|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
10-539 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 549.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDELINK 89
Cdd:COG0488 5 SKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLSEIYEALNKYENLQAKLATHLDNknlHKEINNLINFIESKDAWNIEQKKERFLKEFKL-FEYKNRPISSLSGGEIRKI 168
Cdd:COG0488 85 GDAELRALEAELEELEAKLAEPDED---LERLAELQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSELSGGWRRRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYYLEKK 248
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 249 AQILVSLSKSYETLIKHLKAEEEWLRR-GVKAR-LKRNEGRKERIFKMREEAKknPGEIKRLKLELLRANSSiqkpnfnk 326
Cdd:COG0488 242 AERLEQEAAAYAKQQKKIAKEEEFIRRfRAKARkAKQAQSRIKALEKLEREEP--PRRDKTVEIRFPPPERL-------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 327 QKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-NADIKIGYFDQARAMLN 405
Cdd:COG0488 312 GKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlGETVKIGYFDQHQEELD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 406 SDKSLIELFCpnggdRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:COG0488 392 PDKTVLDELR-----DGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 486 TINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQYLER 539
Cdd:COG0488 467 TLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-637 |
5.43e-143 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 429.76 E-value: 5.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTN 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDELINKNLSEIYEALNKYENLQAKLATHLDNKNLhKEINNLINFIESKDAWNIEQKKERFLKEFKLfeYKNRPISSL 160
Cdd:PRK11147 81 GTVYDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNL-NELAKLQEQLDHHNLWQLENRINEVLAQLGL--DPDAALSSL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 161 SGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGG 240
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 241 YAYYLEKKAQILVSLSKSYETLIKHLKAEEEWLRRGVKARLKRNEGRKERIFKMREEAKKNPGEIKRLKLELLRANSSiq 320
Cdd:PRK11147 238 YDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRERSERREVMGTAKMQVEEASRS-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 321 kpnfnkQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-NADIKIGYFDQ 399
Cdd:PRK11147 316 ------GKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcGTKLEVAYFDQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 400 ARAMLNSDKSLIElfcpNGGD---RVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILD 476
Cdd:PRK11147 390 HRAELDPEKTVMD----NLAEgkqEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 477 EPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE-NGVINiehmSYT-------QYLEREFELRE-FD 547
Cdd:PRK11147 466 EPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIG----RYVggyhdarQQQAQYLALKQpAV 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 548 DFVLNLEKEKGAIKEKQNKKLSYKQNEILNLYPEKIELLEKKIKKLNLELSKTS----DYENTNKLFEELKTLQNELnnl 623
Cdd:PRK11147 542 KKKEEAAAPKAETVKRSSKKLSYKLQRELEQLPQLLEDLEAEIEALQAQVADADffsqPHEQTQKVLADLADAEQEL--- 618
|
650
....*....|....
gi 1751968159 624 eNVYFEVLEFSESL 637
Cdd:PRK11147 619 -EVAFERWEELEAL 631
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-522 |
1.63e-109 |
|
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: 340.76 E-value: 1.63e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 8 KASKKF-GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDEL 86
Cdd:TIGR03719 9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 INKNLSEIYEALNKYENLQAKLATHLDNKN-LHKEINNLINFIESKDAWNIEQKKERFLKEFKLFEyKNRPISSLSGGEI 165
Cdd:TIGR03719 89 VEEGVAEIKDALDRFNEISAKYAEPDADFDkLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPP-WDADVTKLSGGER 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 166 RKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYYL 245
Cdd:TIGR03719 168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 246 EKKAQILVSLSKSYETLIKHLKAEEEWLRRGVKARLKRNEGRKERIFKMREEAKKNPGEikrlklellraNSSIQKPNFN 325
Cdd:TIGR03719 248 EQKQKRLEQEEKEESARQKTLKRELEWVRQSPKGRQAKSKARLARYEELLSQEFQKRNE-----------TAEIYIPPGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 326 K--QKMIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNAD-IKIGYFDQARA 402
Cdd:TIGR03719 317 RlgDKVI-EAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGEtVKLAYVDQSRD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 MLNSDKSLIELFCpNGGDRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDL 482
Cdd:TIGR03719 396 ALDPNKTVWEEIS-GGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1751968159 483 DIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:TIGR03719 475 DVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFE 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-522 |
5.38e-101 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 318.60 E-value: 5.38e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 6 LIKASKKFG-EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLD 84
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 ELINKNLSEIYEALNKYENLQAKLATHLDNKN-LHKEINNLINFIESKDAWNIEQKKERFLKEFKLFEyKNRPISSLSGG 163
Cdd:PRK11819 89 ENVEEGVAEVKAALDRFNEIYAAYAEPDADFDaLAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPP-WDAKVTKLSGG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAY 243
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 244 YLEKKAQILVSLSKSYETLIKHLKAEEEWLRRGVKARLKRNEGRKERIFKMREEA--KKN--------PGEikRLKLELL 313
Cdd:PRK11819 248 WLEQKAKRLAQEEKQEAARQKALKRELEWVRQSPKARQAKSKARLARYEELLSEEyqKRNetneifipPGP--RLGDKVI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 314 RANssiqkpnfnkqkmifelvNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNAD-I 392
Cdd:PRK11819 326 EAE------------------NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 KIGYFDQARAMLNSDKSLIELFcPNGGDRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDV 472
Cdd:PRK11819 388 KLAYVDQSRDALDPNKTVWEEI-SGGLDIIKVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 473 LILDEPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:PRK11819 467 LLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFE 516
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-637 |
7.22e-61 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 214.26 E-value: 7.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDELINKNlse 93
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 iyealNKYENLQAKLAtHLDNKNLHKEINNLINFIESKDAWNIEQKKERFLKEFKLF-EYKNRPISSLSGGEIRKINLCI 172
Cdd:PRK10636 89 -----REYRQLEAQLH-DANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 173 LVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYYLEKKAQIL 252
Cdd:PRK10636 163 ALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 253 V---SLSKSYETLIKHLKAeeeWLRRgVKARLKRNEGRKERIfKMREEAK-------KNPGEIKrlklelLRANSSIQKP 322
Cdd:PRK10636 243 AqqqAMYESQQERVAHLQS---YIDR-FRAKATKAKQAQSRI-KMLERMEliapahvDNPFHFS------FRAPESLPNP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 323 NFNKQKMifelvnaSKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNAD-IKIGYFDQAR 401
Cdd:PRK10636 312 LLKMEKV-------SAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKgIKLGYFAQHQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 -AMLNSDKSLIELFCpnggdRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTN 480
Cdd:PRK10636 385 lEFLRADESPLQHLA-----RLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTN 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 481 DLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI-----NIEhmSYTQYLErefELREFDDFVLNLEK 555
Cdd:PRK10636 460 HLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVepfdgDLE--DYQQWLS---DVQKQENQTDEAPK 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 556 EKGAIKEKQNKKLSYKQNEILNLYP---EKIELLEKKIKKLNLELS----KTSD---YENTNK--LFEELKTLQNELNNL 623
Cdd:PRK10636 535 ENNANSAQARKDQKRREAELRTQTQplrKEIARLEKEMEKLNAQLAqaeeKLGDselYDQSRKaeLTACLQQQASAKSGL 614
|
650
....*....|....
gi 1751968159 624 ENVYFEVLEFSESL 637
Cdd:PRK10636 615 EECEMAWLEAQEQL 628
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
13-537 |
6.66e-59 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 206.28 E-value: 6.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQ-QVDFNTNLSLDELI--NK 89
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQdQFAFEEFTVLDTVImgHT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLSEIYEALNK-YENLQAKLATHLDNKNLHKEinnlinFIEsKDAWNIEQKKERFLKEFKL-FEYKNRPISSLSGGEIRK 167
Cdd:PRK15064 91 ELWEVKQERDRiYALPEMSEEDGMKVADLEVK------FAE-MDGYTAEARAGELLLGVGIpEEQHYGLMSEVAPGWKLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 168 INLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYYLEK 247
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 248 KAQI----LVSLSKSyetlikhlKAEEEWLRRGVkARLKRNEGrKERIFKMReeAKKnpgeIKRLKLELLRAnSSIQKP- 322
Cdd:PRK15064 244 ATQArerlLADNAKK--------KAQIAELQSFV-SRFSANAS-KAKQATSR--AKQ----IDKIKLEEVKP-SSRQNPf 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 323 -NFNKQKMIF----ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNAD-IKIGY 396
Cdd:PRK15064 307 iRFEQDKKLHrnalEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEnANIGY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 FDQARA-MLNSDKSLIELFC---PNGGDRVQVRGhdmhiygYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDV 472
Cdd:PRK15064 387 YAQDHAyDFENDLTLFDWMSqwrQEGDDEQAVRG-------TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 473 LILDEPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATK-LYVFENGVINIeHMSYTQYL 537
Cdd:PRK15064 460 LVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRiIEITPDGVVDF-SGTYEEYL 524
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
335-566 |
8.59e-53 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 189.51 E-value: 8.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 335 NASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYFDQ----------ARAM 403
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVsIPKGLRIGYLPQeppldddltvLDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 LNSDKSLIEL------------FCPNGGDRVQVRGHDM-HIYGY---------LKSFLFPKEFLSQAVSVLSGGEKNRVA 461
Cdd:COG0488 83 LDGDAELRALeaeleeleaklaEPDEDLERLAELQEEFeALGGWeaearaeeiLSGLGFPEEDLDRPVSELSGGWRRRVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 462 LA-LLFTkDYDVLILDEPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQYLERe 540
Cdd:COG0488 163 LArALLS-EPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQ- 240
|
250 260
....*....|....*....|....*.
gi 1751968159 541 felREfddfvLNLEKEKGAIKEKQNK 566
Cdd:COG0488 241 ---RA-----ERLEQEAAAYAKQQKK 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-247 |
4.57e-52 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 187.58 E-value: 4.57e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDfntnlS 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQE-----E 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDEliNKNLseiyealnkYENLQAkLATHLDNKNLHKeinnlinfieskdawnieqkkerFLKEFkLF--EYKNRPISSL 160
Cdd:COG0488 390 LDP--DKTV---------LDELRD-GAPGGTEQEVRG-----------------------YLGRF-LFsgDDAFKPVGVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 161 SGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGG 240
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGG 513
|
....*..
gi 1751968159 241 YAYYLEK 247
Cdd:COG0488 514 YDDYLEK 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
332-524 |
2.21e-49 |
|
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: 168.78 E-value: 2.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-NADIKIGYFDQaramlnsdksl 410
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTwGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ielfcpnggdrvqvrghdmhiygylksflfpkeflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINIL 490
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....
gi 1751968159 491 EEYLMEFKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-233 |
2.14e-40 |
|
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: 144.13 E-value: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQqvdfntnlsl 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 delinknlseiyealnkyenlqaklathldnknlhkeinnlinfieskdawnieqkkerflkefklfeyknrpissLSGG 163
Cdd:cd03221 71 ----------------------------------------------------------------------------LSGG 74
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGK 233
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-536 |
1.21e-34 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 140.00 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 34 IIGKNGEGKSTLLK-----AIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDELINKNLS-----EIYEALNKYEN 103
Cdd:PLN03073 208 LVGRNGTGKTTFLRymamhAIDGIPKNCQILHVEQEVVGDDTTALQCVLNTDIERTQLLEEEAQlvaqqRELEFETETGK 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 104 LQAKLATHLDNKNLHKEINNLINFIESKDAWNIEQKKERFLKEFKLF-EYKNRPISSLSGGEIRKINLCILVLQNPDVLL 182
Cdd:PLN03073 288 GKGANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 183 LDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYYLEKKAQILVSLSKSYETl 262
Cdd:PLN03073 368 LDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFES- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 263 ikhlkaeEEWLRRGVKARlkrnegrkerIFKMREEAKKNPGEIKRLK-LELL-RANSSIQKPNFN---------KQKMIF 331
Cdd:PLN03073 447 -------NERSRSHMQAF----------IDKFRYNAKRASLVQSRIKaLDRLgHVDAVVNDPDYKfefptpddrPGPPII 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNAS-KIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYFDQARAM---LNS 406
Cdd:PLN03073 510 SFSDASfGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfRSAKVRMAVFSQHHVDgldLSS 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 407 DKSLIELFCPNGGDRVQVRGHdmhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT 486
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQKLRAH-------LGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 487 INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQY 536
Cdd:PLN03073 663 VEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-526 |
2.05e-34 |
|
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: 137.34 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAI----------FGTLQLDsGRIIRQND-----KSIAMLAQQVDFN 78
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALmgllphggriSGEVLLD-GRDLLELSealrgRRIGMVFQDPMTQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 TN-LSLDElinknlsEIYEALnkyenlqaklathldnknlhkeinnlINFIESKDAwnIEQKKERFLKEFKLFEYKNRPI 157
Cdd:COG1123 96 LNpVTVGD-------QIAEAL--------------------------ENLGLSRAE--ARARVLELLEAVGLERRLDRYP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGK 233
Cdd:COG1123 141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 234 ISFfnggyayylekkaqilvslsksyetlikhlkaeeewlrrgvkarlkrnEGRKERIFKMREEAKKNPgeikrlkleLL 313
Cdd:COG1123 221 IVE------------------------------------------------DGPPEEILAAPQALAAVP---------RL 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 314 RANSSIQKPNFNKQKMIFELVNASKI--INNKILFK---NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI- 387
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLEVRNLSKRypVRGKGGVRavdDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIl 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 388 -KNADI-------------KIGY-FDQARAMLNSDKSLIE-----LFCPNGGDRVQVRGhdmHIYGYLKSFLFPKEFLSQ 447
Cdd:COG1123 324 fDGKDLtklsrrslrelrrRVQMvFQDPYSSLNPRMTVGDiiaepLRLHGLLSRAERRE---RVAELLERVGLPPDLADR 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 448 AVSVLSGGEKNRV----ALALlftkDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRYFVDKLATKLY 519
Cdd:COG1123 401 YPHELSGGQRQRVaiarALAL----EPKLLILDEPTSALDVSVqaqiLNLLRDLQRELGLTYLFISHDLAVVRYIADRVA 476
|
....*..
gi 1751968159 520 VFENGVI 526
Cdd:COG1123 477 VMYDGRI 483
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-234 |
2.26e-33 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 128.05 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqQVDFNTNLS 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-------------LIDGEDVRK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNLSEIYEALNKYENLQAKlathlDNKNLHKEINNLinfieskDAWNIEQKKERFLKEFKLFEYKNRPISSLSG 162
Cdd:COG4555 68 EPREARRQIGVLPDERGLYDRLTVR-----ENIRYFAELYGL-------FDEELKKRIEELIELLGLEEFLDRRVGELST 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLL---KNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:COG4555 136 GMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILralKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
14-233 |
2.95e-33 |
|
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: 126.81 E-value: 2.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQN----DKSIAMLAQQVDF---NTNlslDEL 86
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGkdltKLSLKELRRKVGLvfqNPD---DQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 INKNLSEiyealnkyenlqaKLATHLDNKNLHKEInnlinfieskdawnIEQKKERFLKEFKLFEYKNRPISSLSGGEIR 166
Cdd:cd03225 89 FGPTVEE-------------EVAFGLENLGLPEEE--------------IEERVEEALELVGLEGLRDRSPFTLSGGQKQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 167 KINL-CILVLqNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK---ICVIFISHDRYFIDNVASRCVEIEGGK 233
Cdd:cd03225 142 RVAIaGVLAM-DPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
1.51e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND-----------KSIAMLA 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKplsampppewrRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 73 QQVDFntnlsLDELINKNLSEIYEALNKYENlqaklathldnknlhkeinnlinfieskdawniEQKKERFLKEFKL-FE 151
Cdd:COG4619 81 QEPAL-----WGGTVRDNLPFPFQLRERKFD---------------------------------RERALELLERLGLpPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 152 YKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLL----KNSKICVIFISHDRYFIDNVASRCV 227
Cdd:COG4619 123 ILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLreylAEEGRAVLWVSHDPEQIERVADRVL 202
|
....*..
gi 1751968159 228 EIEGGKI 234
Cdd:COG4619 203 TLEAGRL 209
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-234 |
2.39e-30 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 119.40 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND----KSIAMLAQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedVARDPaevrRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 QVDFNTNLSLdelinknlseiyealnkYENLQaklathldnknLHKEINNLinfieskDAWNIEQKKERFLKEFKLFEYK 153
Cdd:COG1131 81 EPALYPDLTV-----------------RENLR-----------FFARLYGL-------PRKEARERIDELLELFGLTDAA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMC-EFLEKL--LKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:COG1131 126 DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARrELWELLreLAAEGKTVLLSTHYLEEAERLCDRVAIID 205
|
....
gi 1751968159 231 GGKI 234
Cdd:COG1131 206 KGRI 209
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-236 |
1.25e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQQ 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrlfgkpPRRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 VDFNTN--LSLDELInknlseiyeALNKYENLqaklathldnknlhkeinNLINFIESKDawniEQKKERFLKEFKLFEY 152
Cdd:COG1121 84 AEVDWDfpITVRDVV---------LMGRYGRR------------------GLFRRPSRAD----REAVDEALERVGLEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 153 KNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHDRYFIDNVASRCVEI 229
Cdd:COG1121 133 ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHDLGAVREYFDRVLLL 212
|
....*..
gi 1751968159 230 EGGKISF 236
Cdd:COG1121 213 NRGLVAH 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-234 |
5.56e-29 |
|
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: 113.68 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqqvdfntnlsldelink 89
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI----------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 nlseiyealnkyenlqaklatHLDNKNL----HKEINNLINFIEskdawnieQkkerFLKEFKLFEYKNRPISSLSGGEI 165
Cdd:cd03214 57 ---------------------LLDGKDLaslsPKELARKIAYVP--------Q----ALELLGLAHLADRPFNELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 166 RKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD-----RYfidnvASRCVEIEGGKI 234
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIAhqieLLELLRRLARERGKTVVMVLHDlnlaaRY-----ADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
332-524 |
6.40e-29 |
|
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: 112.72 E-value: 6.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigyfdqaramlnsdksli 411
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 elfcpnggdrvQVRGHDMHIygylksfLFPKEFLSQAVSV--LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI 489
Cdd:cd00267 57 -----------LIDGKDIAK-------LPLEELRRRIGYVpqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*...
gi 1751968159 490 LEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd00267 119 LLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-234 |
2.18e-28 |
|
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: 113.99 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI---------IRQND--KSIAML 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlasLSRRElaRRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 72 AQQVDFNTNLSLDELInknlseiyeALNKYenlqaklaTHLdnknlhkeinNLINFIESKDawniEQKKERFLKEFKLFE 151
Cdd:COG1120 81 PQEPPAPFGLTVRELV---------ALGRY--------PHL----------GLFGRPSAED----REAVEEALERTGLEH 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 152 YKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD-----RYfidnv 222
Cdd:COG1120 130 LADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHDlnlaaRY----- 204
|
250
....*....|..
gi 1751968159 223 ASRCVEIEGGKI 234
Cdd:COG1120 205 ADRLVLLKDGRI 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-234 |
4.12e-28 |
|
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: 111.97 E-value: 4.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 5 ELIKASKKFGEKI-ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII--------RQNDKSIAMLAQQV 75
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILlngkpikaKERRKSIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 DFN--TNLSLDELInknlseiyealnkyenlqaklathLDNKNLHKEinnlinfieskdawniEQKKERFLKEFKLFEYK 153
Cdd:cd03226 81 DYQlfTDSVREELL------------------------LGLKELDAG----------------NEQAETVLKDLDLYALK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:cd03226 121 ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELireLAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
....
gi 1751968159 231 GGKI 234
Cdd:cd03226 201 NGAI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-236 |
5.73e-28 |
|
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: 111.86 E-value: 5.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQQVDFNTN--LSLD 84
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrvfgkpLEKERKRIGYVPQRRSIDRDfpISVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 ELInknlseiyealnkyenlqaklATHLDNK-NLHKEInnlinfieSKDAWnieQKKERFLKEFKLFEYKNRPISSLSGG 163
Cdd:cd03235 89 DVV---------------------LMGLYGHkGLFRRL--------SKADK---AKVDEALERVGLSELADRQIGELSGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKN---SKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElrrEGMTILVVTHDLGLVLEYFDRVLLLNRTVVAS 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-233 |
2.88e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.49 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQnDKSIAMLAQQVDFNTNL 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWN-GEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELinknlsEIYEALNKYENLQAKLATHldnknlhkeinnliNFIESKDAWnieqkkERFLKEFKLFEYKNRPISSLS 161
Cdd:COG4133 80 LGHAD------GLKPELTVRENLRFWAALY--------------GLRADREAI------DEALEAVGLAGLADLPVRQLS 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLL---KNSKICVIFISHDRYFIDNVasRCVEIEGGK 233
Cdd:COG4133 134 AGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-234 |
3.58e-27 |
|
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: 110.11 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQ----NDKSIAMLAQQV-------D---FNT 79
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNLRELRRKVglvfqnpDdqlFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLsLDE----LINKNLSEiyealnkyenlqaklathldnknlhKEInnlinfieskdawniEQKKERFLKEFKLFEYKNR 155
Cdd:COG1122 92 TV-EEDvafgPENLGLPR-------------------------EEI---------------RERVEEALELVGLEHLADR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 156 PISSLSGGEIRKINL-CILVLQnPDVLLLDEPTNHLDVYMCEFLEKLLKN---SKICVIFISHDRYFIDNVASRCVEIEG 231
Cdd:COG1122 131 PPHELSGGQKQRVAIaGVLAME-PEVLVLDEPTAGLDPRGRRELLELLKRlnkEGKTVIIVTHDLDLVAELADRVIVLDD 209
|
...
gi 1751968159 232 GKI 234
Cdd:COG1122 210 GRI 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-249 |
3.88e-27 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 115.76 E-value: 3.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQV--DFNTNL 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHayDFENDL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELINKnlseiyealnkyenlqaklathldnknlhkeinnlinfieskdaWNIEQKKERFLKEF---KLF--EYKNRP 156
Cdd:PRK15064 400 TLFDWMSQ--------------------------------------------WRQEGDDEQAVRGTlgrLLFsqDDIKKS 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:PRK15064 436 VKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
250
....*....|...
gi 1751968159 237 FNGGYAYYLEKKA 249
Cdd:PRK15064 516 FSGTYEEYLRSQG 528
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
332-526 |
6.84e-27 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 107.48 E-value: 6.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKnadikigYFDQaramlnsdksli 411
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-------VLGK------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 elfcPNGGDRVQVRGH------DMHIYGYLKsflfPKEFLSqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:cd03230 63 ----DIKKEPEEVKRRigylpeEPSLYENLT----VRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 486 TINILEEYLMEFK---GALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03230 130 SRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
342-524 |
2.59e-26 |
|
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: 106.78 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 342 NKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI----------KIGY-FDQARAMLnsdk 408
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvDGKDLtklslkelrrKVGLvFQNPDDQF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 slielFCPNGGDRV-------QVRGHDMH--IYGYLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:cd03225 89 -----FGPTVEEEVafglenlGLPEEEIEerVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1751968159 480 NDLDIATINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-234 |
7.75e-26 |
|
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: 104.40 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIAmlaqqvdfntnlSL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-LGKDIK------------KE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DELINKNLSEIYEALNKYENLQAKlathldnKNLHkeinnlinfieskdawnieqkkerflkefklfeyknrpissLSGG 163
Cdd:cd03230 68 PEEVKRRIGYLPEEPSLYENLTVR-------ENLK-----------------------------------------LSGG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYM-CEFLEKL--LKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03230 100 MKQRLALAQALLHDPELLILDEPTSGLDPESrREFWELLreLKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
331-524 |
9.63e-26 |
|
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: 104.19 E-value: 9.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFDqaramlnsDKSL 410
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI--------LID--------GEDL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 IELfcpnggdRVQVRGHDMHIyGYL--KSFLFP-KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATI 487
Cdd:cd03229 65 TDL-------EDELPPLRRRI-GMVfqDFALFPhLTVLENIALGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1751968159 488 NILEEYLM----EFKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03229 137 REVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
329-512 |
1.21e-25 |
|
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: 104.87 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIKIGYFDQARAM--- 403
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwNGEPIRDAREDYRRRLayl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 -----LNSDKSLIE---LFCPNGGdrvqVRGHDMHIYGYLKSF-LfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLI 474
Cdd:COG4133 81 ghadgLKPELTVREnlrFWAALYG----LRADREAIDEALEAVgL--AGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1751968159 475 LDEPTNDLDIATINILEEYLMEFK---GALIFVSHDRYFVD 512
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA 195
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-234 |
2.82e-25 |
|
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: 104.12 E-value: 2.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFG--EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQND---------KSIAML 71
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyINGYSirtdrkaarQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 72 AQqvdFNTnlsldelinknlseIYEALNKYENLQ--AKLathldnKNLHKEInnlinfieskdawnIEQKKERFLKEFKL 149
Cdd:cd03263 81 PQ---FDA--------------LFDELTVREHLRfyARL------KGLPKSE--------------IKEEVELLLRVLGL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSkiCVIFISHDRYFIDNVASR 225
Cdd:cd03263 124 TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPAsrraIWDLILEVRKGR--SIILTTHSMDEAEALCDR 201
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:cd03263 202 IAIMSDGKL 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-252 |
3.75e-25 |
|
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: 110.02 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVD-FNTNLS 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDaLDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNLSEIyeALNKYE-NLQAKLAthldnknlhkeinnLINFIESKdawniEQKKerflkefklfeyknrpISSLS 161
Cdd:TIGR03719 403 VWEEISGGLDII--KLGKREiPSRAYVG--------------RFNFKGSD-----QQKK----------------VGQLS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEG-GKISFFNGG 240
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFEGN 525
|
250
....*....|..
gi 1751968159 241 YAYYLEKKAQIL 252
Cdd:TIGR03719 526 FSEYEEDKKRRL 537
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
347-526 |
6.27e-25 |
|
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: 104.11 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGY-------------FDQARAMLNS----DKS 409
Cdd:COG1124 22 KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrrkafrrrvqmvFQDPYASLHPrhtvDRI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 LIELFCPNGGDRVQVRGHDMhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT--- 486
Cdd:COG1124 102 LAEPLRIHGLPDREERIAEL-----LEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqae 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1751968159 487 -INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG1124 177 iLNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
329-526 |
1.00e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 103.25 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-------NADIKIGYFDQAR 401
Cdd:COG1121 5 PAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkpprRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AMlnsDKSLielfcPnggdrvqVRGHD---MHIYGYLKSFLFPK-----------------EFLSQAVSVLSGGEKNRVA 461
Cdd:COG1121 85 EV---DWDF-----P-------ITVRDvvlMGRYGRRGLFRRPSradreavdealervgleDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 462 LALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-234 |
1.90e-24 |
|
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: 101.80 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFG----EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIamlaqqvdfnT 79
Cdd:cd03255 1 IELKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGE-VRVDGTDI----------S 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLS---LDELINKNLSEIYEA------LNKYENLQaklathldnknlhkeinnLINFIESKDAWNIEQKKERFLKEFKLF 150
Cdd:cd03255 70 KLSekeLAAFRRRHIGFVFQSfnllpdLTALENVE------------------LPLLLAGVPKKERRERAEELLERVGLG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRyFIDNVASRC 226
Cdd:cd03255 132 DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSEtgkeVMELLRELNKEAGTTIVVVTHDP-ELAEYADRI 210
|
....*...
gi 1751968159 227 VEIEGGKI 234
Cdd:cd03255 211 IELRDGKI 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
329-560 |
2.89e-24 |
|
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: 101.86 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI---------KIGYF 397
Cdd:COG4555 1 MI-EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIliDGEDVrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQARAML--NSDKSLIELFC---PNGGDRVQVRghdmhIYGYLKSFLFPkEFLSQAVSVLSGGEKNRVALALLFTKDYDV 472
Cdd:COG4555 80 PDERGLYdrLTVRENIRYFAelyGLFDEELKKR-----IEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 473 LILDEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLErEFELREFDDF 549
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLDELRE-EIGEENLEDA 231
|
250
....*....|.
gi 1751968159 550 VLNLEKEKGAI 560
Cdd:COG4555 232 FVALIGSEEGE 242
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-522 |
4.05e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.82 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 32 IAIIGKNGEGKSTLLKAIFGTLQLDSGriirqndksiamlaqqvDFNTNLSLDELINK-NLSEIYEALNKYENLQAKLAt 110
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLG-----------------DYEEEPSWDEVLKRfRGTELQNYFKKLYNGEIKVV- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 111 hldnknlHKeinnlINFIE---------SKDAwnIEQKKER-----FLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQ 176
Cdd:PRK13409 164 -------HK-----PQYVDlipkvfkgkVREL--LKKVDERgkldeVVERLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 177 NPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKicVIFISHDRYFIDNVASRcVEIEGGKisffNGGYAyylekkaqiL 252
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRqrlnVARLIRELAEGKY--VLVVEHDLAVLDYLADN-VHIAYGE----PGAYG---------V 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 253 VSLSKSyetlikhlkaeeewLRRGVKARLK---RNEG---RKERI-FKMREEAKKNPGEIKrlklellranssIQKPNFN 325
Cdd:PRK13409 294 VSKPKG--------------VRVGINEYLKgylPEENmriRPEPIeFEERPPRDESERETL------------VEYPDLT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 326 KQKMIFEL-VNASKIinnkilfknfstriLQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIkNADIKIGYFDQaraML 404
Cdd:PRK13409 348 KKLGDFSLeVEGGEI--------------YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISYKPQ---YI 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSDKSL-IELFCPNGGDRVqvrgHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:PRK13409 410 KPDYDGtVEDLLRSITDDL----GSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1751968159 484 ----IATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:PRK13409 486 veqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-233 |
5.52e-24 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 98.47 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 5 ELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqqvdfntnlsld 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 elinknlseiyealnkyenlqaklatHLDNKNLHKeinnlinfieskdawnieqkkerflkeFKLFEYKNRP--ISSLSG 162
Cdd:cd00267 57 --------------------------LIDGKDIAK---------------------------LPLEELRRRIgyVPQLSG 83
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHDRYFIDNVASRCVEIEGGK 233
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRelaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-522 |
5.98e-24 |
|
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: 106.41 E-value: 5.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 32 IAIIGKNGEGKSTLLKAIFGTLQLDSGRI------------------------IRQNDKSIAMLAQQVDfntnlsldeLI 87
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGEIKVAHKPQYVD---------LI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 88 NKNLS-EIYEALNKYenlqaklathlDNKNLHKEInnlinfieskdawnieqkkerfLKEFKLFEYKNRPISSLSGGEIR 166
Cdd:COG1245 173 PKVFKgTVRELLEKV-----------DERGKLDEL----------------------AEKLGLENILDRDISELSGGELQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKIcVIFISHDRYFIDNVASRcVEIEGGKisffNGGYA 242
Cdd:COG1245 220 RVAIAAALLRDADFYFFDEPSSYLDIYqrlnVARLIRELAEEGKY-VLVVEHDLAILDYLADY-VHILYGE----PGVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 243 yylekkaqiLVSLSKSyetlikhlkaeeewLRRGVKARLK---RNEG---RKERI-FKMREEAKKNPGEIKrlklellra 315
Cdd:COG1245 294 ---------VVSKPKS--------------VRVGINQYLDgylPEENvriRDEPIeFEVHAPRREKEEETL--------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 316 nssIQKPNFNKQKMIFEL-VNASKIinnkilfknfstriLQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIkNADIKI 394
Cdd:COG1245 342 ---VEYPDLTKSYGGFSLeVEGGEI--------------REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 395 GYFDQaramlnsdksLIElfcPNGGDRVQ--VRGHDMHIYG--YLKS-FLFP---KEFLSQAVSVLSGGEKNRVALALLF 466
Cdd:COG1245 404 SYKPQ----------YIS---PDYDGTVEefLRSANTDDFGssYYKTeIIKPlglEKLLDKNVKDLSGGELQRVAIAACL 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 467 TKDYDVLILDEPTNDLD----IATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:COG1245 471 SRDADLYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-188 |
9.97e-24 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 97.72 E-value: 9.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND-----------KSIAMLAQQVDFNTNLSLDEli 87
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQdltdderkslrKEIGYVFQDPQLFPRLTVRE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 88 nknlsEIYEALNKYENLQAKlathldnknlhkeinnlinfieskdawnIEQKKERFLKEFKLFEYKNRPI----SSLSGG 163
Cdd:pfam00005 79 -----NLRLGLLLKGLSKRE----------------------------KDARAEEALEKLGLGDLADRPVgerpGTLSGG 125
|
170 180
....*....|....*....|....*
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTN 188
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-234 |
1.12e-23 |
|
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: 99.52 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQN---------DKSIAMLAQq 74
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvtgvppeRRNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 vdfntNLSLdelinknlseiYEALNKYENLqaklATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKN 154
Cdd:cd03259 80 -----DYAL-----------FPHLTVAENI----AFGLKLRGVPKA--------------EIRARVRELLELVGLEGLLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 155 RPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:cd03259 126 RYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAklreELREELKELQRELGITTIYVTHDQEEALALADRIAVMN 205
|
....
