN-LLKDLQRELGlAILFITHD 210
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
23-162 |
2.87e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 62.89 E-value: 2.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTmvEQETASYS------FAD----------QTPA 86
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT--ADNREAYRqlfsavFSDfhlfdrllglDGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 87 EKKLLEKW--------RVPVRD--F--QQLSGGEKlKaRLAKGLSV--DADLLLLDE------PtnhldesslQF----- 141
Cdd:COG4615 429 DPARARELlerleldhKVSVEDgrFstTDLSQGQR-K-RLALLVALleDRPILVFDEwaadqdP---------EFrrvfy 497
|
170 180
....*....|....*....|....*
gi 1732943882 142 --LIQQLKSyRG-TVILVSHD-RYF 162
Cdd:COG4615 498 teLLPELKA-RGkTVIAISHDdRYF 521
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
17-159 |
2.91e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 2.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRQDIKMTMVEQETA--- 76
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVswrgeplaklnraqrkaFRRDIQMVFQDSISAvnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 ----------------SYSFADQTPAEKKLLEKWRVPVRDF----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDe 136
Cdd:PRK10419 105 rktvreiireplrhllSLDKAERLARASEMLRAVDLDDSVLdkrpPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD- 183
|
170 180
....*....|....*....|....*...
gi 1732943882 137 SSLQF-LIQQLKSYR---GTVIL-VSHD 159
Cdd:PRK10419 184 LVLQAgVIRLLKKLQqqfGTACLfITHD 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
292-462 |
3.08e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.97 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVS----PSANI-------GYL 358
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGiLKPTSGSVLIRgepiTKENIrevrkfvGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQ----EVFDLPLEQT----PEEL-FDNETYKARghVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEKDVLI 429
Cdd:PRK13652 84 FQnpddQIFSPTVEQDiafgPINLgLDEETVAHR--VSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 430 LDEPTNHLDLPSREQLEETLS----QYGGTLLAVSHD 462
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNdlpeTYGMTVIFSTHQ 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-179 |
3.23e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 60.86 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL----------------RQdi 66
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkksllevRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 KMTMVEQETASYSFA----------------DQTPAEKKLLEKW-RVPVRDFQQ-----LSGGEKLKARLAKGLSVDADL 124
Cdd:PRK13639 79 TVGIVFQNPDDQLFAptveedvafgplnlglSKEEVEKRVKEALkAVGMEGFENkpphhLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK13639 159 IVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKII 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
12-158 |
3.47e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 12 YEVKDLtvfKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT--------------MVEQ---- 73
Cdd:PRK13637 18 FEKKAL---DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvklsdirkkvgLVFQypey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ----ETASYSFA--------DQTPAEKKLLEKWRVPVRDFQ--------QLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:PRK13637 95 qlfeETIEKDIAfgpinlglSEEEIENRVKRAMNIVGLDYEdykdkspfELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180
....*....|....*....|....*....
gi 1732943882 134 LD---ESSLQFLIQQL-KSYRGTVILVSH 158
Cdd:PRK13637 175 LDpkgRDEILNKIKELhKEYNMTIILVSH 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
292-499 |
3.48e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.53 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK------------IILGQETAEGSVWVSPSAN-IGYL 358
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRcinlleqpeagtIRVGDITIDTARSLSQQKGlIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEV------FDL-PLEQTPEELFD---------NETYKARGhvQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYIL 422
Cdd:PRK11264 84 RQHVgfvfqnFNLfPHRTVLENIIEgpvivkgepKEEATARA--RELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 423 EEKDVLILDEPTNHLDLPSREQLEET---LSQYGGTLLAVSHDRYFLEKTTN-----SKLVISDNGIDKQLNDVPTERNE 494
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTirqLAQEKRTMVIVTHEMSFARDVADraifmDQGRIVEQGPAKALFADPQQPRT 240
|
....*
gi 1732943882 495 REELR 499
Cdd:PRK11264 241 RQFLE 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
19-181 |
3.50e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.41 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--------------------NDLAPAQGQILRQDIKM---------- 68
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNlletpdsgqlniaghqfdfsQKPSEKAIRLLRQKVGMvfqqynlwph 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 -TMVEQET-ASYSFADQTPAE-----KKLLEKWRVpvRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD- 135
Cdd:COG4161 97 lTVMENLIeAPCKVLGLSKEQarekaMKLLARLRL--TDKadrfpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDp 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 136 ESSLQF--LIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIEF 181
Cdd:COG4161 175 EITAQVveIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-460 |
3.86e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.11 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETAS--- 77
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 78 -------YSFADQTPAEK-----KLLEK--WRVPVRDFQQ------------------------LSGGEKLKARLAKGLS 119
Cdd:PRK09700 82 igiiyqeLSVIDELTVLEnlyigRHLTKkvCGVNIIDWREmrvraammllrvglkvdldekvanLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 120 VDADLLLLDEPTNHLDESSLQFL---IQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIefkgnYSGYMKFREKKR 196
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV-----CSGMVSDVSNDD 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 197 LTQQreyekqqkMVERieaqmnelaswskkahdqstkkegfkeyhrvkakrtdaQIKSKQKRLEKELEKAKAEPVkpeyt 276
Cdd:PRK09700 237 IVRL--------MVGR--------------------------------------ELQNRFNAMKENVSNLAHETV----- 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 277 vhfsidtskktgkrfLEVQNITKAfgERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVW-----VS 350
Cdd:PRK09700 266 ---------------FEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKrAGGEIRlngkdIS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 351 PSA-------NIGYLTQEV--------FDLPLEQTPEELFDNETYK-ARGHVQSLMRH---------LGFTASQWTEPIK 405
Cdd:PRK09700 329 PRSpldavkkGMAYITESRrdngffpnFSIAQNMAISRSLKDGGYKgAMGLFHEVDEQrtaenqrelLALKCHSVNQNIT 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 406 HMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQ---LEETLSQYGGTLLAVS 460
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEiykVMRQLADDGKVILMVS 466
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
292-348 |
4.21e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 4.21e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG---QETAEGSVW 348
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEVTSGSIL 60
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-166 |
4.37e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.41 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDikmtmveqetaSYSFADQT 84
Cdd:cd03250 6 ASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 P------------AEKKLLEKW--RVP-----VRDFQQ---------------LSGGEklKAR--LAKGLSVDADLLLLD 128
Cdd:cd03250 75 PwiqngtirenilFGKPFDEERyeKVIkacalEPDLEIlpdgdlteigekginLSGGQ--KQRisLARAVYSDADIYLLD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 129 EPTNHLDESSLQFLIQQ-----LKSYRgTVILVSHDRYFLDEA 166
Cdd:cd03250 153 DPLSAVDAHVGRHIFENcilglLLNNK-TRILVTHQLQLLPHA 194
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-158 |
4.50e-10 |
|
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: 59.86 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSY---EVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MT 69
Cdd:cd03249 1 IEFKNVSFrypSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILldGVDIRdlnlrwlrsqIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 MVEQETA----------SYSFADQTPAE--------------KKLLEKWRVPVRDF-QQLSGGEKLKARLAKGLSVDADL 124
Cdd:cd03249 81 LVSQEPVlfdgtiaeniRYGKPDATDEEveeaakkanihdfiMSLPDGYDTLVGERgSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKSYRgTVILVSH 158
Cdd:cd03249 161 LLLDEATSALDaesEKLVQEALDRAMKGR-TTIVIAH 196
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-174 |
5.76e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 61.20 E-value: 5.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----------------NDLAPAQGQIlrqdik 67
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAgleditsgdlfigekrmNDVPPAERGV------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 mTMVEQETASY---------SF------ADQTPAEKK------------LLEkwRVPvrdfQQLSGGEKLKARLAKGLSV 120
Cdd:PRK11000 78 -GMVFQSYALYphlsvaenmSFglklagAKKEEINQRvnqvaevlqlahLLD--RKP----KALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 121 DADLLLLDEPTNHLDES---SLQFLIQQL-KSYRGTVILVSHDRYfldEAAT---KIWSLE 174
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAAlrvQMRIEISRLhKRLGRTMIYVTHDQV---EAMTladKIVVLD 208
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
5-158 |
7.08e-10 |
|
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: 59.55 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKD-LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK----------MTMV 71
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidGQDIRevtldslrraIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 72 EQETA----------SYSFADQTPAE--------------KKLLEKWRVPV--RDFqQLSGGEKLKARLAKGLSVDADLL 125
Cdd:cd03253 81 PQDTVlfndtigyniRYGRPDATDEEvieaakaaqihdkiMRFPDGYDTIVgeRGL-KLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 126 LLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSH 158
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
285-339 |
7.09e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 7.09e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 285 KKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
311-461 |
8.23e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 59.21 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 311 NFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWV--------SPSAN-IGYLTQE--VFD-LPLEQ-------- 369
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAsGSLTLngqdhtttPPSRRpVSMLFQEnnLFShLTVAQniglglnp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 370 ----TPEElfdNETYKARGHVQSLMRHLGFTASQwtepikhMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQ- 444
Cdd:PRK10771 99 glklNAAQ---REKLHAIARQMGIEDLLARLPGQ-------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEm 168
|
170 180
....*....|....*....|
gi 1732943882 445 ---LEETLSQYGGTLLAVSH 461
Cdd:PRK10771 169 ltlVSQVCQERQLTLLMVSH 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
292-347 |
8.97e-10 |
|
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: 58.98 E-value: 8.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSV 347
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPrSGSI 57
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-166 |
1.01e-09 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 58.54 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQ-------ILRQDIKMtmveQETASYSFA 81
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPREV----RRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 DQT--------------------PAEK---------KLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTN 132
Cdd:cd03265 81 DLSvddeltgwenlyiharlygvPGAErreridellDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 133 HLD---ESSLQFLIQQLKSYRG-TVILVSHdryFLDEA 166
Cdd:cd03265 161 GLDpqtRAHVWEYIEKLKEEFGmTILLTTH---YMEEA 195
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-183 |
1.02e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETA----SYSFAD-----------QTPAE 87
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYrklfSAVFTDfhlfdqllgpeGKPAN 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 KKLLEKW--------RVPVRDFQ----QLSGGEklKARLAKGLSV--DADLLLLDE------PtnHLDESSLQFLIQQLK 147
Cdd:PRK10522 422 PALVEKWlerlkmahKLELEDGRisnlKLSKGQ--KKRLALLLALaeERDILLLDEwaadqdP--HFRREFYQVLLPLLQ 497
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 148 SYRGTVILVSH-DRYFldEAATKIWSLEDQTLIEFKG 183
Cdd:PRK10522 498 EMGKTIFAISHdDHYF--IHADRLLEMRNGQLSELTG 532
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-186 |
1.02e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 10 VSYEVKDLTVFK--------NVNASVQQGDIIGIIGKNGAGKSTLLHLIH----------------NDLAPAQ------- 58
Cdd:PRK11174 348 VTIEAEDLEILSpdgktlagPLNFTLPAGQRIALVGPSGAGKTSLLNALLgflpyqgslkingielRELDPESwrkhlsw 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 59 -GQ-------ILRQDIKMTMVE-QETASYSFADQTPAE---KKLLEKWRVPVRDfqQ---LSGGEKLKARLAKGLSVDAD 123
Cdd:PRK11174 428 vGQnpqlphgTLRDNVLLGNPDaSDEQLQQALENAWVSeflPLLPQGLDTPIGD--QaagLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 124 LLLLDEPTNHLDESSLQFLIQQLKSY--RGTVILVSHDRYFLdEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQ-QGDYA 568
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
292-462 |
1.20e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 58.89 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGqetaegsvWVSP-SANIGYLTQEVFDLPleqt 370
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAG--------FIKPdSGKILLNGKDITNLP---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 PEE-----------LFDNET-YK--ARGhvqslMRHLGFTASQWTEPIKHM-----------------SMGERVKCKL-M 418
Cdd:cd03299 68 PEKrdisyvpqnyaLFPHMTvYKniAYG-----LKKRKVDKKEIERKVLEIaemlgidhllnrkpetlSGGEQQRVAIaR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 419 AYILEEKdVLILDEPTNHLDLPSREQLEETLS----QYGGTLLAVSHD 462
Cdd:cd03299 143 ALVVNPK-ILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHD 189
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
292-462 |
1.37e-09 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 58.64 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGER----TLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--SP------------- 351
Cdd:PRK10584 7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGlDDGSSGEVSLvgQPlhqmdeearaklr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 352 SANIGYLTQEVFDLP----LE--QTPEELFDNETYKARGHVQSLMRHLGFtasqwTEPIKHM----SMGERVKCKLMAYI 421
Cdd:PRK10584 87 AKHVGFVFQSFMLIPtlnaLEnvELPALLRGESSRQSRNGAKALLEQLGL-----GKRLDHLpaqlSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 422 LEEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:PRK10584 162 NGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-478 |
1.37e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.45 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-------------LRQDIK 67
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcarltpaKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVEQEtaSYSFADQTPAEKKLLekwRVPVRDFQQlsggEKLKARLA--------------------------KGLSVD 121
Cdd:PRK15439 88 IYLVPQE--PLLFPNLSVKENILF---GLPKRQASM----QKMKQLLAalgcqldldssagslevadrqiveilRGLMRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 122 ADLLLLDEPTNHLDESSLQFLIQQLKSYRGT---VILVSHDryfLDEaatkIWSLEDQTLIEfkgnYSGYMKFREKkrlt 198
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIRELLAQgvgIVFISHK---LPE----IRQLADRISVM----RDGTIALSGK---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 199 qQREYEKQqkmvERIEAqmnelaswskkahdqstkkegfkeyhrVKAKRTDAQIKSKQKRLekeLEKAKAEPVKPeytvh 278
Cdd:PRK15439 224 -TADLSTD----DIIQA---------------------------ITPAAREKSLSASQKLW---LELPGNRRQQA----- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 279 fsidtskkTGKRFLEVQNITkafGERtlFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV-------- 349
Cdd:PRK15439 264 --------AGAPVLTVEDLT---GEG--FRNISLEVRAGEILGLAGVVGAGRTELAETLYGlRPARGGRIMLngkeinal 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 350 SPSANIG----YLTQE------VFDLPLEQTPEELFDNE------TYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERV 413
Cdd:PRK15439 331 STAQRLArglvYLPEDrqssglYLDAPLAWNVCALTHNRrgfwikPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQ 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 414 KCkLMAYILE-EKDVLILDEPTNHLDLPSRE---QLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:PRK15439 411 KV-LIAKCLEaSPQLLIVDEPTRGVDVSARNdiyQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQ 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
292-478 |
1.61e-09 |
|
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: 60.22 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG---------------QETAEGSVWVSPSANIG 356
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwdgeiywsgSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 357 YLTQEVFDLPLEQTPEELF-DNE--------TYKARGH-VQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKD 426
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFlGNEitlpggrmAYNAMYLrAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 427 VLILDEPTNHLDLPSREQLEET---LSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIirdLKAHGVACVYISHKLNEVKAVCDTICVIRD 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-159 |
1.67e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 1.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------LRQDI 66
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidysrkglmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 KMTMVEQ----------ETASYSFADQTPAEKKLLEKWR--------VPVRD--FQQLSGGEKLKARLAKGLSVDADLLL 126
Cdd:PRK13636 85 GMVFQDPdnqlfsasvyQDVSFGAVNLKLPEDEVRKRVDnalkrtgiEHLKDkpTHCLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 1732943882 127 LDEPTNHLD----ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK13636 165 LDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
292-461 |
1.72e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.91 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLF-----KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWV------SPSANIGYLT 359
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLlKPTSGKIIIdgvditDKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QE---VFDLPLEQTPEE--------------LFDNETYKargHVQSLMRHLGFTASQWTE--PIKhMSMGERVKCKLMAY 420
Cdd:PRK13637 83 KKvglVFQYPEYQLFEEtiekdiafgpinlgLSEEEIEN---RVKRAMNIVGLDYEDYKDksPFE-LSGGQKRRVAIAGV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 421 ILEEKDVLILDEPTNHLDLPSREQLEETLS----QYGGTLLAVSH 461
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKelhkEYNMTIILVSH 203
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
308-461 |
1.91e-09 |
|
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: 58.01 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 308 KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV-----------SPSANIGYLTQEVF----------DL 365