gi 1751968159 231 GGKI 234
Cdd:cd03259 206 EGRI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
347-530 |
1.19e-23 |
|
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: 99.89 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAR--------AML--NSDKSL------ 410
Cdd:cd03257 22 DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirrkeiQMVfqDPMSSLnprmti 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ----IELFCPNGGDRVQVRgHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT 486
Cdd:cd03257 102 geqiAEPLRIHGKLSKKEA-RKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 487 -INILEeyLM-----EFKGALIFVSHDRYFVDKLATKLYVFENGVInIEH 530
Cdd:cd03257 181 qAQILD--LLkklqeELGLTLLFITHDLGVVAKIADRVAVMYAGKI-VEE 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-526 |
1.74e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 104.50 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQL--DSGRII-------------------R 62
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvgE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 63 QNDKSIAMLA-QQVDFntnLSLDELINKNLSEIYEALnkyenLQAKLATHLDNKNLHKEINNL--INFiESKDAWnieQK 139
Cdd:TIGR03269 81 PCPVCGGTLEpEEVDF---WNLSDKLRRRIRKRIAIM-----LQRTFALYGDDTVLDNVLEALeeIGY-EGKEAV---GR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 140 KERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEF----LEKLLKNSKICVIFISHD 215
Cdd:TIGR03269 149 AVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 216 RYFIDNVASRCVEIEGGKIsffnggyayyleKKAQILVSLSKSYETLIKHLKAEEEWLRrgvkarlkrnegrKERIFKMR 295
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEI------------KEEGTPDEVVAVFMEGVSEVEKECEVEV-------------GEPIIKVR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 296 EeAKKNPGEIKRlklELLRANSSIQkpnfnkqkmiFElvnaskiinnkilfknfstrILQGEKIGIVGQNGCGKSTFLKI 375
Cdd:TIGR03269 284 N-VSKRYISVDR---GVVKAVDNVS----------LE--------------------VKEGEIFGIVGTSGAGKTTLSKI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 376 LLNLDKLSSGE--IKNAD-----IKIGYFDQARA-----MLNSDKSL-------------IELFCPNGGDRvqvrghdMH 430
Cdd:TIGR03269 330 IAGVLEPTSGEvnVRVGDewvdmTKPGPDGRGRAkryigILHQEYDLyphrtvldnlteaIGLELPDELAR-------MK 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 431 IYGYLKSFLF----PKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLM----EFKGALI 502
Cdd:TIGR03269 403 AVITLKMVGFdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILkareEMEQTFI 482
|
570 580
....*....|....*....|....
gi 1751968159 503 FVSHDRYFVDKLATKLYVFENGVI 526
Cdd:TIGR03269 483 IVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
332-526 |
1.96e-23 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 97.51 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI----------KIGYFDQ 399
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILldGKDLaslspkelarKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 400 ARAMLNsdkslIElfcpnggdrvqvrghdmhiygylksflfpkEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:cd03214 81 ALELLG-----LA------------------------------HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 480 NDLDIA----TINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03214 126 SHLDIAhqieLLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
346-526 |
4.95e-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: 98.17 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIKIGYFDQAR---AML--NSDkslIELFCPNG 418
Cdd:COG1122 17 LDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLvdGKDITKKNLRELRrkvGLVfqNPD---DQLFAPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 419 GDRVqvrghdmhIYGyLKSFLFPKE-----------------FLSQAVSVLSGGEKNRVALA-LLFTKDyDVLILDEPTN 480
Cdd:COG1122 94 EEDV--------AFG-PENLGLPREeirerveealelvglehLADRPPHELSGGQKQRVAIAgVLAMEP-EVLVLDEPTA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 481 DLDIATINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG1122 164 GLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
341-524 |
9.90e-23 |
|
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: 95.53 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFDqaramlnsDKSLIELfcpnggD 420
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI--------LID--------GVDLRDL------D 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 RVQVRGHdmhIyGYL--KSFLFP---KEflsqavSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLM 495
Cdd:cd03228 71 LESLRKN---I-AYVpqDPFLFSgtiRE------NILSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|.
gi 1751968159 496 EFKG--ALIFVSHdRYFVDKLATKLYVFENG 524
Cdd:cd03228 141 ALAKgkTVIVIAH-RLSTIRDADRIIVLDDG 170
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
10-215 |
1.07e-22 |
|
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: 97.12 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIamlaqqvdfnTNLSLDELINK 89
Cdd:cd03219 7 TKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGS-VLFDGEDI----------TGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLS------EIYEALNKYENLQakLATHLDNKnlhkeiNNLINFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGG 163
Cdd:cd03219 76 GIGrtfqipRLFPELTVLENVM--VAAQARTG------SGLLLARARREEREARERAEELLERVGLADLADRPAGELSYG 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPT---NHLDVY-MCEFLEKlLKNSKICVIFISHD 215
Cdd:cd03219 148 QQRRLEIARALATDPKLLLLDEPAaglNPEETEeLAELIRE-LRERGITVLLVEHD 202
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-252 |
2.51e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.35 E-value: 2.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDfntnlSL 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRD-----AL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DEliNKNlseIYEA---------LNKYE-NLQAKLAThldnknlhkeinnlINFiesKDAwniEQKKerflkefklfeyk 153
Cdd:PRK11819 400 DP--NKT---VWEEisggldiikVGNREiPSRAYVGR--------------FNF---KGG---DQQK------------- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 nrPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEG-G 232
Cdd:PRK11819 442 --KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGdS 519
|
250 260
....*....|....*....|
gi 1751968159 233 KISFFNGGYAYYLEKKAQIL 252
Cdd:PRK11819 520 QVEWFEGNFQEYEEDKKRRL 539
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
332-526 |
5.92e-22 |
|
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: 94.52 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-------NADIKIGYFDQARaml 404
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkpleKERKRIGYVPQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSDKSlielFCPNGGDRVQvrghdMHIYGYLKSFLFPK-----------------EFLSQAVSVLSGGEKNRVALALLFT 467
Cdd:cd03235 78 SIDRD----FPISVRDVVL-----MGLYGHKGLFRRLSkadkakvdealervglsELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 468 KDYDVLILDEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
6-237 |
8.46e-22 |
|
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: 94.14 E-value: 8.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 6 LIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdKSIAMLAQQVDFNTNLSLDE 85
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGLGGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 86 LINKNLSeIYealnkyeNLQAklathldnknlhKEINNLINFIEskdawnieqkkerflkEF-KLFEYKNRPISSLSGGE 164
Cdd:cd03220 104 NIYLNGR-LL-------GLSR------------KEIDEKIDEII----------------EFsELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 165 IRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKIcVIFISHDRYFIDNVASRCVEIEGGKISFF 237
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAfqekCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-234 |
1.15e-21 |
|
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: 99.52 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQVD-FNT-- 79
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidLRQIDpaslrRQIGVVLQDVFlFSGti 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 --NLSL-DELInkNLSEIYEAlnkyenlqAKLAthldnkNLHKEINNLinfieskdawniEQKKERFLKEFKlfeyknrp 156
Cdd:COG2274 566 reNITLgDPDA--TDEEIIEA--------ARLA------GLHDFIEAL------------PMGYDTVVGEGG-------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 157 iSSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNskICVIFISHDRYFIDNvASRCVEIEGG 232
Cdd:COG2274 610 -SNLSGGQRQRLAIARALLRNPRILILDEATSALDAeteaIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKG 685
|
..
gi 1751968159 233 KI 234
Cdd:COG2274 686 RI 687
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-234 |
2.11e-21 |
|
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: 92.98 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQQVDF 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 ntnlsldelinknlseIYEALNKYENLqaklaTHLDN-----KNLHKeinnlinfiESKDAwnIEQKKERFLKEFKLFEY 152
Cdd:cd03262 81 ----------------VFQQFNLFPHL-----TVLENitlapIKVKG---------MSKAE--AEERALELLEKVGLADK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 153 KNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMC-EFLE--KLLKNSKICVIFISHDRYFIDNVASRCVEI 229
Cdd:cd03262 129 ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgEVLDvmKDLAEEGMTMVVVTHEMGFAREVADRVIFM 208
|
....*
gi 1751968159 230 EGGKI 234
Cdd:cd03262 209 DDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-234 |
3.08e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 92.81 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKI-ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-------RQNDKSIAMLAQQV 75
Cdd:COG2884 2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLvngqdlsRLKRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 -----DFNtnlsldeLINKnlseiyeaLNKYENLqaKLATHLDNKNlHKEINNLINFIeskdawnieqkkerfLKEFKLF 150
Cdd:COG2884 82 gvvfqDFR-------LLPD--------RTVYENV--ALPLRVTGKS-RKEIRRRVREV---------------LDLVGLS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISSLSGGEirKINLCIL--VLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSK-ICVIFISHDRYFIDNVASR 225
Cdd:COG2884 129 DKAKALPHELSGGE--QQRVAIAraLVNRPELLLADEPTGNLDPETSWEIMELLEeiNRRgTTVLIATHDLELVDRMPKR 206
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:COG2884 207 VLELEDGRL 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
332-526 |
4.18e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 92.43 E-value: 4.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK---------NADIK--IGYFDQa 400
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvlgedvardPAEVRrrIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 401 RAMLNSDKSLIEL------FCPNGGDRVQVRghdmhIYGYLKSF-LfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVL 473
Cdd:COG1131 81 EPALYPDLTVRENlrffarLYGLPRKEARER-----IDELLELFgL--TDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 474 ILDEPTNDLDIATINILEEYLMEFK--GALIFVS-HDRYFVDKLATKLYVFENGVI 526
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAaeGKTVLLStHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-239 |
4.76e-21 |
|
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: 92.63 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGE-KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI--------------IRQNDKSI 68
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidgtdinklkgkaLRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 69 AMLAQQvdFNtnlsldeLINKnlseiyeaLNKYEN-LQAKLATHldnknlhkeinnliNFIESKDAWNIEQKKER---FL 144
Cdd:cd03256 81 GMIFQQ--FN-------LIER--------LSVLENvLSGRLGRR--------------STWRSLFGLFPKEEKQRalaAL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 145 KEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCE----FLEKLLKNSKICVIFISHDRYFID 220
Cdd:cd03256 130 ERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRqvmdLLKRINREEGITVIVSLHQVDLAR 209
|
250
....*....|....*....
gi 1751968159 221 NVASRCVEIEGGKIsFFNG 239
Cdd:cd03256 210 EYADRIVGLKDGRI-VFDG 227
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-234 |
4.97e-21 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 92.18 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKI----ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND------------- 65
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 66 -KSIAMLAQqvdfntnlsldelinknlsEIYEALNKYENLQAKLATHLdnknlhkeinnLINFIESKDawniEQKKERFL 144
Cdd:cd03257 81 rKEIQMVFQ-------------------DPMSSLNPRMTIGEQIAEPL-----------RIHGKLSKK----EARKEAVL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 145 KEFKLF----EYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDR 216
Cdd:cd03257 127 LLLVGVglpeEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDL 206
|
250
....*....|....*...
gi 1751968159 217 YFIDNVASRCVEIEGGKI 234
Cdd:cd03257 207 GVVAKIADRVAVMYAGKI 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
341-540 |
6.82e-21 |
|
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: 97.21 E-value: 6.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGYFDQaRAMLNSDk 408
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidGIDLRqidpaslrrqIGVVLQ-DVFLFSG- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLIE---LFCPNGGD-RVQ-----------VRGHDMhiyGYlksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVL 473
Cdd:COG2274 564 TIREnitLGDPDATDeEIIeaarlaglhdfIEALPM---GY-------DTVVGEGGSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 474 ILDEPTNDLDIATINILEEYLMEFKG--ALIFVSHDRYFVdKLATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKgrTVIIIAHRLSTI-RLADRIIVLDKGRI-VEDGTHEELLARK 700
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
346-480 |
8.78e-21 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 89.24 E-value: 8.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI----------KIGYFDQARAmLNSDKSLIE- 412
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldGQDLtdderkslrkEIGYVFQDPQ-LFPRLTVREn 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 413 LFCPNGGDRVQVRGHDMHIYGYLKSF---LFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTN 480
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLglgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-234 |
9.10e-21 |
|
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: 92.02 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIamlaqqvdfnTN 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGR-ILFDGRDI----------TG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDELINKNLS------EIYEALNKYENLQakLATHL-DNKNLHKEINNLINFIESKDAwnIEQKKERFLKEFKLFEYK 153
Cdd:COG0411 71 LPPHRIARLGIArtfqnpRLFPELTVLENVL--VAAHArLGRGLLAALLRLPRARREERE--ARERAEELLERVGLADRA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPT---NHLDV-YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEI 229
Cdd:COG0411 147 DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETeELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVL 226
|
....*
gi 1751968159 230 EGGKI 234
Cdd:COG0411 227 DFGRV 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-234 |
1.95e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 95.22 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQVD-FNT-- 79
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSItlggvdLRDLDeddlrRRIAVVPQRPHlFDTtl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 --NLSL------DElinknlsEIYEALNkyenlQAKLATHLDN--KNLhkeinnlinfieskDAWnieqkkerflkefkL 149
Cdd:COG4987 426 reNLRLarpdatDE-------ELWAALE-----RVGLGDWLAAlpDGL--------------DTW--------------L 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRpissLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSkiCVIFISHDRYFIDNvASR 225
Cdd:COG4987 466 GEGGRR----LSGGERRRLALARALLRDAPILLLDEPTEGLDAateqALLADLLEALAGR--TVLLITHRLAGLER-MDR 538
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:COG4987 539 ILVLEDGRI 547
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
332-526 |
2.01e-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: 90.24 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINN-----KILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADI------------ 392
Cdd:cd03255 2 ELKNLSKTYGGggekvQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrVDGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 --KIGYFDQARAMLNsDKSLIE------LFCPNGGDRVQVRGHDMhiygyLKSF-LfpKEFLSQAVSVLSGGEKNRVALA 463
Cdd:cd03255 81 rrHIGFVFQSFNLLP-DLTALEnvelplLLAGVPKKERRERAEEL-----LERVgL--GDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 464 LLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRYFVdKLATKLYVFENGVI 526
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
347-526 |
3.17e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 89.57 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGYFDQARAMLN-SDKSLIEL 413
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldGTDIRqldpadlrrnIGYVPQDVTLFYgTLRDNITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 FCPNGGDRVQVRGHDMhiyGYLKSFL--FPKEF---LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:cd03245 101 GAPLADDERILRAAEL---AGVTDFVnkHPNGLdlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1751968159 489 ILEEYLMEFKG--ALIFVSHdRYFVDKLATKLYVFENGVI 526
Cdd:cd03245 178 RLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
10-234 |
5.54e-20 |
|
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: 93.81 E-value: 5.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-------RQNDKSIAMLAQQVDF---NT 79
Cdd:COG1123 272 VRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILfdgkdltKLSRRSLRELRRRVQMvfqDP 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLdeliNKNLS---EIYEALnkyenlqaklathldnknlhkeinnLINFIESKDAwnIEQKKERFLKEFKLF-EYKNR 155
Cdd:COG1123 352 YSSL----NPRMTvgdIIAEPL-------------------------RLHGLLSRAE--RRERVAELLERVGLPpDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 156 PISSLSGGEIRKINLC-ILVLqNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:COG1123 401 YPHELSGGQRQRVAIArALAL-EPKLLILDEPTSALDVSvqaqILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
....
gi 1751968159 231 GGKI 234
Cdd:COG1123 480 DGRI 483
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
330-526 |
7.04e-20 |
|
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: 89.33 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI----------KIGYF 397
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVllDGRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQAramlnsdkslielfcPNGGDRVQVRghDMHIYG---YLKSFLFPKE-----------------FLSQAVSVLSGGEK 457
Cdd:COG1120 81 PQE---------------PPAPFGLTVR--ELVALGrypHLGLFGRPSAedreaveealertglehLADRPVDELSGGER 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLDIA----TINILEEYLMEFKGALIFVSHD-----RYfvdklATKLYVFENGVI 526
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAhqleVLELLRRLARERGRTVVMVLHDlnlaaRY-----ADRLVLLKDGRI 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-234 |
7.63e-20 |
|
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: 88.58 E-value: 7.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGR-------IIRQND---KSIAMLAQQvdfntn 80
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdVVREPRevrRRIGIVFQD------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDElinknlseiyeALNKYENL--QAKLAThLDNKNLHKEINNLINFIEskdawnieqkkerflkefkLFEYKNRPIS 158
Cdd:cd03265 82 LSVDD-----------ELTGWENLyiHARLYG-VPGAERRERIDELLDFVG-------------------LLEAADRLVK 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03265 131 TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtraHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-237 |
9.06e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 9.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 8 KASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIAMLAQQVDFNTNLSLdeli 87
Cdd:COG1134 31 RRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV-NGRVSALLELGAGFHPELTG---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 88 nknlseiyealnkYENLQAKLATHldnkNL-HKEINNLINFIEskdawnieqkkerflkEF-KLFEYKNRPISSLSGGEI 165
Cdd:COG1134 106 -------------RENIYLNGRLL----GLsRKEIDEKFDEIV----------------EFaELGDFIDQPVKTYSSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 166 RKINLCILVLQNPDVLLLDEptnhldVYM---------C-EFLEKLLKNSKIcVIFISHDRYFIDNVASRCVEIEGGKIS 235
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDE------VLAvgdaafqkkClARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLV 225
|
..
gi 1751968159 236 FF 237
Cdd:COG1134 226 MD 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 |
1.09e-19 |
|
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: 88.99 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTL-QLDSGRI--------------IRqnd 65
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVrlfgerrggedvweLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 66 KSIAML--AQQVDFNTNLSLDELInknLSEIYEAL---NKYENLQAKLAthldnknlhkeinnlinfieskDAWnieqkk 140
Cdd:COG1119 78 KRIGLVspALQLRFPRDETVLDVV---LSGFFDSIglyREPTDEQRERA----------------------REL------ 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 141 erfLKEFKLFEYKNRPISSLSGGEIRkinlciLVL------QNPDVLLLDEPTNHLDVYMCE----FLEKLLKNSKICVI 210
Cdd:COG1119 127 ---LELLGLAHLADRPFGTLSQGEQR------RVLiaralvKDPELLILDEPTAGLDLGARElllaLLDKLAAEGAPTLV 197
|
....
gi 1751968159 211 FISH 214
Cdd:COG1119 198 LVTH 201
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-234 |
1.49e-19 |
|
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: 88.32 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKI----ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-----------IRQNDKS 67
Cdd:COG1124 1 MLEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVtfdgrpvtrrrRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 68 IAMLAQQ--VDFNTNLSLDELINknlseiyEALNkyenlqaklathldnknLHKEINnlinfieskdawnIEQKKERFLK 145
Cdd:COG1124 81 VQMVFQDpyASLHPRHTVDRILA-------EPLR-----------------IHGLPD-------------REERIAELLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 146 EFKL-FEYKNRPISSLSGGEIRKInlCI---LVLQnPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRY 217
Cdd:COG1124 124 QVGLpPSFLDRYPHQLSGGQRQRV--AIaraLILE-PELLLLDEPTSALDVSvqaeILNLLKDLREERGLTYLFVSHDLA 200
|
250
....*....|....*..
gi 1751968159 218 FIDNVASRCVEIEGGKI 234
Cdd:COG1124 201 VVAHLCDRVAVMQNGRI 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
353-522 |
2.85e-19 |
|
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: 87.46 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 353 ILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQ---------ARAMLNSdkslielfcpnggdrvQ 423
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQyikadyegtVRDLLSS----------------I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 424 VRGHDMHIYgYLKSFLFP---KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD----IATINILEEYLME 496
Cdd:cd03237 86 TKDFYTHPY-FKTEIAKPlqiEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAEN 164
|
170 180
....*....|....*....|....*.
gi 1751968159 497 FKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
346-524 |
3.01e-19 |
|
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: 86.58 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRI---LQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-----------KNADI-----KIGYFDQARAM--- 403
Cdd:cd03297 10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdsrKKINLppqqrKIGLVFQQYALfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 LNSDKSLI--ELFCPNGGDRVQVRghDMHIYGYLKSFLFpkeflsQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:cd03297 90 LNVRENLAfgLKRKRNREDRISVD--ELLDLLGLDHLLN------RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1751968159 482 LDIATINILEEYLME----FKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03297 162 LDRALRLQLLPELKQikknLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-234 |
3.17e-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: 87.17 E-value: 3.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQND-------------KSIA 69
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVlIDGEDisglseaelyrlrRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 70 MLAQQvdfntnlsldelinknlSEIYEALNKYENLQAKLATHLDNknlhkeinnlinfieskDAWNIEQKKERFLKEFKL 149
Cdd:cd03261 81 MLFQS-----------------GALFDSLTVFENVAFPLREHTRL-----------------SEEEIREIVLEKLEAVGL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLC-ILVLqNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKIC-VIFISHDRYFIDNVAS 224
Cdd:cd03261 127 RGAEDLYPAELSGGMKKRVALArALAL-DPELLLYDEPTAGLDPIASGVIDDLirsLKKELGLtSIMVTHDLDTAFAIAD 205
|
250
....*....|
gi 1751968159 225 RCVEIEGGKI 234
Cdd:cd03261 206 RIAVLYDGKI 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-234 |
3.94e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 86.64 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFG----EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIamlaqqvdf 77
Cdd:COG1136 3 PLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEV-LIDGQDI--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 nTNLS---LDELINKNLSEIY------EALNKYENLQakLATHLDNKnlhkeinnlinfieskDAWNIEQKKERFLKEFK 148
Cdd:COG1136 73 -SSLSereLARLRRRHIGFVFqffnllPELTALENVA--LPLLLAGV----------------SRKERRERARELLERVG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 149 LFEYKNRPISSLSGGEIRKInlCI---LVlQNPDVLLLDEPTNHLD------VYmcEFLEKLLKNSKICVIFISHDRyFI 219
Cdd:COG1136 134 LGDRLDHRPSQLSGGQQQRV--AIaraLV-NRPKLILADEPTGNLDsktgeeVL--ELLRELNRELGTTIVMVTHDP-EL 207
|
250
....*....|....*
gi 1751968159 220 DNVASRCVEIEGGKI 234
Cdd:COG1136 208 AARADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-233 |
7.47e-19 |
|
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: 84.55 E-value: 7.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSG-------------RIIRQNDKSIAM 70
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGsilidgedltdleDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 71 LAQQVDFNTNLSLdelinknlseiyealnkYENLQAklathldnknlhkeinnlinfieskdawnieqkkerflkefklf 150
Cdd:cd03229 81 VFQDFALFPHLTV-----------------LENIAL-------------------------------------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 eyknrpisSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRC 226
Cdd:cd03229 100 --------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPItrreVRALLKSLQAQLGITVVLVTHDLDEAARLADRV 171
|
....*..
gi 1751968159 227 VEIEGGK 233
Cdd:cd03229 172 VVLRDGK 178
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
7.95e-19 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 88.23 E-value: 7.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIAML-AQQVDFNT 79
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGR-ILLDGRDVTGLpPEKRNVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 ---------NLSLdelinknlseiyealnkYENlqakLATHLDNKNLhkeinnlinfieSKDAwnIEQKKERFLKEFKLF 150
Cdd:COG3842 82 vfqdyalfpHLTV-----------------AEN----VAFGLRMRGV------------PKAE--IRARVAELLELVGLE 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 151 EYKNRPISSLSGGEIRKINLC-ILVLQnPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDR 216
Cdd:COG3842 127 GLADRYPHQLSGGQQQRVALArALAPE-PRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQ 196
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-234 |
1.57e-18 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 84.61 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII---------RQNDKSIAMLAQq 74
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYiggrdvtdlPPKDRDIAMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 vdfntNLSLdelinknlseiYEALNKYENLQAKLathldnkNLHKeinnlinfiESKDawNIEQKKERFLKEFKLFEYKN 154
Cdd:cd03301 80 -----NYAL-----------YPHMTVYDNIAFGL-------KLRK---------VPKD--EIDERVREVAELLQIEHLLD 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 155 RPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:cd03301 126 RKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMN 205
|
....
gi 1751968159 231 GGKI 234
Cdd:cd03301 206 DGQI 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-215 |
2.04e-18 |
|
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: 84.60 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAML-AQQVDFNT--- 79
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-LLDGKDITNLpPHKRPVNTvfq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLdelinknlseiYEALNKYENLqaklATHLDNKNLHKEInnlinfieskdawnIEQKKERFLKEFKLFEYKNRPISS 159
Cdd:cd03300 80 NYAL-----------FPHLTVFENI----AFGLRLKKLPKAE--------------IKERVAEALDLVQLEGYANRKPSQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 160 LSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:cd03300 131 LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
10-234 |
3.35e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.42 E-value: 3.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamLAQQVDFNTNLSLDELINK 89
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEI----------TFDGKSYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLS--EIYEALNKYENLQAKLATHLDNKNLHKEINNLINFIESKDawnieqkkerflkefklfeyknRPISSLSGGEIRK 167
Cdd:cd03268 77 LIEapGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAK----------------------KKVKGFSLGMKQR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 168 INLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKlLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03268 135 LGIALALLGNPDLLILDEPTNGLDPDgikeLRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-257 |
3.56e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 88.30 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQ-QVDFntnL 81
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQhQLEF---L 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELINKNLSEIYEalnkyENLQAKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFlkefklfeyknrpisslS 161
Cdd:PRK10636 389 RADESPLQHLARLAP-----QELEQKLRDYLGGFGFQGD--------------KVTEETRRF-----------------S 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGy 241
Cdd:PRK10636 433 GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGD- 511
|
250
....*....|....*.
gi 1751968159 242 ayyLEKKAQILVSLSK 257
Cdd:PRK10636 512 ---LEDYQQWLSDVQK 524
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
345-546 |
7.13e-18 |
|
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: 87.13 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGYFDQaRAMLNSDkSLIE 412
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlgGVDLRdldeddlrrrIAVVPQ-RPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 ---LFCPNGGD--------RVQvrghdmhiygyLKSFL--FPK---EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILD 476
Cdd:COG4987 428 nlrLARPDATDeelwaaleRVG-----------LGDWLaaLPDgldTWLGEGGRRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 477 EPTNDLDIATI-NILEEYLMEFKG-ALIFVSHDRYFVDKlATKLYVFENGVInIEHMSYTQYLEREFELREF 546
Cdd:COG4987 497 EPTEGLDAATEqALLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRI-VEQGTHEELLAQNGRYRQL 566
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-187 |
7.42e-18 |
|
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: 82.87 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIamlaqqvdfnTNLSLDELINKNLS----- 92
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDI----------TGLPPHERARAGIGyvpeg 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 -EIYEALNKYENLQakLATHLDNKnlhkeinnlinfieSKDAWNIEQKKERF--LKEFklfeyKNRPISSLSGGEIRKIN 169
Cdd:cd03224 84 rRIFPELTVEENLL--LGAYARRR--------------AKRKARLERVYELFprLKER-----RKQLAGTLSGGEQQMLA 142
|
170
....*....|....*...
gi 1751968159 170 LCILVLQNPDVLLLDEPT 187
Cdd:cd03224 143 IARALMSRPKLLLLDEPS 160
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-215 |
7.56e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 85.51 E-value: 7.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII----RQNDKS-----IAML 71
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILiggrDVTDLPpkdrnIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 72 AQqvdfntNLSLdelinknlseiYEALNKYENlqakLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFE 151
Cdd:COG3839 81 FQ------SYAL-----------YPHMTVYEN----IAFPLKLRKVPKA--------------EIDRRVREAAELLGLED 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 152 YKNRPISSLSGGE----------IRkinlcilvlqNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHD 215
Cdd:COG3839 126 LLDRKPKQLSGGQrqrvalgralVR----------EPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-236 |
7.83e-18 |
|
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: 82.73 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 21 EINFSANEnEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamLAQQVDFNTNLSLD--------ELINKNLS 92
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIV---------LNGTVLFDSRKKINlppqqrkiGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 eIYEALNKYENLQAKLATHLDNKnlhkeinnlinfieskdawnIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCI 172
Cdd:cd03297 86 -LFPHLNVRENLAFGLKRKRNRE--------------------DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 173 LVLQNPDVLLLDEPTNHLDVYMCE----FLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:cd03297 145 ALAAQPELLLLDEPFSALDRALRLqllpELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQY 212
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
341-526 |
9.01e-18 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 82.30 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARA----MLNSDKSL------ 410
Cdd:cd03226 12 GTEIL-DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSigyvMQDVDYQLftdsvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 --IELFCPNGGDRVQVRGH---DMHIYGYlksflfpKEFLSQAvsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:cd03226 91 eeLLLGLKELDAGNEQAETvlkDLDLYAL-------KERHPLS---LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 486 TINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03226 161 NMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-234 |
9.14e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 82.33 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKsiamlaqqvdfntnlsL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKP----------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DELINKNLSEIYEALNKYENLqaklathldnknlhKEINNLINFIESKDAWNIEQKKE--RFLKEFKLFEYKNRPISSLS 161
Cdd:cd03269 65 DIAARNRIGYLPEERGLYPKM--------------KVIDQLVYLAQLKGLKKEEARRRidEWLERLELSEYANKRVEELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVireLARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
341-529 |
1.32e-17 |
|
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: 80.82 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFDQARAmLNSDKSLIELFCPnggd 420
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI--------TLDGVPV-SDLEKALSSLISV---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 rVQVRGHdmhiygylksfLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEF-KG 499
Cdd:cd03247 80 -LNQRPY-----------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlKD 147
|
170 180 190
....*....|....*....|....*....|.
gi 1751968159 500 -ALIFVSHDRYFVDKlATKLYVFENGVINIE 529
Cdd:cd03247 148 kTLIWITHHLTGIEH-MDKILFLENGKIIMQ 177
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
341-526 |
1.60e-17 |
|
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: 86.35 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQA--RAML-----NS---DKSL 410
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswRRQIawvpqNPylfAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 IE---LFCPNGGD--------RVQV--------RGHDMHI----YGylksflfpkeflsqavsvLSGGEKNRVALALLFT 467
Cdd:COG4988 428 REnlrLGRPDASDeeleaaleAAGLdefvaalpDGLDTPLgeggRG------------------LSGGQAQRLALARALL 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 468 KDYDVLILDEPTNDLDIATinilEEYLME-----FKG-ALIFVSHDRYFVdKLATKLYVFENGVI 526
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAET----EAEILQalrrlAKGrTVILITHRLALL-AQADRILVLDDGRI 549
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-234 |
1.96e-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: 81.95 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIamlaqqvdfnTNL 81
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGE-ILVDGQDI----------TGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELiNKNLSEI---------YEALNKYENLQAKL--ATHLDnknlHKEINNLINFIeskdawnieqkkerfLKEFKLF 150
Cdd:COG1127 73 SEKEL-YELRRRIgmlfqggalFDSLTVFENVAFPLreHTDLS----EAEIRELVLEK---------------LELVGLP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISSLSGGEIRKINLC-ILVLqNPDVLLLDEPTNHLDVYMCEFLEKLLKN----SKICVIFISHDRYFIDNVASR 225
Cdd:COG1127 133 GAADKMPSELSGGMRKRVALArALAL-DPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHDLDSAFAIADR 211
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:COG1127 212 VAVLADGKI 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-237 |
4.19e-17 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 80.31 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSAnENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-------IRQNDK---SIAMLAQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvLKQPQKlrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 QVDFNTNLSLDELINknlseiYEALNKyenlqaklatHLDNKNLHKEInnlinfieskdawnieqkkERFLKEFKLFEYK 153
Cdd:cd03264 80 EFGVYPNFTVREFLD------YIAWLK----------GIPSKEVKARV-------------------DEVLELVNLGDRA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSkiCVIFISHDRYFIDNVASRCVEI 229
Cdd:cd03264 125 KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpeerIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVL 202
|
....*...
gi 1751968159 230 EGGKISFF 237
Cdd:cd03264 203 NKGKLVFE 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-234 |
4.41e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.21 E-value: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-----------RQNDKSIAMLAQQVDFNTNL 81
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlssRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELINKNLSeiyealnKYENLQAKLAThldnknlhkeinnlinfiesKDawniEQKKERFLKEFKLFEYKNRPISSLS 161
Cdd:PRK11231 92 TVRELVAYGRS-------PWLSLWGRLSA--------------------ED----NARVNQAMEQTRINHLADRRLTDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcVIFISHDRyfidNVASR-C---VEIEGGK 233
Cdd:PRK11231 141 GGQRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRELNTQGKT-VVTVLHDL----NQASRyCdhlVVLANGH 215
|
.
gi 1751968159 234 I 234
Cdd:PRK11231 216 V 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-234 |
9.54e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 77.85 E-value: 9.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiaMLAQQVDFNTnlsl 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEIL--------VDGKEVSFAS---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 delinknlseIYEAlnkyenLQAKLAThldnknlhkeinnlinfieskdawnieqkkerflkefklfeyknrpISSLSGG 163
Cdd:cd03216 69 ----------PRDA------RRAGIAM----------------------------------------------VYQLSVG 86
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03216 87 ERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVirrLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-234 |
1.07e-16 |
|
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: 83.65 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQ-VDFNT-- 79
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdLSDLDpaswrRQIAWVPQNpYLFAGti 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 --NLSL------DElinknlsEIYEALnkyenlqaKLAthldnkNLHKEINNLINFIESkdawnieqkkerflkefklfe 151
Cdd:COG4988 428 reNLRLgrpdasDE-------ELEAAL--------EAA------GLDEFVAALPDGLDT--------------------- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 152 yknrPI----SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSkiCVIFISHDRYFIDNvA 223
Cdd:COG4988 466 ----PLgeggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAeteaEILQALRRLAKGR--TVILITHRLALLAQ-A 538
|
250
....*....|.
gi 1751968159 224 SRCVEIEGGKI 234
Cdd:COG4988 539 DRILVLDDGRI 549
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
346-523 |
1.34e-16 |
|
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: 79.05 E-value: 1.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNSDKSL---------IEL--- 413
Cdd:cd03293 20 LEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALlpwltvldnVALgle 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 --FCPNGGDRVQVRgHDMHIYGyLKSFL--FPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI 489
Cdd:cd03293 100 lqGVPKAEARERAE-ELLELVG-LSGFEnaYPHQ--------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1751968159 490 LEEYLM----EFKGALIFVSHDryfVDK---LATKLYVFEN 523
Cdd:cd03293 170 LQEELLdiwrETGKTVLLVTHD---IDEavfLADRVVVLSA 207
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
343-545 |
1.86e-16 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 82.63 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYfdqaramLNSDKSLIELFcpNGGDR 421
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGK-------LRQDQFAFEEF--TVLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 422 VqVRGH-DM--------HIY------------------------GY---------LKSFLFPKEFLSQAVSVLSGGEKNR 459
Cdd:PRK15064 85 V-IMGHtELwevkqerdRIYalpemseedgmkvadlevkfaemdGYtaearagelLLGVGIPEEQHYGLMSEVAPGWKLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 460 VALA-LLFTkDYDVLILDEPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQYLE 538
Cdd:PRK15064 164 VLLAqALFS-NPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMT 242
|
....*..
gi 1751968159 539 REFELRE 545
Cdd:PRK15064 243 AATQARE 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-233 |
2.53e-16 |
|
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: 77.04 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqqvdfntnlsldeLIN-KNLS 92
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-------------------------LIDgVDLR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIyealnkyenlqaklathlDNKNLHKEInnlinfieskdAWnIEQkkerflkEFKLFeykNRPISS--LSGGEIRKINL 170
Cdd:cd03228 68 DL------------------DLESLRKNI-----------AY-VPQ-------DPFLF---SGTIREniLSGGQRQRIAI 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 171 CILVLQNPDVLLLDEPTNHLDVYM-CEFLEKLLKNSKIC-VIFISHDRYFIDNvASRCVEIEGGK 233
Cdd:cd03228 108 ARALLRDPPILILDEATSALDPETeALILEALRALAKGKtVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-215 |
2.63e-16 |
|
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: 78.28 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFG----EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQ 73
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 Q--------VDFNTNLSLDelinknlseiyealnkyenlqaklathldnknlhkeinnlINFIESKDAwniEQKKERFLK 145
Cdd:cd03293 81 QdallpwltVLDNVALGLE----------------------------------------LQGVPKAEA---RERAEELLE 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 146 EFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:cd03293 118 LVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD 191
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-225 |
2.77e-16 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.97 E-value: 2.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI---------IRQND--KSIAMLA 72
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvatTPSRElaKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 73 QQVDFNTNLSLDELInknlseiyeALNKYENLQAKLathldNKNLHKEINNLINFieskdawnieqkkerflkeFKLFEY 152
Cdd:COG4604 82 QENHINSRLTVRELV---------AFGRFPYSKGRL-----TAEDREIIDEAIAY-------------------LDLEDL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 153 KNRPISSLSGGEiRKINLCILVL-QNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfIdNVASR 225
Cdd:COG4604 129 ADRYLDELSGGQ-RQRAFIAMVLaQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD---I-NFASC 201
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
341-526 |
3.35e-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: 76.87 E-value: 3.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIKIGYFDQARAMLnsdkslielfcpng 418
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRldGADISQWDPNELGDHV-------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 419 gdrvqvrghdmhiyGYL--KSFLFPKeflSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLME 496
Cdd:cd03246 79 --------------GYLpqDDELFSG---SIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAA 141
|
170 180 190
....*....|....*....|....*....|...
gi 1751968159 497 FKGA---LIFVSHdRYFVDKLATKLYVFENGVI 526
Cdd:cd03246 142 LKAAgatRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
10-186 |
3.93e-16 |
|
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: 77.97 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQND-----------KSIAMLAQQvdf 77
Cdd:cd03218 7 SKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlLDGQDitklpmhkrarLGIGYLPQE--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 ntnlsldelinknlSEIYEALNKYENLQAKLATHLDNKnlhkeinnlinfieskdaWNIEQKKERFLKEFKLFEYKNRPI 157
Cdd:cd03218 84 --------------ASIFRKLTVEENILAVLEIRGLSK------------------KEREEKLEELLEEFHITHLRKSKA 131
|
170 180
....*....|....*....|....*....
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEP 186
Cdd:cd03218 132 SSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-215 |
4.48e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.59 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFG-----EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIamlaqqvdfn 78
Cdd:COG1101 2 LELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSIL-IDGKDV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 TNLSlDELINKNLSEIY--------EALNKYENLQakLATHLDNK-NLHKEINNlinfieskdawnieQKKERF---LKE 146
Cdd:COG1101 71 TKLP-EYKRAKYIGRVFqdpmmgtaPSMTIEENLA--LAYRRGKRrGLRRGLTK--------------KRRELFrelLAT 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 147 FKL-FEykNR---PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFL----EKLLKNSKICVIFISHD 215
Cdd:COG1101 134 LGLgLE--NRldtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIVEENNLTTLMVTHN 208
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-234 |
4.69e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 79.81 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKsiamlaqqvDFNTNLSL 83
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-NGR---------DLFTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DElinknlSEI------YeALNK----YENLqaklATHLDNKNLhkeinnlinfieSKDAwnIEQKKERFLKEFKLFEYK 153
Cdd:COG1118 73 RE------RRVgfvfqhY-ALFPhmtvAENI----AFGLRVRPP------------SKAE--IRARVEELLELVQLEGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLC-ILVlQNPDVLLLDEPTNHLDVYMCEFLEK----LLKNSKICVIFISHDR---YfidNVASR 225
Cdd:COG1118 128 DRYPSQLSGGQRQRVALArALA-VEPEVLLLDEPFGALDAKVRKELRRwlrrLHDELGGTTVFVTHDQeeaL---ELADR 203
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:COG1118 204 VVVMNQGRI 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
331-530 |
6.97e-16 |
|
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: 77.22 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKL-----SSGEIknadikigYFDqARAMLN 405
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEV--------LLD-GKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 406 SDKSLIELFCpnggdRVQ-VRGH----DMHIY----------GYLksflfPKEFLSQAVSV------------------- 451
Cdd:cd03260 72 LDVDVLELRR-----RVGmVFQKpnpfPGSIYdnvayglrlhGIK-----LKEELDERVEEalrkaalwdevkdrlhalg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 452 LSGGEKNRVALALLFTKDYDVLILDEPTNDLD-IATINIlEEYLMEFKG--ALIFVSHDRYFVDKLATKLYVFENGVInI 528
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDpISTAKI-EELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRL-V 219
|
..
gi 1751968159 529 EH 530
Cdd:cd03260 220 EF 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
329-526 |
7.96e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.01 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKI-INNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----------KNADI----- 392
Cdd:COG2884 1 MI-RFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngqdlsrlKRREIpylrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 KIGY-FDQARamLNSDKSLIElfcpNggdrV----QVRGHDMHIYGYL------------KSFLFPKEflsqavsvLSGG 455
Cdd:COG2884 80 RIGVvFQDFR--LLPDRTVYE----N----ValplRVTGKSRKEIRRRvrevldlvglsdKAKALPHE--------LSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 456 EKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEF--KG-ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG2884 142 EQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInrRGtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
332-526 |
1.30e-15 |
|
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: 76.02 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI--------KIGY-FDQA 400
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIliDGRDVtgvpperrNIGMvFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 401 R---------------AMLNSDKSLIElfcpnggDRVQVRGHDMHIYGYLKSFlfpkeflsqaVSVLSGGEKNRVALALL 465
Cdd:cd03259 82 AlfphltvaeniafglKLRGVPKAEIR-------ARVRELLELVGLEGLLNRY----------PHELSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 466 FTKDYDVLILDEPTNDLD-IATINILEE---YLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03259 145 LAREPSLLLLDEPLSALDaKLREELREElkeLQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
1.32e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 77.05 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKF----GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAM 70
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVlvdgkpVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 71 LAQQvdfntnlslDELinknlseiYEALNKYENlqakLATHLDNKNLHKeinnlinfieskdawniEQKKER---FLKEF 147
Cdd:COG1116 85 VFQE---------PAL--------LPWLTVLDN----VALGLELRGVPK-----------------AERRERareLLELV 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 148 KLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:COG1116 127 GLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQETGKTVLFVTHD 198
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
346-524 |
1.92e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 76.67 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNSDKSL---------IELfcP 416
Cdd:COG1116 27 LDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQEPALlpwltvldnVAL--G 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 417 ---NGGDRVQVRGHDMH---IYGyLKSFL--FPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:COG1116 105 lelRGVPKAERRERARElleLVG-LAGFEdaYPHQ--------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1751968159 489 ILEEYLM----EFKGALIFVSHDryfVD---KLATKLYVFENG 524
Cdd:COG1116 176 RLQDELLrlwqETGKTVLFVTHD---VDeavFLADRVVVLSAR 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-187 |
2.59e-15 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 75.79 E-value: 2.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIamlaqqvdfnTNLSLDELINKNLS- 92
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI-RFDGEDI----------TGLPPHRIARLGIGy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 -----EIYEALNKYENLQAKLATHLDnknlhkeinnlinfiESKDAWNIEQKKERF--LKEFKlfeykNRPISSLSGGEi 165
Cdd:COG0410 83 vpegrRIFPSLTVEENLLLGAYARRD---------------RAEVRADLERVYELFprLKERR-----RQRAGTLSGGE- 141
|
170 180
....*....|....*....|....*
gi 1751968159 166 RKInLCI---LVLqNPDVLLLDEPT 187
Cdd:COG0410 142 QQM-LAIgraLMS-RPKLLLLDEPS 164
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
329-526 |
3.98e-15 |
|
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: 75.40 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI-------------K 393
Cdd:COG1127 5 MI-EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILvdGQDItglsekelyelrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 394 IGYFDQARAMLNS-----------------DKSLIElfcpnggDRVQVRGHDMHIYGYLKsfLFPKEflsqavsvLSGGE 456
Cdd:COG1127 84 IGMLFQGGALFDSltvfenvafplrehtdlSEAEIR-------ELVLEKLELVGLPGAAD--KMPSE--------LSGGM 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 457 KNRVALA----LlftkDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG1127 147 RKRVALAralaL----DPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
330-526 |
4.99e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 74.69 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINN-----KILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYF-DQARAM 403
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLsERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 LNSDK------------SL-----IELfcPNGGDRVQVRGHDMHIYGYLKSF-LfpKEFLSQAVSVLSGGEKNRVAL--A 463
Cdd:COG1136 83 LRRRHigfvfqffnllpELtalenVAL--PLLLAGVSRKERRERARELLERVgL--GDRLDHRPSQLSGGQQQRVAIarA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 464 LLftKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRyFVDKLATKLYVFENGVI 526
Cdd:COG1136 159 LV--NRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
347-508 |
5.38e-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: 78.10 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIK------------IGYFDQARAMLNsdKSL---I 411
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqIAWVPQHPFLFA--GTIaenI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 ELFCPnGGDRVQVRG--HDMHIYGYLKSFLFPKEF-LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:TIGR02857 417 RLARP-DASDAEIREalERAGLDEFVAALPQGLDTpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
170 180
....*....|....*....|..
gi 1751968159 489 ILEEYLMEFKG--ALIFVSHDR 508
Cdd:TIGR02857 496 EVLEALRALAQgrTVLLVTHRL 517
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-214 |
8.53e-15 |
|
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: 74.19 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQ-VDFNTNLs 82
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSIlidgqdIREVTldslrRAIGVVPQDtVLFNDTI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNLS----EIYEAlnkyenlqAKLAthldnkNLHKEINNLinfiesKDAWNiEQKKERFLKefklfeyknrpis 158
Cdd:cd03253 92 GYNIRYGRPDatdeEVIEA--------AKAA------QIHDKIMRF------PDGYD-TIVGERGLK------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 159 sLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKicVIFISH 214
Cdd:cd03253 138 -LSGGEKQRVAIARAILKNPPILLLDEATSALDTHtereIQAALRDVSKGRT--TIVIAH 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
337-529 |
9.31e-15 |
|
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: 73.41 E-value: 9.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 337 SKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKnadIKIGYFDQARAMLNSDKSLIEL--F 414
Cdd:cd03268 7 TKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEIT---FDGKSYQKNIEALRRIGALIEApgF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNGGDRVQVRGHDMhIYGYLKSFLfpKEFL---------SQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:cd03268 84 YPNLTARENLRLLAR-LLGIRKKRI--DEVLdvvglkdsaKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1751968159 486 TINILEEYLMEFK--GALIFV-SHDRYFVDKLATKLYVFENGVINIE 529
Cdd:cd03268 161 GIKELRELILSLRdqGITVLIsSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
19-234 |
9.68e-15 |
|
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: 73.78 E-value: 9.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQVD--FNT---NLS 82
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldgtdIRQLDpadlrRNIGYVPQDVTlfYGTlrdNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNlSEIYEAlnkyenlqAKLATHLDNKNLHKEINNLinfieskdawnieQKKERFlkefklfeyknrpiSSLSG 162
Cdd:cd03245 100 LGAPLADD-ERILRA--------AELAGVTDFVNKHPNGLDL-------------QIGERG--------------RGLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDvYMCE--FLEKL--LKNSKICVIfISHdRYFIDNVASRCVEIEGGKI 234
Cdd:cd03245 144 GQRQAVALARALLNDPPILLLDEPTSAMD-MNSEerLKERLrqLLGDKTLII-ITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
342-539 |
9.82e-15 |
|
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: 74.19 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 342 NKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSG--EIKNADIK---IGYFDQARAMLNSDKSL------ 410
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGsiLIDGQDIRevtLDSLRRAIGVVPQDTVLfndtig 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 --IELFCPNGGDRVQVRGHDM-HIYGYLKSFlfPKEFLSQavsV------LSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:cd03253 93 ynIRYGRPDATDEEVIEAAKAaQIHDKIMRF--PDGYDTI---VgerglkLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 482 LDIATINILEEYLME-FKG-ALIFVSHD-RYFVDklATKLYVFENGVInIEHMSYTQYLER 539
Cdd:cd03253 168 LDTHTEREIQAALRDvSKGrTTIVIAHRlSTIVN--ADKIIVLKDGRI-VERGTHEELLAK 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
19-236 |
1.05e-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: 73.56 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI----IRQNDKSIAMLAQQVDFNTNLSLdelinknlsei 94
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgFDVVKEPAEARRRLGFVSDSTGL----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALNKYENLQAKLATH-LDNKNLHKEINNLINFIESKdawnieqkkerflkefklfEYKNRPISSLSGGEIRKINLCIL 173
Cdd:cd03266 90 YDRLTARENLEYFAGLYgLKGDELTARLEELADRLGME-------------------ELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 174 VLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKiCVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMatraLREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVY 216
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-234 |
1.30e-14 |
|
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: 73.77 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEK----IILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII--------------RQN 64
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltllsgkelRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 65 DKSIAMLAQQvdFNtnlsldelinknlseIYEALNKYEN--LQAKLAtHLDNKNLHKEINNLINFIeskdawNIEQKKER 142
Cdd:cd03258 81 RRRIGMIFQH--FN---------------LLSSRTVFENvaLPLEIA-GVPKAEIEERVLELLELV------GLEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 143 FlkefklfeyknrpISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSK--ICVIFISHDRYF 218
Cdd:cd03258 137 Y-------------PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRElgLTIVLITHEMEV 203
|
250
....*....|....*.
gi 1751968159 219 IDNVASRCVEIEGGKI 234
Cdd:cd03258 204 VKRICDRVAVMEKGEV 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-236 |
1.41e-14 |
|
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: 73.52 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-------IRQNDKSIAMLAQQVDFNTNLSL 83
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpWKRRKKFLRRIGVVFGQKTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DelinknLSEIyealnkyenlqaklathlDNKNLHKEINNLinfieskDAWNIEQKKERFLKEFKLFEYKNRPISSLSGG 163
Cdd:cd03267 109 D------LPVI------------------DSFYLLAAIYDL-------PPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVaqenIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLY 234
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-231 |
1.44e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.98 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 27 NENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKsIAMLAQQVDFNTNLSLDELinknLSEIyealnkyenlqa 106
Cdd:cd03237 23 SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQYIKADYEGTVRDL----LSSI------------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 107 klathldnknlhkeinnlinfieSKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEP 186
Cdd:cd03237 86 -----------------------TKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 187 TNHLDVYMCEFLEKLLK----NSKICVIFISHDRYFIDNVASRCVEIEG 231
Cdd:cd03237 143 SAYLDVEQRLMASKVIRrfaeNNEKTAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-527 |
1.60e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIAML----AQQVDFN 78
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT-LEIGGNPCARLtpakAHQLGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 ---------TNLSLDELINKNLSEIYEALNKYENLQAKLATHLDnknLHKEINNLinfieskdawnieqkkerflkefkl 149
Cdd:PRK15439 90 lvpqepllfPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLD---LDSSAGSL------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 fEYKNRPISSLSGGEIRkinlcilvlqNPDVLLLDEPTNHLDVYMCEFL---EKLLKNSKICVIFISHDRYFIDNVASRc 226
Cdd:PRK15439 142 -EVADRQIVEILRGLMR----------DSRILILDEPTASLTPAETERLfsrIRELLAQGVGIVFISHKLPEIRQLADR- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 227 veieggkISFFNGGYayylekkaqilVSLSKSYETLikhlkaeeewlrrgvkarlkrneGRKERIFKMREEAKKNP-GEI 305
Cdd:PRK15439 210 -------ISVMRDGT-----------IALSGKTADL-----------------------STDDIIQAITPAAREKSlSAS 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 306 KRLKLELL--RANSSIQKPNFNKQKMIFElvnaskiinnkiLFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLS 383
Cdd:PRK15439 249 QKLWLELPgnRRQQAAGAPVLTVEDLTGE------------GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 384 SGEIKNADIKIGYFDQARAM------LNSDKSLIELF--CPNGGDRVQVRGHDMHIY-----------GYLKSFLFPKEF 444
Cdd:PRK15439 317 GGRIMLNGKEINALSTAQRLarglvyLPEDRQSSGLYldAPLAWNVCALTHNRRGFWikparenavleRYRRALNIKFNH 396
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 445 LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI---ATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVF 521
Cdd:PRK15439 397 AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVsarNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
....*.
gi 1751968159 522 ENGVIN 527
Cdd:PRK15439 477 HQGEIS 482
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
331-506 |
1.72e-14 |
|
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: 71.31 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILlnldklsSGEIKnadikigyfdqaramlnsdksl 410
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKIL-------SGLYK---------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ielfcPNGGdRVQVRGHDMHIYGylksflfPKEFLSQAVSV---LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATI 487
Cdd:cd03216 52 -----PDSG-EILVDGKEVSFAS-------PRDARRAGIAMvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEV 118
|
170 180
....*....|....*....|..
gi 1751968159 488 NILEEYLMEFKG---ALIFVSH 506
Cdd:cd03216 119 ERLFKVIRRLRAqgvAVIFISH 140
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
332-526 |
1.77e-14 |
|
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: 72.67 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYF---DQARAMLNSDK 408
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppkDRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLIelfcPNggdrvqVRGHDMHIYGyLKSFLFPK-----------------EFLSQAVSVLSGGEKNRVALALLFTKDYD 471
Cdd:cd03301 82 ALY----PH------MTVYDNIAFG-LKLRKVPKdeidervrevaellqieHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 472 VLILDEPTNDLD----IATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03301 151 VFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
350-526 |
1.78e-14 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 72.79 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 350 STRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-----------KIGYFDQARAMLN--SDKSLIELFcp 416
Cdd:cd03266 25 SFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFdvvkepaearrRLGFVSDSTGLYDrlTARENLEYF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 417 ngGDRVQVRGHDMHI-YGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLM 495
Cdd:cd03266 103 --AGLYGLKGDELTArLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|....
gi 1751968159 496 EFKG---ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03266 181 QLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-244 |
2.11e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 76.82 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQ-VDfNTNLSLDELINknLS 92
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHhVD-GLDLSSNPLLY--MM 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIYEALnkyenLQAKLATHLDNKNLhkeINNLinfieskdawnieqkkerflkefklfeyKNRPISSLSGGEIRKINLCI 172
Cdd:PLN03073 597 RCFPGV-----PEQKLRAHLGSFGV---TGNL----------------------------ALQPMYTLSGGQKSRVAFAK 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 173 LVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFFNGGYAYY 244
Cdd:PLN03073 641 ITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
344-507 |
2.15e-14 |
|
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: 72.85 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 344 ILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI--------------KIGY----------- 396
Cdd:COG4181 27 IL-KGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRlaGQDLfaldedararlrarHVGFvfqsfqllptl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 ------------------FDQARAMLnsdkslielfcpnggDRVQVrGHDMHIYgylksflfPKEflsqavsvLSGGEKN 458
Cdd:COG4181 106 talenvmlplelagrrdaRARARALL---------------ERVGL-GHRLDHY--------PAQ--------LSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 459 RVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHD 507
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHD 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-234 |
2.44e-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: 73.10 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQQV- 75
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedLTDSKKDINKLRRKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 ----DFNtnlsldeLINkNLSeiyeALnkyENLqaKLA-THLdnKNLHKEinnlinfieskDAwniEQKKERFLKEFKLF 150
Cdd:COG1126 81 mvfqQFN-------LFP-HLT----VL---ENV--TLApIKV--KKMSKA-----------EA---EERAMELLERVGLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISSLSGGE-----I-RKinLCIlvlqNPDVLLLDEPTNHLDVYMC-EFLE--KLLKNSKICVIFISHDRYFIDN 221
Cdd:COG1126 128 DKADAYPAQLSGGQqqrvaIaRA--LAM----EPKVMLFDEPTSALDPELVgEVLDvmRDLAKEGMTMVVVTHEMGFARE 201
|
250
....*....|...
gi 1751968159 222 VASRCVEIEGGKI 234
Cdd:COG1126 202 VADRVVFMDGGRI 214
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-192 |
2.46e-14 |
|
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: 73.31 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-----------RQNDKSIAMLA 72
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 73 QQVDFNTNLSLDELInknlseiyeALNKyenlqaklathldnknlhkeinnlinfIESKDAWNIEQKKE-----RFLKEF 147
Cdd:TIGR03873 82 QDSDTAVPLTVRDVV---------ALGR---------------------------IPHRSLWAGDSPHDaavvdRALART 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1751968159 148 KLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV 192
Cdd:TIGR03873 126 ELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDV 170
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-215 |
2.80e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.95 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQlDSGRIiRQNDKSI------------AMLAQQVDFNTNLSldel 86
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEI-LLNGRPLsdwsaaelarhrAYLSQQQSPPFAMP---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 inknlseIYEalnkYenlqakLATHLDNKNLHKEINNLINFIESKdawnieqkkerflkeFKLFEYKNRPISSLSGGEIR 166
Cdd:COG4138 86 -------VFQ----Y------LALHQPAGASSEAVEQLLAQLAEA---------------LGLEDKLSRPLTQLSGGEWQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 167 KINLCILVLQ-----NPD--VLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHD 215
Cdd:COG4138 134 RVRLAAVLLQvwptiNPEgqLLLLDEPMNSLDVAQQAALDRLLRelcQQGITVVMSSHD 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-229 |
2.82e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND----KSIAMLAQQVD 76
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdveaLSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 77 F---NTNLSLDelinKNLSEIYEaLNKYENLqAKLATHldnknlhkeinnlinfiESKDAWNIEQKKERflkeFKLFEYK 153
Cdd:PRK09536 81 SvpqDTSLSFE----FDVRQVVE-MGRTPHR-SRFDTW-----------------TETDRAAVERAMER----TGVAQFA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFIsHDRyfidNVASR-CVE 228
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINhqvrTLELVRRLVDDGKTAVAAI-HDL----DLAARyCDE 208
|
.
gi 1751968159 229 I 229
Cdd:PRK09536 209 L 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-524 |
3.65e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.51 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKS---------------------------TLLKAIFGTLqldsgRIIRQNdkS 67
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvtalsilrllpsppvvypsgdirfhgeSLLHASEQTL-----RGVRGN--K 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 68 IAMLAQQvdfnTNLSLDEL--INKNLseiYEALNKYENLQAKLAthldnknlHKEInnlinfIESKDAWNIEQKKERfLK 145
Cdd:PRK15134 94 IAMIFQE----PMVSLNPLhtLEKQL---YEVLSLHRGMRREAA--------RGEI------LNCLDRVGIRQAAKR-LT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 146 EFKlfeyknrpiSSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK----ICVIFISHD----RY 217
Cdd:PRK15134 152 DYP---------HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqelnMGLLFITHNlsivRK 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 218 FIDNVA----SRCVEIEGGKISFFNGGYAYylekkAQILvslsksyetlikhLKAEeewlrrgvkarlkrNEGRKERIfk 293
Cdd:PRK15134 223 LADRVAvmqnGRCVEQNRAATLFSAPTHPY-----TQKL-------------LNSE--------------PSGDPVPL-- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 294 mreEAKKNPgeikRLKLELLRAnssiqkpNFNKQKMIFElvnasKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFL 373
Cdd:PRK15134 269 ---PEPASP----LLDVEQLQV-------AFPIRKGILK-----RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTG 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 374 KILLNLDKlSSGEIKNADIKIGYFDQaRAMLNSDKSLIELFC-PNGG--DRVQV-----RGHDMHiygylKSFLFPKEFL 445
Cdd:PRK15134 330 LALLRLIN-SQGEIWFDGQPLHNLNR-RQLLPVRHRIQVVFQdPNSSlnPRLNVlqiieEGLRVH-----QPTLSAAQRE 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 446 SQAVSVL-----------------SGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFV 504
Cdd:PRK15134 403 QQVIAVMeevgldpetrhrypaefSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVqaqiLALLKSLQQKHQLAYLFI 482
|
570 580
....*....|....*....|
gi 1751968159 505 SHDRYFVDKLATKLYVFENG 524
Cdd:PRK15134 483 SHDLHVVRALCHQVIVLRQG 502
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-234 |
5.43e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.74 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI--------------IRqndKSIAMLAQQVDfntn 80
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTItvggmvlseetvwdVR---RQVGMVFQNPD---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 lsldelinknlseiyealNKY--ENLQAKLATHLDNKNLHKEinnliNFIESKDAwnieqkkerFLKEFKLFEYKNRPIS 158
Cdd:PRK13635 92 ------------------NQFvgATVQDDVAFGLENIGVPRE-----EMVERVDQ---------ALRQVGMEDFLNREPH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfIDNVAS--RCVEIEGG 232
Cdd:PRK13635 140 RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD---LDEAAQadRVIVMNKG 216
|
..