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRfYDPQKGQILIdgidirdisrkSLRSMIGVVLQDTFlfsgtimeniRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 366 PLEQTPEELFDNETYKARGHvqSLMRHL--GFtASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSRE 443
Cdd:cd03254 100 GRPNATDEEVIEAAKEAGAH--DFIMKLpnGY-DTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEK 176
|
170 180
....*....|....*....|
gi 1732943882 444 QLEETLS--QYGGTLLAVSH 461
Cdd:cd03254 177 LIQEALEklMKGRTSIIIAH 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
292-461 |
1.96e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.01 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFG--ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV-----------SPSANIGY 357
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfYDVDSGRILIdghdvrdytlaSLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVFdlpleqtpeeLF-----DNETYKARGHVQSLMRHLGFTAsQWTEPIKHM---------------SMGERVKCKL 417
Cdd:cd03251 81 VSQDVF----------LFndtvaENIAYGRPGATREEVEEAARAA-NAHEFIMELpegydtvigergvklSGGQRQRIAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 418 MAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESERLVQAALERLmkNRTTFVIAH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
290-478 |
2.08e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.96 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 290 RFLEVqniTKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQE-TAEGSVWVS-------PSANIGYLTQ 360
Cdd:PRK10908 3 RFEHV---SKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSghditrlKNREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EV------FDLPLEQTpeeLFDN----------ETYKARGHVQSLMRHLGFTASQWTEPIKhMSMGERVKCKLMAYILEE 424
Cdd:PRK10908 80 QIgmifqdHHLLMDRT---VYDNvaipliiagaSGDDIRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 425 KDVLILDEPTNHLDLPSRE---QLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISD 478
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEgilRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-174 |
2.23e-09 |
|
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: 57.87 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVK---DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQD------------ 65
Cdd:cd03248 8 LKGIVKFQNVTFAYPtrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 66 IKMTMVEQETA--SYSFAD-------QTPAEKKLLEKWRVPVRDF----------------QQLSGGEKLKARLAKGLSV 120
Cdd:cd03248 88 SKVSLVGQEPVlfARSLQDniayglqSCSFECVKEAAQKAHAHSFiselasgydtevgekgSQLSGGQKQRVAIARALIR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 121 DADLLLLDEPTNHLDESSLQFLIQQLKSY--RGTVILVSHdRYFLDEAATKIWSLE 174
Cdd:cd03248 168 NPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLD 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-180 |
2.25e-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: 59.73 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 9 NVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----QDIKM-------TMVEQ- 73
Cdd:TIGR02203 335 NVTfrYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdghdlADYTLaslrrqvALVSQd 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ---------ETASYSFADQTPAEK---------------KLLEKWRVPVRD-FQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:TIGR02203 415 vvlfndtiaNNIAYGRTEQADRAEieralaaayaqdfvdKLPLGLDTPIGEnGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 129 EPTNHLDESS---LQFLIQQLKSYRgTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR02203 495 EATSALDNESerlVQAALERLMQGR-TTLVIAH-RLSTIEKADRIVVMDDGRIVE 547
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
5-158 |
2.30e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.60 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFK-----NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT---------- 69
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 ------MVEQETASYSFAD----------------QTPAEKKLLEKWR-VPVRD--FQQ----LSGGEKLKARLAKGLSV 120
Cdd:PRK13649 83 irkkvgLVFQFPESQLFEEtvlkdvafgpqnfgvsQEEAEALAREKLAlVGISEslFEKnpfeLSGGQMRRVAIAGILAM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 121 DADLLLLDEPTNHLDES---SLQFLIQQLKSYRGTVILVSH 158
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKgrkELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
296-480 |
2.96e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 296 NITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVW--------VSPSA-NIGYLTQEV--- 362
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLFigekrmndVPPAErGVGMVFQSYaly 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 ----------FDLPLEQTPEelfdNETYKARGHVQSLMR--HLgftasqWTEPIKHMSMGERVKCKLMAYILEEKDVLIL 430
Cdd:PRK11000 88 phlsvaenmsFGLKLAGAKK----EEINQRVNQVAEVLQlaHL------LDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 431 DEPTNHLDLPSREQLEETLS----QYGGTLLAVSHDRyfLEKTT-NSKLVISDNG 480
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISrlhkRLGRTMIYVTHDQ--VEAMTlADKIVVLDAG 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
308-461 |
3.12e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 57.12 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 308 KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVW---VSPSA--------NIGYLTQEVF----------Dl 365
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRlVELSSGSILidgVDISKiglhdlrsRISIIPQDPVlfsgtirsnlD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 366 PLEQ-TPEELFDN-ETYKARGHVQSLMRHLGFTAsqwTEPIKHMSMGERvkcKLMAY---ILEEKDVLILDEPTNHLDLP 440
Cdd:cd03244 100 PFGEySDEELWQAlERVGLKEFVESLPGGLDTVV---EEGGENLSVGQR---QLLCLaraLLRKSKILVLDEATASVDPE 173
|
170 180
....*....|....*....|...
gi 1732943882 441 SREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03244 174 TDALIQKTIREAfkDCTVLTIAH 196
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
4-167 |
3.40e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 57.84 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVF--KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDIK 67
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfekLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 MTMVEQE------TASYSFA----DQTPAEKKLLEKWRVPVRDF----------QQLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:PRK13648 87 IVFQNPDnqfvgsIVKYDVAfgleNHAVPYDEMHRRVSEALKQVdmleradyepNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 128 DEPTNHLD---ESSLQFLIQQLKSYRG-TVILVSHDryfLDEAA 167
Cdd:PRK13648 167 DEATSMLDpdaRQNLLDLVRKVKSEHNiTIISITHD---LSEAM 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-62 |
3.64e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 57.79 E-value: 3.64e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL 62
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL 64
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-267 |
4.15e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLT---------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQILRQDIKMTMVEQETASYSFA--- 81
Cdd:TIGR01271 1220 VQGLTakyteagraVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR-LLSTEGEIQIDGVSWNSVTLQTWRKAFGvip 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 ------------DQTPAEKKLLEK-WRV-------------PVR-DFQQ------LSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:TIGR01271 1299 qkvfifsgtfrkNLDPYEQWSDEEiWKVaeevglksvieqfPDKlDFVLvdggyvLSNGHKQLMCLARSILSKAKILLLD 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 129 EPTNHLDESSLQFLIQQLKSYRG--TVILVSHDRYFLdeaatkiwsLEDQTLIEFKGNysgymkfrekkrltQQREYEKQ 206
Cdd:TIGR01271 1379 EPSAHLDPVTLQIIRKTLKQSFSncTVILSEHRVEAL---------LECQQFLVIEGS--------------SVKQYDSI 1435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 207 QKMverieaqMNElASWSKKAHDQSTKKEGFKEYHRVKAKR-TDAQIKSKQKRLEKELEKAK 267
Cdd:TIGR01271 1436 QKL-------LNE-TSLFKQAMSAADRLKLFPLHRRNSSKRkPQPKITALREEAEEEVQNTR 1489
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-135 |
4.18e-09 |
|
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: 57.94 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------------------------LRQ 64
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIkhsgrisfssqfswimpgtikeniifgvsydeyrYKS 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 65 DIKMTMVEQETASYSFADQTP-AEKKLlekwrvpvrdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD 135
Cdd:cd03291 132 VVKACQLEEDITKFPEKDNTVlGEGGI------------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
281-437 |
4.35e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 281 IDTSKKTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGS---------VWVSP 351
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGtleiggnpcARLTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 352 SA--NIG-YLT-QE-------------VFDLPLEQTPEElfdnetyKARGHVQSLMRHLGFTASQWTEPIKHMSMGErvk 414
Cdd:PRK15439 81 AKahQLGiYLVpQEpllfpnlsvkeniLFGLPKRQASMQ-------KMKQLLAALGCQLDLDSSAGSLEVADRQIVE--- 150
|
170 180
....*....|....*....|...
gi 1732943882 415 ckLMAYILEEKDVLILDEPTNHL 437
Cdd:PRK15439 151 --ILRGLMRDSRILILDEPTASL 171
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-167 |
4.53e-09 |
|
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: 58.68 E-value: 4.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHL-------------IHNDLAPAQGQILR--QDIKM 68
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIlsgvyphgtwdgeIYWSGSPLKASNIRdtERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVEQETA----------------------SYSFADQTPAEKKLLEKWRVPV----RDFQQLSGGEKLKARLAKGLSVDA 122
Cdd:TIGR02633 81 VIIHQELTlvpelsvaeniflgneitlpggRMAYNAMYLRAKNLLRELQLDAdnvtRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 123 DLLLLDEPTNHLDESSLQFL---IQQLKSYRGTVILVSHDryfLDEAA 167
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILldiIRDLKAHGVACVYISHK---LNEVK 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
291-461 |
5.34e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 5.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 291 FLEVQNITKAF-GERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLLKI-------------ILGQETAEGSVWVSPSANIG 356
Cdd:PRK11288 4 YLSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKIlsgnyqpdagsilIDGQEMRFASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 357 YLTQEVFDLP---------LEQTPEE--LFDNETYKARghVQSLMRHLGFTASQWTePIKHMSMGERVKCKLMAYILEEK 425
Cdd:PRK11288 83 IIYQELHLVPemtvaenlyLGQLPHKggIVNRRLLNYE--AREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 426 DVLILDEPTNHLDLPSREQLE---ETLSQYGGTLLAVSH 461
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFrviRELRAEGRVILYVSH 198
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
4-159 |
5.42e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 56.83 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTM------------- 70
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplhararrgigy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQETASY---SFADQTPA----------------EKKLLEKWRVP-VRDF--QQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK10895 83 LPQEASIFrrlSVYDNLMAvlqirddlsaeqredrANELMEEFHIEhLRDSmgQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 129 EPTNHLDESS---LQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK10895 163 EPFAGVDPISvidIKRIIEHLRDSGLGVLITDHN 196
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
321-468 |
5.95e-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: 56.08 E-value: 5.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 321 AIIGPNGSGKTTLLKIILGQETAEGSvwvsPSANIGYLTQEVF---------DLPLEqtpeeLFDNETYKARGHV----Q 387
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELP----PNSKGGAHDPKLIregevraqvKLAFE-----NANGKKYTITRSLaileN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 388 SLMRHLGftASQW--TEPIKHMSMGERVKCKL-----MAYILEEK-DVLILDEPTNHLDLPSREQ-----LEETLSQYGG 454
Cdd:cd03240 97 VIFCHQG--ESNWplLDMRGRCSGGEKVLASLiirlaLAETFGSNcGILALDEPTTNLDEENIEEslaeiIEERKSQKNF 174
|
170
....*....|....
gi 1732943882 455 TLLAVSHDRYFLEK 468
Cdd:cd03240 175 QLIVITHDEELVDA 188
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
22-180 |
6.12e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 6.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLI----------------HNDLA----PAQGQILRQDIKM------------- 68
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprsgtlniagnHFDFSktpsDKAIRELRRNVGMvfqqynlwphltv 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 --TMVEQETASYSFADQTPAE--KKLLEKWRVpvRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-ESS 138
Cdd:PRK11124 100 qqNLIEAPCRVLGLSKDQALAraEKLLERLRL--KPYadrfpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpEIT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 139 LQF--LIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK11124 178 AQIvsIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVE 221
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
15-206 |
6.70e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 15 KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR--------------------QDIKMTMVEQE 74
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRngevsviaisaglsgqltgiENIEFKMLCMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASYSFADQTPAEKKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFL---IQQLKSYRG 151
Cdd:PRK13546 115 FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCldkIYEFKEQNK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 152 TVILVSHDRYFLDEAATKIWSLEDQTLIEFKG------NYSGYMKFREKKRLTQQREYEKQ 206
Cdd:PRK13546 195 TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGElddvlpKYEAFLNDFKKKSKAEQKEFRNK 255
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
298-461 |
6.95e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 6.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 298 TKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE---GSVWVS---PSANI----GYLTQEVFDLP- 366
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnftGTILANnrkPTKQIlkrtGFVTQDDILYPh 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 367 -----------LEQTPEELFDNETYKArghVQSLMRHLGFTASQWT----EPIKHMSMGERVKCKLMAYILEEKDVLILD 431
Cdd:PLN03211 155 ltvretlvfcsLLRLPKSLTKQEKILV---AESVISELGLTKCENTiignSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|...
gi 1732943882 432 EPTNHLDLPSREQLEET---LSQYGGTLLAVSH 461
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTlgsLAQKGKTIVTSMH 264
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
292-462 |
8.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.67 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF--GERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLL------------KI-ILGQE-TAEGSVWVspSANI 355
Cdd:PRK13647 5 IEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLlhlngiylpqrgRVkVMGREvNAENEKWV--RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQE---------VFD------LPLEQTPEELFD--NETYKARGHVQslMRHlgftasqwtEPIKHMSMGERVKCKLM 418
Cdd:PRK13647 82 GLVFQDpddqvfsstVWDdvafgpVNMGLDKDEVERrvEEALKAVRMWD--FRD---------KPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 419 AYILEEKDVLILDEPTNHLDLPSREQLEETL---SQYGGTLLAVSHD 462
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILdrlHNQGKTVIVATHD 197
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
32-167 |
8.50e-09 |
|
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: 57.43 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 32 IIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------RQDIKMTmVEQETASYSFADQT------------------ 84
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsRKGIFLP-PEKRRIGYVFQEARlfphlsvrgnlrygmkra 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 85 -PAEKK--------------LLEkwRVPVRdfqqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS----LQFLIQQ 145
Cdd:TIGR02142 104 rPSERRisferviellgighLLG--RLPGR----LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLERL 177
|
170 180
....*....|....*....|..
gi 1732943882 146 LKSYRGTVILVSHDryfLDEAA 167
Cdd:TIGR02142 178 HAEFGIPILYVSHS---LQEVL 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
294-462 |
9.51e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 56.33 E-value: 9.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 294 VQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKiILG--QETAEGSV---------WVSPS--ANIGYLTQ 360
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLGrhQPPSEGEIlldaqplesWSSKAfaRKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EvfdLPLEQ--TPEELFDNETY-----------KARGHVQSLMRHLGFTasqwtePIKH-----MSMGERVKCKLMAYIL 422
Cdd:PRK10575 93 Q---LPAAEgmTVRELVAIGRYpwhgalgrfgaADREKVEEAISLVGLK------PLAHrlvdsLSGGERQRAWIAMLVA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 423 EEKDVLILDEPTNHLDLPSREQ---LEETLSQYGG-TLLAVSHD 462
Cdd:PRK10575 164 QDSRCLLLDEPTSALDIAHQVDvlaLVHRLSQERGlTVIAVLHD 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
292-349 |
9.65e-09 |
|
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: 56.05 E-value: 9.65e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 292 LEVQNITKAFGER----TLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV 349
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERpTSGSVLV 64
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-159 |
9.91e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 56.19 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT----------MVEQE 74
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATdvpvqernvgFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASY---------SF------ADQTPAEKKLLEKWRVPVRDFQ----------QLSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:cd03296 83 YALFrhmtvfdnvAFglrvkpRSERPPEAEIRAKVHELLKLVQldwladrypaQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 130 PTNHLD---ESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:cd03296 163 PFGALDakvRKELRRWLRRLHDELHvTTVFVTHD 196
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
292-348 |
1.05e-08 |
|
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: 55.76 E-value: 1.05e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVW 348
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSIR 61
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
292-462 |
1.17e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 56.25 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVS------PSANIGYLTQEVFD 364
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfVPYQHGSITLDgkpvegPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 LPLEQTPE------ELFDNETYKARGHVQSLMRHLGFTASQwTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PRK11248 82 LPWRNVQDnvafglQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180
....*....|....*....|....*...
gi 1732943882 439 LPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:PRK11248 161 AFTREQMQTLLLKLwqetGKQVLLITHD 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-434 |
1.21e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.83 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RQDI------ 66
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhRRAVcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -----------------------------------KMTMVEQETASYSFADQtPAEKkllekwrvpvrdfqqLSGGEKLK 111
Cdd:NF033858 81 mpqglgknlyptlsvfenldffgrlfgqdaaerrrRIDELLRATGLAPFADR-PAGK---------------LSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 112 ARLAKGLSVDADLLLLDEPTNHLDE-SSLQF--LIQQLKSYRG--TVILvshdryfldeaATkiwsledqtliefkgnys 186
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPlSRRQFweLIDRIRAERPgmSVLV-----------AT------------------ 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 187 GYMKfrekkrltqqreyekqqkmveriEAQ-------MNElaswskkahdqstkkeGfkeyhRVKAKRTDAQIKSK--QK 257
Cdd:NF033858 196 AYME-----------------------EAErfdwlvaMDA----------------G-----RVLATGTPAELLARtgAD 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 258 RLEK--------ELEKAKAEPVKPEYTVHFSIDTSkktgkrfLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSG 329
Cdd:NF033858 232 TLEAafiallpeEKRRGHQPVVIPPRPADDDDEPA-------IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCG 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 330 KTTLLKIILG-QETAEGSVW-----VSPS-----ANIGYLTQEvFDLPLEQTPEE-------LFDNETYKARGHVQSLMR 391
Cdd:NF033858 305 KSTTMKMLTGlLPASEGEAWlfgqpVDAGdiatrRRVGYMSQA-FSLYGELTVRQnlelharLFHLPAAEIAARVAEMLE 383
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1732943882 392 HLGFTASQWTEPIKhMSMGERVKCKLMAYILEEKDVLILDEPT 434
Cdd:NF033858 384 RFDLADVADALPDS-LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-131 |
1.24e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.34 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV---FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---------------------------- 61
Cdd:COG1129 258 EVEGLSVggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrldgkpvrirsprdairagiayvpedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 -----LRQDIK--MTMVEQET-ASYSFADQtPAEKKLLEKWR-----------VPVRdfqQLSGGEKLKARLAKGLSVDA 122
Cdd:COG1129 338 geglvLDLSIRenITLASLDRlSRGGLLDR-RRERALAEEYIkrlriktpspeQPVG---NLSGGNQQKVVLAKWLATDP 413
|
....*....
gi 1732943882 123 DLLLLDEPT 131
Cdd:COG1129 414 KVLILDEPT 422
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2-166 |
1.47e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVfknvnaSVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI--------------- 66
Cdd:PRK10070 32 EQILEKTGLSLGVKDASL------AIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVdiakisdaelrevrr 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -KMTMVEQETA---SYSFADQT---------PAEK---KLLEKWR-VPVRDF-----QQLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK10070 106 kKIAMVFQSFAlmpHMTVLDNTafgmelagiNAEErreKALDALRqVGLENYahsypDELSGGMRQRVGLARALAINPDI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKS-YRGTVILVSHDryfLDEA 166
Cdd:PRK10070 186 LLMDEAFSALDpliRTEMQDELVKLQAkHQRTIVFISHD---LDEA 228
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-173 |
1.55e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.78 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQ----------------------- 64
Cdd:PRK13638 5 SDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkpldyskrgllalrqqvatvfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 -------------DIKMTMVEQETASYSFADQTPAEKKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPT 131
Cdd:PRK13638 85 dpeqqifytdidsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 132 NHLD---ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSL 173
Cdd:PRK13638 165 AGLDpagRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
292-347 |
1.70e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.70 E-value: 1.70e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSV 347
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPdAGEV 63
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-184 |
1.77e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 56.27 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL------------RQDIkmT 69
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFidgedvthrsiqQRDI--C 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 MVEQETASY---SFADQTPAEKKLL----EKWRVPVRD---------FQ-----QLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK11432 82 MVFQSYALFphmSLGENVGYGLKMLgvpkEERKQRVKEalelvdlagFEdryvdQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 129 EPTNHLDES---SLQFLIQQL-KSYRGTVILVSHDRyfldeaaTKIWSLEDQTLIEFKGN 184
Cdd:PRK11432 162 EPLSNLDANlrrSMREKIRELqQQFNITSLYVTHDQ-------SEAFAVSDTVIVMNKGK 214
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
14-176 |
1.78e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLTVFK-NVNAS-VQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlrqdikmtmveqetasySFADQTPAEKKll 91
Cdd:cd03222 7 VKRYGVFFlLVELGvVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND-----------------EWDGITPVYKP-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 92 ekwrvpvrDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-ESSLQF--LIQQLKSY-RGTVILVSHDRYFLDEAA 167
Cdd:cd03222 68 --------QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDiEQRLNAarAIRRLSEEgKKTALVVEHDLAVLDYLS 139
|
....*....
gi 1732943882 168 TKIWSLEDQ 176
Cdd:cd03222 140 DRIHVFEGE 148
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-187 |
1.82e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLTV--FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RQDIKMTMV---EQETAS 77
Cdd:PRK15439 271 VEDLTGegFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMlngkeinalstAQRLARGLVylpEDRQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 78 YSFAD-------------------QTPAEKKLLEKWR----VPVRDFQQ----LSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:PRK15439 351 GLYLDaplawnvcalthnrrgfwiKPARENAVLERYRralnIKFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 131 TNHLDESS---LQFLIQQLKSYRGTVILVSHDryfLDEaatkIWSLEDQTLIEFKGNYSG 187
Cdd:PRK15439 431 TRGVDVSArndIYQLIRSIAAQNVAVLFISSD---LEE----IEQMADRVLVMHQGEISG 483
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
286-462 |
1.99e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 286 KTGKRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWVSpSANIGYLTQE--- 361
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEILFD-GENIPAMSRSrly 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --------VFDLPLEQTPEELFDNETYKARGHVQ--------SLMRHL---GFTASQWTEPiKHMSMGERVKCKLMAYIL 422
Cdd:PRK11831 81 tvrkrmsmLFQSGALFTDMNVFDNVAYPLREHTQlpapllhsTVMMKLeavGLRGAAKLMP-SELSGGMARRAALARAIA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 423 EEKDVLILDEPTNHLDLPSREQL----EETLSQYGGTLLAVSHD 462
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLvkliSELNSALGVTCVVVSHD 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-159 |
2.02e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.48 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT-------MVEQ--- 73
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaergVVFQneg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ---------------ETASYSFADQTPAEKKLLEKwrVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:PRK11248 81 llpwrnvqdnvafglQLAGVEKMQRLEIAHQMLKK--VGLEGAEkryiwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 134 LD---ESSLQFLIqqLKSYRGT---VILVSHD 159
Cdd:PRK11248 159 LDaftREQMQTLL--LKLWQETgkqVLLITHD 188
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
5-186 |
2.24e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 56.89 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEV--KDLTVFkNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDIKM 68
Cdd:PRK13657 335 VEFDDVSFSYdnSRQGVE-DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdirtvtrasLRRNIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVE--------QETASYSFADQTPAEKKLLEKwRVPVRDF----------------QQLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK13657 414 VFQDaglfnrsiEDNIRVGRPDATDEEMRAAAE-RAQAHDFierkpdgydtvvgergRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKSYRGTVIlVSHdRYFLDEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK13657 493 LILDEATSALDvetEAKVKAALDELMKGRTTFI-IAH-RLSTVRNADRILVFDNGRVVE-SGSFD 554
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
292-512 |
2.40e-08 |
|
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: 56.73 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG---QETAEGSV-----------WVSPSANIG- 356
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqYEPTSGRIiyhvalcekcgYVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 357 -------YLTQEVFDL----------------PLEQTPEELFDNET-------------YKARGHVQSLMRHLGFTasQW 400
Cdd:TIGR03269 81 pcpvcggTLEPEEVDFwnlsdklrrrirkriaIMLQRTFALYGDDTvldnvlealeeigYEGKEAVGRAVDLIEMV--QL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 401 TEPIKH----MSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPS----REQLEETLSQYGGTLLAVSHDRYFLEKTTNs 472
Cdd:TIGR03269 159 SHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSD- 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1732943882 473 KLVISDNGIDKQLNDVPTERNEREELRLKLETERQEVLGK 512
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVAVFMEGVSEVEKECEVEVGE 277
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-159 |
2.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 55.40 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFK-----NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------ 61
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipanlkkikevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 -LRQDIKMTM------VEQETASYSFA--------DQTPAEKK---LLEKWRVPvRDFQ-----QLSGGEKLKARLAKGL 118
Cdd:PRK13645 87 rLRKEIGLVFqfpeyqLFQETIEKDIAfgpvnlgeNKQEAYKKvpeLLKLVQLP-EDYVkrspfELSGGQKRRVALAGII 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 119 SVDADLLLLDEPTNHLD----ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHN 210
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-164 |
2.67e-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: 55.07 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 26 SVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG-------------------------QILRQDIKMTMVEQetasysF 80
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeildefrgselqnyftKLLEGDVKVIVKPQ------Y 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 ADQTPAEKK-----LLEKW----------------RVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---E 136
Cdd:cd03236 96 VDLIPKAVKgkvgeLLKKKdergkldelvdqlelrHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqR 175
|
170 180
....*....|....*....|....*...
gi 1732943882 137 SSLQFLIQQLKSYRGTVILVSHDRYFLD 164
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-348 |
2.76e-08 |
|
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: 56.23 E-value: 2.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-F----------KNVNASVQQGDIIGIIGKNGAGKS----TLLHLIHNDLAPAQGQIL--RQDI--------- 66
Cdd:COG4172 8 SVEDLSVaFgqgggtveavKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILfdGQDLlglserelr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -----KMTMVEQE--TA---SYSFADQ-------------TPAEKK---LLEKWRVP-----VRDF-QQLSGGEKLKARL 114
Cdd:COG4172 88 rirgnRIAMIFQEpmTSlnpLHTIGKQiaevlrlhrglsgAAARARaleLLERVGIPdperrLDAYpHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 115 AKGLSVDADLLLLDEPTNHLDeSSLQF----LIQQLKSYRGT-VILVSHD----RYFLDEAATkiwsledqtliefkgny 185
Cdd:COG4172 168 AMALANEPDLLIADEPTTALD-VTVQAqildLLKDLQRELGMaLLLITHDlgvvRRFADRVAV----------------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 186 sgyMKfrekkrltqqreyekQQKMVERIEAQmnELasWSKKAHDqstkkegfkeYhrvkakrTDAQIKSKQKRLEKELEk 265
Cdd:COG4172 230 ---MR---------------QGEIVEQGPTA--EL--FAAPQHP----------Y-------TRKLLAAEPRGDPRPVP- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 266 AKAEPVkpeytvhfsidtskktgkrfLEVQNITKAF-GERTLFKNT----------NFTIQHGEKVAIIGPNGSGKTTLL 334
Cdd:COG4172 270 PDAPPL--------------------LEARDLKVWFpIKRGLFRRTvghvkavdgvSLTLRRGETLGLVGESGSGKSTLG 329
|
410
....*....|....
gi 1732943882 335 KIILGQETAEGSVW 348
Cdd:COG4172 330 LALLRLIPSEGEIR 343
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-183 |
2.95e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.19 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKD--LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQETA----- 76
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SYSFADQTPAEKKL-----------LEKWRVP-------VRDF--------------QQLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK13640 85 KVGIVFQNPDNQFVgatvgddvafgLENRAVPrpemikiVRDVladvgmldyidsepANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 125 LLLDEPTNHLDES---SLQFLIQQLKSYRG-TVILVSHDryfLDEAatkiwSLEDQTLIEFKG 183
Cdd:PRK13640 165 IILDESTSMLDPAgkeQILKLIRKLKKKNNlTVISITHD---IDEA-----NMADQVLVLDDG 219
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-165 |
2.96e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLI-----HNDLapaQGQIL-------RQDIKM 68
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIfegeelqASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 T------MVEQETASYSfaDQTPAE-----------------------KKLLEKWRV------PVRDfqqLSGGEKLKAR 113
Cdd:PRK13549 79 TeragiaIIHQELALVK--ELSVLEniflgneitpggimdydamylraQKLLAQLKLdinpatPVGN---LGLGQQQLVE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 114 LAKGLSVDADLLLLDEPTNHLDESSLQFL---IQQLKSYRGTVILVSHDryfLDE 165
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLldiIRDLKAHGIACIYISHK---LNE 205
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
292-499 |
2.99e-08 |
|
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: 56.84 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGE--RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSV------WVSPSAN-----IGYL 358
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIqidgvsWNSVTLQtwrkaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFDL---------PLEQ-TPEELFD-NETYKARGHVQSLMRHLGFtasQWTEPIKHMSMGERVKCKLMAYILEEKDV 427
Cdd:TIGR01271 1298 PQKVFIFsgtfrknldPYEQwSDEEIWKvAEEVGLKSVIEQFPDKLDF---VLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 428 LILDEPTNHLDLPSREQLEETLSQ-YGGTLLAVSHDRYFLEKTTNSKLVISDNGIdKQLNDVPTERNEREELR 499
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQsFSNCTVILSEHRVEALLECQQFLVIEGSSV-KQYDSIQKLLNETSLFK 1446
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-166 |
3.33e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMT-------------MVEQ-------------- 73
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirsprdaialgigMVHQhfmlvpnltvaeni 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ----ETASYSFADQTPAEKKLLE-----KWRV----PVRDfqqLSGGEK-----LKArlakgLSVDADLLLLDEPTNHL- 134
Cdd:COG3845 102 vlglEPTKGGRLDRKAARARIRElseryGLDVdpdaKVED---LSVGEQqrveiLKA-----LYRGARILILDEPTAVLt 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 135 ----DEsslqfLIQQLKSYRG---TVILVSHDryfLDEA 166
Cdd:COG3845 174 pqeaDE-----LFEILRRLAAegkSIIFITHK---LREV 204
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
4-174 |
3.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 54.81 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVK-DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQDIK-------- 67
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitKENIRevrkfvgl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 ----------MTMVEQETA---------SYSFADQTPAEKKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK13652 83 vfqnpddqifSPTVEQDIAfgpinlgldEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 129 EPTNHLDESSLQFLIQQL----KSYRGTVILVSHDRYFLDEAATKIWSLE 174
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYVMD 212
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
297-465 |
3.79e-08 |
|
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: 54.34 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 297 ITKAFGERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSANIGYLTQEVfdlpleqtpeelfd 376
Cdd:cd03237 6 MKKTLGEFTL-EVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYI-------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 377 neTYKARGHVQSLMRHL---GFTASQW-TEPIKHMSM-------------GERVKCKLMAYILEEKDVLILDEPTNHLDL 439
Cdd:cd03237 71 --KADYEGTVRDLLSSItkdFYTHPYFkTEIAKPLQIeqildrevpelsgGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 440 PSREQLEETLSQYG----GTLLAVSHDRYF 465
Cdd:cd03237 149 EQRLMASKVIRRFAenneKTAFVVEHDIIM 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-159 |
3.93e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 54.61 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTV-------FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL---------------RQDI---- 66
Cdd:PRK11300 7 SVSGLMMrfggllaVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhieglpghqiaRMGVvrtf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 -------KMTMVE-------QETASYSFAD--QTPA----EKKLLEK---W--RVPVRDFQQ-----LSGGEKLKARLAK 116
Cdd:PRK11300 87 qhvrlfrEMTVIEnllvaqhQQLKTGLFSGllKTPAfrraESEALDRaatWleRVGLLEHANrqagnLAYGQQRRLEIAR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 117 GLSVDADLLLLDEPT---NHLDESSLQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK11300 167 CMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNvTVLLIEHD 213
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
292-461 |
4.42e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERT---LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIL-------GQETAEG---------------- 345
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQnlyqptgGQVLLDGvplvqydhhylhrqva 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 346 SVWVSP-------SANIGYltqevfdlPLEQTPEELFDNETYKARGH------VQSLMRHLGFTASQwtepikhMSMGER 412
Cdd:TIGR00958 559 LVGQEPvlfsgsvRENIAY--------GLTDTPDEEIMAAAKAANAHdfimefPNGYDTEVGEKGSQ-------LSGGQK 623
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732943882 413 VKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGGTLLAVSH 461
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-168 |
5.49e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 54.95 E-value: 5.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQE-----TA 76
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnrhvnTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SYSFA-----------------DQTPA---EKKLLEKWR-VPVRDF-----QQLSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:PRK09452 92 FQSYAlfphmtvfenvafglrmQKTPAaeiTPRVMEALRmVQLEEFaqrkpHQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 131 TNHLD---ESSLQFLIQQLKSYRG-TVILVSHDRyflDEAAT 168
Cdd:PRK09452 172 LSALDyklRKQMQNELKALQRKLGiTFVFVTHDQ---EEALT 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
311-459 |
5.52e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 5.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 311 NFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSANIGYLTQEVFDLPLEQ-------------------TP 371
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDewqrnntdmlspgeddtgrTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 372 EELFDNETyKARGHVQSLMRHLGFTAsQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEE---T 448
Cdd:PRK10938 103 AEIIQDEV-KDPARCEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAEllaS 180
|
170
....*....|.