gi 1751968159 233 KI 234
Cdd:PRK13635 217 EI 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-234 |
6.08e-14 |
|
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: 71.99 E-value: 6.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQ--QVDFntnl 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQerNVGF---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 sldelINKNLSeIYEALNKYEN----LQAKLATHLDNKNLhkeinnlinfieskdawnIEQKKERFLKEFKLFEYKNRPI 157
Cdd:cd03296 79 -----VFQHYA-LFRHMTVFDNvafgLRVKPRSERPPEAE------------------IRAKVHELLKLVQLDWLADRYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCE----FLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGK 233
Cdd:cd03296 135 AQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKelrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR 214
|
.
gi 1751968159 234 I 234
Cdd:cd03296 215 I 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
346-526 |
8.38e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.65 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKnADIKIGyfdqaramlnsdkSLIEL---FCPN--GGD 420
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-VNGRVS-------------ALLELgagFHPEltGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 RVQVRGhdmHIYGYLKSF---LFPK--------EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEptndldiatinI 489
Cdd:COG1134 108 NIYLNG---RLLGLSRKEideKFDEivefaelgDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-----------V 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 490 L-----------EEYLMEFK---GALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG1134 174 LavgdaafqkkcLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
332-526 |
9.24e-14 |
|
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: 70.99 E-value: 9.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI-------------KIGY 396
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLidGEDIsglseaelyrlrrRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 FDQARAMLNS-----------------DKSLIElfcpnggDRVQvrgHDMHIYGyLKSF--LFPKEflsqavsvLSGGEK 457
Cdd:cd03261 82 LFQSGALFDSltvfenvafplrehtrlSEEEIR-------EIVL---EKLEAVG-LRGAedLYPAE--------LSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
347-524 |
9.35e-14 |
|
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: 71.00 E-value: 9.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-----------KNADIKIGYFDQARAMLN--SDKSLIEL 413
Cdd:cd03263 19 DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirtdrKAARQSLGYCPQFDALFDelTVREHLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 FCpnggdrvQVRGH-----DMHIYGYLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:cd03263 99 YA-------RLKGLpkseiKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1751968159 489 ILEEYLMEFKG--ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03263 171 AIWDLILEVRKgrSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-236 |
1.17e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 70.94 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIIldEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQN---------DKSIAMLAQQ 74
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqdltalppaERPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 vdfnTNLsldelinknlseiYEALNKYENLQAKLATHLdnkNLhkeinnlinfieskdawNIEQKK--ERFLKEFKLFEY 152
Cdd:COG3840 80 ----NNL-------------FPHLTVAQNIGLGLRPGL---KL-----------------TAEQRAqvEQALERVGLAGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 153 KNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfID---NVASR 225
Cdd:COG3840 123 LDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD---PEdaaRIADR 199
|
250
....*....|.
gi 1751968159 226 CVEIEGGKISF 236
Cdd:COG3840 200 VLLVADGRIAA 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
347-545 |
1.19e-13 |
|
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: 73.78 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNL---DKLSSGEIKNADI------------KIGY-FDQARAMLNS---D 407
Cdd:COG1123 23 DGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRdllelsealrgrRIGMvFQDPMTQLNPvtvG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 408 KSLIELFCPNGGDRVQVRGHDMHIygyLKSFLFPkEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT- 486
Cdd:COG1123 103 DQIAEALENLGLSRAEARARVLEL---LEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTq 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 487 ---INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLEREFELRE 545
Cdd:COG1123 179 aeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI-VEDGPPEEILAAPQALAA 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
346-526 |
1.35e-13 |
|
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: 70.25 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKnadikigyfdqaraMLNSDKSLIEL---FCPN--GGD 420
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT--------------VRGRVSSLLGLgggFNPEltGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 RVQVRGhdmHIYGYLKSFLFPK-----------EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI 489
Cdd:cd03220 104 NIYLNG---RLLGLSRKEIDEKideiiefselgDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1751968159 490 LEEYLMEFK---GALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03220 181 CQRRLRELLkqgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-215 |
1.48e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 71.68 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIAmlaqqvdfntnlsl 83
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE-VLWDGEPLD-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DELINK--NLSE---IYEALNKYENLQ--AKLathldnKNLHKeinnlinfiesKDAwniEQKKERFLKEFKLFEYKNRP 156
Cdd:COG4152 67 PEDRRRigYLPEergLYPKMKVGEQLVylARL------KGLSK-----------AEA---KRRADEWLERLGLGDRANKK 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHD 215
Cdd:COG4152 127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVireLAAKGTTVIFSSHQ 188
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-234 |
1.75e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.96 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSI------------A 69
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGE-VRLNGRPLadwspaelarrrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 70 MLAQQvdfnTNLSLDELInknlSEIYeALNKYenlqaklathlDNKNLHKEINNLInfieskdawnieqkkERFLKEFKL 149
Cdd:PRK13548 80 VLPQH----SSLSFPFTV----EEVV-AMGRA-----------PHGLSRAEDDALV---------------AAALAQVDL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKIN----LCILVLQNPD--VLLLDEPTNHLDVYMCEFLEKLLKN----SKICVIFISHD---- 215
Cdd:PRK13548 125 AHLAGRDYPQLSGGEQQRVQlarvLAQLWEPDGPprWLLLDEPTSALDLAHQHHVLRLARQlaheRGLAVIVVLHDlnla 204
|
250 260
....*....|....*....|
gi 1751968159 216 -RYfidnvASRCVEIEGGKI 234
Cdd:PRK13548 205 aRY-----ADRIVLLHQGRL 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-540 |
1.87e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 1.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQA--RAMLNSDKSLIELF--------- 414
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAalRQAISVVSQRVHLFsatlrdnll 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 --CPNGGDR------VQVrghdmhiyGyLKSFLFPKEFLS--------QavsvLSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:PRK11160 436 laAPNASDEalievlQQV--------G-LEKLLEDDKGLNawlgeggrQ----LSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 479 TNDLDIAT-INILEEYLMEFKG-ALIFVSHDRYFVDKLaTKLYVFENGVInIEHMSYTQYLERE 540
Cdd:PRK11160 503 TEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQF-DRICVMDNGQI-IEQGTHQELLAQQ 564
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
348-537 |
2.12e-13 |
|
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: 70.60 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFD--QARAmLNSDKSLIELFCPNGGD-RVQV 424
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkQRRA-FRRDVQLVFQDSPSAVNpRMTV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 425 R---GHDMH-------------IYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI---- 484
Cdd:TIGR02769 108 RqiiGEPLRhltsldeseqkarIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqa 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 485 ATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYL 537
Cdd:TIGR02769 188 VILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI-VEECDVAQLL 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-234 |
2.16e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.55 E-value: 2.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAI------------FGTLQLDSGRIIRQNDKSI 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 69 AMLAQQVDFntnlsldelinknlseIYEALNKYEnlqaklathldnknlHKEInnLINFIESKDAWNIEQKKE------R 142
Cdd:PRK11264 81 RQLRQHVGF----------------VFQNFNLFP---------------HRTV--LENIIEGPVIVKGEPKEEatararE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 143 FLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMC-EFLEKL--LKNSKICVIFISHDRYFI 219
Cdd:PRK11264 128 LLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNTIrqLAQEKRTMVIVTHEMSFA 207
|
250
....*....|....*
gi 1751968159 220 DNVASRCVEIEGGKI 234
Cdd:PRK11264 208 RDVADRAIFMDQGRI 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
344-540 |
2.54e-13 |
|
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: 69.88 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 344 ILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIK----------IGYFDQARAMLNSdkSLI 411
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIllDGVDIRdlnlrwlrsqIGLVSQEPVLFDG--TIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 E--LFCPNGGDRVQVR--GHDMHIYGYLKSflFPKEF---LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI 484
Cdd:cd03249 95 EniRYGKPDATDEEVEeaAKKANIHDFIMS--LPDGYdtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 485 ATINILEEYLMEF-KGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:cd03249 173 ESEKLVQEALDRAmKGRTTIVIAHRLSTIRNADLIAVLQNGQV-VEQGTHDELMAQK 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-235 |
2.99e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 69.74 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSG----------------RIIRQndk 66
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglkvndpkvdeRLIRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 67 SIAMLAQQvdFNtnlsldelinknlseIYEALNKYEN-----LQAKLATHLDNKNLHKEInnlinfieskdawnieqkke 141
Cdd:PRK09493 78 EAGMVFQQ--FY---------------LFPHLTALENvmfgpLRVRGASKEEAEKQAREL-------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 142 rfLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYM-CEFLE--KLLKNSKICVIFISHDRYF 218
Cdd:PRK09493 121 --LAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELrHEVLKvmQDLAEEGMTMVIVTHEIGF 198
|
250
....*....|....*..
gi 1751968159 219 IDNVASRCVEIEGGKIS 235
Cdd:PRK09493 199 AEKVASRLIFIDKGRIA 215
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
329-506 |
3.12e-13 |
|
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: 69.73 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILL-NLDKLSSGEIK-------NADI-----KIG 395
Cdd:COG1119 2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVRlfgerrgGEDVwelrkRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 396 YFDQAramlnsdksLIELFcpnggdRVQVRGHDMHIYGYLKSF-LFPK-------------------EFLSQAVSVLSGG 455
Cdd:COG1119 82 LVSPA---------LQLRF------PRDETVLDVVLSGFFDSIgLYREptdeqrerarellellglaHLADRPFGTLSQG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 456 EKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSH 506
Cdd:COG1119 147 EQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
10-234 |
3.76e-13 |
|
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: 69.29 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEkIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIamlaqqvdfnTNLSLDeliNK 89
Cdd:cd03299 7 SKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-NGKDI----------TNLPPE---KR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLSEIYE--ALNKYENLQAKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRK 167
Cdd:cd03299 72 DISYVPQnyALFPHMTVYKNIAYGLKKRKVDKK--------------EIERKVLEIAEMLGIDHLLNRKPETLSGGEQQR 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 168 INLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK----NSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03299 138 VAIARALVVNPKILLLDEPFSALDVRTKEKLREELKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-222 |
3.76e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 69.36 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQnDKSIAMLA-----QQVD 76
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE-GEDISTLKpeiyrQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 77 --FNTNLSLDELINKNLSEIYEALNKYENlqaklathldnknlhkeinnlinfieskdawniEQKKERFLKEFKLFEYK- 153
Cdd:PRK10247 85 ycAQTPTLFGDTVYDNLIFPWQIRNQQPD---------------------------------PAIFLDDLERFALPDTIl 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 154 NRPISSLSGGEIRKINLcILVLQN-PDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFI---DNV 222
Cdd:PRK10247 132 TKNIAELSGGEKQRISL-IRNLQFmPKVLLLDEITSALDESnkhnVNEIIHRYVREQNIAVLWVTHDKDEInhaDKV 207
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-186 |
4.02e-13 |
|
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: 69.23 E-value: 4.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAMLAqqVDFNTNLSLDELINK 89
Cdd:TIGR04406 8 IKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKI-LIDGQDITHLP--MHERARLGIGYLPQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 nlSEIYEALNKYENLQAKLAThldnknlhkeinnlinfIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKIN 169
Cdd:TIGR04406 85 --ASIFRKLTVEENIMAVLEI-----------------RKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVE 145
|
170
....*....|....*..
gi 1751968159 170 LCILVLQNPDVLLLDEP 186
Cdd:TIGR04406 146 IARALATNPKFILLDEP 162
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-236 |
4.08e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.08 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIAmlaqqvdfNTNLSLDElINKNLSEI 94
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKII-IDGVDIT--------DKKVKLSD-IRKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEalnkYENLQaklathLDNKNLHKEIN-NLINFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCIL 173
Cdd:PRK13637 89 FQ----YPEYQ------LFEETIEKDIAfGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 174 VLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKgrdeILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCEL 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-232 |
4.43e-13 |
|
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: 69.00 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKF-----GEKII--LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQNDksiamlaQ 73
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlVRHDG-------G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 QVDFnTNLSLDELINKNLSEI-Y-----------------------------EALNKYENLQAKLathldnkNLHKEInn 123
Cdd:COG4778 76 WVDL-AQASPREILALRRRTIgYvsqflrviprvsaldvvaepllergvdreEARARARELLARL-------NLPERL-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 124 linfieskdaWNIeqkkerflkefklfeyknrPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLE 199
Cdd:COG4778 146 ----------WDL-------------------PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanrAVVVELIE 196
|
250 260 270
....*....|....*....|....*....|...
gi 1751968159 200 KlLKNSKICVIFISHDRYFIDNVASRCVEIEGG 232
Cdd:COG4778 197 E-AKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
342-484 |
5.50e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 5.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 342 NKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFdqaramlnSDKSLIE--------L 413
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML--------SSRQLARrlallpqhH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 FCPNG-------------------------GDRVQVRGHDMHIygylksflfpKEFLSQAVSVLSGGEKNRVALALLFTK 468
Cdd:PRK11231 86 LTPEGitvrelvaygrspwlslwgrlsaedNARVNQAMEQTRI----------NHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170
....*....|....*.
gi 1751968159 469 DYDVLILDEPTNDLDI 484
Cdd:PRK11231 156 DTPVVLLDEPTTYLDI 171
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-235 |
6.09e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.83 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIAMLAQQV------ 75
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGS-ISLCGEPVPSRARHArqrvgv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 --DFNtNLSLDELINKNLseiyEALNKYENLQAKLATHLdnknlhkeINNLINFIEskdawnIEQKKErflkefklfeyk 153
Cdd:PRK13537 85 vpQFD-NLDPDFTVRENL----LVFGRYFGLSAAAARAL--------VPPLLEFAK------LENKAD------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 nRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKIcVIFISHdryFIDNvASR---- 225
Cdd:PRK13537 134 -AKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPqarhLMWERLRSLLARGKT-ILLTTH---FMEE-AERlcdr 207
|
250
....*....|.
gi 1751968159 226 -CVEIEGGKIS 235
Cdd:PRK13537 208 lCVIEEGRKIA 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
12-234 |
6.20e-13 |
|
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: 69.45 E-value: 6.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 12 KFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQNDKSIAMLAQQVDFNTNLSLdelinkN 90
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVsFRGQDLYQLDRKQRRAFRRDVQL------V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 91 LSEIYEALNKYENLQAKLATHLDNknlhkeinnlinfIESKDAWNIEQKKERFLKEFKL-FEYKNRPISSLSGGEIRKIN 169
Cdd:TIGR02769 94 FQDSPSAVNPRMTVRQIIGEPLRH-------------LTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 170 LCILVLQNPDVLLLDEPTNHLDVYM----CEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLqaviLELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
7-234 |
6.80e-13 |
|
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: 70.53 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 7 IKASKKFGEkIILDeINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIAMLAQQVDFNTNlsldel 86
Cdd:TIGR02142 3 ARFSKRLGD-FSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIV-LNGRTLFDSRKGIFLPPE------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 iNKNLSEIYEalnkyenlQAKLATHLDNKNlhkeinNLINFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIR 166
Cdd:TIGR02142 74 -KRRIGYVFQ--------EARLFPHLSVRG------NLRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-216 |
7.11e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 70.36 E-value: 7.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIAML-AQQVDFNT-- 79
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-LDGQDITHVpAENRHVNTvf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 -NLSLdelinknlseiYEALNKYENLQAKLATHldnKNLHKEINNLInfiesKDAwnieqkkerfLKEFKLFEYKNRPIS 158
Cdd:PRK09452 93 qSYAL-----------FPHMTVFENVAFGLRMQ---KTPAAEITPRV-----MEA----------LRMVQLEEFAQRKPH 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDR 216
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrKQMQNELKALQRKLGITFVFVTHDQ 205
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
17-506 |
7.71e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 17 IILDEINFSANENekIAIIGKNGEGKSTLLKAIFGTLQLDSGRiiRQNDksiamlaqqvdFN--TNLSLDELiNKNLSEI 94
Cdd:PRK10938 19 LQLPSLTLNAGDS--WAFVGANGSGKSALARALAGELPLLSGE--RQSQ-----------FShiTRLSFEQL-QKLVSDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALNkyenlqaklaTHL------DNKNLHKEINNLinfiESKDawniEQKKERFLKEFKLFEYKNRPISSLSGGEIRKI 168
Cdd:PRK10938 83 WQRNN----------TDMlspgedDTGRTTAEIIQD----EVKD----PARCEQLAQQFGITALLDRRFKYLSTGETRKT 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKnSKICVIFIShDRY-----FIDNVA--SRCVEIEGGkisff 237
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVAsrqqLAELLASLHQ-SGITLVLVL-NRFdeipdFVQFAGvlADCTLAETG----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 238 nggyayyleKKAQILVslsksyETLIKHLKAEEewlrrgvkarlkRNEGrkerifkmreeakknpgeikrlkLELLRANS 317
Cdd:PRK10938 218 ---------EREEILQ------QALVAQLAHSE------------QLEG-----------------------VQLPEPDE 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 318 SIQKPNFNKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKIL-----------LNL--DKLSS 384
Cdd:PRK10938 248 PSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLfgRRRGS 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 385 GE-IknADIK--IGYFDQAramLNSDKslielfcpnggdRVQVRGHDMHIYGYLKSFlfpkeFLSQAVS----------- 450
Cdd:PRK10938 328 GEtI--WDIKkhIGYVSSS---LHLDY------------RVSTSVRNVILSGFFDSI-----GIYQAVSdrqqklaqqwl 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 451 ---------------VLSGGEKNRVALALLFTKDYDVLILDEPTNDLDiaTIN------ILEEYLMEFKGALIFVSH 506
Cdd:PRK10938 386 dilgidkrtadapfhSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD--PLNrqlvrrFVDVLISEGETQLLFVSH 460
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-215 |
8.56e-13 |
|
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: 67.98 E-value: 8.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQL-----DSGRI------IRQND------- 65
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVlldgkdIYDLDvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 66 KSIAMLAQQVD-FNTNLsldelinknlseiyealnkYENLQAKLATHldnknlhkeinnlinfiESKDAWNIEQKKERFL 144
Cdd:cd03260 81 RRVGMVFQKPNpFPGSI-------------------YDNVAYGLRLH-----------------GIKLKEELDERVEEAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 145 KEFKLFEY-KNRPI-SSLSGGEIRKinLCI---LVLQnPDVLLLDEPTNHLDVYMCEFLEKLLK--NSKICVIFISHD 215
Cdd:cd03260 125 RKAALWDEvKDRLHaLGLSGGQQQR--LCLaraLANE-PEVLLLDEPTSALDPISTAKIEELIAelKKEYTIVIVTHN 199
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
341-523 |
8.60e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.79 E-value: 8.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGeiknadiKIGYFDQARAMLNSDKSlielFCPNGGD 420
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG-------RIGMPEGEDLLFLPQRP----YLPLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 RVQVrghdmhIYGYLKsflfpkeflsqavsVLSGGEKNRVALA-LLFTKDyDVLILDEPTNDLDIAT----INILEEYLM 495
Cdd:cd03223 81 REQL------IYPWDD--------------VLSGGEQQRLAFArLLLHKP-KFVFLDEATSALDEESedrlYQLLKELGI 139
|
170 180
....*....|....*....|....*...
gi 1751968159 496 efkgALIFVSHdRYFVDKLATKLYVFEN 523
Cdd:cd03223 140 ----TVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
347-526 |
8.67e-13 |
|
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: 68.51 E-value: 8.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-----------KIGYFDQARAMLNSDKSLIELFC 415
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvpwkrrkkflrRIGVVFGQKTQLWWDLPVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 416 PNGgdrvqvrghdmHIYGyLKSFLFPK------------EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:cd03267 118 LLA-----------AIYD-LPPARFKKrldelselldleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1751968159 484 IATI----NILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03267 186 VVAQenirNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
332-524 |
1.07e-12 |
|
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: 67.60 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGeKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-----------KIGYFDQ- 399
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQdvlkqpqklrrRIGYLPQe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 400 --------ARAMLNSDKSLIElfCPNGGDRVQVRG--HDMHIYgylksflfpkEFLSQAVSVLSGGEKNRVALALLFTKD 469
Cdd:cd03264 81 fgvypnftVREFLDYIAWLKG--IPSKEVKARVDEvlELVNLG----------DRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 470 YDVLILDEPTNDLDIATINILEEYLMEF-KGALIFVS-HDRYFVDKLATKLYVFENG 524
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELgEDRIVILStHIVEDVESLCNQVAVLNKG 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-234 |
1.49e-12 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 67.05 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKII-LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-------RQNDKSIAMLAQQ- 74
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsDLRGRAIPYLRRKi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 -VDFNTNLSLDELinknlseiyealNKYENLQakLATHLDNKNlHKEInnlinfieskdawnieQKKERFLKEFKLFEYK 153
Cdd:cd03292 81 gVVFQDFRLLPDR------------NVYENVA--FALEVTGVP-PREI----------------RKRVPAALELVGLSHK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISS-LSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV-YMCEFLEKLLKNSK--ICVIFISHDRYFIDNVASRCVEI 229
Cdd:cd03292 130 HRALPAeLSGGEQQRVAIARAIVNSPTILIADEPTGNLDPdTTWEIMNLLKKINKagTTVVVATHAKELVDTTRHRVIAL 209
|
....*
gi 1751968159 230 EGGKI 234
Cdd:cd03292 210 ERGKL 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
325-508 |
1.61e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.43 E-value: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 325 NKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIKIGYFDQARA 402
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 MLNSDKSLIELFcpngGDRV--------QVRGH--DM-HIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALA--LLFTKd 469
Cdd:PRK10247 82 QVSYCAQTPTLF----GDTVydnlifpwQIRNQqpDPaIFLDDLERFALPDTILTKNIAELSGGEKQRISLIrnLQFMP- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1751968159 470 yDVLILDEPTNDLDIAT---IN-ILEEYLMEFKGALIFVSHDR 508
Cdd:PRK10247 157 -KVLLLDEITSALDESNkhnVNeIIHRYVREQNIAVLWVTHDK 198
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-215 |
1.97e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLS 82
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDElinKNLSEIYEALNKYENLQAklathldnknlhkeinnlinfieskdawnieqkkerfLKEFKLFEYKNRPISSLSG 162
Cdd:PRK09544 84 LTV---NRFLRLRPGTKKEDILPA-------------------------------------LKRVQAGHLIDAPMQKLSG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK09544 124 GETQRVLLARALLNRPQLLVLDEPTQGVDVngqvALYDLIDQLRRELDCAVLMVSHD 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
355-484 |
2.04e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 355 QGEKIGIVGQNGCGKSTFLKIL-----LNL-------------------------DKLSSGEIKNAdIKIGYFDQARAML 404
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgeliPNLgdyeeepswdevlkrfrgtelqnyfKKLYNGEIKVV-HKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 nsDKSLIELFcpnggDRVQVRGhdmhIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI 484
Cdd:PRK13409 177 --KGKVRELL-----KKVDERG----KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-234 |
2.07e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 67.35 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKaifgTLQL----DSGRIirqndkSIAmlAQQVDFNT 79
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR----VLNLletpDSGQL------NIA--GHQFDFSQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLDE--LINKNLSEIYEalnkyenlQAKLATHLdnknlhkeiNNLINFIE--------SKDAWNIEQKKerFLKEFKL 149
Cdd:COG4161 71 KPSEKAirLLRQKVGMVFQ--------QYNLWPHL---------TVMENLIEapckvlglSKEQAREKAMK--LLARLRL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRC 226
Cdd:COG4161 132 TDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIireLSQTGITQVIVTHEVEFARKVASQV 211
|
....*...
gi 1751968159 227 VEIEGGKI 234
Cdd:COG4161 212 VYMEKGRI 219
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
329-507 |
2.10e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.49 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILlnldklsSGEIKNADIKIGYFDQA-------- 400
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-------SGELSPDSGEVRLNGRPladwspae 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 401 ----RAMLNSDKSL---------IEL-FCPNGGDRVQVRG---HDMHIYGYLksflfpkEFLSQAVSVLSGGEKNRVALA 463
Cdd:PRK13548 74 larrRAVLPQHSSLsfpftveevVAMgRAPHGLSRAEDDAlvaAALAQVDLA-------HLAGRDYPQLSGGEQQRVQLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 464 LLFT------KDYDVLILDEPTNDLDIA----TINILEEYLMEFKGALIFVSHD 507
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLAhqhhVLRLARQLAHERGLAVIVVLHD 200
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-233 |
2.44e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI----------IRQNDKSIAMLAQ 73
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvparARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 qvdFNtNLSLDELINKNLSeiyeALNKYENLQAklathldnknlhKEINNLINfieskdawnieqkkerFLKEFKLFEYK 153
Cdd:PRK13536 122 ---FD-NLDLEFTVRENLL----VFGRYFGMST------------REIEAVIP----------------SLLEFARLESK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 -NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKIcVIFISHDRYFIDNVASRCVE 228
Cdd:PRK13536 166 aDARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHarhlIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCV 244
|
....*
gi 1751968159 229 IEGGK 233
Cdd:PRK13536 245 LEAGR 249
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
349-526 |
2.54e-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: 66.36 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 349 FSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAR---AMLNSDKSL---------IEL--- 413
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrpvSMLFQENNLfahltveqnVGLgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 ----FCPNGGDRVQVRGHDMHIYGYLKSFlfPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI 489
Cdd:cd03298 97 pglkLTAEDRQAIEVALARVGLAGLEKRL--PGE--------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1751968159 490 LEEYLMEF----KGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03298 167 MLDLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
2.68e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 67.52 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKF-GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiamlaqqvdfnt 79
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRG--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 nlslDELINKNLSEIyealNKYENLqakLATHLDNKNLHKEINNLINFIESK---DAWNIEQKKERFLKEFKLFEYKNRP 156
Cdd:PRK13652 66 ----EPITKENIREV----RKFVGL---VFQNPDDQIFSPTVEQDIAFGPINlglDEETVAHRVSSALHMLGLEELRDRV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGG 232
Cdd:PRK13652 135 PHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQgvkeLIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
..
gi 1751968159 233 KI 234
Cdd:PRK13652 215 RI 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
346-524 |
2.68e-12 |
|
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: 66.69 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----KNADI----------------KIGYFDQ-ARAM- 403
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhDGGWVdlaqaspreilalrrrTIGYVSQfLRVIp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 ----LnsD---KSLIELfcpnGGDR--VQVRGHDMhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLI 474
Cdd:COG4778 107 rvsaL--DvvaEPLLER----GVDReeARARAREL-----LARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 475 LDEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:COG4778 176 LDEPTASLDAANRAVVVELIEEAKArgtAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-215 |
2.84e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQNDKSIAMLAQQVDFNT 79
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLDElinknlSEIYEALNKYENLQAKLathldnknlhkeinnlinfiESKDAWNIEQKKER---FLKEFKLFEYKNRP 156
Cdd:PRK10895 81 GYLPQE------ASIFRRLSVYDNLMAVL--------------------QIRDDLSAEQREDRaneLMEEFHIEHLRDSM 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHD 215
Cdd:PRK10895 135 GQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIiehLRDSGLGVLITDHN 196
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-515 |
3.53e-12 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.43 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 355 QGEKIGIVGQNGCGKSTFLKILL-----NL-------------------------DKLSSGEIKNAdIKIGYFDQARAML 404
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSgelkpNLgdydeepswdevlkrfrgtelqdyfKKLANGEIKVA-HKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSD-KSLIElfcpnggdRVQVRGhdmhIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:COG1245 177 KGTvRELLE--------KVDERG----KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|....*.
gi 1751968159 484 I----ATINILEEYLMEFKgALIFVSHDRYFVDKLA 515
Cdd:COG1245 245 IyqrlNVARLIRELAEEGK-YVLVVEHDLAILDYLA 279
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
349-507 |
3.88e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.79 E-value: 3.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 349 FSTRILQGEKIGIVGQNGCGKSTFLKILLNLdKLSSGEIKNADIKIGYFDQA-----RAMLNSDKS---------LIELF 414
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhRAYLSQQQSppfampvfqYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNGGDRVQVRGHDMHIYGYLKsfLFPKefLSQAVSVLSGGEKNRVALALLF-----TKDYD--VLILDEPTNDLDIATI 487
Cdd:COG4138 94 QPAGASSEAVEQLLAQLAEALG--LEDK--LSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|...
gi 1751968159 488 NILEEYLMEFK---GALIFVSHD 507
Cdd:COG4138 170 AALDRLLRELCqqgITVVMSSHD 192
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
345-522 |
4.13e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLN--LDKLSSGEIKNADIKIGyfdqaramlnSDKSLIELFCPNG--GD 420
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG----------REASLIDAIGRKGdfKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 RVQVrghdMHIYGYLKSFLFPKEFlsqavSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI----LEEYLME 496
Cdd:COG2401 115 AVEL----LNAVGLSDAVLWLRRF-----KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARR 185
|
170 180
....*....|....*....|....*.
gi 1751968159 497 FKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:COG2401 186 AGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-234 |
4.50e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.80 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRiIRQNDKSIAMLA---QQVDFntn 80
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH-IRFHGTDVSRLHardRKVGF--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 lsldelINKNLSeIYEALNKYENLQAKLaTHLDNKnlhkeinnlinfiESKDAWNIEQKKERFLKEFKLFEYKNRPISSL 160
Cdd:PRK10851 79 ------VFQHYA-LFRHMTVFDNIAFGL-TVLPRR-------------ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 161 SGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK10851 138 SGGQKQRVALARALAVEPQILLLDEPFGALDAQvrkeLRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
318-525 |
4.55e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.93 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 318 SIQKPNFNKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI---------- 387
Cdd:PRK13536 29 AKASIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItvlgvpvpar 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 388 -KNADIKIGY---FDQARAMLNSDKSLIelfcpnggdrVQVRGHDMH---IYGYLKSFLFPKEFLSQA---VSVLSGGEK 457
Cdd:PRK13536 109 aRLARARIGVvpqFDNLDLEFTVRENLL----------VFGRYFGMStreIEAVIPSLLEFARLESKAdarVSDLSGGMK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEF--KG-ALIFVSHDRYFVDKLATKLYVFENGV 525
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGkTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-215 |
4.71e-12 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.93 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI---------IRQNDKS--IAMLAQQVD-FNTNL 81
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssLDQDEVRrrVSVCAQDAHlFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELI-NKNLS--EIYEALNkyenlQAKLATHLDnknlhkEINNLINFIESKDAwnieqkkerflkefklfeyknrpiS 158
Cdd:TIGR02868 426 RENLRLaRPDATdeELWAALE-----RVGLADWLR------ALPDGLDTVLGEGG------------------------A 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMC-EFLEKLLK-NSKICVIFISHD 215
Cdd:TIGR02868 471 RLSGGERQRLALARALLADAPILLLDEPTEHLDAETAdELLEDLLAaLSGRTVVLITHH 529
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
7-237 |
5.19e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 65.26 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 7 IKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIfgtlqldSGRIIRQNDKSiamlaqqvdfntnlsldel 86
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGRRTGLGVSG------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 inknlsEIYealnkyenlqaklathLDNKNLHK-EINNLINFIESKDAwnieqkkerFLKEFKLFE--YKNRPISSLSGG 163
Cdd:cd03213 67 ------EVL----------------INGRPLDKrSFRKIIGYVPQDDI---------LHPTLTVREtlMFAAKLRGLSGG 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHD-RYFIDNVASRCVEIEGGKISFF 237
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRrlaDTGRTIICSIHQpSSEIFELFDKLLLLSQGRVIYF 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-235 |
5.67e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.75 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII----RQND-----KSIAML 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFigekRMNDvppaeRGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 72 AQQVdfntnlsldelinknlsEIYEALNKYENLQ--AKLAthldnknlhkeinnlinfieSKDAWNIEQKKERFLKEFKL 149
Cdd:PRK11000 81 FQSY-----------------ALYPHLSVAENMSfgLKLA--------------------GAKKEEINQRVNQVAEVLQL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRYFIDNVASR 225
Cdd:PRK11000 124 AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADK 203
|
250
....*....|
gi 1751968159 226 CVEIEGGKIS 235
Cdd:PRK11000 204 IVVLDAGRVA 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
329-526 |
6.03e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 66.31 E-value: 6.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIgyfDQARAmLNSDK 408
Cdd:PRK11264 3 AI-EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTARS-LSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLIElfcpnggdrvQVRGHDMHIYgylKSF-LFP----------------KEFLSQAVSV-------------------- 451
Cdd:PRK11264 78 GLIR----------QLRQHVGFVF---QNFnLFPhrtvleniiegpvivkGEPKEEATARarellakvglagketsyprr 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 452 LSGGEKNRVALALLFTKDYDVLILDEPTNDLD-------IATINILEEYlmefKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQE----KRTMVIVTHEMSFARDVADRAIFMDQG 220
|
..