gi 1732943882 449 LSQYGGTLLAV 459
Cdd:PRK10938 181 LHQSGITLVLV 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-159 |
5.72e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.50 E-value: 5.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNV--SYEVKD--LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQG--QILRQDI------KM 68
Cdd:PRK10535 1 MTALLELKDIrrSYPSGEeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyRVAGQDVatldadAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 TMVEQETASYSF----------ADQT---PA-----EKK--------LLEKWRVPVR-DFQ--QLSGGEKLKARLAKGLS 119
Cdd:PRK10535 81 AQLRREHFGFIFqryhllshltAAQNvevPAvyaglERKqrllraqeLLQRLGLEDRvEYQpsQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 120 VDADLLLLDEPTNHLDESS---LQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSgeeVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-159 |
6.36e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 54.32 E-value: 6.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDIKMTMVEQET------- 75
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLVIQKTrfkkikk 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 --------------ASYSFADQT---------------PAE-----KKLLEKWRVPVRDFQQ----LSGGEKLKARLAKG 117
Cdd:PRK13651 100 ikeirrrvgvvfqfAEYQLFEQTiekdiifgpvsmgvsKEEakkraAKYIELVGLDESYLQRspfeLSGGQKRRVALAGI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 118 LSVDADLLLLDEPTNHLD-ESSLQFL--IQQLKSYRGTVILVSHD 159
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDpQGVKEILeiFDNLNKQGKTIILVTHD 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-169 |
6.57e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.60 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------------L 62
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarslsqqkglirqL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 RQDIKM-----------TMVEQETASYSFADQTPAE------KKLLEKWRVPVRDF---QQLSGGEKLKARLAKGLSVDA 122
Cdd:PRK11264 84 RQHVGFvfqnfnlfphrTVLENIIEGPVIVKGEPKEeataraRELLAKVGLAGKETsypRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 123 DLLLLDEPTNHLD-ESSLQFL--IQQLKSYRGTVILVSHDRYFLDEAATK 169
Cdd:PRK11264 164 EVILFDEPTSALDpELVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADR 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-158 |
7.34e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 7.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLT-------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQD------------- 65
Cdd:PRK13538 3 EARNLAcerderiLFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepirRQRdeyhqdllylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 66 --IK--MTMVEQETASYSFADQTPAEK--KLLEKW------RVPVRdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:PRK13538 83 pgIKteLTALENLRFYQRLHGPGDDEAlwEALAQVglagfeDVPVR---QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180
....*....|....*....|....*...
gi 1732943882 134 LDESSLQFLIQQLKSYR---GTVILVSH 158
Cdd:PRK13538 160 IDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
292-349 |
7.83e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.31 E-value: 7.83e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 292 LEVQNITKAF----GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWV 349
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPtSGSVLV 64
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-170 |
8.10e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 53.59 E-value: 8.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVKDLT-VFKNVNASVQQGDIIGIIGKNGAGKST-LLHL--IHndlAPAQGQI--LRQDI-------- 66
Cdd:PRK13647 1 MDNIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTlLLHLngIY---LPQRGRVkvMGREVnaenekwv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 --KMTMVEQETASYSFA------------DQTPAEKKLLEKWR-----VPVRDFQQ-----LSGGEKLKARLAKGLSVDA 122
Cdd:PRK13647 78 rsKVGLVFQDPDDQVFSstvwddvafgpvNMGLDKDEVERRVEealkaVRMWDFRDkppyhLSYGQKKRVAIAGVLAMDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 123 DLLLLDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKI 170
Cdd:PRK13647 158 DVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQV 208
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-158 |
8.29e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLTvfkNVNASVQQGDIIGIIGKNGAGKSTLLHL-------------IHNDlapaqGQILR-QDIK------------ 67
Cdd:NF040905 14 VKALD---DVNLSVREGEIHALCGENGAGKSTLMKVlsgvyphgsyegeILFD-----GEVCRfKDIRdsealgiviihq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 -------MTMVE-----QETASYSFAD--QTPAE-KKLLEkwRV--------PVRDF----QQLsggeklkARLAKGLSV 120
Cdd:NF040905 86 elalipyLSIAEniflgNERAKRGVIDwnETNRRaRELLA--KVgldespdtLVTDIgvgkQQL-------VEIAKALSK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 121 DADLLLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSH 158
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAqgiTSIIISH 197
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
289-462 |
8.36e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.58 E-value: 8.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 289 KRFLEVQNITKAFG---ERTLFKNTNFTIQHGEKVAIIGPNGSGKTT-------LLK------IILGQETAEGSVWvsps 352
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrlidgLLEaesgqiIIDGDLLTEENVW---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 353 aNIGYLTQEVFDLPLEQ----TPEE---------LFDNETYKARghVQSLMRHLGFTASQWTEPIKhMSMGERVKCKLMA 419
Cdd:PRK13650 78 -DIRHKIGMVFQNPDNQfvgaTVEDdvafglenkGIPHEEMKER--VNEALELVGMQDFKEREPAR-LSGGQKQRVAIAG 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 420 YILEEKDVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIkgirDDYQMTVISITHD 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-158 |
9.82e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.53 E-value: 9.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 14 VKDLTvfkNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILrqdIKMTMVEQETASYSFA------------ 81
Cdd:PRK11288 17 VKALD---DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL---IDGQEMRFASTTAALAagvaiiyqelhl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 --DQTPAE---------------KKLLEKW--------------RVPVRDfqqLSGGEKLKARLAKGLSVDADLLLLDEP 130
Cdd:PRK11288 91 vpEMTVAEnlylgqlphkggivnRRLLNYEareqlehlgvdidpDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 131 TNHLD--ESSLQF-LIQQLKSyRGTVIL-VSH 158
Cdd:PRK11288 168 TSSLSarEIEQLFrVIRELRA-EGRVILyVSH 198
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-180 |
9.83e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.68 E-value: 9.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------LRQDIKMTM------------- 70
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagyhitpetgnknlkkLRKKVSLVFqfpeaqlfentvl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 --VEQETASYSFADQTPAEKKLleKW--RVPVRD-------FQqLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSL 139
Cdd:PRK13641 105 kdVEFGPKNFGFSEDEAKEKAL--KWlkKVGLSEdliskspFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 140 QFLIQQLKSYRG---TVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK13641 182 KEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
292-461 |
1.00e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 53.24 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII-----LGQE-TAEGSV------WVSPSANIGYLT 359
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEvTITGSIvynghnIYSPRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QE---VFDLPlEQTPEELFDNETYKAR-----------GHVQSLMRhlgfTASQWTEPIKH-------MSMGERVKCKLM 418
Cdd:PRK14239 86 KEigmVFQQP-NPFPMSIYENVVYGLRlkgikdkqvldEAVEKSLK----GASIWDEVKDRlhdsalgLSGGQQQRVCIA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1732943882 419 AYILEEKDVLILDEPTNHLDLPSREQLEETL----SQYggTLLAVSH 461
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLlglkDDY--TMLLVTR 205
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
292-339 |
1.13e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.55 E-value: 1.13e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-157 |
1.17e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.35 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------LRQDIKMTMVEQETASYSFA------ 81
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrqaLQKNLVAYVPQSEEVDWSFPvlvedv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 ------------------DQTPAEKKLLekwRVPVRDFQ-----QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS 138
Cdd:PRK15056 101 vmmgryghmgwlrrakkrDRQIVTAALA---RVDMVEFRhrqigELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|.
gi 1732943882 139 LQFLIQQLKSYR--GTVILVS 157
Cdd:PRK15056 178 EARIISLLRELRdeGKTMLVS 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-168 |
1.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 53.17 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 1 MKEIVTLTNVSYEVK---DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LR 63
Cdd:PRK13642 1 MNKILEVENLVFKYEkesDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVkidgelltaenvwnLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 64 QDIKMTM-----------VEQETAsYSFADQTPAEKKLLEK-----WRVPVRDFQ-----QLSGGEKLKARLAKGLSVDA 122
Cdd:PRK13642 81 RKIGMVFqnpdnqfvgatVEDDVA-FGMENQGIPREEMIKRvdealLAVNMLDFKtrepaRLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 123 DLLLLDEPTNHLD---ESSLQFLIQQLK-SYRGTVILVSHDryfLDEAAT 168
Cdd:PRK13642 160 EIIILDESTSMLDptgRQEIMRVIHEIKeKYQLTVLSITHD---LDEAAS 206
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
279-461 |
1.33e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 54.28 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 279 FSIDTSKKTGKRFLEVQNITKAfGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQEtaEGSVWVSPSANI--- 355
Cdd:TIGR00955 14 VAQDGSWKQLVSRLRGCFCRER-PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS--PKGVKGSGSVLLngm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 -----------GYLTQEVFDLPLEQTPEELF--------DNETYKARGH-VQSLMRHLGFTASQWT-----EPIKHMSMG 410
Cdd:TIGR00955 91 pidakemraisAYVQQDDLFIPTLTVREHLMfqahlrmpRRVTKKEKRErVDEVLQALGLRKCANTrigvpGRVKGLSGG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1732943882 411 ERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL---SQYGGTLLAVSH 461
Cdd:TIGR00955 171 ERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLkglAQKGKTIICTIH 224
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-177 |
1.49e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.04 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF--------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAP-AQGQILR-QDIKMTMVEQ--------- 73
Cdd:COG4178 364 ALEDLTLRtpdgrpllEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLWPyGSGRIARpAGARVLFLPQrpylplgtl 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 -ETASYSFADQTPAEKKL---LEKWRVP--------VRDFQQ-LSGGEKLK---AR--LAKglsvdADLLLLDEPTNHLD 135
Cdd:COG4178 443 rEALLYPATAEAFSDAELreaLEAVGLGhlaerldeEADWDQvLSLGEQQRlafARllLHK-----PDWLFLDEATSALD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 136 ESSLQFLIQQLKS--YRGTVILVSHdRYFLDEAATKIWSLEDQT 177
Cdd:COG4178 518 EENEAALYQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
274-465 |
1.71e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.82 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 274 EYTVHFSIDTSKKTGKRfLEVQNITKAFGERTL-FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVW--- 348
Cdd:PRK10522 306 PYKAEFPRPQAFPDWQT-LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQPQSGEILldg 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 349 --VSPSANIGY--LTQEVF-DLPL---------EQTPEELFDNetYKARGHVQSLMRHLGFTASQwtepIKhMSMGERVK 414
Cdd:PRK10522 385 kpVTAEQPEDYrkLFSAVFtDFHLfdqllgpegKPANPALVEK--WLERLKMAHKLELEDGRISN----LK-LSKGQKKR 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 415 CKLMAYILEEKDVLILDEPTNHLDLPSR----EQLEETLSQYGGTLLAVSH-DRYF 465
Cdd:PRK10522 458 LALLLALAEERDILLLDEWAADQDPHFRrefyQVLLPLLQEMGKTIFAISHdDHYF 513
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
316-466 |
1.82e-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: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 316 HGEKVAIIGPNGSGKTTLLKIILGQetaegsvwvspsanigyltqevfdLPLEQTPEELFDNETYKARGHVQSLMRHLGF 395
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE------------------------LGPPGGGVIYIDGEDILEEVLDQLLLIIVGG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 396 TasqwtepiKHMSMGERVKCKLMAYILEEK-DVLILDEPTNHLDLPSREQLEE---------TLSQYGGTLLAVSHDRYF 465
Cdd:smart00382 57 K--------KASGSGELRLRLALALARKLKpDVLILDEITSLLDAEQEALLLLleelrllllLKSEKNLTVILTTNDEKD 128
|
.
gi 1732943882 466 L 466
Cdd:smart00382 129 L 129
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
11-156 |
1.82e-07 |
|
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: 51.64 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 11 SYEVKDLT---------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDI----------KMT 69
Cdd:cd03369 6 EIEVENLSvryapdlppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEidGIDIstipledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 MVEQETASYS---------FADQTpaEKKLLEKWRVPvRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSlQ 140
Cdd:cd03369 86 IIPQDPTLFSgtirsnldpFDEYS--DEEIYGALRVS-EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT-D 161
|
170
....*....|....*...
gi 1732943882 141 FLIQQL--KSYRGTVILV 156
Cdd:cd03369 162 ALIQKTirEEFTNSTILT 179
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-187 |
1.84e-07 |
|
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: 51.88 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVK----DLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA---QGQILRQDIKMT-MVEQET 75
Cdd:cd03233 3 TLSWRNISFTTGkgrsKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKeFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ASYSFADQtpaekkllEKWRVP---VR---DF----------QQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS- 138
Cdd:cd03233 83 GEIIYVSE--------EDVHFPtltVRetlDFalrckgnefvRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTa 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 139 LQFL--IQQLKSYRGTVILVShdryfLDEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:cd03233 155 LEILkcIRTMADVLKTTTFVS-----LYQASDEIYDLFDKVLVLYEGRqiYYG 202
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
306-448 |
1.94e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.55 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 306 LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSvwVSPSANIGYLTQEVFDLPLEQTPEELF----DNETY 380
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGElEPSEGK--IKHSGRISFSSQFSWIMPGTIKENIIFgvsyDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 381 KARGHVQSLMRHLGFTASQWTEPIKH----MSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFES 201
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
301-461 |
2.35e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 52.43 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 301 FGERTLFkNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSPSANIGYLTQE-----------VFDLPLE 368
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGKVTVGDIVVSSTSKQKeikpvrkkvgvVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 369 QTPEEL-----------FDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHL 437
Cdd:PRK13643 96 QLFEETvlkdvafgpqnFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 1732943882 438 DLPSR---EQLEETLSQYGGTLLAVSH 461
Cdd:PRK13643 176 DPKARiemMQLFESIHQSGQTVVLVTH 202
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-159 |
2.53e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 51.70 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 17 LTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAPAQGQILRQDIKmTMVEQETASY----------SFA--- 81
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAglDDGSSGEVSLVGQPLH-QMDEEARAKLrakhvgfvfqSFMlip 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 82 -------DQTPA-------------EKKLLEKWRVPVRDFQ---QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS 138
Cdd:PRK10584 102 tlnalenVELPAllrgessrqsrngAKALLEQLGLGKRLDHlpaQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
|
170 180
....*....|....*....|....*
gi 1732943882 139 ----LQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK10584 182 gdkiADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-166 |
2.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 52.30 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 11 SYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LR------------Q 64
Cdd:PRK13632 16 SYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenlkeIRkkigiifqnpdnQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 DIKMTmVEQETA----------------SYSFADQTPAEKKLlekwrvpVRDFQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK13632 96 FIGAT-VEDDIAfglenkkvppkkmkdiIDDLAKKVGMEDYL-------DKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1732943882 129 EPTNHLD----ESSLQFLIQQLKSYRGTVILVSHDryfLDEA 166
Cdd:PRK13632 168 ESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEA 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
289-461 |
2.59e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 53.31 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 289 KRFLEVQNITKAFGERTLFKNT-----------------------NFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEG 345
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASNDpvtieaedleilspdgktlagplNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQG 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 346 SVWVSpsanigylTQEVFDLPLE----------QTPeELF-----DNETYkARGH-----VQSLMRHLG---FTASQ--- 399
Cdd:PRK11174 405 SLKIN--------GIELRELDPEswrkhlswvgQNP-QLPhgtlrDNVLL-GNPDasdeqLQQALENAWvseFLPLLpqg 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 400 WTEPIKH----MSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSH 461
Cdd:PRK11174 475 LDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTH 542
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
292-484 |
2.88e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 51.89 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII-LGQETAEGSVWVSpSANIGYLTQ-----EVFD- 364
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInFLEKPSEGSIVVN-GQTINLVRDkdgqlKVADk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 --LPLEQT------------------------PEELFDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLM 418
Cdd:PRK10619 85 nqLRLLRTrltmvfqhfnlwshmtvlenvmeaPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 419 AYILEEKDVLILDEPTNHLD---LPSREQLEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGIDKQ 484
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-158 |
3.24e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 51.70 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF-------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAP---AQGQI----------------LRQ 64
Cdd:PRK14239 7 QVSDLSVYynkkkalNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIvynghniysprtdtvdLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 65 DIKMT--------MVEQETASYSFADQTPAEKKLLEK-----------WRvPVRDFQQ-----LSGGEKLKARLAKGLSV 120
Cdd:PRK14239 87 EIGMVfqqpnpfpMSIYENVVYGLRLKGIKDKQVLDEavekslkgasiWD-EVKDRLHdsalgLSGGQQQRVCIARVLAT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 121 DADLLLLDEPTNHLDESSLQFLIQQLKSYRG--TVILVSH 158
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTR 205
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
303-462 |
3.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.09 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSpSANIGYLTQEVFDLPLEQT-------PE-E 373
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlKPTTGTVTVD-DITITHKTKDKYIRPVRKRigmvfqfPEsQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 374 LFDN-----------------ETYKARGHvqSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:PRK13646 98 LFEDtvereiifgpknfkmnlDEVKNYAH--RLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|
gi 1732943882 437 LDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLqtdeNKTIILVSHD 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-164 |
3.28e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLI--HNDLAPAQGQILRQDIKMTMVEQETASYS 79
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 ---FADQTPAE------KKLLEKWRVPVRDFQQL----------------------------------SGGEKLKARLAK 116
Cdd:CHL00131 85 gifLAFQYPIEipgvsnADFLRLAYNSKRKFQGLpeldplefleiineklklvgmdpsflsrnvnegfSGGEKKRNEILQ 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 117 GLSVDADLLLLDEPTNHLDESSLQFL---IQQLKSYRGTVILVSHDRYFLD 164
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSIILITHYQRLLD 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
292-462 |
3.61e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.80 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF--GERTL--FKNTNFTIQHGEKVAIIGPNGSGKTTLLKII--LGQETAeGSVWVS-------PSANIGYL 358
Cdd:PRK10535 5 LELKDIRRSYpsGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLDKPTS-GTYRVAgqdvatlDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVF-----------DLPLEQT---PEELFDNETYKARGHVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEE 424
Cdd:PRK10535 84 RREHFgfifqryhllsHLTAAQNvevPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 425 KDVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSHD 462
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLrdrGHTVIIVTHD 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-180 |
4.43e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 4.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHL------IHNDLAPAQGQIL------------- 62
Cdd:PRK14246 8 EDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLyfgkdifqidaik 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 -RQDIKMTMVEQ---------ETASYSFADQTPAEKKLLEK-----------WRvPVRD-----FQQLSGGEKLKARLAK 116
Cdd:PRK14246 88 lRKEVGMVFQQPnpfphlsiyDNIAYPLKSHGIKEKREIKKiveeclrkvglWK-EVYDrlnspASQLSGGQQQRLTIAR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 117 GLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKSyRGTVILVSHDRYFLDEAATKIWSLEDQTLIE 180
Cdd:PRK14246 167 ALALKPKVLLMDEPTSMIDivnSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVE 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
306-448 |
5.06e-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: 52.99 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 306 LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSvwVSPSANIGYLTQEVFDLPLEQTPEELF----DNETY 380
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGElEPSEGK--IKHSGRISFSPQTSWIMPGTIKDNIIFglsyDEYRY 518
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 381 KARGHVQSLMRHLGFTASQWTEPIKH----MSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEET 448
Cdd:TIGR01271 519 TSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
292-339 |
5.33e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.33 E-value: 5.33e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNITKAFGERT-LF--------KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:PRK15112 5 LEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAG 61
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
285-339 |
5.44e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 51.14 E-value: 5.44e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 285 KKTGKRFLEVQNITKAFG--ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTG 57
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
5-186 |
6.63e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVS--YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILR-----QDIKMT-------M 70
Cdd:PRK11176 342 IEFRNVTftYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdghdlRDYTLAslrnqvaL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 VEQE----------------TASYSFADQTPAEK-----KLLEKWR-----VPVRDFQQLSGGEKLKARLAKGLSVDADL 124
Cdd:PRK11176 422 VSQNvhlfndtianniayarTEQYSREQIEEAARmayamDFINKMDngldtVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 125 LLLDEPTNHLD---ESSLQFLIQQLKSYRgTVILVSHdRYFLDEAATKIWSLEDQTLIEfKGNYS 186
Cdd:PRK11176 502 LILDEATSALDtesERAIQAALDELQKNR-TSLVIAH-RLSTIEKADEILVVEDGEIVE-RGTHA 563
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
276-438 |
6.74e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 276 TVHFSIDTSKKTGKRfleVQNITKAFGE---RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVSP 351
Cdd:PTZ00243 645 GGHEATPTSERSAKT---PKMKTDDFFElepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfEISEGRVWAER 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 352 SanIGYLTQEVFDLPLEQTPEELFDNETYKARGH----VQSLMRHL----GFTASQWTEPIKHMSMGERVKCKLMAYILE 423
Cdd:PTZ00243 722 S--IAYVPQQAWIMNATVRGNILFFDEEDAARLAdavrVSQLEADLaqlgGGLETEIGEKGVNLSGGQKARVSLARAVYA 799
|
170
....*....|....*
gi 1732943882 424 EKDVLILDEPTNHLD 438
Cdd:PTZ00243 800 NRDVYLLDDPLSALD 814
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
4-147 |
6.77e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.93 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEV----KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHN--DLAPAQGQILRQDIKMTMVEQETAS 77
Cdd:cd03232 3 VLTWKNLNYTVpvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRSTG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 78 YsfADQTPAEKKLLeKWRVPVR---DFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLK 147
Cdd:cd03232 83 Y--VEQQDVHSPNL-TVREALRfsaLLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-159 |
7.93e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 23 VNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-----------RQDIKMTMV------EQE--TASYSFAD- 82
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYldgkpidirspRDAIRAGIMlcpedrKAEgiIPVHSVADn 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 83 --------QTPAEKKLLEKW------------RVPVRDFQQ----LSGGEKLKARLAKGLSVDADLLLLDEPTNHLD--- 135
Cdd:PRK11288 352 inisarrhHLRAGCLINNRWeaenadrfirslNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvga 431
|
170 180
....*....|....*....|....
gi 1732943882 136 ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK11288 432 KHEIYNVIYELAAQGVAVLFVSSD 455
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
292-461 |
9.64e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.42 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK-------IILGQETaEGSVWV------SPSAN---- 354
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV-EGEILLdgediyDPDVDvvel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 355 ---IGYltqeVFdlpleQTPEEL----FDNETYKARGH-----------VQSLMRHlgftASQWTEpikhmsmgerVKCK 416
Cdd:COG1117 91 rrrVGM----VF-----QKPNPFpksiYDNVAYGLRLHgikskseldeiVEESLRK----AALWDE----------VKDR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 417 LMAYILE-----------------EKDVLILDEPTNHLDLPSREQLEETL----SQYggTLLAVSH 461
Cdd:COG1117 148 LKKSALGlsggqqqrlciaralavEPEVLLMDEPTSALDPISTAKIEELIlelkKDY--TIVIVTH 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-209 |
9.81e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 50.42 E-value: 9.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIhNDLAPAQGQI----------------------L 62
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVrvegrveffnqniyerrvnlnrL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 63 RQDIKMTMVEQETASYSFADQTPAEKKLLeKWRVPV------------------------RDFQQLSGGEKLKARLAKGL 118
Cdd:PRK14258 87 RRQVSMVHPKPNLFPMSVYDNVAYGVKIV-GWRPKLeiddivesalkdadlwdeikhkihKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 119 SVDADLLLLDEPTNHLDESS---LQFLIQQLK-SYRGTVILVSHDRYfldeaatKIWSLEDQTLIeFKGNYSgymkfrek 194
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIAsmkVESLIQSLRlRSELTMVIVSHNLH-------QVSRLSDFTAF-FKGNEN-------- 229
|
250
....*....|....*
gi 1732943882 195 kRLTQQREYEKQQKM 209
Cdd:PRK14258 230 -RIGQLVEFGLTKKI 243
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
292-462 |
1.01e-06 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 49.89 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSPS------------ANIGYL 358
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPRDAGNIIIDDEdisllplhararRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQE--------VFD--LPLEQTPEELfDNETYKARG-------HVQSLMRHLGftasqwtepiKHMSMGERVKCKLMAYI 421
Cdd:PRK10895 84 PQEasifrrlsVYDnlMAVLQIRDDL-SAEQREDRAnelmeefHIEHLRDSMG----------QSLSGGERRRVEIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1732943882 422 LEEKDVLILDEPTNHLDLPSR---EQLEETLSQYGGTLLAVSHD 462
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLGVLITDHN 196
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
292-480 |
1.06e-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: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSANIGYLTQEVFDLPLEQT 370
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRAtSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 PE--ELFdnetykARGHVQSLMRHLGFTAS--QWTEPIKH------------------MSMGERVKCKLMAYILEEKDVL 428
Cdd:PRK11614 86 PEgrRVF------SRMTVEENLAMGGFFAErdQFQERIKWvyelfprlherriqragtMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 429 ILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSH---------DR-YFLEkttNSKLVISDNG 480
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLreqGMTIFLVEQnanqalklaDRgYVLE---NGHVVLEDTG 221
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-187 |
1.24e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.20 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA---QGQIL------------------RQD---IKMTMVEQE-- 74
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLlngmpidakemraisayvQQDdlfIPTLTVREHlm 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 -TASYSFADQTPAEKK------LLEkwRVPVRDFQQ-----------LSGGEKLKARLAKGLSVDADLLLLDEPTNHLDE 136
Cdd:TIGR00955 122 fQAHLRMPRRVTKKEKrervdeVLQ--ALGLRKCANtrigvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 137 SSLQFLIQQLK--SYRG-TVILVSHdryfldEAATKIWSLEDQTLIEFKGN--YSG 187
Cdd:TIGR00955 200 FMAYSVVQVLKglAQKGkTIICTIH------QPSSELFELFDKIILMAEGRvaYLG 249
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
292-449 |
1.32e-06 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK----IILGQETAEGSVWV----------------SP 351
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELlgrtvqregrlardirKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 352 SANIGYLTQEvFDL------------------PLEQTPEELFDNETyKARGhVQSLMRhLGFtASQWTEPIKHMSMGERV 413
Cdd:PRK09984 85 RANTGYIFQQ-FNLvnrlsvlenvligalgstPFWRTCFSWFTREQ-KQRA-LQALTR-VGM-VHFAHQRVSTLSGGQQQ 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 414 KCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETL 449
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTL 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
292-461 |
1.40e-06 |
|
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: 49.39 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERT---LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIL-------GQETAEG---------------- 345
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLEnfyqpqgGQVLLDGkpisqyehkylhskvs 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 346 SVWVSP-------SANIGYLTQEVfdlPLEQTPEElfdNETYKARGHVQslmrhlGFTASQWT---EPIKHMSMGERVKC 415
Cdd:cd03248 92 LVGQEPvlfarslQDNIAYGLQSC---SFECVKEA---AQKAHAHSFIS------ELASGYDTevgEKGSQLSGGQKQRV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1732943882 416 KLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
289-468 |
1.43e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.94 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 289 KRFLEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV------------SPSANI 355
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGiHEPTKGTITInninynkldhklAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQEVFDLPLEQTPEELFDN-------------ETYKARGHVQSLMRHLGFTASqWTEPIKHMSMGERVKCKLMAYIL 422
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGrhltkkvcgvniiDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 423 EEKDVLILDEPTNHLDLPSREQLEETLSQY---GGTLLAVSH---------DRYFLEK 468
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrkeGTAIVYISHklaeirricDRYTVMK 219
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-167 |
1.57e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 50.02 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI------------------LRQdiKMTMVEQ--------E 74
Cdd:PRK13634 24 YDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkpLRK--KVGIVFQfpehqlfeE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 TASYSFA--------DQTPAEKK-------------LLEkwRVPVrdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNH 133
Cdd:PRK13634 102 TVEKDICfgpmnfgvSEEDAKQKaremielvglpeeLLA--RSPF----ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 134 LDESSLQFLIQ---QLKSYRG-TVILVSHDryfLDEAA 167
Cdd:PRK13634 176 LDPKGRKEMMEmfyKLHKEKGlTTVLVTHS---MEDAA 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
8-159 |
1.57e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 49.78 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEVKDLTVF-------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIH--NDLAP---AQGQI-------------- 61
Cdd:PRK14243 7 TETVLRTENLNVYygsflavKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlNDLIPgfrVEGKVtfhgknlyapdvdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 --LRQDIKMTMVEQETASYSFADQTPAEKK----------LLEK-------WRvPVRD-----FQQLSGGEKLKARLAKG 117
Cdd:PRK14243 87 veVRRRIGMVFQKPNPFPKSIYDNIAYGARingykgdmdeLVERslrqaalWD-EVKDklkqsGLSLSGGQQQRLCIARA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1732943882 118 LSVDADLLLLDEPTNHLDESS---LQFLIQQLKSyRGTVILVSHD 159
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPIStlrIEELMHELKE-QYTIIIVTHN 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-179 |
1.66e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 49.73 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMVEQET----------ASYSFADQTPAEKKLL 91
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvgVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 92 EKWRVPVRDFQ-----------------------------QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS---L 139
Cdd:PRK13643 104 KDVAFGPQNFGipkekaekiaaeklemvgladefwekspfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArieM 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 140 QFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLEDQTLI 179
Cdd:PRK13643 184 MQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
10-159 |
1.71e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 10 VSYEVKDLTV--FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI----------------------LRQD 65
Cdd:PRK10762 256 VRLKVDNLSGpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVtldghevvtrspqdglangivyISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 66 IK-------MTMVE-------QETASYSFADQTPAEKKLLEKW------RVPVRDfQQ---LSGGEKLKARLAKGLSVDA 122
Cdd:PRK10762 336 RKrdglvlgMSVKEnmsltalRYFSRAGGSLKHADEQQAVSDFirlfniKTPSME-QAiglLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 123 DLLLLDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK10762 415 KVLILDEPTRGVDvgaKKEIYQLINQFKAEGLSIILVSSE 454
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
20-175 |
1.79e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.10 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 20 FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------------LRQDIKMTMVEQE-------- 74
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghditrlknrevpfLRRQIGMIFQDHHllmdrtvy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 75 --------TASYSFAD----QTPAEKK--LLEKWR-VPVrdfqQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDES-- 137
Cdd:PRK10908 98 dnvaipliIAGASGDDirrrVSAALDKvgLLDKAKnFPI----QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAls 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1732943882 138 -SLQFLIQQLKSYRGTVILVSHDRYFLDEAATKIWSLED 175
Cdd:PRK10908 174 eGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-180 |
2.21e-06 |
|
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: 50.51 E-value: 2.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQDIkmTMVEQETASYSF---- 80
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfslkdidrhtLRQFI--NYLPQEPYIFSGsile 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 81 -----ADQTPAEKKLLEKWRVP-----VRDFQQ------------LSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS 138
Cdd:TIGR01193 567 nlllgAKENVSQDEIWAACEIAeikddIENMPLgyqtelseegssISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1732943882 139 LQFLIQQL-KSYRGTVILVSHdRYFLDEAATKIWSLEDQTLIE 180
Cdd:TIGR01193 647 EKKIVNNLlNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
272-337 |
2.53e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 50.21 E-value: 2.53e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1732943882 272 KPEytVHFSIDTSKKTGKRFLEVQNITKAFGERTL--FKNTNFTIQHGEKVAIIGPNGSGKTTLLKII 337
Cdd:PRK11160 321 KPE--VTFPTTSTAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-447 |
2.60e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.76 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKI------------ILGQETAEG-SVWVSPSANIGYL 358
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlielypearVSGEVYLDGqDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFDLP--------LEQTPEELFDNETYKARGHVQSLMRHLGFTASQWTE-------PIKHMSMGERVKCKLMAYILE 423
Cdd:PRK14247 84 VQMVFQIPnpipnlsiFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDEvkdrldaPAGKLSGGQQQRLCIARALAF 163
|
170 180
....*....|....*....|....