gi 1751968159 525 VI 526
Cdd:PRK11264 221 RI 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-526 |
6.28e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 21 EINFSANENEKIAIIGKNGEGKST-------LLKAIFGTLQLDSGRIIRQNDKSIAMLAQqvdfnTNLSLDELINKNLSE 93
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSEQ-----SAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 IYE----ALNKYENLQAKLATHLdnkNLHKEINNLINFIESKdawnieqkkeRFLKEFKLFEYK---NRPISSLSGGEIR 166
Cdd:PRK10261 109 IFQepmtSLNPVFTVGEQIAESI---RLHQGASREEAMVEAK----------RMLDQVRIPEAQtilSRYPHQLSGGMRQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCV------EIEGGKIS- 235
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLvmyqgeAVETGSVEq 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 236 -FFNGGYAYylekkaqilvslSKSYETLIKHLKAEE--EWLRRGVKARLKRNEGRKERIfkmrEEAKKNPGEiKRLKLEL 312
Cdd:PRK10261 256 iFHAPQHPY------------TRALLAAVPQLGAMKglDYPRRFPLISLEHPAKQEPPI----EQDTVVDGE-PILQVRN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 313 LRANSSIQKPNFNKQKMIFELVnaskiinnkilfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNL------------- 379
Cdd:PRK10261 319 LVTRFPLRSGLLNRVTREVHAV------------EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLvesqggeiifngq 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 380 --DKLSSGEIKNADIKIGY-FDQARAMLNSDK----SLIELFCPNG---GDRVQVRGHDMHIYGYLK---SFLFPKEFls 446
Cdd:PRK10261 387 riDTLSPGKLQALRRDIQFiFQDPYASLDPRQtvgdSIMEPLRVHGllpGKAAAARVAWLLERVGLLpehAWRYPHEF-- 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 447 qavsvlSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:PRK10261 465 ------SGGQRQRICIARALALNPKVIIADEAVSALDVSIrgqiINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY 538
|
....
gi 1751968159 523 NGVI 526
Cdd:PRK10261 539 LGQI 542
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
18-234 |
6.51e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 68.31 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIA------------MLAQQVD-FNTNLSlD 84
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEI-LLNGQPIAdyseaalrqaisVVSQRVHlFSATLR-D 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 ELI----NKNLSEIYEALNKYEnlqakLATHLDNKnlhkeinnlinfiESKDAWnieqkkerfLKEfklfeyKNRPissL 160
Cdd:PRK11160 433 NLLlaapNASDEALIEVLQQVG-----LEKLLEDD-------------KGLNAW---------LGE------GGRQ---L 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 161 SGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKicVIFISHDRYFIDNVASRCVeIEGGKI 234
Cdd:PRK11160 477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeterQILELLAEHAQNKT--VLMITHRLTGLEQFDRICV-MDNGQI 551
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
344-529 |
6.62e-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: 65.53 E-value: 6.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 344 ILFK-NFSTRilQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIK-----------IGYFDQARamlnsdks 409
Cdd:cd03224 15 ILFGvSLTVP--EGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIrfDGRDITglppheraragIGYVPEGR-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 liELFcPN----------GGDRVQVRGHDM--HIYGylksfLFP--KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLIL 475
Cdd:cd03224 85 --RIF-PEltveenlllgAYARRRAKRKARleRVYE-----LFPrlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 476 DEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVINIE 529
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDegvTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-215 |
7.34e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.72 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 22 INFSANENEKIAIIGKNGEGKSTLLKAIFGTLQlDSGRIiRQNDKSI------------AMLAQQVDFNTNLSLdelink 89
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSI-QFAGQPLeawsaaelarhrAYLSQQQTPPFAMPV------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 nlseiyealnkYENLQAKLATHLDNKNLHKEINNLINFIESKDawnieqkkerflkefKLfeykNRPISSLSGGEIRKIN 169
Cdd:PRK03695 87 -----------FQYLTLHQPDKTRTEAVASALNEVAEALGLDD---------------KL----GRSVNQLSGGEWQRVR 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 170 LCILVLQ-----NPD--VLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHD 215
Cdd:PRK03695 137 LAAVVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSelcQQGIAVVMSSHD 192
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
353-507 |
7.56e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 353 ILQG--------EKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQ-ARAMLNSD------KSLIELFCPN 417
Cdd:PRK10584 25 ILTGvelvvkrgETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEeARAKLRAKhvgfvfQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 418 GGDRVQV----RGHDMHiygylKSFLFPKEFLSQ---------AVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI 484
Cdd:PRK10584 105 ALENVELpallRGESSR-----QSRNGAKALLEQlglgkrldhLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
|
170 180
....*....|....*....|....*..
gi 1751968159 485 ATINILEEYLM----EFKGALIFVSHD 507
Cdd:PRK10584 180 QTGDKIADLLFslnrEHGTTLILVTHD 206
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
343-524 |
9.82e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 64.49 E-value: 9.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNldKLSSGEIKnADIKIGYFDQaraMLNSDKSLIELfcpnggdrv 422
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAG--RRTGLGVS-GEVLINGRPL---DKRSFRKIIGY--------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 423 qVRGHDMHIygylkSFLFPKEFLSQAV--SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEF-KG 499
Cdd:cd03213 87 -VPQDDILH-----PTLTVRETLMFAAklRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDT 160
|
170 180
....*....|....*....|....*...
gi 1751968159 500 A--LIFVSHD-RYFVDKLATKLYVFENG 524
Cdd:cd03213 161 GrtIICSIHQpSSEIFELFDKLLLLSQG 188
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
350-547 |
1.32e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 66.27 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 350 STRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-----------------KNADIKIgYFDQARAMLNSDKSL-- 410
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllgmkddewraVRSDIQM-IFQDPLASLNPRMTIge 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 -----IELFCPNGG-----DRVQVRghdMHIYGYLKSFL--FPKEFlsqavsvlSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:PRK15079 120 iiaepLRTYHPKLSrqevkDRVKAM---MLKVGLLPNLInrYPHEF--------SGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 479 TNDLDIA----TINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFengviniehmsytqYLEREFELREFD 547
Cdd:PRK15079 189 VSALDVSiqaqVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM--------------YLGHAVELGTYD 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-227 |
1.38e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.05 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAmlAQQVDFNTNLsldeLINKNLSE 93
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-LWQGEPIR--RQRDEYHQDL----LYLGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 IYEALNKYENLQAKLAthldnknLHKEINNlinfiesKDAWNIeqkkerfLKEFKLFEYKNRPISSLSGGEIRKINLCIL 173
Cdd:PRK13538 85 IKTELTALENLRFYQR-------LHGPGDD-------EALWEA-------LAQVGLAGFEDVPVRQLSAGQQRRVALARL 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 174 VLQNPDVLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHDRYFIDNVASRCV 227
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQGVARLEALLAqhaEQGGMVILTTHQDLPVASDKVRKL 200
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
348-526 |
1.42e-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: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI---------------KIG--------------YFD 398
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsdlrgraipylrrKIGvvfqdfrllpdrnvYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 QARAMLNSDKS--LIELFCPNGGDRVQVRGhdmhiygylKSFLFPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILD 476
Cdd:cd03292 99 VAFALEVTGVPprEIRKRVPAALELVGLSH---------KHRALPAE--------LSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 477 EPTNDLDIATINILEEYLMEF--KGALIFVS-HDRYFVDKLATKLYVFENGVI 526
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKInkAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-231 |
1.57e-11 |
|
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: 67.12 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEkiildeinFS-------ANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirQNDKSIAMLAQQV 75
Cdd:COG1245 341 LVEYPDLTKSYGG--------FSleveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 DFNTNLSLDELINKNLSEIYEalNKYenLQAKLATHLdnkNLHKeinnlinfieskdawnieqkkerflkefkLFEyknR 155
Cdd:COG1245 411 SPDYDGTVEEFLRSANTDDFG--SSY--YKTEIIKPL---GLEK-----------------------------LLD---K 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 156 PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEG 231
Cdd:COG1245 452 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
329-564 |
1.60e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 66.26 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNA----------DIKIGYFD 398
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlharDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 QA----RAMLNSDKSLIELFC------PNGG--DRVQVRGHDMHIYGYLKSflfpkEFLSQavsvLSGGEKNRVALALLF 466
Cdd:PRK10851 81 QHyalfRHMTVFDNIAFGLTVlprrerPNAAaiKAKVTQLLEMVQLAHLAD-----RYPAQ----LSGGQKQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 467 TKDYDVLILDEPTNDLDIATINILEEYLM----EFKGALIFVSHDRYFVDKLATKLYVFENGviNIEHMSYTQYLEREFE 542
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRqlheELKFTSVFVTHDQEEAMEVADRVVVMSQG--NIEQAGTPDQVWREPA 229
|
250 260
....*....|....*....|....*.
gi 1751968159 543 LRefddFVLNLEKE----KGAIKEKQ 564
Cdd:PRK10851 230 TR----FVLEFMGEvnrlQGTIRGGQ 251
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-232 |
1.61e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.14 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 16 KIILDEINFSANENEKIAIIGKNGEGKSTLLKAI-----FGtlqldSGRIIRQNDKSIAMLAQQVDF------------N 78
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpYG-----SGRIARPAGARVLFLPQRPYLplgtlreallypA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 TNLSLDElinknlSEIYEALNKYeNLQAkLATHLDNknlhkeinnlinfiesKDAWNIEqkkerflkefklfeyknrpis 158
Cdd:COG4178 451 TAEAFSD------AELREALEAV-GLGH-LAERLDE----------------EADWDQV--------------------- 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 159 sLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNS--KICVIFISHdRYFIDNVASRCVEIEGG 232
Cdd:COG4178 486 -LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREElpGTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-231 |
1.61e-11 |
|
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: 62.94 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 16 KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFnTNLSLDELInknlseIY 95
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYL-PLGTLREQL------IY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 96 ealnkyenlqaklathldnknlhkeinnlinfieskdAWNIEqkkerflkefklfeyknrpissLSGGEIRKINLCILVL 175
Cdd:cd03223 87 -------------------------------------PWDDV----------------------LSGGEQQRLAFARLLL 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 176 QNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKICVIFISHdRYFIDNVASRCVEIEG 231
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDG 162
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
343-526 |
2.15e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.71 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFD--QARAM--------------LNS 406
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraQRKAFrrdiqmvfqdsisaVNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 407 DKS--------LIELFCPNGGDRvQVRGHDMhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:PRK10419 105 RKTvreiirepLRHLLSLDKAER-LARASEM-----LRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 479 TNDLDI----ATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK10419 179 VSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
347-526 |
2.21e-11 |
|
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: 63.93 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADI---------KIGYFDQaraMLNSDKSLielfc 415
Cdd:cd03265 17 RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatVAGHDVvreprevrrRIGIVFQ---DLSVDDEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 416 pNGGDRVQVRGhdmHIYGY-----------LKSFLFPKEFLSQAVSVLSGGEKNR--VALALLFTKdyDVLILDEPTNDL 482
Cdd:cd03265 89 -TGWENLYIHA---RLYGVpgaerrerideLLDFVGLLEAADRLVKTYSGGMRRRleIARSLVHRP--EVLFLDEPTIGL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1751968159 483 DIATINILEEYLMEFK---GALIFV-SHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03265 163 DPQTRAHVWEYIEKLKeefGMTILLtTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
349-507 |
2.23e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.57 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 349 FSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKlSSGEIKNADIKIGYFDQA-----RAMLNSDKS---------LIELF 414
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAelarhRAYLSQQQTppfampvfqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNGGDRVQVRghdmHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTK-------DYDVLILDEPTNDLDIATI 487
Cdd:PRK03695 94 QPDKTRTEAVA----SALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|...
gi 1751968159 488 NILEEYLMEFKGALIFV---SHD 507
Cdd:PRK03695 170 AALDRLLSELCQQGIAVvmsSHD 192
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-214 |
2.68e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI--------IRQ----NDKSIAM 70
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrIRSprdaIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 71 LAQqvDFNtnlsldeLInknlseiyEALNKYENL----QAKLATHLDNKNLHKEInnlinfieskdawnieqkkERFLKE 146
Cdd:COG3845 85 VHQ--HFM-------LV--------PNLTVAENIvlglEPTKGGRLDRKAARARI-------------------RELSER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 147 FKLFEYKNRPISSLSGG-----EIRKinlciLVLQNPDVLLLDEPTNHL-----DvymcEFLE--KLLKNSKICVIFISH 214
Cdd:COG3845 129 YGLDVDPDAKVEDLSVGeqqrvEILK-----ALYRGARILILDEPTAVLtpqeaD----ELFEilRRLAAEGKSIIFITH 199
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-191 |
2.86e-11 |
|
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: 63.83 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 8 KASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLD---SGRI--------IRQNDKSIAMLAQQVD 76
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkPDQFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 77 FNTNLSldelinknlseIYEALNKYENLqaKLATHLDNKNLHKEINNLInfieskdawnieqkkerfLKEFKLFEYKNRP 156
Cdd:cd03234 92 LLPGLT-----------VRETLTYTAIL--RLPRKSSDAIRKKRVEDVL------------------LRDLALTRIGGNL 140
|
170 180 190
....*....|....*....|....*....|....*
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:cd03234 141 VKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-215 |
2.93e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 64.34 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQ-VDFNTnl 81
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgVVFQN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 sldelinknlseiyEALNKYENLQAKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKNRPISSLS 161
Cdd:PRK11248 79 --------------EGLLPWRNVQDNVAFGLQLAGVEKM--------------QRLEIAHQMLKKVGLEGAEKRYIWQLS 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK11248 131 GGQRQRVGIARALAANPQLLLLDEPFGALDAFtreqMQTLLLKLWQETGKQVLLITHD 188
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
356-523 |
3.35e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 356 GEKIGIVGQNGCGKSTFLKIL--------------LNLDKLSSGE-------IKNADIKIGYFDQARAMLNSDKSLIELF 414
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMamhaidgipkncqiLHVEQEVVGDdttalqcVLNTDIERTQLLEEEAQLVAQQRELEFE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNGGDRVQVRGHD---------MHIYGYLK------------SFL----FPKEFLSQAVSVLSGGEKNRVALALLFTKD 469
Cdd:PLN03073 283 TETGKGKGANKDGVdkdavsqrlEEIYKRLElidaytaearaaSILaglsFTPEMQVKATKTFSGGWRMRIALARALFIE 362
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 470 YDVLILDEPTNDLDIATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFEN 523
Cdd:PLN03073 363 PDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHG 416
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
341-526 |
3.65e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.96 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGY-------FD--- 398
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILidGVDIRdltleslrrqIGVvpqdtflFSgti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 ---------------------QARAMlnsdkSLIELFcPNGGD-RVQVRGHDmhiygylksflfpkeflsqavsvLSGGE 456
Cdd:COG1132 431 renirygrpdatdeeveeaakAAQAH-----EFIEAL-PDGYDtVVGERGVN-----------------------LSGGQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 457 KNRVALA--LLftKDYDVLILDEPTNDLDIAT-INILE--EYLMefKGA-LIFVSHdryfvdKLAT-----KLYVFENGV 525
Cdd:COG1132 482 RQRIAIAraLL--KDPPILILDEATSALDTETeALIQEalERLM--KGRtTIVIAH------RLSTirnadRILVLDDGR 551
|
.
gi 1751968159 526 I 526
Cdd:COG1132 552 I 552
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
3.86e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.94 E-value: 3.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKSIAMLAQQVDFNTNLSLDELINKNLS 92
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVlikgepIKYDKKSLLEVRKTVGIVFQNPDDQLFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EiyealnkyenlqaKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCI 172
Cdd:PRK13639 98 E-------------DVAFGPLNLGLSKE--------------EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 173 LVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSKICVIFIS-HDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
329-496 |
3.94e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAM----- 403
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAChylgh 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 ---LNSDKSLIE--LFCPN--GGDRVQVR--------GHDMHI-YGYlksflfpkeflsqavsvLSGGEKNRVALALLFT 467
Cdd:PRK13539 81 rnaMKPALTVAEnlEFWAAflGGEELDIAaaleavglAPLAHLpFGY-----------------LSAGQKRRVALARLLV 143
|
170 180
....*....|....*....|....*....
gi 1751968159 468 KDYDVLILDEPTNDLDIATINILEEyLME 496
Cdd:PRK13539 144 SNRPIWILDEPTAALDAAAVALFAE-LIR 171
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-234 |
3.97e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.83 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIfGTLQLDSGRIIRQNDKSIAMLAqqvDFNTNLSLDELinkn 90
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQTINLVR---DKDGQLKVADK---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 91 lseiyealNKYENLQAKLATHLDNKNLHKEINNLINFIESK------DAWNIEQKKERFLKEFKLFEY-KNRPISSLSGG 163
Cdd:PRK10619 85 --------NQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiqvlglSKQEARERAVKYLAKVGIDERaQGKYPVHLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMC----EFLEKLLKNSKICVIfISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVgevlRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKI 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
332-578 |
4.13e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.59 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKL--SSGEI---------------------- 387
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIiyhvalcekcgyverpskvgep 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 388 ------KNADIKIGYFDQARAMLNSDKSLIEL-----FCPNGGDRVQVRG-HDMHIYGYLKsflfpKEFLSQAVSV---- 451
Cdd:TIGR03269 82 cpvcggTLEPEEVDFWNLSDKLRRRIRKRIAImlqrtFALYGDDTVLDNVlEALEEIGYEG-----KEAVGRAVDLiemv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 452 ------------LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINI----LEEYLMEFKGALIFVSHDRYFVDKLA 515
Cdd:TIGR03269 157 qlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 516 TKLYVFENGVINIE---------HMSYTQYLEREFELREFDDF--VLNLEK-----EKGAIKEKQNKKLSYKQNEILNL 578
Cdd:TIGR03269 237 DKAIWLENGEIKEEgtpdevvavFMEGVSEVEKECEVEVGEPIikVRNVSKryisvDRGVVKAVDNVSLEVKEGEIFGI 315
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
331-496 |
4.20e-11 |
|
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: 63.36 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINN-KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFD-----QAR--- 401
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkalrQLRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AMLNSDKSLIElfcpnggdRVQVRGHDMHiyGYL--KSF------LFPKE----------------FLSQAVSVLSGGEK 457
Cdd:cd03256 81 GMIFQQFNLIE--------RLSVLENVLS--GRLgrRSTwrslfgLFPKEekqralaalervglldKAYQRADQLSGGQQ 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLME 496
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKR 189
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
33-215 |
4.26e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 62.25 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 33 AIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQ--VDFNTNLSLDELInknlseiyeALNKYENLQA-KLA 109
Cdd:NF040873 22 AVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRseVPDSLPLTVRDLV---------AMGRWARRGLwRRL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 110 THLDnknlHKEInnlinfieskdawnieqkkERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNH 189
Cdd:NF040873 93 TRDD----RAAV-------------------DDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180
....*....|....*....|....*....
gi 1751968159 190 LDVYMCEFLEKLLK---NSKICVIFISHD 215
Cdd:NF040873 150 LDAESRERIIALLAeehARGATVVVVTHD 178
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
11-215 |
4.43e-11 |
|
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: 63.82 E-value: 4.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQvdfntnlsLDELINKN 90
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE--------LRELRRKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 91 LSEIYEALNKYENLqaklaTHLDNKNLHKEINNLinfieskDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINL 170
Cdd:cd03294 104 ISMVFQSFALLPHR-----TVLENVAFGLEVQGV-------PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 171 CILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD 215
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLirreMQDELLRLQAELQKTIVFITHD 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-214 |
4.50e-11 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 65.57 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI---------IRQND--KSIAMLAQQVD-FNT-- 79
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIlidgvdirdLTLESlrRQIGVVPQDTFlFSGti 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 --NLSL------DElinknlsEIYEAlnkyenlqAKLAthldnkNLHKEINNLINFIESkdawnieqkkerflkefklfe 151
Cdd:COG1132 431 reNIRYgrpdatDE-------EVEEA--------AKAA------QAHEFIEALPDGYDT--------------------- 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 152 yknrPI----SSLSGGEIRKInlCI--LVLQNPDVLLLDEPTNHLDVYMcEF-----LEKLLKNsKIcVIFISH 214
Cdd:COG1132 469 ----VVgergVNLSGGQRQRI--AIarALLKDPPILILDEATSALDTET-EAliqeaLERLMKG-RT-TIVIAH 533
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-479 |
4.98e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.42 E-value: 4.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiamlaQQVDFNTN 80
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG--------EPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LsldELINKNLSEIYEALNkyenlqakLATHL---DNKNLHKEINN--LINfieskdaWN-IEQKKERFLKEFKLFEYKN 154
Cdd:COG1129 74 R---DAQAAGIAIIHQELN--------LVPNLsvaENIFLGREPRRggLID-------WRaMRRRARELLARLGLDIDPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 155 RPISSLSGG-----EIRKInlcilVLQNPDVLLLDEPT---NHLDVymceflEKL------LKNSKICVIFISHdryFID 220
Cdd:COG1129 136 TPVGDLSVAqqqlvEIARA-----LSRDARVLILDEPTaslTEREV------ERLfriirrLKAQGVAIIYISH---RLD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 221 ---NVASRCVEIEGGKisffnggyayylekkaqilvslsksyetLIKHLKAEE---EWLrrgVKARLkrneGRK-ERIFK 293
Cdd:COG1129 202 evfEIADRVTVLRDGR----------------------------LVGTGPVAElteDEL---VRLMV----GRElEDLFP 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 294 MREEAkknPGEIkRLKLEllranssiqkpNFNKQKMifelvnaskiinnkilFKNFSTRILQGEKIGIVGQNGCGKSTFL 373
Cdd:COG1129 247 KRAAA---PGEV-VLEVE-----------GLSVGGV----------------VRDVSFSVRAGEILGIAGLVGAGRTELA 295
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 374 KILLNLDKLSSGEI----KNADIK---------IGYF--DQARAMLNSDKSL--------IELFCPNG------------ 418
Cdd:COG1129 296 RALFGADPADSGEIrldgKPVRIRsprdairagIAYVpeDRKGEGLVLDLSIrenitlasLDRLSRGGlldrrreralae 375
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 419 --GDRVQVRGHDMHiygylksflfpkeflsQAVSVLSGGEKNRVALA-LLFTkDYDVLILDEPT 479
Cdd:COG1129 376 eyIKRLRIKTPSPE----------------QPVGNLSGGNQQKVVLAkWLAT-DPKVLILDEPT 422
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
347-581 |
5.74e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGY-------------------FDQARAMLNSD 407
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyirpvrkrigmvfqFPESQLFEDTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 408 KSLIELFCPNGG---DRVQVRGHDMhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD- 483
Cdd:PRK13646 104 EREIIFGPKNFKmnlDEVKNYAHRL-----LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 484 ---IATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLEREFELREFDDFVLNLEKEKGAI 560
Cdd:PRK13646 179 qskRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI-VSQTSPKELFKDKKKLADWHIGLPEIVQLQYDF 257
|
250 260
....*....|....*....|....
gi 1751968159 561 KEKQN---KKLSYKQNEILNLYPE 581
Cdd:PRK13646 258 EQKYQtklKDIALTEEEFVSLYKE 281
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-226 |
5.82e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 63.71 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiamlaQQVDFNTNLSLDelINKNLSEIYEAL 98
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDG--------KPIDYSRKGLMK--LRESVGMVFQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 NKyenlqaklatHLDNKNLHKEIN-NLINFIESKDawNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQN 177
Cdd:PRK13636 92 DN----------QLFSASVYQDVSfGAVNLKLPED--EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 178 PDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfIDNVASRC 226
Cdd:PRK13636 160 PKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD---IDIVPLYC 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
347-540 |
8.78e-11 |
|
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: 62.25 E-value: 8.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDqaramLNSDKSLI-----ELFCPNGGDR 421
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-----LASLRRQIglvsqDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 422 VQVRghdmhiYG----------------YLKSFL--FPKEF---LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTN 480
Cdd:cd03251 94 ENIA------YGrpgatreeveeaaraaNAHEFImeLPEGYdtvIGERGVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 481 DLDIATINILE---EYLMEFKGALIfVSHdRYFVDKLATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:cd03251 168 ALDTESERLVQaalERLMKNRTTFV-IAH-RLSTIENADRIVVLEDGKI-VERGTHEELLAQG 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
330-485 |
8.82e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 8.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLK------------ILLNLDKLSSGEIKNADIKIGYF 397
Cdd:PRK10575 11 TFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKmlgrhqppsegeILLDAQPLESWSSKAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQ----ARAMLNSDKSLIELFCPNGG-------DRVQVrghDMHIygylkSFLFPKEFLSQAVSVLSGGEKNRVALALLF 466
Cdd:PRK10575 91 PQqlpaAEGMTVRELVAIGRYPWHGAlgrfgaaDREKV---EEAI-----SLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170
....*....|....*....
gi 1751968159 467 TKDYDVLILDEPTNDLDIA 485
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIA 181
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
333-511 |
8.90e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 333 LVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK-NADIKIGYFDQAramLNSDKSL- 410
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrNGKLRIGYVPQK---LYLDTTLp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 --IELFCpnggdRVQVRGHDMHIYGYLKSfLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI---- 484
Cdd:PRK09544 84 ltVNRFL-----RLRPGTKKEDILPALKR-VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVngqv 157
|
170 180
....*....|....*....|....*..
gi 1751968159 485 ATINILEEYLMEFKGALIFVSHDRYFV 511
Cdd:PRK09544 158 ALYDLIDQLRRELDCAVLMVSHDLHLV 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
15-236 |
9.33e-11 |
|
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: 61.18 E-value: 9.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIAMLaqqvdfntnlsldeliNKNLSEI 94
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEIT-LDGVPVSDL----------------EKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALNKyenlqaklATHLDNKNLHkeiNNLinfieskdawnieqkKERFlkefklfeyknrpisslSGGEIRKINLCILV 174
Cdd:cd03247 77 ISVLNQ--------RPYLFDTTLR---NNL---------------GRRF-----------------SGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 175 LQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcvIFISHDRYFIDNVASRCVeIEGGKISF 236
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKDKTL--IWITHHLTGIEHMDKILF-LENGKIIM 176
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-202 |
1.00e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDK--------SIAMLAQQVDFNTNLSLDE 85
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDiddpdvaeACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 86 -------LINKNLSEIYEALNKYeNLQAklATHLdnknlhkeinnlinfieskdawnieqkkerflkefklfeyknrPIS 158
Cdd:PRK13539 93 nlefwaaFLGGEELDIAAALEAV-GLAP--LAHL-------------------------------------------PFG 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLL 202
Cdd:PRK13539 127 YLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
332-526 |
1.17e-10 |
|
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: 61.53 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----KNADI----KIGYFDQARAM 403
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgKPLDIaarnRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 LNSDK---SLIELFCPNGGDRVQVRGHdmhIYGYLKSF-LFPKEflSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:cd03269 82 YPKMKvidQLVYLAQLKGLKKEEARRR---IDEWLERLeLSEYA--NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 480 NDLDIATINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAgktVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
342-526 |
1.21e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 342 NKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI------------KNADIKIGYFDQaRAMLNSDKS 409
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyasKEVARRIGLLAQ-NATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 LIELFC----PNGGDRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:PRK10253 98 VQELVArgryPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1751968159 486 -TINILE--EYLMEFKG-ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK10253 178 hQIDLLEllSELNREKGyTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
329-526 |
1.24e-10 |
|
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: 61.97 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----KNA------DIKIGYFD 398
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDAtdvpvqERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 QARA----MLNSDKSLIEL------FCPNGgDRVQVRGHD----MHIYGYLKSFlfPKEflsqavsvLSGGEKNRVALAL 464
Cdd:cd03296 81 QHYAlfrhMTVFDNVAFGLrvkprsERPPE-AEIRAKVHEllklVQLDWLADRY--PAQ--------LSGGQRQRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 465 LFTKDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03296 150 ALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
347-504 |
1.32e-10 |
|
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: 61.27 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARamLNSDKSLIE----LFcpNGGDRV 422
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED--LRSSLTIIPqdptLF--SGTIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 423 QVRGHDMH----IYGYLKsflfpkefLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLME-F 497
Cdd:cd03369 101 NLDPFDEYsdeeIYGALR--------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREeF 172
|
....*..