gi 1732943882 424 EKDVLILDEPTNHLDLPSREQLEE 447
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIES 187
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
8-190 |
3.26e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 8 TNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDiKMTMVEQET--------ASYS 79
Cdd:PTZ00243 664 TDDFFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAER-SIAYVPQQAwimnatvrGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 FADQTPAEKkLLEKWRVPV--RDFQQL---------------SGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFL 142
Cdd:PTZ00243 743 FFDEEDAAR-LADAVRVSQleADLAQLgggleteigekgvnlSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERV 821
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 143 IQQ--LKSYRG-TVILVSHDRYFLDEaATKIWSLEDQTlIEFKGNYSGYMK 190
Cdd:PTZ00243 822 VEEcfLGALAGkTRVLATHQVHVVPR-ADYVVALGDGR-VEFSGSSADFMR 870
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
286-462 |
4.16e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 286 KTGKRFLEVQNITKAF---GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKiILGQETAEGSVWVSPSANIGYLTQEV 362
Cdd:PRK14246 2 EAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLIEIYDSKIKVDGKVLYFGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 FDLPLEQTPEE---------------LFDNETYKARGH-----------VQSLMRHLGF---TASQWTEPIKHMSMGERV 413
Cdd:PRK14246 81 FQIDAIKLRKEvgmvfqqpnpfphlsIYDNIAYPLKSHgikekreikkiVEECLRKVGLwkeVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 414 KCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHD 462
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-158 |
4.34e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 5 VTLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHN--DLAP---AQGQILR--QDI-KMTMVE-QET 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLdgQDIfKMDVIElRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 76 ASYSFADQTP---------------------AEKKLLEKWRVPVRDFQ--------------QLSGGEKLKARLAKGLSV 120
Cdd:PRK14247 84 VQMVFQIPNPipnlsifenvalglklnrlvkSKKELQERVRWALEKAQlwdevkdrldapagKLSGGQQQRLCIARALAF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 121 DADLLLLDEPTNHLD---ESSLQFLIQQLKSyRGTVILVSH 158
Cdd:PRK14247 164 QPEVLLADEPTANLDpenTAKIESLFLELKK-DMTIVLVTH 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
292-462 |
4.41e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 47.89 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTL----FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVW--------VSPSA----- 353
Cdd:PRK11629 6 LQCDNLCKRYQEGSVqtdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTpTSGDVIfngqpmskLSSAAkaelr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 --NIGYLTQEVFDLP----LEQTPEELF--DNETYKARGHVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEK 425
Cdd:PRK11629 86 nqKLGFIYQFHHLLPdftaLENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLS----QYGGTLLAVSHD 462
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGelnrLQGTAFLVVTHD 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
292-339 |
6.05e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 47.68 E-value: 6.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTG 53
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-165 |
6.29e-06 |
|
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: 49.03 E-value: 6.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 2 KEIVTLTNVS--YEVKDLTVFK---NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI---LRQD-IKMT--- 69
Cdd:TIGR03269 277 EPIIKVRNVSkrYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEwVDMTkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 70 ------------MVEQETASYSFAD-----------QTPAE--------------------KKLLEKWRvpvrdfQQLSG 106
Cdd:TIGR03269 357 pdgrgrakryigILHQEYDLYPHRTvldnlteaiglELPDElarmkavitlkmvgfdeekaEEILDKYP------DELSE 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 107 GEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR----GTVILVSHDRYFLDE 165
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAReemeQTFIIVSHDMDFVLD 493
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
292-434 |
6.47e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLLKI-------------IL--GQETAEGSVWVSPSANI 355
Cdd:NF040905 2 LEMRGITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMKVlsgvyphgsyegeILfdGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 356 GYLTQEVFDLPLEQTPEELF-DNETYK--------ARGHVQSLMRHLGFTASQWTePIKHMSMGervKCKL--MAYILeE 424
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFlGNERAKrgvidwneTNRRARELLAKVGLDESPDT-LVTDIGVG---KQQLveIAKAL-S 155
|
170
....*....|..
gi 1732943882 425 KDV--LILDEPT 434
Cdd:NF040905 156 KDVklLILDEPT 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-158 |
7.56e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 7 LTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIK-------------MTMVEQ 73
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfksskealengISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 E--------------TASYS----FADQTPA---EKKLLEKWRV---PVRDFQQLSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:PRK10982 81 ElnlvlqrsvmdnmwLGRYPtkgmFVDQDKMyrdTKAIFDELDIdidPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 130 PTNHLDESSLQFL---IQQLKSYRGTVILVSH 158
Cdd:PRK10982 161 PTSSLTEKEVNHLftiIRKLKERGCGIVYISH 192
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
292-361 |
7.66e-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: 48.17 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVqNITKAFGERTLfkNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-------GSVWVSPSAN---------I 355
Cdd:COG4148 3 LEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDsgrirlgGEVLQDSARGiflpphrrrI 79
|
....*.
gi 1732943882 356 GYLTQE 361
Cdd:COG4148 80 GYVFQE 85
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
19-170 |
9.33e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 47.77 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQiLR---QDI--------KMTMVEQETASY--------- 78
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH-IRfhgTDVsrlhardrKVGFVFQHYALFrhmtvfdni 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 79 SFA------DQTPAEK-------KLLEKWRVP---VRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSL 139
Cdd:PRK10851 96 AFGltvlprRERPNAAaikakvtQLLEMVQLAhlaDRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDaqvRKEL 175
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 140 QFLIQQL-KSYRGTVILVSHDRYFLDEAATKI 170
Cdd:PRK10851 176 RRWLRQLhEELKFTSVFVTHDQEEAMEVADRV 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
303-461 |
1.03e-05 |
|
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: 47.15 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIL-------------GQETAEGSV-WVspSANIGYLTQE--VFD-- 364
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsgeilldGVDIRDLNLrWL--RSQIGLVSQEpvLFDgt 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 365 ------LPLEQTPEELFDNETYKARGH--VQSLMR----HLGFTASQwtepikhMSMGERVKCKLMAYILEEKDVLILDE 432
Cdd:cd03249 93 iaenirYGKPDATDEEVEEAAKKANIHdfIMSLPDgydtLVGERGSQ-------LSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190
....*....|....*....|....*....|.
gi 1732943882 433 PTNHLDLPSREQLEETLSQY--GGTLLAVSH 461
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-165 |
1.12e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.10 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLTVF--------KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL--RQDIK--------------- 67
Cdd:COG3845 259 EVENLSVRddrgvpalKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRldGEDITglsprerrrlgvayi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 ------------MTMVE------QETASYS---FADQTPAE---KKLLEKWRV-------PVRdfqQLSGGEKLKARLAK 116
Cdd:COG3845 339 pedrlgrglvpdMSVAEnlilgrYRRPPFSrggFLDRKAIRafaEELIEEFDVrtpgpdtPAR---SLSGGNQQKVILAR 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 117 GLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR--GT-VILVSHDryfLDE 165
Cdd:COG3845 416 ELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdaGAaVLLISED---LDE 464
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
292-480 |
1.30e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 46.55 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEgsvwvSPSANIgylTQEVFDL---PLE 368
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPR-----SGTLNI---AGNHFDFsktPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 369 QTPEELFDN-----ETYKARGH---VQSL----MRHLGFTASQWTEPIK-----------------HMSMGERVKCKLMA 419
Cdd:PRK11124 75 KAIRELRRNvgmvfQQYNLWPHltvQQNLieapCRVLGLSKDQALARAEkllerlrlkpyadrfplHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1732943882 420 YILEEKDVLILDEPTNHLDLPSREQ----LEEtLSQYGGTLLAVSHDRYFLEKTTnSKLVISDNG 480
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQivsiIRE-LAETGITQVIVTHEVEVARKTA-SRVVYMENG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-468 |
1.45e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.93 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKS----TLLHLIH-----------------------NDLAPAQGQILR-QDIKMTMVE 72
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEqagglvqcdkmllrrrsrqvielSEQSAAQMRHVRgADMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 73 QETA-------------------SYSFADQTPAEKKLLEKWRVP------VRDFQQLSGGEKLKARLAKGLSVDADLLLL 127
Cdd:PRK10261 113 PMTSlnpvftvgeqiaesirlhqGASREEAMVEAKRMLDQVRIPeaqtilSRYPHQLSGGMRQRVMIAMALSCRPAVLIA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 128 DEPTNHLDeSSLQFLIQQL-----KSYRGTVILVSHDRYFLDEAAtkiwsleDQTLIEFKGNYSGYMKFREKKRLTQQRE 202
Cdd:PRK10261 193 DEPTTALD-VTIQAQILQLikvlqKEMSMGVIFITHDMGVVAEIA-------DRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 203 YEKQQKMVERIEAQmnelaswskKAHDQSTKkegFKEYHRVKAKRTDAQIKSKQkrlekeleKAKAEPVkpeytvhfsid 282
Cdd:PRK10261 265 TRALLAAVPQLGAM---------KGLDYPRR---FPLISLEHPAKQEPPIEQDT--------VVDGEPI----------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 283 tskktgkrfLEVQNITKAFGERT-LF----------KNTNFTIQHGEKVAIIGPNGSGKTT----LLKIIlgqETAEGSV 347
Cdd:PRK10261 314 ---------LQVRNLVTRFPLRSgLLnrvtrevhavEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLV---ESQGGEI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 348 --------WVSPSA------NIGYLTQEVF-DLPLEQT-------P---EELFDNETYKARghVQSLMRHLGFTASQ-WT 401
Cdd:PRK10261 382 ifngqridTLSPGKlqalrrDIQFIFQDPYaSLDPRQTvgdsimePlrvHGLLPGKAAAAR--VAWLLERVGLLPEHaWR 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 402 EPiKHMSMGERVK-CKLMAYILEEKdVLILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHDRYFLEK 468
Cdd:PRK10261 460 YP-HEFSGGQRQRiCIARALALNPK-VIIADEAVSALDVSIRGQIINLLldlqRDFGIAYLFISHDMAVVER 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
292-512 |
1.46e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 46.99 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTL-FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSpSANIGYLTQE-------- 361
Cdd:PRK13639 2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGiLKPTSGEVLIK-GEPIKYDKKSllevrktv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 --VFDLPLEQ----TPEE---------LFDNETYKARghVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEKD 426
Cdd:PRK13639 81 giVFQNPDDQlfapTVEEdvafgplnlGLSKEEVEKR--VKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 427 VLILDEPTNHLDLPSREQ---LEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNGIDKQ------LNDVPTERNerEE 497
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQimkLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEgtpkevFSDIETIRK--AN 235
|
250
....*....|....*
gi 1732943882 498 LRLKLETERQEVLGK 512
Cdd:PRK13639 236 LRLPRVAHLIEILNK 250
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-158 |
1.48e-05 |
|
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: 46.33 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI--------------LRQdiKMTMVEQETASYS----- 79
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskiglhdLRS--RISIIPQDPVLFSgtirs 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 80 ----FADQTPAE----------KKLLEKwrVPVR-DFQQLSGGEKLKA--R----LAKGLSVDADLLLLDEPTNHLDESS 138
Cdd:cd03244 97 nldpFGEYSDEElwqalervglKEFVES--LPGGlDTVVEEGGENLSVgqRqllcLARALLRKSKILVLDEATASVDPET 174
|
170 180
....*....|....*....|...
gi 1732943882 139 LQfLIQQ-LKSYRG--TVILVSH 158
Cdd:cd03244 175 DA-LIQKtIREAFKdcTVLTIAH 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-167 |
1.98e-05 |
|
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: 47.02 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQI-----------LRQDIK-----MTMVEQEtAS-------- 77
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIrlggevlqdsaRGIFLPphrrrIGYVFQE-ARlfphlsvr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 78 ----YSFADQTPAEKK--------------LLEkwRVPvrdfQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS- 138
Cdd:COG4148 96 gnllYGRKRAPRAERRisfdevvellgighLLD--RRP----ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARk 169
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 139 ------LQFLIQQLksyRGTVILVSHDryfLDEAA 167
Cdd:COG4148 170 aeilpyLERLRDEL---DIPILYVSHS---LDEVA 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
6-183 |
2.44e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 47.18 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 6 TLTNVSYEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA--QGQILRQDIKMT--------MVEQ-- 73
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTkqilkrtgFVTQdd 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 74 ---------ETASYSFADQTPAEKKLLEKWRVPVRDFQQL------------------SGGEKLKARLAKGLSVDADLLL 126
Cdd:PLN03211 150 ilyphltvrETLVFCSLLRLPKSLTKQEKILVAESVISELgltkcentiignsfirgiSGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 127 LDEPTNHLDESSLQFLIQQLKS--YRGTVILVShdryfLDEAATKIWSLEDQTLIEFKG 183
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSlaQKGKTIVTS-----MHQPSSRVYQMFDSVLVLSEG 283
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
20-159 |
2.47e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 46.07 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 20 FKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIL-------RQDIkMTMVEQET-----ASYSFADQTPAE 87
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqLRDL-YALSEAERrrllrTEWGFVHQHPRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 88 -------------KKLL--------------EKW--RVPV---------RDFqqlSGGEKLKARLAKGLSVDADLLLLDE 129
Cdd:PRK11701 101 glrmqvsaggnigERLMavgarhygdirataGDWleRVEIdaariddlpTTF---SGGMQQRLQIARNLVTHPRLVFMDE 177
|
170 180 190
....*....|....*....|....*....|....