gi 1751968159 498 KGALIFV 504
Cdd:cd03369 173 TNSTILT 179
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-234 |
1.41e-10 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 61.73 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI-IRQNDKSI---AMLAQQVDF--NTNLSLDELIN 88
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlVDGHDLALadpAWLRRQVGVvlQENVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 89 KNLSEIYEALNKYENLQ-AKLAthldnkNLHKEINNLinfIESKDAWNIEQKkerflkefklfeyknrpiSSLSGGEIRK 167
Cdd:cd03252 94 DNIALADPGMSMERVIEaAKLA------GAHDFISEL---PEGYDTIVGEQG------------------AGLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 168 INLCILVLQNPDVLLLDEPTNHLDvYMCEflEKLLKN-SKIC----VIFISHDRYFIDNvASRCVEIEGGKI 234
Cdd:cd03252 147 IAIARALIHNPRILIFDEATSALD-YESE--HAIMRNmHDICagrtVIIIAHRLSTVKN-ADRIIVMEKGRI 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
329-526 |
1.43e-10 |
|
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: 61.83 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKI----INNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI---------------KN 389
Cdd:cd03258 1 MI-ELKNVSKVfgdtGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVlvdgtdltllsgkelRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 390 ADIKIGYFDQARAMLNSDKslielfcpnggdrvqVRG---HDMHIYGYLKSFLFPK-----EF--LSQAV----SVLSGG 455
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRT---------------VFEnvaLPLEIAGVPKAEIEERvlellELvgLEDKAdaypAQLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 456 EKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
8-234 |
1.48e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 62.41 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 8 KASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamlaqqvdfntnlsLDELI 87
Cdd:PRK13633 15 ESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY---------------------VDGLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 88 NKNLSEIYEALNK----YENLQAKLATHLDNKNLHKEINNLinFIESKDawnIEQKKERFLKEFKLFEYKNRPISSLSGG 163
Cdd:PRK13633 74 TSDEENLWDIRNKagmvFQNPDNQIVATIVEEDVAFGPENL--GIPPEE---IRERVDESLKKVGMYEYRRHAPHLLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHdryFIDNV--ASRCVEIEGGKI 234
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSgrreVVNTIKELNKKYGITIILITH---YMEEAveADRIIVMDSGKV 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
348-539 |
1.88e-10 |
|
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: 63.58 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGyfDQARAMLNSDKSLIE----LF--------- 414
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA--DYTLASLRRQVALVSqdvvLFndtiannia 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 --CPNGGDRVQVRghDMHIYGYLKSFL--FPKEF---LSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATI 487
Cdd:TIGR02203 428 ygRTEQADRAEIE--RALAAAYAQDFVdkLPLGLdtpIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 488 NILE---EYLMEFKGALIfVSHdRYFVDKLATKLYVFENGVInIEHMSYTQYLER 539
Cdd:TIGR02203 506 RLVQaalERLMQGRTTLV-IAH-RLSTIEKADRIVVMDDGRI-VERGTHNELLAR 557
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
353-522 |
2.19e-10 |
|
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: 59.89 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 353 ILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQaramlnsdkslielfcpnggdrvqvrghdmhiy 432
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ--------------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 433 gYLKsflfpkeflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI----ATINILEEYLMEFKGALIFVSHDR 508
Cdd:cd03222 69 -YID---------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDL 132
|
170
....*....|....
gi 1751968159 509 YFVDKLATKLYVFE 522
Cdd:cd03222 133 AVLDYLSDRIHVFE 146
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
347-524 |
3.09e-10 |
|
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: 60.56 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNSDKSLIE-------------- 412
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPwltvrenialavdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 -LFCPNGGDRVQVRGHDMHIYGYlksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILE 491
Cdd:TIGR01184 82 vLPDLSKSERRAIVEEHIALVGL-------TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1751968159 492 EYLM----EFKGALIFVSHDryfVDK---LATKLYVFENG 524
Cdd:TIGR01184 155 EELMqiweEHRVTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-526 |
3.19e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.01 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGriirqndkSIAMLAQQVDFNtn 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAG--------SILIDGQEMRFA-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 lSLDELINKNLSEIYEALNKY------ENLqakLATHLDNKnlhkeinnlINFIESKDAwnIEQKKERfLKEFKLFEYKN 154
Cdd:PRK11288 72 -STTAALAAGVAIIYQELHLVpemtvaENL---YLGQLPHK---------GGIVNRRLL--NYEAREQ-LEHLGVDIDPD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 155 RPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVeieg 231
Cdd:PRK11288 136 TPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVireLRAEGRVILYVSHRMEEIFALCDAIT---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 232 gkiSFFNGGYAYYLEKKAQIlvslskSYETLikhlkaeeewlrrgVKARLKRNEGrkeRIFKMREEAkknPGEIkRLKLE 311
Cdd:PRK11288 212 ---VFKDGRYVATFDDMAQV------DRDQL--------------VQAMVGREIG---DIYGYRPRP---LGEV-RLRLD 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 312 LLRAnSSIQKPnfnkqkmifelvnaskiinnkilfKNFSTRilQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknad 391
Cdd:PRK11288 262 GLKG-PGLREP------------------------ISFSVR--AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV---- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 392 ikigYFDQARAMLNSDKSLIE---LFCPNggDR-----VQV-----------RGHdmhiygYLKSFLF---------PKE 443
Cdd:PRK11288 311 ----YLDGKPIDIRSPRDAIRagiMLCPE--DRkaegiIPVhsvadninisaRRH------HLRAGCLinnrweaenADR 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 444 FL----------SQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI---ATI-NILEEyLMEFKGALIFVSHDRY 509
Cdd:PRK11288 379 FIrslniktpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVgakHEIyNVIYE-LAAQGVAVLFVSSDLP 457
|
570
....*....|....*..
gi 1751968159 510 FVDKLATKLYVFENGVI 526
Cdd:PRK11288 458 EVLGVADRIVVMREGRI 474
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
331-526 |
3.32e-10 |
|
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: 60.24 E-value: 3.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIgyFDQARAMLNSDKSL 410
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL--TDDKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ------IELFcPN---------------GGDRVQVRGHDMHiygYLKSF-LFPKEflSQAVSVLSGGEKNRVALALLFTK 468
Cdd:cd03262 79 gmvfqqFNLF-PHltvlenitlapikvkGMSKAEAEERALE---LLEKVgLADKA--DAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 469 DYDVLILDEPTNDLDIATIN-ILE--EYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGeVLDvmKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-216 |
3.35e-10 |
|
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: 62.69 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIA-------------------MLAQQ 74
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI-AVNGVPLAdadadswrdqiawvpqhpfLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 VDFNTNLSLDElinKNLSEIYEALnkyenlqaklathldnknlhkeinnlinfiESKDAWNIEQKKERFLkEFKLFEYKN 154
Cdd:TIGR02857 412 IAENIRLARPD---ASDAEIREAL------------------------------ERAGLDEFVAALPQGL-DTPIGEGGA 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 155 RpissLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKicVIFISHDR 216
Cdd:TIGR02857 458 G----LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDaeteAEVLEALRALAQGRT--VLLVTHRL 517
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
347-507 |
3.36e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI------------KIGYFDQaramlNSDKSL---- 410
Cdd:PRK13635 24 KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvrrQVGMVFQ-----NPDNQFvgat 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ----IELFCPNGG-------DRVQVRGHDMHIygylksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:PRK13635 99 vqddVAFGLENIGvpreemvERVDQALRQVGM----------EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|....*
gi 1751968159 480 NDLD-------IATINILEEYLMEfkgALIFVSHD 507
Cdd:PRK13635 169 SMLDprgrrevLETVRQLKEQKGI---TVLSITHD 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-234 |
3.71e-10 |
|
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: 60.78 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGE-KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAML 71
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedIREQDpvelrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 72 AQQVDFNTNLSLDELInknlsEIYEALNKyenlqaklathldnknlhkeinnlinfieskdaWNIEQKKERFLKEFKL-- 149
Cdd:cd03295 81 IQQIGLFPHMTVEENI-----ALVPKLLK---------------------------------WPKEKIRERADELLALvg 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 ---FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLE----KLLKNSKICVIFISHDryfIDN- 221
Cdd:cd03295 123 ldpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQeefkRLQQELGKTIVFVTHD---IDEa 199
|
250
....*....|....*
gi 1751968159 222 --VASRCVEIEGGKI 234
Cdd:cd03295 200 frLADRIAIMKNGEI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
329-508 |
3.85e-10 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 61.70 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----KNADI-------KIGY- 396
Cdd:COG1118 1 MSIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIvlngRDLFTnlpprerRVGFv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 ------------FD----------------QARAMlnsdkSLIELfcpnggdrVQVRGhdmhiygylksflFPKEFLSQa 448
Cdd:COG1118 81 fqhyalfphmtvAEniafglrvrppskaeiRARVE-----ELLEL--------VQLEG-------------LADRYPSQ- 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 449 vsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLM----EFKGALIFVSHDR 508
Cdd:COG1118 134 ---LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRrlhdELGGTTVFVTHDQ 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-236 |
3.86e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII----------RQNDKSIAMLAQQvdfNTNLSLDelin 88
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpfkrrKEFARRIGVVFGQ---RSQLWWD---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 89 knlseiyealnkyenlqakLAThLDNKNLHKEINNLinfieSKDAWniEQKKERFLKEFKLFEYKNRPISSLSGGEIRKI 168
Cdd:COG4586 111 -------------------LPA-IDSFRLLKAIYRI-----PDAEY--KKRLDELVELLDLGELLDTPVRQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDVYMC----EFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISF 236
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKeairEFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIY 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
330-524 |
4.01e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKI-GYFDQARAM----- 403
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVpSRARHARQRvgvvp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 ----LNSDKSLIElfcpnggdRVQVRGHDMHIYGYLKSFLFPK--EFL---SQA---VSVLSGGEKNRVALALLFTKDYD 471
Cdd:PRK13537 87 qfdnLDPDFTVRE--------NLLVFGRYFGLSAAAARALVPPllEFAkleNKAdakVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 472 VLILDEPTNDLDIATINILEEYLMEF--KGALIFV-SHDRYFVDKLATKLYVFENG 524
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLtTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
343-506 |
4.05e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--------------KNADIKIGYFDQARAMLNSDK 408
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdsiARGLLYLGHAPGIKTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLiELFCPNGGD--------RVQVRGhdmhiygylksflfpkeFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTN 480
Cdd:cd03231 93 NL-RFWHADHSDeqveealaRVGLNG-----------------FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 1751968159 481 DLDIATINILEEYL---MEFKGALIFVSH 506
Cdd:cd03231 155 ALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
348-529 |
4.94e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNS-----------DKSLIELFCP 416
Cdd:PRK11614 23 EVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAvaivpegrrvfSRMTVEENLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 417 NGG---DRVQVRGHDMHIYGylksfLFPK--EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTndLDIATINILE 491
Cdd:PRK11614 103 MGGffaERDQFQERIKWVYE-----LFPRlhERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS--LGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 492 -----EYLMEfKGALIF-VSHDRYFVDKLATKLYVFENGVINIE 529
Cdd:PRK11614 176 ifdtiEQLRE-QGMTIFlVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
332-526 |
6.07e-10 |
|
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: 60.01 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINN-KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI------------KIGYFD 398
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEdireqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 QAramlnsdkslIELFcP--------------NGGDRVQVRghdMHIYGYLKSF-LFPKEFLSQAVSVLSGGEKNRVALA 463
Cdd:cd03295 82 QQ----------IGLF-PhmtveenialvpklLKWPKEKIR---ERADELLALVgLDPAEFADRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 464 LLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
356-515 |
6.14e-10 |
|
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: 60.07 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 356 GEKIGIVGQNGCGKSTFLKILL-----NLDKLssGEIKNADIKIGYF------DQARAMLNSDKSLIELfcPNGGDRV-- 422
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAgklkpNLGKF--DDPPDWDEILDEFrgselqNYFTKLLEGDVKVIVK--PQYVDLIpk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 423 QVRG---------HDMHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA---TINIL 490
Cdd:cd03236 102 AVKGkvgellkkkDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARL 181
|
170 180
....*....|....*....|....*
gi 1751968159 491 EEYLMEFKGALIFVSHDRYFVDKLA 515
Cdd:cd03236 182 IRELAEDDNYVLVVEHDLAVLDYLS 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-214 |
6.42e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 59.93 E-value: 6.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiAMLAQQVDFNTN 80
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGE----VYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLdelINKNLSEIYEALNKYENLQAklathLDNKNLHKEINNLInfiesKDAWNIEQKKERFLKEFKLF-EYKNR---P 156
Cdd:PRK14247 77 VIE---LRRRVQMVFQIPNPIPNLSI-----FENVALGLKLNRLV-----KSKKELQERVRWALEKAQLWdEVKDRldaP 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 157 ISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK--ICVIFISH 214
Cdd:PRK14247 144 AGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKkdMTIVLVTH 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-234 |
7.17e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 60.39 E-value: 7.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQndksiamlaqqvdfntnlSLDELINKNLSEIYEAL 98
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS------------------GIDTGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 N-KYENLQAKLATHLDNKNLHKEINNL-INFIEskdawnIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQ 176
Cdd:PRK13644 80 GiVFQNPETQFVGRTVEEDLAFGPENLcLPPIE------IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 177 NPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcVIFISHDRYFIdNVASRCVEIEGGKI 234
Cdd:PRK13644 154 EPECLIFDEVTSMLDpdsgIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-192 |
7.34e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.04 E-value: 7.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKsiamLAQQVDfntNLSLDELINKNLSE 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP----LDFQRD---SIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 IYEALNKYENLQAKLATHLDNKnlhkeinnlinfieskdawnIEQKkerfLKEFKLFEYKNRPISSLSGGEIRKINLCIL 173
Cdd:cd03231 84 IKTTLSVLENLRFWHADHSDEQ--------------------VEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARL 139
|
170
....*....|....*....
gi 1751968159 174 VLQNPDVLLLDEPTNHLDV 192
Cdd:cd03231 140 LLSGRPLWILDEPTTALDK 158
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-234 |
7.91e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 7.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKaifgTLQL----DSGRIirqndkSIAmlAQQVDFNT 79
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR----VLNLlempRSGTL------NIA--GNHFDFSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLDE--LINKNLSEIYEalnkyenlQAKLATHLdnknlhKEINNLInfiE--------SKDAWNieQKKERFLKEFKL 149
Cdd:PRK11124 71 TPSDKAirELRRNVGMVFQ--------QYNLWPHL------TVQQNLI---EapcrvlglSKDQAL--ARAEKLLERLRL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRC 226
Cdd:PRK11124 132 KPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIireLAETGITQVIVTHEVEVARKTASRV 211
|
....*...
gi 1751968159 227 VEIEGGKI 234
Cdd:PRK11124 212 VYMENGHI 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-240 |
8.41e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.03 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDsgriiRQNDKSIAMLAQQVDFNTNLS 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGD-----KSAGSHIELLGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDelINKNLSE---IYEALNKYENLqaklaTHLDNKnlhkeinnLINFIESKDAWNI-------EQKKE--RFLKEFKLF 150
Cdd:PRK09984 79 RD--IRKSRANtgyIFQQFNLVNRL-----SVLENV--------LIGALGSTPFWRTcfswftrEQKQRalQALTRVGMV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD-----VYMcEFLEKLLKNSKICVIFISHDRYFIDNVASR 225
Cdd:PRK09984 144 HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDpesarIVM-DTLRDINQNDGITVVVTLHQVDYALRYCER 222
|
250
....*....|....*
gi 1751968159 226 CVEIEGGKIsFFNGG 240
Cdd:PRK09984 223 IVALRQGHV-FYDGS 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
8.46e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 8.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamlaqqvdFNTNlslDELINKNLSEIYEAL 98
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIE---------------WIFK---DEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 NKYeNLQAKLATHLDN-KNLHKEINNLINFIE--------SKD--------AWNIEQKKERFLKEFKLF----EYKNRPI 157
Cdd:PRK13651 85 EKL-VIQKTRFKKIKKiKEIRRRVGVVFQFAEyqlfeqtiEKDiifgpvsmGVSKEEAKKRAAKYIELVgldeSYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcVIFISHDryfIDNV---ASRCVEIE 230
Cdd:PRK13651 164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgvKEILEIFDNLNKQGKT-IILVTHD---LDNVlewTKRTIFFK 239
|
....
gi 1751968159 231 GGKI 234
Cdd:PRK13651 240 DGKI 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-223 |
9.85e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 59.75 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFG---EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDK----------- 66
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 67 SIAMLAQQVDfntnlsldelinknlseiyealNKY--ENLQAKLATHLDNKNL-HKEInnlinfieskdawnieqkKERF 143
Cdd:PRK13650 82 KIGMVFQNPD----------------------NQFvgATVEDDVAFGLENKGIpHEEM------------------KERV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 144 LKEFKLF---EYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDr 216
Cdd:PRK13650 122 NEALELVgmqDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD- 200
|
....*..
gi 1751968159 217 yfIDNVA 223
Cdd:PRK13650 201 --LDEVA 205
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
10-234 |
1.03e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 59.70 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAML--AQQVDFNTNLSLdeLI 87
Cdd:PRK10419 19 SGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV-SWRGEPLAKLnrAQRKAFRRDIQM--VF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 88 NKNLSeiyeALNKYENLQAKLA------THLDNKNLHKEINNLINFIESKDAwnIEQKkerflkefklfeyknRPiSSLS 161
Cdd:PRK10419 96 QDSIS----AVNPRKTVREIIReplrhlLSLDKAERLARASEMLRAVDLDDS--VLDK---------------RP-PQLS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVlqagVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-234 |
1.03e-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: 59.16 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKS-----IAMLAQQV-----DF 77
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIlidgidIRDISRKslrsmIGVVLQDTflfsgTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 NTNLSLDELINKnlseiyealNKYENLQAKLAthldnkNLHKEINNLINFIESkdawnieQKKERFlkefklfeyknrpi 157
Cdd:cd03254 94 MENIRLGRPNAT---------DEEVIEAAKEA------GAHDFIMKLPNGYDT-------VLGENG-------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYM----CEFLEKLLKNSKicVIFISHDRYFIDNvASRCVEIEGGK 233
Cdd:cd03254 138 GNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETekliQEALEKLMKGRT--SIIIAHRLSTIKN-ADKILVLDDGK 214
|
.
gi 1751968159 234 I 234
Cdd:cd03254 215 I 215
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
347-526 |
1.05e-09 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 59.75 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-------------KIGYFDQaramlNSDKSLIEL 413
Cdd:TIGR04520 19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLdtldeenlweirkKVGMVFQ-----NPDNQFVGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 -------FCP-NGG-------DRVQVRGHDMHIYGYLKsflfpkeflsQAVSVLSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:TIGR04520 94 tveddvaFGLeNLGvpreemrKRVDEALKLVGMEDFRD----------REPHLLSGGQKQRVAIAGVLAMRPDIIILDEA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 479 TNDLD-------IATINILEEylmEFKGALIFVSHDryfVDK--LATKLYVFENGVI 526
Cdd:TIGR04520 164 TSMLDpkgrkevLETIRKLNK---EEGITVISITHD---MEEavLADRVIVMNKGKI 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-518 |
1.06e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-------------KNADI---KIGYFDQARAMLNSDK 408
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsklssaAKAELrnqKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLIELFCP--NGG---DRVQVRGHDMhiygyLKSFLFPKEFLSQAvSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:PRK11629 104 ALENVAMPllIGKkkpAEINSRALEM-----LAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 1751968159 484 IATINILEEYLMEFK----GALIFVSHDRYFVDKLATKL 518
Cdd:PRK11629 178 ARNADSIFQLLGELNrlqgTAFLVVTHDLQLAKRMSRQL 216
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
329-526 |
1.11e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.34 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI---------KNADIK------ 393
Cdd:PRK09493 1 MI-EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvndPKVDERlirqea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 394 ------IGYFDQARAMLNSdkslieLFCPnggdrVQVRGHDMHIYGYLKSFLFPKEFLSQAV----SVLSGGEKNRVALA 463
Cdd:PRK09493 80 gmvfqqFYLFPHLTALENV------MFGP-----LRVRGASKEEAEKQARELLAKVGLAERAhhypSELSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 464 LLFTKDYDVLILDEPTNDLD-------IATINILEEYLMefkgALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDpelrhevLKVMQDLAEEGM----TMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
325-524 |
1.20e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 59.62 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 325 NKQKMI-FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGY--FDQAR 401
Cdd:PRK13632 3 NKSVMIkVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKenLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AML-----NSDKSLIELFCPN----GGDRVQVRGHDMH--IYGYLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTKDY 470
Cdd:PRK13632 83 KKIgiifqNPDNQFIGATVEDdiafGLENKKVPPKKMKdiIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 471 DVLILDEPTNDLDIATINILEEYLMEF----KGALIFVSHDryfVDK--LATKLYVFENG 524
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD---MDEaiLADKVIVFSEG 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
3-231 |
1.28e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGekiildeiNFS-------ANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqnDKSIAMLAQQV 75
Cdd:PRK13409 340 LVEYPDLTKKLG--------DFSleveggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYI 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 DFNTNLSLDELInknlseiyealnkyenlqAKLATHLDNKNLHKEINNLINfieskdawnIEqkkerflkefKLFEyknR 155
Cdd:PRK13409 410 KPDYDGTVEDLL------------------RSITDDLGSSYYKSEIIKPLQ---------LE----------RLLD---K 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 156 PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVymcE-------FLEKLLKNSKICVIFISHDRYFIDNVASRCVE 228
Cdd:PRK13409 450 NVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV---EqrlavakAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
...
gi 1751968159 229 IEG 231
Cdd:PRK13409 527 FEG 529
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-234 |
1.34e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 23 NFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND---------KSIAMLAQQVDFNTNLSLDELInknlse 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrRPVSMLFQENNLFSHLTVAQNI------ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 iyeALNKYENLqaKLathldnknlhkeinnlinfieskdawNIEQKK--ERFLKEFKLFEYKNRPISSLSGGEIRKINL- 170
Cdd:PRK10771 93 ---GLGLNPGL--KL--------------------------NAAQREklHAIARQMGIEDLLARLPGQLSGGQRQRVALa 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 171 -CiLVLQNPdVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfIDN---VASRCVEIEGGKI 234
Cdd:PRK10771 142 rC-LVREQP-ILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHS---LEDaarIAPRSLVVADGRI 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-526 |
1.42e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrQNDKSIAMLAQQVDFNTNLS 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTIT-INNINYNKLDHKLAAQLGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 ldeLINKNLSEIYEaLNKYENLQakLATHLDNKNLHkeinnlINFIESKDawnIEQKKERFLKEFKLFEYKNRPISSLSG 162
Cdd:PRK09700 84 ---IIYQELSVIDE-LTVLENLY--IGRHLTKKVCG------VNIIDWRE---MRVRAAMMLLRVGLKVDLDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIEGGkisffng 239
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLImnqLRKEGTAIVYISHKLAEIRRICDRYTVMKDG------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 240 gyayylekkaqilvslSKSYETLIKHLKAEEewlrrgvKARLKRNEGRKERIFKMREEAKKNPGEIkrlklellranssi 319
Cdd:PRK09700 222 ----------------SSVCSGMVSDVSNDD-------IVRLMVGRELQNRFNAMKENVSNLAHET-------------- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 320 qkpnfnkqkmIFELVNASKIINNKIlfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIgyfdQ 399
Cdd:PRK09700 265 ----------VFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI----S 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 400 ARAMLNSDKSLIEL---------FCPNGGDRvqvrgHDMHIYGYLKSFLF------------------PKEFLS------ 446
Cdd:PRK09700 329 PRSPLDAVKKGMAYitesrrdngFFPNFSIA-----QNMAISRSLKDGGYkgamglfhevdeqrtaenQRELLAlkchsv 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 447 -QAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI---ATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:PRK09700 404 nQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVgakAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFC 483
|
....
gi 1751968159 523 NGVI 526
Cdd:PRK09700 484 EGRL 487
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
18-234 |
1.44e-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: 58.78 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQND-----KSIAMLAQQVdFNTNLSLDEL 86
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRIlidghdVRDYTlaslrRQIGLVSQDV-FLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 I-----NKNLSEIYEAlnkyenlqAKLAthldnkNLHKEINNLINFIESkdawNIEqkkERFLKefklfeyknrpissLS 161
Cdd:cd03251 96 IaygrpGATREEVEEA--------ARAA------NAHEFIMELPEGYDT----VIG---ERGVK--------------LS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKicVIFISHDRYFIDNvASRCVEIEGGKI 234
Cdd:cd03251 141 GGQRQRIAIARALLKDPPILILDEATSALDTeserLVQAALERLMKNRT--TFVIAHRLSTIEN-ADRIVVLEDGKI 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
329-526 |
1.68e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 59.33 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIFELVNASKIINNKI-----LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI------KNADIKIGYF 397
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdEKNKKKTKEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQARAMLNSDKSLIELFCPNGGDRVQVR---------------GHDMhIYG-----------------YLKSFLFPKEFL 445
Cdd:PRK13651 81 EKVLEKLVIQKTRFKKIKKIKEIRRRVGvvfqfaeyqlfeqtiEKDI-IFGpvsmgvskeeakkraakYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 446 SQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD-IATINILE--EYLMEFKGALIFVSHDRYFVDKLATKLYVFE 522
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 1751968159 523 NGVI 526
Cdd:PRK13651 240 DGKI 243
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
345-524 |
1.93e-09 |
|
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: 57.86 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE---------------IKNADIK--I--GY-FDQAR--- 401
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSvsvpgsiayvsqepwIQNGTIRenIlfGKpFDEERyek 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 ----AMLNSDkslIELFCpnGGDRVQV--RGhdmhiygylksflfpkeflsqaVSvLSGGEKNRVALALLFTKDYDVLIL 475
Cdd:cd03250 100 vikaCALEPD---LEILP--DGDLTEIgeKG----------------------IN-LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 476 DEPTNDLDIATinilEEYLME--FKGAL------IFVSHDRYFVDKlATKLYVFENG 524
Cdd:cd03250 152 DDPLSAVDAHV----GRHIFEncILGLLlnnktrILVTHQLQLLPH-ADQIVVLDNG 203
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
350-515 |
2.26e-09 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 59.36 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 350 STRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQA------RAM----------LNSDKSL--- 410
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrplrRRMqmvfqdpyasLNPRMTVgdi 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 ----IELFCPNGGDRVQVRGHDM---------HIYGYlksflfPKEFlsqavsvlSGGEKNRV----ALALlftkDYDVL 473
Cdd:COG4608 118 iaepLRIHGLASKAERRERVAELlelvglrpeHADRY------PHEF--------SGGQRQRIgiarALAL----NPKLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 474 ILDEPTNDLDIA----TINILEEYLMEFKGALIFVSHD----RYFVDKLA 515
Cdd:COG4608 180 VCDEPVSALDVSiqaqVLNLLEDLQDELGLTYLFISHDlsvvRHISDRVA 229
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-222 |
2.37e-09 |
|
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: 57.54 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFG--TLQLDSGRIIRQnDKSIamlaqqvdfnTNLSLDELINKNL 91
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFK-GEDI----------TDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 92 SEIYEALNKYENLqaklathldnknlhkeinNLINFIeskdawnieqkkeRFLKEfklfeyknrpisSLSGGEIRKINLC 171
Cdd:cd03217 80 FLAFQYPPEIPGV------------------KNADFL-------------RYVNE------------GFSGGEKKRNEIL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 172 ILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNV 222
Cdd:cd03217 117 QLLLLEPDLAILDEPDSGLDIDALRLVAEVinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
330-524 |
2.39e-09 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 57.06 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASkiinNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFDQARAMLNSDKS 409
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI--------TLDGKPVTRRSPRD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 LIEL---FCPngGDRvqvrghdmHIYGylksfLFPKEFLSQ---AVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:cd03215 72 AIRAgiaYVP--EDR--------KREG-----LVLDLSVAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 484 IATINILEEYLMEFK---GALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03215 137 VGAKAEIYRLIRELAdagKAVLLISSELDELLGLCDRILVMYEG 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-502 |
2.50e-09 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 58.05 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLD---KLSSGEI--KNADIKIGYFDQARAMLNSDKSLIE--- 412
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQIlfNGQPRKPDQFQKCVAYVRQDDILLPglt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 -----LFCpnggdrVQVRGHDmHIYGYLKSFLFPKEFLSQA---------VSVLSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:cd03234 98 vretlTYT------AILRLPR-KSSDAIRKKRVEDVLLRDLaltriggnlVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180
....*....|....*....|....*...
gi 1751968159 479 TNDLDIAT----INILEEYLMEFKGALI 502
Cdd:cd03234 171 TSGLDSFTalnlVSTLSQLARRNRIVIL 198
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
328-539 |
2.76e-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: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 328 KMIFELVNASkIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IG 395
Cdd:cd03254 2 EIEFENVNFS-YDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidGIDIRdisrkslrsmIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 396 YFDQARAMLN-SDKSLIELFCPNGGDRV------QVRGHD--MH-IYGYlksflfpKEFLSQAVSVLSGGEKNRVALALL 465
Cdd:cd03254 81 VVLQDTFLFSgTIMENIRLGRPNATDEEvieaakEAGAHDfiMKlPNGY-------DTVLGENGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 466 FTKDYDVLILDEPTNDLDIATINILEE---YLMEFKGALIfVSHdRYFVDKLATKLYVFENGVInIEHMSYTQYLER 539
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEaleKLMKGRTSII-IAH-RLSTIKNADKILVLDDGKI-IEEGTHDELLAK 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
316-508 |
2.87e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.46 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 316 NSSIQKPNFNKQKM---IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNA 390
Cdd:PRK11607 2 NDAIPRPQAKTRKAltpLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImlDGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 391 DIK--------IGYFDQARAM-------------LNSDKslielfCPNGgdRVQVRGHDMhiygylKSFLFPKEFLSQAV 449
Cdd:PRK11607 82 DLShvppyqrpINMMFQSYALfphmtveqniafgLKQDK------LPKA--EIASRVNEM------LGLVHMQEFAKRKP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 450 SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD--------IATINILEEYlmefkGAL-IFVSHDR 508
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILERV-----GVTcVMVTHDQ 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
10-234 |
2.88e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.15 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiAMLAQQVDfNTNLSLDElink 89
Cdd:PRK11247 19 SKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAEARE-DTRLMFQD---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 nlseiyealnkyenlqAKL---ATHLDNKNLhkeinNLinfiesKDAWniEQKKERFLKEFKLFEYKNRPISSLSGGEIR 166
Cdd:PRK11247 90 ----------------ARLlpwKKVIDNVGL-----GL------KGQW--RDAALQALAAVGLADRANEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-234 |
2.96e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIfgtlqldsGRIIRQNDKSIAMLAQQVDFNTNL-SLDEL-INKNLS 92
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--------NRLIEIYDSKIKVDGKVLYFGKDIfQIDAIkLRKEVG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIYEALNKYENLqaklathldnkNLHKEINNLINFIESKDAWNIEQKKERFLKEFKL----FEYKNRPISSLSGGEIRKI 168
Cdd:PRK14246 94 MVFQQPNPFPHL-----------SIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK--ICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKneIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
353-515 |
2.97e-09 |
|
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: 58.91 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 353 ILQGEKIGIVGQNGCGKSTFLKILLNLDK---LSSGEI--KNADI-------------------------------KIGY 396
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEIlfDGEDLlklsekelrkirgreiqmifqdpmtslnpvmTVGD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 F-------------DQARAMLnsdkslIELFcpnggDRVQVRGHDMHIYGYlksflfPKEFlsqavsvlSGGEKNRV--A 461
Cdd:COG0444 108 QiaeplrihgglskAEARERA------IELL-----ERVGLPDPERRLDRY------PHEL--------SGGMRQRVmiA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 462 LALLFtkDYDVLILDEPTNDLDiATI--NILEeyLM-----EFKGALIFVSHD----RYFVDKLA 515
Cdd:COG0444 163 RALAL--EPKLLIADEPTTALD-VTIqaQILN--LLkdlqrELGLAILFITHDlgvvAEIADRVA 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
3.12e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.22 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiamlaQQVDfntnlsldeliNKNLSEIYE-- 96
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNN--------QAIT-----------DDNFEKLRKhi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 97 --ALNKYEN------LQAKLATHLDN-----KNLHKEINNLinfieskdawnieqkkerfLKEFKLFEYKNRPISSLSGG 163
Cdd:PRK13648 86 giVFQNPDNqfvgsiVKYDVAFGLENhavpyDEMHRRVSEA-------------------LKQVDMLERADYEPNALSGG 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDarqnLLDLVRKVKSEHNITIISITHD 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-234 |
3.88e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.52 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQndksiamlAQQVDFNTNLSLDELINKNLSEIYE- 96
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFN--------GQPMSKLSSAAKAELRNQKLGFIYQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 97 -----ALNKYENLQAKLathldnknlhkeinnlinFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLC 171
Cdd:PRK11629 96 hhllpDFTALENVAMPL------------------LIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 172 ILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVaSRCVEIEGGKI 234
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARnadsIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
332-507 |
4.09e-09 |
|
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: 57.25 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI--------KIGYFDQAR 401
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIllDGKDItnlpphkrPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 A----------------MLNSDKSLIELFCPNGGDRVQVrghdmhiygylksflfpKEFLSQAVSVLSGGEKNRVALALL 465
Cdd:cd03300 82 AlfphltvfeniafglrLKKLPKAEIKERVAEALDLVQL-----------------EGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1751968159 466 FTKDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHD 507
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHD 190
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
352-507 |
4.37e-09 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 56.47 E-value: 4.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 352 RILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYFDQARAMlnsDKSL---------IELFCPNGGDR 421
Cdd:NF040873 14 TIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVrRAGGARVAYVPQRSEV---PDSLpltvrdlvaMGRWARRGLWR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 422 VQVRGHDMHIYGYLKSfLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG-- 499
Cdd:NF040873 91 RLTRDDRAAVDDALER-VGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArg 169
|
....*....
gi 1751968159 500 -ALIFVSHD 507
Cdd:NF040873 170 aTVVVVTHD 178
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
10-233 |
4.40e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGrIIRQNDKSIAMLAQQ-------VDFNTNLS 82
Cdd:PRK11300 12 MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGG-TILLRGQHIEGLPGHqiarmgvVRTFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LdelinknlseiYEALNKYENLQakLATHldnknLHKEINNLINFIESKDAWNIEQKK-ER---FLKEFKLFEYKNRPIS 158
Cdd:PRK11300 91 L-----------FREMTVIENLL--VAQH-----QQLKTGLFSGLLKTPAFRRAESEAlDRaatWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEP--------TNHLDvymcEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIE 230
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPaaglnpkeTKELD----ELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
...
gi 1751968159 231 GGK 233
Cdd:PRK11300 229 QGT 231
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
358-526 |
4.69e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.89 E-value: 4.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 358 KIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADIKIGYFDQARAML-----NSDKsliELFCPN------------G 418
Cdd:PRK13652 32 RIAVIGPNGAGKSTLFRHFNGILKPTSGSvlIRGEPITKENIREVRKFVglvfqNPDD---QIFSPTveqdiafgpinlG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 419 GDRVQVRghdmHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD-------IATINIL- 490
Cdd:PRK13652 109 LDEETVA----HRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDpqgvkelIDFLNDLp 184
|
170 180 190
....*....|....*....|....*....|....*.
gi 1751968159 491 EEYLMefkgALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13652 185 ETYGM----TVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
348-524 |
4.85e-09 |
|
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: 57.06 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRilQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIK-----------IGY-------------FDQAR 401
Cdd:cd03219 20 SFSVR--PGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfDGEDITglppheiarlgIGRtfqiprlfpeltvLENVM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AMLNSDKSLIELFCPNGGDRVQVRGHDMHIygyLKsFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:cd03219 98 VAAQARTGSGLLLARARREEREARERAEEL---LE-RVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1751968159 482 LDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:cd03219 174 LNPEETEELAELIRELRErgiTVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
341-506 |
4.87e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 59.05 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGeiknadiKIGYFDQARAMLNSDK------SLIELF 414
Cdd:COG4178 374 DGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG-------RIARPAGARVLFLPQRpylplgTLREAL 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 C-PNGGDRV---QVRG--HDMHIyGYLKSFLFPKEFLSQavsVLSGGEKNRVALA-LLFTKDyDVLILDEPTNDLDIATi 487
Cdd:COG4178 447 LyPATAEAFsdaELREalEAVGL-GHLAERLDEEADWDQ---VLSLGEQQRLAFArLLLHKP-DWLFLDEATSALDEEN- 520
|
170 180
....*....|....*....|....*
gi 1751968159 488 nilEEYLME------FKGALIFVSH 506
Cdd:COG4178 521 ---EAALYQllreelPGTTVISVGH 542
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
333-526 |
6.21e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.12 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 333 LVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIK----------IGYFDQARA 402
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRmndvppaergVGMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 M---LN-------------SDKSLIELFCPNGGDRVQVrGHdmhiygylksflfpkeFLSQAVSVLSGGEKNRVALALLF 466
Cdd:PRK11000 86 LyphLSvaenmsfglklagAKKEEINQRVNQVAEVLQL-AH----------------LLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 467 TKDYDVLILDEPTNDLDIA-------TINILEEYLmefKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAAlrvqmriEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-234 |
6.56e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 33 AIIGKNGEGKSTLLK-------AIFGTLQLDSGRIIRQNDKS----IAMLAQQVDFNTNLSLDELINKNLSEIYEALNKY 101
Cdd:PRK10575 41 GLIGHNGSGKSTLLKmlgrhqpPSEGEILLDAQPLESWSSKAfarkVAYLPQQLPAAEGMTVRELVAIGRYPWHGALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 102 enlqaklathldNKNLHKEINNLINFIEskdawnieqkkerfLKEFKlfeykNRPISSLSGGEIRKINLCILVLQNPDVL 181
Cdd:PRK10575 121 ------------GAADREKVEEAISLVG--------------LKPLA-----HRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 182 LLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRyfidNVASR-C---VEIEGGKI 234
Cdd:PRK10575 170 LLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHDI----NMAARyCdylVALRGGEM 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
18-234 |
6.87e-09 |
|
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: 58.98 E-value: 6.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDK-----SIAMLAQQVDFNTNLSLDEL 86
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngfsLKDIDRhtlrqFINYLPQEPYIFSGSILENL 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 InknlseiyealnkyenLQAKLATHLDnknlhkEINNLINFIESKDawNIEQKKERFLKEFklfeykNRPISSLSGGEIR 166
Cdd:TIGR01193 569 L----------------LGAKENVSQD------EIWAACEIAEIKD--DIENMPLGYQTEL------SEEGSSISGGQKQ 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLDVYM-CEFLEKLLKNSKICVIFISHdRYFIDNVASRCVEIEGGKI 234
Cdd:TIGR01193 619 RIALARALLTDSKVLILDESTSNLDTITeKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-234 |
6.90e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 57.53 E-value: 6.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGriirqndkSIAMLAQQVDFNTNlsldeliNKNLSEI 94
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSG--------TITIAGYHITPETG-------NKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALNKYenLQAKLATHLDNKNLHKEINNLINFIESKDawNIEQKKERFLKEFKLFE-YKNRPISSLSGGEIRKINLCIL 173
Cdd:PRK13641 84 RKKVSLV--FQFPEAQLFENTVLKDVEFGPKNFGFSED--EAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 174 VLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKIC---VIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
345-506 |
7.27e-09 |
|
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: 56.21 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--------KNADIK------IGYFDQARAMLNSDKSL 410
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrwngtplaEQRDEPhenilyLGHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 iELFCPNGG----------DRVQVRGHDmHIygylksflfpkeflsqAVSVLSGGEKNRVALALLFTKDYDVLILDEPTN 480
Cdd:TIGR01189 95 -HFWAAIHGgaqrtiedalAAVGLTGFE-DL----------------PAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 1751968159 481 DLDIATINILEEYL---MEFKGALIFVSH 506
Cdd:TIGR01189 157 ALDKAGVALLAGLLrahLARGGIVLLTTH 185
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-234 |
7.33e-09 |
|
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: 56.35 E-value: 7.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 30 EKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII---------RQNDKSIAMLAQQVDFNTNLSLDELINKNLSeiyealnk 100
Cdd:cd03298 25 EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvtaaPPADRPVSMLFQENNLFAHLTVEQNVGLGLS-------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 101 yenlqaklathldnKNLHkeinnlinfIESKDawniEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDV 180
Cdd:cd03298 97 --------------PGLK---------LTAED----RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 181 LLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03298 150 LLLDEPFAALDPAlraeMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
361-514 |
8.20e-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: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 361 IVGQNGCGKSTFLKILlnldKLSSGEIKNADIKIGYFDQARAMLNSDKSLIEL-FCPNGGDRVQVRgHDMHIygYLKSFL 439
Cdd:cd03240 27 IVGQNGAGKTTIIEAL----KYALTGELPPNSKGGAHDPKLIREGEVRAQVKLaFENANGKKYTIT-RSLAI--LENVIF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 440 FPKE----FLSQAVSVLSGGEKN------RVALALLFTKDYDVLILDEPTNDLD-----IATINILEEYLMEFKGALIFV 504
Cdd:cd03240 100 CHQGesnwPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVI 179
|
170
....*....|
gi 1751968159 505 SHDRYFVDKL 514
Cdd:cd03240 180 THDEELVDAA 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
8.88e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 56.92 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFG--EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndkSIamlaqqvdFNT 79
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEI------KI--------DGI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 NLSLDEL--INKNLSEIYEAL-NKYENLQAK--LATHLDNKNLH-KEINNLINfiESKDAWNIEqkkerflkefklfEYK 153
Cdd:PRK13632 72 TISKENLkeIRKKIGIIFQNPdNQFIGATVEddIAFGLENKKVPpKKMKDIID--DLAKKVGME-------------DYL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD------VYmcEFLEKLLKNSKICVIFISHDryfIDNV--ASR 225
Cdd:PRK13632 137 DKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkreIK--KIMVDLRKTRKKTLISITHD---MDEAilADK 211
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:PRK13632 212 VIVFSEGKL 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-234 |
9.09e-09 |
|
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: 55.30 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDKS-----IAMLAQQvdfntnls 82
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadISQWDPNelgdhVGYLPQD-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 lDELINKNLSEiyealnkyenlqaklathldnknlhkeinnlinfieskdawNIeqkkerflkefklfeyknrpissLSG 162
Cdd:cd03246 85 -DELFSGSIAE-----------------------------------------NI-----------------------LSG 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKIC---VIFISHDRYFIdNVASRCVEIEGGKI 234
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAgatRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-234 |
1.08e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIEL--IKASKKFGEKII--LDEINFSANENEKIAIIGKNGEGKSTLLKaIFGTLQLDSGRIIRQNDKSIAMLaqqvdf 77
Cdd:PRK10535 3 ALLELkdIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKPTSGTYRVAGQDVATL------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 nTNLSLDELINKNLSEIYEalnKYEnlqakLATHLD-NKNLhkEINNLINFIESKdawnieQKKER---FLKEFKLFEYK 153
Cdd:PRK10535 76 -DADALAQLRREHFGFIFQ---RYH-----LLSHLTaAQNV--EVPAVYAGLERK------QRLLRaqeLLQRLGLEDRV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSKI---CVIFISHDRYfIDNVASRCVEIE 230
Cdd:PRK10535 139 EYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrghTVIIVTHDPQ-VAAQAERVIEIR 217
|
....
gi 1751968159 231 GGKI 234
Cdd:PRK10535 218 DGEI 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-234 |
1.18e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKF-GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-------RQNDKSIAMLAQQ 74
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghditRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 75 VDF---NTNLSLDELINKNLS-EIYEALNKYENLQAKLATHLDNKNLhkeinnlinfieskdawnieqkkerflkefkLF 150
Cdd:PRK10908 81 IGMifqDHHLLMDRTVYDNVAiPLIIAGASGDDIRRRVSAALDKVGL-------------------------------LD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 EYKNRPISsLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK---ICVIFISHDRYFIDNVASRCV 227
Cdd:PRK10908 130 KAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRML 208
|
....*..
gi 1751968159 228 EIEGGKI 234
Cdd:PRK10908 209 TLSDGHL 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-524 |
1.30e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.21 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKnADIKIGYFDQARAMLNSDKS 409
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK-VDGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 LIELFC----PNGGDRVQV--------RGHDMHIYGYLKSFL--------FPKEF---LSQAVSVLSGGEKNRVALALLF 466
Cdd:PRK14246 89 RKEVGMvfqqPNPFPHLSIydniayplKSHGIKEKREIKKIVeeclrkvgLWKEVydrLNSPASQLSGGQQQRLTIARAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 467 TKDYDVLILDEPTNDLDIATINILEEYLMEFKG--ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
332-526 |
1.32e-08 |
|
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: 55.23 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLD--KLSSGEI--KNADIKigyfdqarAMLNSD 407
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEIlfKGEDIT--------DLPPEE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 408 KSLIELFCpnggdrvqvrghdmhiygylkSFLFPKEFlsQAVSV----------LSGGEKNRVALALLFTKDYDVLILDE 477
Cdd:cd03217 74 RARLGIFL---------------------AFQYPPEI--PGVKNadflryvnegFSGGEKKRNEILQLLLLEPDLAILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 478 PTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKL-ATKLYVFENGVI 526
Cdd:cd03217 131 PDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIkPDRVHVLYDGRI 183
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
324-539 |
1.33e-08 |
|
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: 57.83 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 324 FNKQKMIFELVNA-SKIINNKILFK---------NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIK 393
Cdd:TIGR01193 458 FINKKKRTELNNLnGDIVINDVSYSygygsnilsDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 394 IGYFD--QARAMLNS--------DKSLIE--LFCPNGG---DRVQVRGHDMHIYGYLKSFlfPKEF---LSQAVSVLSGG 455
Cdd:TIGR01193 538 LKDIDrhTLRQFINYlpqepyifSGSILEnlLLGAKENvsqDEIWAACEIAEIKDDIENM--PLGYqteLSEEGSSISGG 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 456 EKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFK-GALIFVSHdRYFVDKLATKLYVFENGVInIEHMSYT 534
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLDHGKI-IEQGSHD 693
|
....*
gi 1751968159 535 QYLER 539
Cdd:TIGR01193 694 ELLDR 698
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
1.45e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.02 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFG----EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSI-------A 69
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-TLDGVPVtgpgadrG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 70 MLAQQvdfntnlsldelinknlseiyEALNKYENLQAKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKL 149
Cdd:COG4525 80 VVFQK---------------------DALLPWLNVLDNVAFGLRLRGVPKA--------------ERRARAEELLALVGL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 150 FEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD 215
Cdd:COG4525 125 ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALtreqMQELLLDVWQRTGKGVFLITHS 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
338-527 |
1.69e-08 |
|
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: 55.42 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 338 KIINNKILFKNFSTRIL-----QGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI--------KIGYFDQARA 402
Cdd:cd03299 2 KVENLSKDWKEFKLKNVsleveRGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllNGKDItnlppekrDISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 M---LNSDKSLIELFCPNGGDRVQVRGHDMHIYGYLKSflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:cd03299 82 LfphMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI----DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 480 NDLDIAT----INILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVIN 527
Cdd:cd03299 158 SALDVRTkeklREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
343-526 |
1.76e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 56.21 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI------------KNADI--KIG------------- 395
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvKLSDIrkKVGlvfqypeyqlfee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 396 --YFDQARAMLNSDKSLIELFcpnggDRVQvrgHDMHIYGylksfLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVL 473
Cdd:PRK13637 100 tiEKDIAFGPINLGLSEEEIE-----NRVK---RAMNIVG-----LDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 474 ILDEPTNDLD-------IATINILEEylmEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13637 167 ILDEPTAGLDpkgrdeiLNKIKELHK---EYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
347-507 |
2.10e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 56.25 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-----------KIGY-FDQaRAMLNSDKSLIELF 414
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYvpfkrrkefarRIGVvFGQ-RSQLWWDLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNGgdrvqvrghdmHIYG-----------YLKSFLFPKEFLSQAVSVLSGGEKNR--VALALLftKDYDVLILDEPTND 481
Cdd:COG4586 118 RLLK-----------AIYRipdaeykkrldELVELLDLGELLDTPVRQLSLGQRMRceLAAALL--HRPKILFLDEPTIG 184
|
170 180 190
....*....|....*....|....*....|
gi 1751968159 482 LDIAT----INILEEYLMEFKGALIFVSHD 507
Cdd:COG4586 185 LDVVSkeaiREFLKEYNRERGTTILLTSHD 214
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
335-486 |
2.33e-08 |
|
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: 54.58 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 335 NASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNldKLSSGEIKNADIKIGyfdqaramlNSDKSLIELF 414
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN--RTEGNVSVEGDIHYN---------GIPYKEFAEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPngGDRVQVRGHDMHIygylkSFLFPKEFL--------SQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT 486
Cdd:cd03233 81 YP--GEIIYVSEEDVHF-----PTLTVRETLdfalrckgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-526 |
2.59e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 55.45 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 335 NASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNA-------DIKIgYFDQARamLN 405
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlaGTAplaeareDTRL-MFQDAR--LL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 406 SDKSLIElfcpNGGdrVQVRGHdmhiygylksflfPKEFLSQAV-------------SVLSGGEKNRVALALLFTKDYDV 472
Cdd:PRK11247 94 PWKKVID----NVG--LGLKGQ-------------WRDAALQALaavgladranewpAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 473 LILDEPTNDLDIAT---INILEEYLMEFKG-ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK11247 155 LLLDEPLGALDALTrieMQDLIESLWQQHGfTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-234 |
2.62e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 55.38 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKA-------IFGTLQLDSGRIIRQNDKSIA----MLAQQVDFNTNL 81
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTlsrlmtpAHGHVWLDGEHIQHYASKEVArrigLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 82 SLDELINKNLSEIYEALNKYENlqaklathldnknlhkeinnlinfiESKDAWNieqkkeRFLKEFKLFEYKNRPISSLS 161
Cdd:PRK10253 97 TVQELVARGRYPHQPLFTRWRK-------------------------EDEEAVT------KAMQATGITHLADQSVDTLS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDIShqidLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
10-74 |
2.71e-08 |
|
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: 54.40 E-value: 2.71e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQndKSIAMLAQQ 74
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GSIAYVSQE 74
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
329-485 |
2.90e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.09 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI----------KNADIkigyfd 398
Cdd:COG4604 1 MI-EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvattPSREL------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 399 qAR--AMLNSDKSLI------EL-----FcPNGGDRVQVRGHDmHIYGYLkSFL----FPKEFLSQavsvLSGGEKNRVA 461
Cdd:COG4604 74 -AKrlAILRQENHINsrltvrELvafgrF-PYSKGRLTAEDRE-IIDEAI-AYLdledLADRYLDE----LSGGQRQRAF 145
|
170 180
....*....|....*....|....
gi 1751968159 462 LALLFTKDYDVLILDEPTNDLDIA 485
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMK 169
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
10-210 |
2.95e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.59 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKA----------IFGTLQLDSGRIIRQNDKSIAMLAQQvdfnt 79
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAlafrspkgvkGSGSVLLNGMPIDAKEMRAISAYVQQ----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 nlslDELINKNLSeIYEALNkyenLQAKLATHldnKNLHKEinnlinfieskdawnieQKKER---FLKEFKLFEYKNRP 156
Cdd:TIGR00955 107 ----DDLFIPTLT-VREHLM----FQAHLRMP---RRVTKK-----------------EKRERvdeVLQALGLRKCANTR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 157 I------SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKN------SKICVI 210
Cdd:TIGR00955 158 IgvpgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlaqkgkTIICTI 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
355-486 |
3.61e-08 |
|
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: 56.21 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 355 QGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAR-----AMLNSDKSL--------IELFCPNGGDR 421
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEvrrrvSVCAQDAHLfdttvrenLRLARPDATDE 439
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 422 ------VQVRGHDmhiygYLKSFlfpKEFLSQAV----SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT 486
Cdd:TIGR02868 440 elwaalERVGLAD-----WLRAL---PDGLDTVLgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-515 |
3.95e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 55.04 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 335 NASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLsSGEIKnADIKIGYFDQA----RAMLNSDKSL 410
Cdd:PRK14258 12 NLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVR-VEGRVEFFNQNiyerRVNLNRLRRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 IELFCP-----------NGGDRVQVRG--HDMHIYGYLKSFLFPKEF-------LSQAVSVLSGGEKNRVALALLFTKDY 470
Cdd:PRK14258 90 VSMVHPkpnlfpmsvydNVAYGVKIVGwrPKLEIDDIVESALKDADLwdeikhkIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 471 DVLILDEPTNDLD-IATINI---LEEYLMEFKGALIFVSHDRYFVDKLA 515
Cdd:PRK14258 170 KVLLMDEPCFGLDpIASMKVeslIQSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
10-191 |
4.07e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQ---------LDSGRIIRQNDKSIAMLAQQVDFNTN 80
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQgnnftgtilANNRKPTKQILKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDE-LINKNLSEIYEALNKYENLQAKLAThLDNKNLHKEINNLINfieskdawnieqkkerflkefklfeykNRPISS 159
Cdd:PLN03211 155 LTVREtLVFCSLLRLPKSLTKQEKILVAESV-ISELGLTKCENTIIG---------------------------NSFIRG 206
|
170 180 190
....*....|....*....|....*....|..
gi 1751968159 160 LSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:PLN03211 207 ISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-215 |
4.90e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 20 DEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII--------------RQNDKSIAMLAQQ--VDFNTNLSL 83
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmkddewRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 84 DELINKNLSEIYEALNKYEnLQAKLATHLDNKNLhkeINNLINfieskdawnieqkkeRFLKEFklfeyknrpisslSGG 163
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQE-VKDRVKAMMLKVGL---LPNLIN---------------RYPHEF-------------SGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYM----CEFLEKLLKNSKICVIFISHD 215
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIqaqvVNLLQQLQREMGLSLIFIAHD 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
20-215 |
5.08e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.12 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 20 DEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQlDSGRI---IRQNDKSIAMLAQQvdfntnlSLDELINKNLSEIYE 96
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLA-ANGRIggsATFNGREILNLPEK-------ELNKLRAEQISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 97 ----ALNKYENLQAKLATHLdnkNLHKEINNLINFIESK---DAWNIEQKKER---FLKEFklfeyknrpisslSGGEIR 166
Cdd:PRK09473 105 dpmtSLNPYMRVGEQLMEVL---MLHKGMSKAEAFEESVrmlDAVKMPEARKRmkmYPHEF-------------SGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 167 KINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVtvqaQIMTLLNELKREFNTAIIMITHD 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-192 |
5.12e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI----------IRQNDKSIAMLAQQVDFNTNLSLDELIn 88
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsilgqptrqaLQKNLVAYVPQSEEVDWSFPVLVEDVV- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 89 knlseiyeALNKYENLqaklathldnknlhkeinNLINFIESKDawniEQKKERFLKEFKLFEYKNRPISSLSGGEIRKI 168
Cdd:PRK15056 102 --------MMGRYGHM------------------GWLRRAKKRD----RQIVTAALARVDMVEFRHRQIGELSGGQKKRV 151
|
170 180
....*....|....*....|....
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDV 192
Cdd:PRK15056 152 FLARAIAQQGQVILLDEPFTGVDV 175
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
325-508 |
5.19e-08 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 55.11 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 325 NKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI------------KNADI 392
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiQQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 KIGYfdQARAmLNSDKSLielfcpngGDRVqvrghdmhiyGY-LKSFLFPKE-----------------FLSQAVSVLSG 454
Cdd:PRK11432 81 CMVF--QSYA-LFPHMSL--------GENV----------GYgLKMLGVPKEerkqrvkealelvdlagFEDRYVDQISG 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 455 GEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKGAL----IFVSHDR 508
Cdd:PRK11432 140 GQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFnitsLYVTHDQ 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
341-502 |
5.26e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.50 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK------NADIK---IGYFDQARAMLNSDKSLI 411
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqptRQALQknlVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 ElfcpnggDRVQvrghdMHIYGYLKSFLFPK-----------------EFLSQAVSVLSGGEKNRVALALLFTKDYDVLI 474
Cdd:PRK15056 98 E-------DVVM-----MGRYGHMGWLRRAKkrdrqivtaalarvdmvEFRHRQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190
....*....|....*....|....*....|..
gi 1751968159 475 LDEPTNDLDIAT----INILEEYLMEFKGALI 502
Cdd:PRK15056 166 LDEPFTGVDVKTeariISLLRELRDEGKTMLV 197
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
341-530 |
5.77e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFkNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADikiGYFD--------QARAM--------- 403
Cdd:PRK11124 14 AHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG---NHFDfsktpsdkAIRELrrnvgmvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 -------LNSDKSLIELFCPNGG-DRVQVRGHDMHIYGYLKSFLFPKEFLSQavsvLSGGEKNRVALALLFTKDYDVLIL 475
Cdd:PRK11124 90 qynlwphLTVQQNLIEAPCRVLGlSKDQALARAEKLLERLRLKPYADRFPLH----LSGGQQQRVAIARALMMEPQVLLF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 476 DEPTNDLD--IAT--INILEEyLMEFKGALIFVSHDRYFVDKLATKLYVFENGVInIEH 530
Cdd:PRK11124 166 DEPTAALDpeITAqiVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHI-VEQ 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
347-540 |
6.92e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 53.64 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADI----------KIGYFDQARAMLN-SDKSLIEL 413
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRvlVDGHDLaladpawlrrQVGVVLQENVLFNrSIRDNIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 FCPnggdrvqvrGHDMHIYGYLKSFLFPKEFLS------------QAVSvLSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:cd03252 99 ADP---------GMSMERVIEAAKLAGAHDFISelpegydtivgeQGAG-LSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 482 LDIATINILEEYLMEF-KGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:cd03252 169 LDYESEHAIMRNMHDIcAGRTVIIIAHRLSTVKNADRIIVMEKGRI-VEQGSHDELLAEN 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
341-530 |
7.20e-08 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFkNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADikiGYFD--------QARAM--------- 403
Cdd:COG4161 14 SHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG---HQFDfsqkpsekAIRLLrqkvgmvfq 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 -------LNSDKSLIELFCP-NGGDRVQVRGHDMHIYGYL----KSFLFPKEflsqavsvLSGGEKNRVALALLFTKDYD 471
Cdd:COG4161 90 qynlwphLTVMENLIEAPCKvLGLSKEQAREKAMKLLARLrltdKADRFPLH--------LSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 472 VLILDEPTNDLDIATINILEEYLMEFKGALI---FVSHDRYFVDKLATKLYVFENGVInIEH 530
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGItqvIVTHEVEFARKVASQVVYMEKGRI-IEQ 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-214 |
7.31e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.27 E-value: 7.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI---------IRQND--KSIAMLAQQ-------V 75
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSIlidgvdiskIGLHDlrSRISIIPQDpvlfsgtI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 DFNtnlsLDELINKNLSEIYEALNKyenlqaklaTHLdnKNLHKEINNLINFIESKDAWNieqkkerflkefklfeyknr 155
Cdd:cd03244 95 RSN----LDPFGEYSDEELWQALER---------VGL--KEFVESLPGGLDTVVEEGGEN-------------------- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 156 pissLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKN--SKICVIFISH 214
Cdd:cd03244 140 ----LSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREafKDCTVLTIAH 196
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-270 |
7.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.35 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDeINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGrIIRQNDKSIAMLAQQVDFNTnlsldelINKNLS 92
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEG-KVTVGDIVVSSTSKQKEIKP-------VRKKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIYEalnkYENLQAKLATHLDNKNLHKEinnliNF-IESKDAWNIEQKKERFLKEFKLFeYKNRPISsLSGGEIRKINLC 171
Cdd:PRK13643 88 VVFQ----FPESQLFEETVLKDVAFGPQ-----NFgIPKEKAEKIAAEKLEMVGLADEF-WEKSPFE-LSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 172 ILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcVIFISHdryFIDNVASRcveieggkisffnGGYAYYLEK 247
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDpkarIEMMQLFESIHQSGQT-VVLVTH---LMDDVADY-------------ADYVYLLEK 219
|
250 260
....*....|....*....|...