gi 1732943882 130 PTNHLDES---SLQFLIQQLKSYRG-TVILVSHD 159
Cdd:PRK11701 178 PTGGLDVSvqaRLLDLLRGLVRELGlAVVIVTHD 211
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
313-442 |
2.52e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 313 TIQHGEKVAIIGPNGSGKTTLLKII-------LGQETAEGSvW-----------------------VSPSANIGYLTQ-- 360
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILsgelipnLGDYEEEPS-WdevlkrfrgtelqnyfkklyngeIKVVHKPQYVDLip 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EVF-----DLpLEQTPEelfdnetykaRGHVQSLMRHLGFTASqWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:PRK13409 174 KVFkgkvrEL-LKKVDE----------RGKLDEVVERLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
....*..
gi 1732943882 436 HLDLPSR 442
Cdd:PRK13409 242 YLDIRQR 248
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
292-499 |
2.64e-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: 46.00 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGE--RTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIL------GQETAEGSVWVSPSAN-----IGYL 358
Cdd:cd03289 3 MTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGDIQIDGVSWNSVPLQkwrkaFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 359 TQEVFDL---------PLEQ-TPEELFD-NETYKARGHVQSLMRHLGFTASQWTEPIKHmsmGERVKCKLMAYILEEKDV 427
Cdd:cd03289 83 PQKVFIFsgtfrknldPYGKwSDEEIWKvAEEVGLKSVIEQFPGQLDFVLVDGGCVLSH---GHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 428 LILDEPTNHLDLPSREQLEETLSQ-YGGTLLAVSHDRYFLEKTTNSKLVISDNGIdKQLNDVPTERNEREELR 499
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKV-RQYDSIQKLLNEKSHFK 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
292-334 |
3.12e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 45.85 E-value: 3.12e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1732943882 292 LEVQNITKAFGERT-----LFKNTNFTIQHGEKVAIIGPNGSGKTTLL 334
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFI 50
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
313-462 |
3.36e-05 |
|
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: 46.70 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 313 TIQHGEKVAIIGPNGSGKTTLLKIILGQET-------------------------------AEGSVWVSpsanigYLTQE 361
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKpnlgdydeepswdevlkrfrgtelqdyfkklANGEIKVA------HKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 VFDLP--LEQTPEELFdnETYKARGHVQSLMRHLGFTASqWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDL 439
Cdd:COG1245 169 VDLIPkvFKGTVRELL--EKVDERGKLDELAEKLGLENI-LDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|....*...
gi 1732943882 440 psREQLE-----ETLSQYGGTLLAVSHD 462
Cdd:COG1245 246 --YQRLNvarliRELAEEGKYVLVVEHD 271
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
292-464 |
3.64e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 45.22 E-value: 3.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE-GSVWVSPSAN--------IGYLTQev 362
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTAtrgdrsrfMAYLGH-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 363 fdLP-LEQ---TPEEL-FDN--ETYKARGHVQSLMRHLGFTASQWTePIKHMSMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:PRK13543 90 --LPgLKAdlsTLENLhFLCglHGRRAKQMPGSALAIVGLAGYEDT-LVRQLSAGQKKRLALARLWLSPAPLWLLDEPYA 166
|
170 180 190
....*....|....*....|....*....|..
gi 1732943882 436 HLDLPSREQLEETLSQY---GGTLLAVSHDRY 464
Cdd:PRK13543 167 NLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
302-438 |
4.38e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 4.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 302 GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ--ETAEGSVWVSPSanIGYLTQ-------EVFDLPLEQTPe 372
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElpPRSDASVVIRGT--VAYVPQvswifnaTVRDNILFGSP- 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 373 elFDNETYKARGHVQSLMRHL----GFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLD 438
Cdd:PLN03130 705 --FDPERYERAIDVTALQHDLdllpGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-267 |
4.65e-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: 45.23 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 13 EVKDLT---------VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNdLAPAQGQILRQDI---KMTMVEQETA---- 76
Cdd:cd03289 4 TVKDLTakyteggnaVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGDIQIDGVswnSVPLQKWRKAfgvi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 -SYSFADQTPAEKKL--------LEKWRVPVR--------------DFQQ------LSGGEKLKARLAKGLSVDADLLLL 127
Cdd:cd03289 83 pQKVFIFSGTFRKNLdpygkwsdEEIWKVAEEvglksvieqfpgqlDFVLvdggcvLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 128 DEPTNHLDESSLQFLIQQLK-SYRGTVILVSHDRYfldEAAtkiwsLEDQTLIEFKGNysgymkfrekkrltQQREYEKQ 206
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKqAFADCTVILSEHRI---EAM-----LECQRFLVIEEN--------------KVRQYDSI 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 207 QKMVerieaqmNElASWSKKAHDQSTKKEGFKEYHRVKAKR-TDAQIKSKQKRLEKELEKAK 267
Cdd:cd03289 221 QKLL-------NE-KSHFKQAISPSDRLKLFPRRNSSKSKRkPRPQIQALQEETEEEVQDTR 274
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-159 |
4.86e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKST----LLHLIhndlaPAQGQI-----------------LRQDIKMTM------ 70
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIwfdgqplhnlnrrqllpVRHRIQVVFqdpnss 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 71 ------VEQETA--------SYSFADQTPAEKKLLE--------KWRVPvrdfQQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK15134 375 lnprlnVLQIIEeglrvhqpTLSAAQREQQVIAVMEevgldpetRHRYP----AEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190
....*....|....*....|....*....|....*
gi 1732943882 129 EPTNHLDESSLQFLIQQLKS----YRGTVILVSHD 159
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSlqqkHQLAYLFISHD 485
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
290-462 |
5.55e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.08 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 290 RFLEVQNITKAFGERTLFKNTN---FTIQHGEKVAIIGPNGSGKTTLLKIILGQ-ETAEGSVWVS----PSANIGYLTQE 361
Cdd:PRK13642 3 KILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLfEEFEGKVKIDgellTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 362 VFdlPLEQTPEELFDNETYK---ARG-------------HVQSLMRHLGFTASQWTEPIKhMSMGERVKCKLMAYILEEK 425
Cdd:PRK13642 83 IG--MVFQNPDNQFVGATVEddvAFGmenqgipreemikRVDEALLAVNMLDFKTREPAR-LSGGQKQRVAVAGIIALRP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1732943882 426 DVLILDEPTNHLDLPSREQ----LEETLSQYGGTLLAVSHD 462
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEimrvIHEIKEKYQLTVLSITHD 200
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
293-463 |
5.96e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 5.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 293 EVQNITKAF-GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKII-LGQETAEGSVWV-----------SPSANIGYLT 359
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqRVFDPQSGRILIdgtdirtvtraSLRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QE--VFDLPLEQ---------TPEELfdnetYKARGHVQSL---MRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEK 425
Cdd:PRK13657 416 QDagLFNRSIEDnirvgrpdaTDEEM-----RAAAERAQAHdfiERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDP 490
|
170 180 190
....*....|....*....|....*....|....*...
gi 1732943882 426 DVLILDEPTNHLDLPSREQLEETLSqyggtllAVSHDR 463
Cdd:PRK13657 491 PILILDEATSALDVETEAKVKAALD-------ELMKGR 521
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
18-462 |
6.03e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.85 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 18 TVFKNVNASVQQGDIIGIIGKNGAGKS----TLLHLIH---------------NDLAPAQGQILRQ--DIKMTMVEQETA 76
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPsppvvypsgdirfhgESLLHASEQTLRGvrGNKIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SySFADQTPAEKKLLEKW--------------------RVPVR-------DF-QQLSGGEKLKARLAKGLSVDADLLLLD 128
Cdd:PRK15134 103 V-SLNPLHTLEKQLYEVLslhrgmrreaargeilncldRVGIRqaakrltDYpHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 129 EPTNHLDeSSLQFLIQQLksyrgtvilvshdryfldeaatkiwsledqtLIEFKGNYSGYMKFrekkrLTqqreyekqqk 208
Cdd:PRK15134 182 EPTTALD-VSVQAQILQL-------------------------------LRELQQELNMGLLF-----IT---------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 209 mverieaqmNELASWSKKAHDQSTKKEGfkeyHRVKAKRTDAQIKSKQKRLEKELekAKAEPVKpeYTVHFSIDTSkktg 288
Cdd:PRK15134 215 ---------HNLSIVRKLADRVAVMQNG----RCVEQNRAATLFSAPTHPYTQKL--LNSEPSG--DPVPLPEPAS---- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 289 kRFLEVQNITKAF-----------GERTLFKNTNFTIQHGEKVAIIGPNGSGKTT----LLKIIlgqeTAEGSVWVSPSA 353
Cdd:PRK15134 274 -PLLDVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI----NSQGEIWFDGQP 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 NIGYLTQEVfdLPLEQTPEELFD--NETYKARGHVQSLM------RHLGFTASQWTEP-IKHM----------------- 407
Cdd:PRK15134 349 LHNLNRRQL--LPVRHRIQVVFQdpNSSLNPRLNVLQIIeeglrvHQPTLSAAQREQQvIAVMeevgldpetrhrypaef 426
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 408 SMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQ---LEETLSQ-YGGTLLAVSHD 462
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQkHQLAYLFISHD 485
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-158 |
6.43e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 3 EIVTLTNVS-----YEVKDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIK---------- 67
Cdd:PRK13631 20 IILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYigdkknnhel 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 68 ------------------MTMVEQETASYSFAD--------------QTPAEKKLLEKW-------------RVPVrdfq 102
Cdd:PRK13631 100 itnpyskkiknfkelrrrVSMVFQFPEYQLFKDtiekdimfgpvalgVKKSEAKKLAKFylnkmglddsyleRSPF---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1732943882 103 QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD---ESSLQFLIQQLKSYRGTVILVSH 158
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLILDAKANNKTVFVITH 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
292-462 |
6.59e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK-------IILGQEtAEGSVW----------VSPSA- 353
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR-VEGKVTfhgknlyapdVDPVEv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 354 --NIGYltqeVFDLPlEQTPEELFDNETYKAR-----GHVQSLMRHLGFTASQWTEpIK--------HMSMGERVKCKLM 418
Cdd:PRK14243 90 rrRIGM----VFQKP-NPFPKSIYDNIAYGARingykGDMDELVERSLRQAALWDE-VKdklkqsglSLSGGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1732943882 419 AYILEEKDVLILDEPTNHLDLPSREQLEETLSQYGG--TLLAVSHD 462
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
99-159 |
7.88e-05 |
|
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: 44.17 E-value: 7.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 99 RDFQQLSGGEKLKARLAK--GLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR---GTVILVSHD 159
Cdd:cd03270 133 RSAPTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRdlgNTVLVVEHD 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
103-183 |
9.02e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 44.32 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 103 QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESSLQFLIQQLKSY--RGTVILVSHDryfLDEAAtkiwSLEDQTLIE 180
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLadRLTVIIVTHN---LAQAA----RISDRAALF 235
|
...
gi 1732943882 181 FKG 183
Cdd:PRK14271 236 FDG 238
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
292-344 |
1.04e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 1.04e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAE 344
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYE 54
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
292-349 |
1.26e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 44.45 E-value: 1.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTL-FKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV 349
Cdd:PRK11650 4 LKLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERiTSGEIWI 63
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
311-461 |
1.32e-04 |
|
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: 44.74 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 311 NFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSPSANIGYLTQEVF-------------DLPLEQTPEELFD 376
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRILGElWPVYGGRLTKPAKGKLFYVPQRPYmtlgtlrdqiiypDSSEDMKRRGLSD 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 377 NETYKARGHVQ---SLMRHLGFTASQ-WTEpikHMSMGERVKCKlMAYILEEK-DVLILDEPTNHLDLPSREQLEETLSQ 451
Cdd:TIGR00954 552 KDLEQILDNVQlthILEREGGWSAVQdWMD---VLSGGEKQRIA-MARLFYHKpQFAILDECTSAVSVDVEGYMYRLCRE 627
|
170
....*....|
gi 1732943882 452 YGGTLLAVSH 461
Cdd:TIGR00954 628 FGITLFSVSH 637
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
292-469 |
1.79e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 42.63 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSANI-----GYLTQEVF--- 363
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlcTYQKQLCFvgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 364 ------DLPLEQTPeeLFDNETYKARGHVQSLMRHlgFTASQWTE-PIKHMSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:PRK13540 82 rsginpYLTLRENC--LYDIHFSPGAVGITELCRL--FSLEHLIDyPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1732943882 437 LDLPSREQLEETLSQY---GGTLLAVSHDRYFLEKT 469
Cdd:PRK13540 158 LDELSLLTIITKIQEHrakGGAVLLTSHQDLPLNKA 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
292-462 |
1.83e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.49 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPS------------ANIGYLT 359
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRveffnqniyerrVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 360 QE---VFDLPlEQTPEELFDNETYKAR-----------GHVQSLMRhlgfTASQWTEpIKH--------MSMGERVKCKL 417
Cdd:PRK14258 88 RQvsmVHPKP-NLFPMSVYDNVAYGVKivgwrpkleidDIVESALK----DADLWDE-IKHkihksaldLSGGQQQRLCI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1732943882 418 MAYILEEKDVLILDEPTNHLDlPSREQLEETLSQYGG-----TLLAVSHD 462
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLD-PIASMKVESLIQSLRlrselTMVIVSHN 210
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
314-462 |
1.89e-04 |
|
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: 42.56 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 314 IQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSANIGYLTQEVfdlpleqtpeelfdnetykarghvqslmrhl 393
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYI------------------------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 394 gftasqwtepikHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY----GGTLLAVSHD 462
Cdd:cd03222 71 ------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHD 131
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-170 |
1.91e-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: 41.96 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 35 IIGKNGAGKSTLLhlihndlapaqgqilrqdikmtmveqETASYSFADQTPAEKKLLEKWR---VPVRDFQ------QLS 105
Cdd:cd03227 26 ITGPNGSGKSTIL--------------------------DAIGLALGGAQSATRRRSGVKAgciVAAVSAEliftrlQLS 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 106 GGEKLKARLAKGLS----VDADLLLLDEPTNHLDESSLQFLIQQLKSYRG---TVILVSHDRYFLDEAATKI 170
Cdd:cd03227 80 GGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkgaQVIVITHLPELAELADKLI 151
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
293-349 |
1.92e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.64 E-value: 1.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1732943882 293 EVQNITKAF----GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSVWV 349
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERpTSGRVLV 64
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
292-481 |
1.95e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.52 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF---------GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET-AEGSV-W------------ 348
Cdd:PRK10419 4 LNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpSQGNVsWrgeplaklnraq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 349 ------------------VSPSANIGYLTQEvfdlPLEQTPEelFDNETYKARghVQSLMRHLGFTASQWTEPIKHMSMG 410
Cdd:PRK10419 84 rkafrrdiqmvfqdsisaVNPRKTVREIIRE----PLRHLLS--LDKAERLAR--ASEMLRAVDLDDSVLDKRPPQLSGG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 411 --ERVkCKLMAYILEEKdVLILDEPTNHLDLPSREQ---LEETLSQYGGT-LLAVSHDRYFLEKTTNSKLVISDNGI 481
Cdd:PRK10419 156 qlQRV-CLARALAVEPK-LLILDEAVSNLDLVLQAGvirLLKKLQQQFGTaCLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
292-437 |
2.06e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAF-GERTLfKNTNFTIQHGEKVAIIGPNGSGKTTLLKII-------------LGQETAEGSVWVSPSANIGY 357
Cdd:PRK10762 5 LQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLtgiytrdagsilyLGKEVTFNGPKSSQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 358 LTQEVFDLPLEQTPEELF-DNETYKARGHVQ---------SLMRHLGFTASQWTePIKHMSMGERVKCKLMAYILEEKDV 427
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFlGREFVNRFGRIDwkkmyaeadKLLARLNLRFSSDK-LVGELSIGEQQMVEIAKVLSFESKV 162
|
170
....*....|
gi 1732943882 428 LILDEPTNHL 437
Cdd:PRK10762 163 IIMDEPTDAL 172
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
303-480 |
2.54e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 43.15 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLK-------------IILGQETA-EGSVWvspsaNIGYLTQEVFDLPLE 368
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnallipsegkvYVDGLDTSdEENLW-----DIRNKAGMVFQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 369 QT------------PEELfDNETYKARGHVQSLMRHLGFTASQWTEPikHM-SMGERVKCKLMAYILEEKDVLILDEPTN 435
Cdd:PRK13633 97 QIvativeedvafgPENL-GIPPEEIRERVDESLKKVGMYEYRRHAP--HLlSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1732943882 436 HLDLPSREQLEETL----SQYGGTLLAVSHdrYFLEKTTNSKLVISDNG 480
Cdd:PRK13633 174 MLDPSGRREVVNTIkelnKKYGITIILITH--YMEEAVEADRIIVMDSG 220
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
294-541 |
2.62e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 294 VQNITKAFGERTLFK-----NTNFTIQHGEKVAIIGPNGSGKTTLLKIILG---QETAEGSV--WVSPsANIGYLtQEVF 363
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGliiSETGQTIVgdYAIP-ANLKKI-KEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 364 DLPLE-----QTPE-ELFDN------------------ETYKargHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMA 419
Cdd:PRK13645 87 RLRKEiglvfQFPEyQLFQEtiekdiafgpvnlgenkqEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 420 YILEEKDVLILDEPTNHLDLPSREQ----LEETLSQYGGTLLAVSHDRYFLEKTTNSKLVISDNG-IDKqlnDVPTERNE 494
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDfinlFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKvISI---GSPFEIFS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1732943882 495 REELRLKLETERQevlgKLSFMMpndkgYKELDQAFNELTKRIKELD 541
Cdd:PRK13645 241 NQELLTKIEIDPP----KLYQLM-----YKLKNKGIDLLNKNIRTIE 278
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-65 |
3.52e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 3.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 15 KDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQD 65
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND 446
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-158 |
3.64e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.52 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 19 VFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIH-----NDLAPAQGQI----------------LRQDIKM--------- 68
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVrlfgrniyspdvdpieVRREVGMvfqypnpfp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 69 --TMVEQETASYSFADQTPAEKKLLE--KWRVP-----------VRDF-QQLSGGEKLKARLAKGLSVDADLLLLDEPTN 132
Cdd:PRK14267 99 hlTIYDNVAIGVKLNGLVKSKKELDErvEWALKkaalwdevkdrLNDYpSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180
....*....|....*....|....*....
gi 1732943882 133 HLD---ESSLQFLIQQLKSyRGTVILVSH 158
Cdd:PRK14267 179 NIDpvgTAKIEELLFELKK-EYTIVLVTH 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
302-438 |
3.94e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.46 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 302 GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA---EGSVWVSPSAN-------IGYLTQEVFDLPLEQTP 371
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgviTGEILINGRPLdknfqrsTGYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 372 EELfdneTYKArghvqsLMRHLGftasqwTEPIKHMSMGervkCKLMAyileEKDVLILDEPTNHLD 438
Cdd:cd03232 98 EAL----RFSA------LLRGLS------VEQRKRLTIG----VELAA----KPSILFLDEPTSGLD 140
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-67 |
4.22e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 42.96 E-value: 4.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQIlrqDIK 67
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIK 84
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
308-462 |
4.48e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 42.05 E-value: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 308 KNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETA-EGSVWVSPSA----NIGYLTQE---VFdlpleQTPEELFDNET 379
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVkSGEIFYNNQAitddNFEKLRKHigiVF-----QNPDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 380 YK---ARG-------------HVQSLMRHLGFTASQWTEPiKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSRE 443
Cdd:PRK13648 101 VKydvAFGlenhavpydemhrRVSEALKQVDMLERADYEP-NALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180
....*....|....*....|...
gi 1732943882 444 QL----EETLSQYGGTLLAVSHD 462
Cdd:PRK13648 180 NLldlvRKVKSEHNITIISITHD 202
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
292-462 |
4.55e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 42.12 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 292 LEVQNITKAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQET---AEGSVWVS--------PSANIGYLTQ 360
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTgdvtlngePLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 361 EVFDLPLEQTPEELFdneTYKARG--------HVQ---SLMRHLGFTASQWTE----------PIKHMSMGE--RVK-CK 416
Cdd:PRK13547 82 ARLRAVLPQAAQPAF---AFSAREivllgrypHARragALTHRDGEIAWQALAlagatalvgrDVTTLSGGElaRVQfAR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 417 LMAYILEEKDV------LILDEPTNHLDLPSREQLEETL----SQYGGTLLAVSHD 462
Cdd:PRK13547 159 VLAQLWPPHDAaqppryLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHD 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
292-331 |
5.15e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 42.75 E-value: 5.15e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1732943882 292 LEVQNITKAFG----ERTLFKNTNFTIQHGEKVAIIGPNGSGKT 331
Cdd:COG4172 7 LSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKS 50
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
303-339 |
5.36e-04 |
|
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: 41.70 E-value: 5.36e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG 339
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQR 50
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
279-333 |
5.67e-04 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 42.70 E-value: 5.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1732943882 279 FSI---DTSKKTGKRF-------LEVQNITKAF-GERTL-FKNTNFTIQHGEKVAIIGPNGSGKTTL 333
Cdd:PRK11176 319 FAIldlEQEKDEGKRVierakgdIEFRNVTFTYpGKEVPaLRNINFKIPAGKTVALVGRSGSGKSTI 385
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
303-484 |
5.81e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWVSPSANIGYLTQE--VFDLPLEQTP--EELFDNE 378
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAYVPQVswIFNATVRENIlfGSDFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 379 TYKARGHVQSLMRHL----GFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNHLDLPSREQLEETLSQY-- 452
Cdd:PLN03232 709 RYWRAIDVTALQHDLdllpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDel 788
|
170 180 190
....*....|....*....|....*....|...
gi 1732943882 453 -GGTLLAVSHDRYFLEKTtnSKLVISDNGIDKQ 484
Cdd:PLN03232 789 kGKTRVLVTNQLHFLPLM--DRIILVSEGMIKE 819
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
32-159 |
6.20e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 32 IIGIIGKNGAGKSTLLHLIH--------------NDLAP-----------------------AQGQI------------- 61
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAIRyalygkarsrsklrSDLINvgseeasvelefehggkryrierRQGEFaefleakpserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 62 -------------LRQDIKMTMVEQETASYSFADQTPAEKKLLEKWRVpVRDFQQLSGGEKLKARLAKGLSvdadlLLLD 128
Cdd:COG0419 105 alkrllgleiyeeLKERLKELEEALESALEELAELQKLKQEILAQLSG-LDPIETLSGGERLRLALADLLS-----LILD 178
|
170 180 190
....*....|....*....|....*....|.
gi 1732943882 129 epTNHLDESSLQFLIQQLKSYRgtviLVSHD 159
Cdd:COG0419 179 --FGSLDEERLERLLDALEELA----IITHV 203
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
237-461 |
6.92e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.79 E-value: 6.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 237 FKEYHRVKAKRTDAQIKSKQKRLEKELEKAKAEPVKPEYTVHFSIDTSKKTGKRFLEVQNITKAFG----ERTLFKNTNF 312
Cdd:TIGR00956 705 FRRGSLKRAKKAGETSASNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKikkeKRVILNNVDG 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 313 TIQHGEKVAIIGPNGSGKTTLLKIILGQETA----EGSVWV-------SPSANIGYLTQEvfDLPLEQT----------- 370
Cdd:TIGR00956 785 WVKPGTLTALMGASGAGKTTLLNVLAERVTTgvitGGDRLVngrpldsSFQRSIGYVQQQ--DLHLPTStvreslrfsay 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 371 ---PEELFDNETYKargHVQSLMRHLGFTASQ-----------WTEPIKHMSMGervkCKLMAyilEEKDVLILDEPTNH 436
Cdd:TIGR00956 863 lrqPKSVSKSEKME---YVEEVIKLLEMESYAdavvgvpgeglNVEQRKRLTIG----VELVA---KPKLLLFLDEPTSG 932
|
250 260 270
....*....|....*....|....*....|
gi 1732943882 437 LDlpSRE-----QLEETLSQYGGTLLAVSH 461
Cdd:TIGR00956 933 LD--SQTawsicKLMRKLADHGQAILCTIH 960
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-157 |
8.56e-04 |
|
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: 42.12 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPA-QGQIL---RQ-DIK---------MTMVEQETA----------- 76
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFingKPvDIRnpaqairagIAMVPEDRKrhgivpilgvg 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 ---------SYSFADQTPAEKKL----LEKWRVPVRDFQ------QLSGGEKLKARLAKGLSVDADLLLLDEPTNHLD-- 135
Cdd:TIGR02633 358 knitlsvlkSFCFKMRIDAAAELqiigSAIQRLKVKTASpflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDvg 437
|
170 180
....*....|....*....|...
gi 1732943882 136 -ESSLQFLIQQLKSYRGTVILVS 157
Cdd:TIGR02633 438 aKYEIYKLINQLAQEGVAIIVVS 460
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
299-347 |
9.58e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 40.71 E-value: 9.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1732943882 299 KAFGERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSV 347
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV 63
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
303-340 |
1.55e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 41.24 E-value: 1.55e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQ 340
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRH 364
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-83 |
1.68e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.54 E-value: 1.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1732943882 21 KNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDIKMTMveqetASYSFADQ 83
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF-----GDYSYRSQ 87
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
292-337 |
1.96e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 40.37 E-value: 1.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1732943882 292 LEVQNItkaFGertlFKNTNFTIQHGEKV-AIIGPNGSGKTTLLKII 337
Cdd:COG3950 6 LTIENF---RG----FEDLEIDFDNPPRLtVLVGENGSGKTTLLEAI 45
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
303-461 |
1.96e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 40.39 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 303 ERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLL------------KIILGQETAEGSVwvsPSANIGYLTQE---VFDLPL 367
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLqhlngllqptsgTVTIGERVITAGK---KNKKLKPLRKKvgiVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 368 EQTPEEL-----------FDNETYKARGHVQSLMRHLGFTASQWTEPIKHMSMGERVKCKLMAYILEEKDVLILDEPTNH 436
Cdd:PRK13634 96 HQLFEETvekdicfgpmnFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180
....*....|....*....|....*....
gi 1732943882 437 LDLPSREQLEE---TLSQYGG-TLLAVSH 461
Cdd:PRK13634 176 LDPKGRKEMMEmfyKLHKEKGlTTVLVTH 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
97-159 |
2.26e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.26e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 97 PVRDFQQLSGGEKLKARLAKGLSvdADLL----LLDEPTNHL---DESSLQFLIQQLKSYRGTVILVSHD 159
Cdd:PRK00635 470 PERALATLSGGEQERTALAKHLG--AELIgityILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHD 537
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
4-158 |
2.46e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 4 IVTLTNVSYEVKDLTVFkNVNASVQQGDIIGIIGKNGAGKSTLLHLIHNDLAPAQGQILRQDI----------------- 66
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakpyctyighnl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 67 --KMTMVEQETAS-----YSFADQTPAEKKLLEKWRVPVRDFQQLSGGEKLKARLAKGLSVDADLLLLDEPTNHLDESS- 138
Cdd:PRK13541 80 glKLEMTVFENLKfwseiYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENr 159
|
170 180
....*....|....*....|..
gi 1732943882 139 --LQFLIQQLKSYRGTVILVSH 158
Cdd:PRK13541 160 dlLNNLIVMKANSGGIVLLSSH 181
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
22-170 |
3.08e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 39.72 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 22 NVNASVQQGDIIGIIGKNGAGKS----TLLHLI--------------HNDL----APAQGQILRQDIKMTMVEQETA--- 76
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvsslAIMGLIdypgrvmaeklefnGQDLqrisEKERRNLVGAEVAMIFQDPMTSlnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 77 SYSFADQTPAEKKLLE----KWR----------VPVRDFQ--------QLSGGEKLKARLAKGLSVDADLLLLDEPTNHL 134
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQggnkKTRrqraidllnqVGIPDPAsrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTAL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1732943882 135 D----ESSLQFLIQQLKSYRGTVILVSHDRYFLDEAATKI 170
Cdd:PRK11022 185 DvtiqAQIIELLLELQQKENMALVLITHDLALVAEAAHKI 224
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
98-166 |
4.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 98 VRDFQQLSGGEK------LKARLAKGLSVDADLLLLDEPTNHLDE---SSLQFLIQ-QLKSYRG--TVILVSHDRYFLDE 165
Cdd:PRK01156 796 VEGIDSLSGGEKtavafaLRVAVAQFLNNDKSLLIMDEPTAFLDEdrrTNLKDIIEySLKDSSDipQVIMISHHRELLSV 875
|
.
gi 1732943882 166 A 166
Cdd:PRK01156 876 A 876
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
100-164 |
4.81e-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: 4.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 100 DFQQLSGGEKLKARLAKGLSVDAD---LLLLDEPTNHLDESSLQFLIQQLKS---YRGTVILVSHDRYFLD 164
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKElsrNGAQLILTTHSPLLLD 303
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
306-355 |
4.85e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.85e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 306 LFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWVSPSANI 355
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERlYDPTEGDIIINDSHNL 450
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
305-462 |
5.51e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 38.71 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 305 TLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIILG-QETAEGSVWV--SPSAN------IGYLTQ-EVFDLPLEQTPEEL 374
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfVRLASGKISIlgQPTRQalqknlVAYVPQsEEVDWSFPVLVEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1732943882 375 FDNETYkarGHVQSLMRHLGFTASQWTEPIKHMSM-------------GERVKCKLMAYILEEKDVLILDEPTNHLDLPS 441
Cdd:PRK15056 101 VMMGRY---GHMGWLRRAKKRDRQIVTAALARVDMvefrhrqigelsgGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....
gi 1732943882 442 REQ---LEETLSQYGGTLLAVSHD 462
Cdd:PRK15056 178 EARiisLLRELRDEGKTMLVSTHN 201
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
320-337 |
6.49e-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: 38.91 E-value: 6.49e-03
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
9-53 |
7.56e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 7.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1732943882 9 NVSYEvkDLTVFKNVNASVQQGDIIGIIGKNGAGKSTLLHLIHND 53
Cdd:PRK10938 267 VVSYN--DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
99-159 |
8.17e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 8.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1732943882 99 RDFQQLSGGEKLKARLAK--GLSVDADLLLLDEPTNHLDESSLQFLIQQLKSYR---GTVILVSHD 159
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATqiGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRdlgNTLIVVEHD 549
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
309-349 |
8.18e-03 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 37.72 E-value: 8.18e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1732943882 309 NTNFTIQHGEKVAIIGPNGSGKTTLLKIILGQETAEGSVWV 349
Cdd:pfam00006 6 DGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYA 46
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
302-338 |
8.35e-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: 37.34 E-value: 8.35e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1732943882 302 GERTLFKNTNFTIQHGEKVAIIGPNGSGKTTLLKIIL 338
Cdd:cd03227 6 RFPSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG 42
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
403-467 |
9.56e-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: 38.14 E-value: 9.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1732943882 403 PIKHMSMGERVKCKLMAYILE---EKDVLILDEPTNHLDLPSREQLEETL---SQYGGTLLAVSHDRYFLE 467
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLSalpKGGLLLIDEPESGLHPKLLRRLLELLkelSRNGAQLILTTHSPLLLD 303
|
|
| |