gi 1751968159 248 KAQILVSLSKSYETLIKHLKAEE 270
Cdd:PRK13643 220 GHIISCGTPSDVFQEVDFLKAHE 242
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
332-526 |
7.61e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 54.69 E-value: 7.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFD---------QAR- 401
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI--------LIGgrdvtdlppKDRn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 -AML-----------------------NSDKSLIElfcpnggDRVQVRGHDMHIYGYLKSflFPKEflsqavsvLSGGEK 457
Cdd:COG3839 77 iAMVfqsyalyphmtvyeniafplklrKVPKAEID-------RRVREAAELLGLEDLLDR--KPKQ--------LSGGQR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLD----IATINILEEYLMEFKGALIFVSHDRyfVD--KLATKLYVFENGVI 526
Cdd:COG3839 140 QRVALGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHDQ--VEamTLADRIAVMNDGRI 212
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
328-506 |
7.66e-08 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 53.27 E-value: 7.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 328 KMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADI-KIGYFDqaramL 404
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidGVDIsKIGLHD-----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSDKSLIE----LF--------CPNGG----------DRVQvrghdmhiygyLKSFLFPKEFLSQAV-----SVLSGGEK 457
Cdd:cd03244 77 RSRISIIPqdpvLFsgtirsnlDPFGEysdeelwqalERVG-----------LKEFVESLPGGLDTVveeggENLSVGQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 458 NRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLME-FKGA-LIFVSH 506
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREaFKDCtVLTIAH 196
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
332-526 |
9.37e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 54.33 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 332 ELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADI--------KIGYFDQAR 401
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIllDGRDVtglppekrNVGMVFQDY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 A----------------MLNSDKSLIElfcpnggDRVQvrghDM----HIYGYLKSflFPKEflsqavsvLSGGEKNRVA 461
Cdd:COG3842 87 AlfphltvaenvafglrMRGVPKAEIR-------ARVA----ELlelvGLEGLADR--YPHQ--------LSGGQQQRVA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 462 LALLFTKDYDVLILDEPTNDLD----IATINILEEYLMEFKGALIFVSHDRY--FVdkLATKLYVFENGVI 526
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHDQEeaLA--LADRIAVMNDGRI 214
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
355-520 |
9.47e-08 |
|
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: 51.61 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 355 QGEKIGIVGQNGCGKSTFLKILlnldklssgeiknadikigyfdqARAMLNSDKSLIELFCPNGGDRVQVRGHDMHIYGY 434
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-----------------------ARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 435 LKSflfpkeflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT---------INILEEYLMEFKGALIFVS 505
Cdd:smart00382 58 KAS--------------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTT 123
|
170
....*....|....*
gi 1751968159 506 HDRYFVDKLATKLYV 520
Cdd:smart00382 124 NDEKDLGPALLRRRF 138
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
361-507 |
1.03e-07 |
|
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: 51.98 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 361 IVGQNGCGKSTFLK-ILLNLDKLSSGEIKNADIKIGYFdqaramlnsdKSLIELFcpnggdrvqvrghdmhiygylksFL 439
Cdd:cd03227 26 ITGPNGSGKSTILDaIGLALGGAQSATRRRSGVKAGCI----------VAAVSAE-----------------------LI 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 440 FpkeFLSQavsvLSGGEKNRVALALLF----TKDYDVLILDEPTNDLDIATINILEEYLMEF--KGA-LIFVSHD 507
Cdd:cd03227 73 F---TRLQ----LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAqVIVITHL 140
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
329-483 |
1.06e-07 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 53.07 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 329 MIfELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI---------KNADI-----KI 394
Cdd:COG1126 1 MI-EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTItvdgedltdSKKDInklrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 395 GY-F-------------------------------DQARAMLnsdkslielfcpnggDRVQVRGHdMHIYgylksflfPK 442
Cdd:COG1126 80 GMvFqqfnlfphltvlenvtlapikvkkmskaeaeERAMELL---------------ERVGLADK-ADAY--------PA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1751968159 443 EflsqavsvLSGGEKNRV----ALALlftkDYDVLILDEPTNDLD 483
Cdd:COG1126 136 Q--------LSGGQQQRVaiarALAM----EPKVMLFDEPTSALD 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
1.14e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII--RQN-DKSIAMLAQQVDF-- 77
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfeRQSiKKDLCTYQKQLCFvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 -----NTNLSLDElinknlseiyealNKYENLqaklatHLDNKNLhkEINNLINFieskdawnieqkkerflkeFKLFEY 152
Cdd:PRK13540 81 hrsgiNPYLTLRE-------------NCLYDI------HFSPGAV--GITELCRL-------------------FSLEHL 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 1751968159 153 KNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:PRK13540 121 IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
343-506 |
1.30e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.50 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIKigyfdQARAMLNSDksLieLFCpnggd 420
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVlwQGEPIR-----RQRDEYHQD--L--LYL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 rvqvrGHdmhiYGYLKSFLFPKEFLS---------------QA-------------VSVLSGGEKNRVALALLFTKDYDV 472
Cdd:PRK13538 80 -----GH----QPGIKTELTALENLRfyqrlhgpgddealwEAlaqvglagfedvpVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1751968159 473 LILDEPTNDLDIATINILEEYLMEF---KGALIFVSH 506
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-214 |
1.52e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAMlaqqvdfNTNlsldeliNKNLsei 94
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV-TIGERVITA-------GKK-------NKKL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 yEALNKYENLQAKLATH-LDNKNLHKEIN-NLINF-IESKDAwniEQKKERFLKEFKLFE-YKNRPISSLSGGEIRKINL 170
Cdd:PRK13634 81 -KPLRKKVGIVFQFPEHqLFEETVEKDICfGPMNFgVSEEDA---KQKAREMIELVGLPEeLLARSPFELSGGQMRRVAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 171 C-ILVLQnPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISH 214
Cdd:PRK13634 157 AgVLAME-PEVLVLDEPTAGLDPKgrkeMMEMFYKLHKEKGLTTVLVTH 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
355-526 |
1.54e-07 |
|
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: 54.42 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 355 QGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIG------Y-------------FD------------QARAM 403
Cdd:COG4615 357 RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTadnreaYrqlfsavfsdfhlFDrllgldgeadpaRAREL 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 LNsdksLIELfcpngGDRVQVRGHdmhiygylksflfpkEFLSQAvsvLSGGEKNRVAL--ALLftKDYDVLILDEPTND 481
Cdd:COG4615 437 LE----RLEL-----DHKVSVEDG---------------RFSTTD---LSQGQRKRLALlvALL--EDRPILVFDEWAAD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 482 LDIATINIL-EEYLMEFK--G-ALIFVSHD-RYFvdKLATKLYVFENGVI 526
Cdd:COG4615 488 QDPEFRRVFyTELLPELKarGkTVIAISHDdRYF--DLADRVLKMDYGKL 535
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-222 |
1.65e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.85 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 21 EINFSANENekiAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQND----KSIAMLAQQVDFNTNLSLDELINKNLS-EIY 95
Cdd:COG3593 18 SIELSDDLT---VLVGENNSGKSSILEALRLLLGPSSSRKFDEEDfylgDDPDLPEIEIELTFGSLLSRLLRLLLKeEDK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 96 EAL-NKYENLQAKLATHLdnknlhKEINNLINFIESKDAWNIE-------QKKERFLKEFKLF--EYKNRPISSLSGGEI 165
Cdd:COG3593 95 EELeEALEELNEELKEAL------KALNELLSEYLKELLDGLDlelelslDELEDLLKSLSLRieDGKELPLDRLGSGFQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 166 R--KINLCILVLQ-----NPDVLLLDEPTNHLDVYMCEFLEKLLKN---SKICVIFISHDRYFIDNV 222
Cdd:COG3593 169 RliLLALLSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKElseKPNQVIITTHSPHLLSEV 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-237 |
1.70e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.90 E-value: 1.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIamlaqqvdfntnLSLDELINKNLSEIyeal 98
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV------------IAISAGLSGQLTGI---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 nkyENLQAK-LATHLDNKNLHKEINNLINFIEskdawnieqkkerflkefkLFEYKNRPISSLSGGEIRKINLCILVLQN 177
Cdd:PRK13546 104 ---ENIEFKmLCMGFKRKEIKAMTPKIIEFSE-------------------LGEFIYQPVKKYSSGMRAKLGFSINITVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 178 PDVLLLDEPtnhLDVYMCEFLEKLL------KNSKICVIFISHDRYFIDNVASRCVEIEGGKISFF 237
Cdd:PRK13546 162 PDILVIDEA---LSVGDQTFAQKCLdkiyefKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
160-526 |
1.71e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 54.31 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 160 LSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHD----RYFIDNVA----SRCV 227
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTvqaqILDLLKDLQRELGMALLLITHDlgvvRRFADRVAvmrqGEIV 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 228 EiEGgkisffnggyayyleKKAQILVSLSKSYeTliKHLKAEEEwlrRGVKARLkrnegrkerifkmREEAKknpgeikr 307
Cdd:COG4172 237 E-QG---------------PTAELFAAPQHPY-T--RKLLAAEP---RGDPRPV-------------PPDAP-------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 308 lklELLRANS-----SIQKPNFNKQKMIFELVNaskiinnkilfkNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKl 382
Cdd:COG4172 274 ---PLLEARDlkvwfPIKRGLFRRTVGHVKAVD------------GVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 383 SSGEIKNADIKIGYFDQaRAM--LNSD---------KSL-------------IELFCPnGGDRVQVRGH----------- 427
Cdd:COG4172 338 SEGEIRFDGQDLDGLSR-RALrpLRRRmqvvfqdpfGSLsprmtvgqiiaegLRVHGP-GLSAAERRARvaealeevgld 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 428 --DMHIYgylksflfPKEFlsqavsvlSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGAL 501
Cdd:COG4172 416 paARHRY--------PHEF--------SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVqaqiLDLLRDLQREHGLAY 479
|
410 420
....*....|....*....|....*
gi 1751968159 502 IFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:COG4172 480 LFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
435-528 |
1.78e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 53.09 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 435 LKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT----INILEEYLMEFKGALIFVSHDRYF 510
Cdd:PRK13645 134 LKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQ 213
|
90
....*....|....*....
gi 1751968159 511 VDKLATKLYVFENG-VINI 528
Cdd:PRK13645 214 VLRIADEVIVMHEGkVISI 232
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
352-484 |
1.78e-07 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 53.69 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 352 RILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAR-----AMLNSDKSL---------IEL---- 413
Cdd:PRK09536 25 SVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasrrvASVPQDTSLsfefdvrqvVEMgrtp 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 414 ----FCPNG-GDRVQVRgHDMHIYGYlksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDI 484
Cdd:PRK09536 105 hrsrFDTWTeTDRAAVE-RAMERTGV-------AQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-220 |
1.88e-07 |
|
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: 52.75 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 34 IIGKNGEGKSTLLKAIFGTLQLDSGRiirqndksiamlaqqvdFNTNLSLDELINK-NLSEIYEALNKYENLQAKLATHL 112
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGK-----------------FDDPPDWDEILDEfRGSELQNYFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 113 DNKNL-HKEIN-NLINFIESKDAWNieqKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHL 190
Cdd:cd03236 94 QYVDLiPKAVKgKVGELLKKKDERG---KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|....
gi 1751968159 191 DVY----MCEFLEKLLKNSKiCVIFISHDRYFID 220
Cdd:cd03236 171 DIKqrlnAARLIRELAEDDN-YVLVVEHDLAVLD 203
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
323-526 |
2.24e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.41 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 323 NFNKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigyfdqara 402
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 MLnsdkslielfcpNGGDRVQVRGHDMHIYGYLKSF-LFP-----------------------------------KEFLS 446
Cdd:PRK09452 72 ML------------DGQDITHVPAENRHVNTVFQSYaLFPhmtvfenvafglrmqktpaaeitprvmealrmvqlEEFAQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 447 QAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDiatINILEEYLMEFKG-------ALIFVSHDRYFVDKLATKLY 519
Cdd:PRK09452 140 RKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD---YKLRKQMQNELKAlqrklgiTFVFVTHDQEEALTMSDRIV 216
|
....*..
gi 1751968159 520 VFENGVI 526
Cdd:PRK09452 217 VMRDGRI 223
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-220 |
2.31e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFgtlqldsGRIIRQNDKSIAMLaQQVDFNTN 80
Cdd:COG2401 28 AIVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALKGTPVAGCVDV-PDNQFGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDE--LINKNLSEIYEALNkyenlQAKLAthldnknlhkeinnlinfieskDAWNieqkkerFLkefklfeyknRPIS 158
Cdd:COG2401 100 ASLIDaiGRKGDFKDAVELLN-----AVGLS----------------------DAVL-------WL----------RRFK 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEF----LEKLLKNSKICVIFISHDRYFID 220
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRvarnLQKLARRAGITLVVATHHYDVID 201
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
347-483 |
2.43e-07 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 52.09 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAraMLNSDKSLI----ELF-------- 414
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK--YLHSKVSLVgqepVLFarslqdni 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 415 ------CPNggDRVQVRGHDMHIYGYLKSF-LFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:cd03248 109 ayglqsCSF--ECVKEAAQKAHAHSFISELaSGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALD 182
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
341-518 |
2.44e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 2.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAM--------LNSDKSLIE 412
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMaylghlpgLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 ---LFCPNGGDRV-QVRGHDMHIYGYlksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:PRK13543 102 nlhFLCGLHGRRAkQMPGSALAIVGL-------AGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
|
170 180 190
....*....|....*....|....*....|...
gi 1751968159 489 ILEEYL---MEFKGALIFVSHDRYFVDKLATKL 518
Cdd:PRK13543 175 LVNRMIsahLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-234 |
2.75e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKII----LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLdSGRIIrqndksiamlAQQVD 76
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVM----------AEKLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 77 FNTN--LSLDE-----LINKNLSEIYE----ALNK-----YENLQAkLATHL--DNKNLHKEINNLINFIESKDAwnieq 138
Cdd:PRK11022 70 FNGQdlQRISEkerrnLVGAEVAMIFQdpmtSLNPcytvgFQIMEA-IKVHQggNKKTRRQRAIDLLNQVGIPDP----- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 139 kkerflkEFKLFEYKNRpissLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISH 214
Cdd:PRK11022 144 -------ASRLDVYPHQ----LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITH 212
|
250 260
....*....|....*....|
gi 1751968159 215 DRYFIDNVASRCVEIEGGKI 234
Cdd:PRK11022 213 DLALVAEAAHKIIVMYAGQV 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-229 |
2.99e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.47 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIamlaqqvdfnTNLSLDELINKNLSEI 94
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTV-TVDDITI----------THKTKDKYIRPVRKRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALNKYEnlqaklaTHLDNKNLHKEINnlinFIESKDAWNIEQKKERFLKEFKLFEYKNRPISS----LSGGEIRKINL 170
Cdd:PRK13646 88 GMVFQFPE-------SQLFEDTVEREII----FGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQspfqMSGGQMRKIAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 171 CILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDryfIDNVASRCVEI 229
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDpqskRQVMRLLKSLQTDENKTIILVSHD---MNEVARYADEV 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-229 |
3.23e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiaMLAQQVDFNTNlslDELINK 89
Cdd:PRK10982 5 SKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL--------FQGKEIDFKSS---KEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NLSEIYEALNkyenlQAKLATHLDNKNLHKeinnlinfiESKDAWNIEQKK-----ERFLKEFKLFEYKNRPISSLSGGE 164
Cdd:PRK10982 74 GISMVHQELN-----LVLQRSVMDNMWLGR---------YPTKGMFVDQDKmyrdtKAIFDELDIDIDPRAKVATLSVSQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 165 IRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDryfIDNVASRCVEI 229
Cdd:PRK10982 140 MQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIirkLKERGCGIVYISHK---MEEIFQLCDEI 204
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-191 |
3.24e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 52.09 E-value: 3.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFgtlqldsgriiRQNdksiamlaqqvDFNTNLSLDELINKNLS 92
Cdd:PRK14239 15 YNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSIN-----------RMN-----------DLNPEVTITGSIVYNGH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIYealnkyenlqaklATHLDNKNLHKEINNL--------------------INFIesKDAWNIEQKKERFLKEFKLF-E 151
Cdd:PRK14239 73 NIY-------------SPRTDTVDLRKEIGMVfqqpnpfpmsiyenvvyglrLKGI--KDKQVLDEAVEKSLKGASIWdE 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1751968159 152 YKNRPISS---LSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:PRK14239 138 VKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
280-506 |
3.84e-07 |
|
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: 53.21 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 280 RLKRNEGRKERIFKMREEAKKNPGEIKRLKLEllranssiqkpnFNKQKMIFElvNASKII-NNKILFKNFSTRILQGEK 358
Cdd:TIGR00954 415 SGNFKRPRVEEIESGREGGRNSNLVPGRGIVE------------YQDNGIKFE--NIPLVTpNGDVLIESLSFEVPSGNN 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 359 IGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYFDQARAMlnSDKSLIE-LFCPNGGDRVQVRG-HDMHIYGYL 435
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLtKPAKGKLFYVPQRPYM--TLGTLRDqIIYPDSSEDMKRRGlSDKDLEQIL 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 436 K----SFLFPKEFLSQAVS----VLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKGALIFVSH 506
Cdd:TIGR00954 559 DnvqlTHILEREGGWSAVQdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
347-524 |
3.92e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 3.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigyfdQARAML--NSDKSLIELFCPNGGDRVQV 424
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLV-----------QCDKMLlrRRSRQVIELSEQSAAQMRHV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 425 RGHDM-HIYGYLKSFLFP---------------------------------------KEFLSQAVSVLSGGEKNRVALAL 464
Cdd:PRK10261 102 RGADMaMIFQEPMTSLNPvftvgeqiaesirlhqgasreeamveakrmldqvripeaQTILSRYPHQLSGGMRQRVMIAM 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 465 LFTKDYDVLILDEPTNDLDIAT-------INILEEylmEFKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK10261 182 ALSCRPAVLIADEPTTALDVTIqaqilqlIKVLQK---EMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-191 |
4.13e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 52.90 E-value: 4.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IR---QND--KSIAMLAQQ-VDFNTNlslde 85
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRIlidgqdIRdvtQASlrAAIGIVPQDtVLFNDT----- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 86 lINKNL---------SEIYEAlnkyenlqAKLAtHLDnknlhkeinnliNFIES-KDAWNIeQKKERFLKefklfeyknr 155
Cdd:COG5265 448 -IAYNIaygrpdaseEEVEAA--------ARAA-QIH------------DFIESlPDGYDT-RVGERGLK---------- 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 1751968159 156 pissLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:COG5265 495 ----LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
360-524 |
4.45e-07 |
|
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: 52.41 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 360 GIVGQNGCGKSTFLKILLNLDKLSSGEIK---------NADI-------KIGY-FDQARamlnsdkslieLF-------- 414
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevlqdsARGIflpphrrRIGYvFQEAR-----------LFphlsvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 -------CPNGGDRVQVR--------GHdmhiygylksflfpkeFLSQAVSVLSGGEKNRVAL--ALLftKDYDVLILDE 477
Cdd:COG4148 98 llygrkrAPRAERRISFDevvellgiGH----------------LLDRRPATLSGGERQRVAIgrALL--SSPRLLLMDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 478 PTNDLDIATIN-ILeEYLM----EFKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:COG4148 160 PLAALDLARKAeIL-PYLErlrdELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
348-507 |
4.47e-07 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 51.29 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIkigyfdqarAMLNSDK---SLI----ELFC--- 415
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIlwNGQDL---------TALPPAErpvSMLfqenNLFPhlt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 416 --------------PNGGDRVQVRG--HDMHIYGYLKSFlfPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:COG3840 88 vaqniglglrpglkLTAEQRAQVEQalERVGLAGLLDRL--PGQ--------LSGGQRQRVALARCLVRKRPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|..
gi 1751968159 480 NDLDIA----TINILEEYLMEFKGALIFVSHD 507
Cdd:COG3840 158 SALDPAlrqeMLDLVDELCRERGLTVLMVTHD 189
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-215 |
4.68e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDkSIAMLAQQVDFNtnls 82
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGE-NIPAMSRSRLYT---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 ldelINKNLSEIYEA------LNKYENLQAKLA--THLDNKNLHKEINNLINFIESKDAWNIeqkkerflkefklfeykn 154
Cdd:PRK11831 82 ----VRKRMSMLFQSgalftdMNVFDNVAYPLRehTQLPAPLLHSTVMMKLEAVGLRGAAKL------------------ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 155 RPiSSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSKICV--IFISHD 215
Cdd:PRK11831 140 MP-SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISelNSALGVtcVVVSHD 203
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
227-306 |
5.21e-07 |
|
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: 47.57 E-value: 5.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 227 VEIEGGKISFFNGGYAYYLEKKAQILVSLSKSYETLIKHLKAEEEWLRR-GVKARL-KRNEGRKERIFKMREEAKKNPGE 304
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRfRAKASKaKQAQSRIKALEKMERIEKPERDK 80
|
..
gi 1751968159 305 IK 306
Cdd:pfam12848 81 PK 82
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
347-507 |
5.99e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIKIGYFDQARAML-----NSDK----SLIELFC 415
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfyNNQAITDDNFEKLRKHIgivfqNPDNqfvgSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 416 PNGGDRVQVRGHDMHiyGYLKSFLFPKEFLSQAVS---VLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT----IN 488
Cdd:PRK13648 106 AFGLENHAVPYDEMH--RRVSEALKQVDMLERADYepnALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnlLD 183
|
170
....*....|....*....
gi 1751968159 489 ILEEYLMEFKGALIFVSHD 507
Cdd:PRK13648 184 LVRKVKSEHNITIISITHD 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
334-512 |
7.09e-07 |
|
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: 49.63 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 334 VNASKIINNKIlfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNldklSSGEIKNADIKIGYFDQARAMLNSDKSLIel 413
Cdd:cd03238 1 LTVSGANVHNL--QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISFLPKFSRNKLIFIDQLQFLI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 414 fcpnggdrvqvrghDMHIyGYLKsflfpkefLSQAVSVLSGGEKNRVALA--LLFTKDYDVLILDEPTNDLDIATINILE 491
Cdd:cd03238 73 --------------DVGL-GYLT--------LGQKLSTLSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....
gi 1751968159 492 EY---LMEFKGALIFVSHDRYFVD 512
Cdd:cd03238 130 EVikgLIDLGNTVILIEHNLDVLS 153
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-206 |
7.68e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII---RQNDKSI----------------AMLAQQVDFN 78
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindSHNLKDInlkwwrskigvvsqdpLLFSNSIKNN 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 TNLSL---------DELINKNLSEIYEALNKYENLQAKLATHLDNKNLHKEINNLI----NFIESKDAWNIEQKKERFLK 145
Cdd:PTZ00265 480 IKYSLyslkdlealSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIemrkNYQTIKDSEVVDVSKKVLIH 559
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 146 EF------KLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK 206
Cdd:PTZ00265 560 DFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-234 |
8.15e-07 |
|
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: 50.51 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKF----GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiaMLAQQvDF 77
Cdd:COG4181 7 PIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTV---------RLAGQ-DL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 NTnlsLDE-------------------LINkNLSeiyeALnkyEN--LQAKLATHldnknlhkeinnlinfiesKDAwni 136
Cdd:COG4181 77 FA---LDEdararlrarhvgfvfqsfqLLP-TLT----AL---ENvmLPLELAGR-------------------RDA--- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 137 EQKKERFLKEFKLFE-YKNRPiSSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIF 211
Cdd:COG4181 124 RARARALLERVGLGHrLDHYP-AQLSGGEQQRVALARAFATEPAILFADEPTGNLDaatgEQIIDLLFELNRERGTTLVL 202
|
250 260
....*....|....*....|....*.
gi 1751968159 212 ISHDRyfidNVASRC---VEIEGGKI 234
Cdd:COG4181 203 VTHDP----ALAARCdrvLRLRAGRL 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-187 |
8.39e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIamlaqqVDFNTN 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVF-DGKDI------TDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 LSLDELIN--KNLSEIYEALNKYENLQaklathldnknlhkeinnLINFIESKDAWniEQKKERFLKEF-KLFEYKNRPI 157
Cdd:PRK11614 76 KIMREAVAivPEGRRVFSRMTVEENLA------------------MGGFFAERDQF--QERIKWVYELFpRLHERRIQRA 135
|
170 180 190
....*....|....*....|....*....|
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPT 187
Cdd:PRK11614 136 GTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
348-524 |
8.74e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 51.75 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSS--GEI--KNADIKI-GYFDQARA---------MLNSDKSLIE- 412
Cdd:TIGR02633 19 GIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIywSGSPLKAsNIRDTERAgiviihqelTLVPELSVAEn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 LFCpngGDRVQVRGHDMHiygYLKSFLFPKEFLSQ----------AVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDL 482
Cdd:TIGR02633 99 IFL---GNEITLPGGRMA---YNAMYLRAKNLLRElqldadnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1751968159 483 DIATINILEEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
347-526 |
9.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.85 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYfdqaramlnSDKSLIE-------------- 412
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY---------DKKSLLEvrktvgivfqnpdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 -LFCP-----------NGG---DRVQVRGHDMhiygyLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDE 477
Cdd:PRK13639 90 qLFAPtveedvafgplNLGlskEEVEKRVKEA-----LKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 478 PTNDLD----IATINILeeYLMEFKGALIFVS-HDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13639 164 PTSGLDpmgaSQIMKLL--YDLNKEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-191 |
9.04e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 50.81 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKA------------IFGTLQLDsGRIIRQND-------KSIAMLAQ 73
Cdd:COG1117 21 YGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlipgarVEGEILLD-GEDIYDPDvdvvelrRRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 74 QvdfnTN---LSLdelinknlseiyealnkYENLQAKLATH-LDNKNLHKEInnlinfIES--KDA--WNieqkkerflk 145
Cdd:COG1117 100 K----PNpfpKSI-----------------YDNVAYGLRLHgIKSKSELDEI------VEEslRKAalWD---------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 146 efklfEYKNR---PISSLSGGEIRKinLCI---LVLQnPDVLLLDEPTNHLD 191
Cdd:COG1117 143 -----EVKDRlkkSALGLSGGQQQR--LCIaraLAVE-PEVLLMDEPTSALD 186
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
331-526 |
9.09e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINN----KILFkNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI-------------- 392
Cdd:PRK13643 4 FEKVNYTYQPNSpfasRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 --KIGY-FDQARAMLNSDKSLIEL-FCP-NGG----DRVQVRGHDMHIYGylksflFPKEFLSQAVSVLSGGEKNRVALA 463
Cdd:PRK13643 83 rkKVGVvFQFPESQLFEETVLKDVaFGPqNFGipkeKAEKIAAEKLEMVG------LADEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 464 LLFTKDYDVLILDEPTNDLD-IATINILE--EYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDpKARIEMMQlfESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
340-540 |
1.13e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 50.34 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 340 INNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDK--LSSGEI--KNADI---------KIGYF--------- 397
Cdd:TIGR01978 10 VEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTIlfKGQDLlelepderaRAGLFlafqypeei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 ------DQARAMLNSDKSlielfcPNGGDRVQVRGHDMHIYGYLKSFLFPKEFLSQAVSV-LSGGEKNRVALALLFTKDY 470
Cdd:TIGR01978 90 pgvsnlEFLRSALNARRS------ARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 471 DVLILDEPTNDLDIATINILEEYLMEFKG---ALIFVSHDRYFVDKLA-TKLYVFENGVINIE-HMSYTQYLERE 540
Cdd:TIGR01978 164 KLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSgDVELAKELEAK 238
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-60 |
1.15e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.72 E-value: 1.15e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI 60
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI 65
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
347-507 |
1.16e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNAdikigyfDQARAMLNSDkSLIELFCPNGGDRVQvRG 426
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-------GQDVATLDAD-ALAQLRREHFGFIFQ-RY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 427 HDM-H-----------IYGYLKSflfpKEFLSQAV----------------SVLSGGEKNRVALALLFTKDYDVLILDEP 478
Cdd:PRK10535 96 HLLsHltaaqnvevpaVYAGLER----KQRLLRAQellqrlgledrveyqpSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
170 180 190
....*....|....*....|....*....|...
gi 1751968159 479 TNDLD----IATINILEEyLMEFKGALIFVSHD 507
Cdd:PRK10535 172 TGALDshsgEEVMAILHQ-LRDRGHTVIIVTHD 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
356-529 |
1.33e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.50 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 356 GEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGYFDQARAMLN-SDKSLIELFCPNGGD-- 420
Cdd:PRK13657 361 GQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILidGTDIRtvtraslrrnIAVVFQDAGLFNrSIEDNIRVGRPDATDee 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 ------RVQvrGHDmhiygylksFLFPKEFLSQAV-----SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATini 489
Cdd:PRK13657 441 mraaaeRAQ--AHD---------FIERKPDGYDTVvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVET--- 506
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1751968159 490 lEEYLmefKGALIFVSHDR-YFV--DKLAT-----KLYVFENGVInIE 529
Cdd:PRK13657 507 -EAKV---KAALDELMKGRtTFIiaHRLSTvrnadRILVFDNGRV-VE 549
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-192 |
1.63e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 51.12 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRqnDKSIAMLAQQ--VDFNTNLSLDELINKN 90
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRIlidgtdIR--TVTRASLRRNiaVVFQDAGLFNRSIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 91 LS---------EIYEAlnkyenlqAKLATHLDnknlhkeinnlinFIESKDAWNIEQKKERFlkefklfeyknrpiSSLS 161
Cdd:PRK13657 429 IRvgrpdatdeEMRAA--------AERAQAHD-------------FIERKPDGYDTVVGERG--------------RQLS 473
|
170 180 190
....*....|....*....|....*....|.
gi 1751968159 162 GGEIRKINLCILVLQNPDVLLLDEPTNHLDV 192
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDV 504
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
19-234 |
1.64e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 50.12 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI----IRQNDKSIAMLAQQVDFNTNLSLDELINknlSEI 94
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgREVNAENEKWVRSKVGLVFQDPDDQVFS---STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEalnkyenlqaKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILV 174
Cdd:PRK13647 98 WD----------DVAFGPVNMGLDKD--------------EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 175 LQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKIcVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDprgqETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-233 |
1.65e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 50.60 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiaMLAQQvdfntNLS 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI---------MLDGV-----DLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNLSEIYE--ALNKYENLQAKLATHLDNKNLHKEinnlinfieskdawNIEQKKERFLKEFKLFEYKNRPISSL 160
Cdd:PRK11607 85 HVPPYQRPINMMFQsyALFPHMTVEQNIAFGLKQDKLPKA--------------EIASRVNEMLGLVHMQEFAKRKPHQL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 161 SGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYM-----CEFLEKLLKNSKICVIfISHDRYFIDNVASRCVEIEGGK 233
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmqLEVVDILERVGVTCVM-VTHDQEEAMTMAGRIAIMNRGK 227
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
348-507 |
1.85e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRilQGEKIGIVGQNGCGKS-TFLKI--------------------LLNL-----DKLSSGEIK----------NAD 391
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSqTAFALmgllaangriggsatfngreILNLpekelNKLRAEQISmifqdpmtslNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 392 IKIG-----------YFDQARAMLNSDKSLIELFCPNGGDRVQvrghdmhiygylksfLFPKEFlsqavsvlSGGEKNRV 460
Cdd:PRK09473 114 MRVGeqlmevlmlhkGMSKAEAFEESVRMLDAVKMPEARKRMK---------------MYPHEF--------SGGMRQRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 461 --ALALLFTKDydVLILDEPTNDLDI---ATI-NILEEYLMEFKGALIFVSHD 507
Cdd:PRK09473 171 miAMALLCRPK--LLIADEPTTALDVtvqAQImTLLNELKREFNTAIIMITHD 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-507 |
1.98e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 33 AIIGKNGEGKSTLLKAIFGTLQLDSGriirqndkSIAMLAQQVDFNTNLSLDElinKNLSEIYEALNKYENLqaklaTHL 112
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAG--------SILYLGKEVTFNGPKSSQE---AGIGIIHQELNLIPQL-----TIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 113 DNKNLHKEINNLINFIESKDAWnieQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV 192
Cdd:PRK10762 98 ENIFLGREFVNRFGRIDWKKMY---AEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 193 YMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIEGGKisfFNGgyayylEKKAQILvslskSYETLIKHL--- 266
Cdd:PRK10762 175 TETESLFRVireLKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ---FIA------EREVADL-----TEDSLIEMMvgr 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 267 KAEEEWLRrgvkarlkrnegrkerifkmreeAKKNPGEiKRLKLELLrANSSIQkpnfnkqkmifelvNASkiinnkilf 346
Cdd:PRK10762 241 KLEDQYPR-----------------------LDKAPGE-VRLKVDNL-SGPGVN--------------DVS--------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 knFSTRilQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK-----------IGYFDQAR-------AM-LN 405
Cdd:PRK10762 273 --FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTldGHEVVtrspqdglangIVYISEDRkrdglvlGMsVK 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 406 SDKSLIEL--FCPNGGdrvQVRGHD--MHIYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALAL-LFTKDyDVLILDEPTN 480
Cdd:PRK10762 349 ENMSLTALryFSRAGG---SLKHADeqQAVSDFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARgLMTRP-KVLILDEPTR 424
|
490 500 510
....*....|....*....|....*....|
gi 1751968159 481 DLDIATINILEEYLMEFKG---ALIFVSHD 507
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
347-507 |
2.00e-06 |
|
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: 49.56 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADIkigyfdqaRAMlnSDKSLIELfcpnggdrvqv 424
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvlIDGQDI--------AAM--SRKELREL----------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 425 RGHDMHIYgyLKSF-LFP-------------------KEFLSQAVSV----------------LSGGEKNRVALALLFTK 468
Cdd:cd03294 100 RRKKISMV--FQSFaLLPhrtvlenvafglevqgvprAEREERAAEAlelvglegwehkypdeLSGGMQQRVGLARALAV 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1751968159 469 DYDVLILDEPTNDLDIATINILEEYLM----EFKGALIFVSHD 507
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLrlqaELQKTIVFITHD 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
452-530 |
2.18e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.31 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 452 LSGGEKNR--VALALLftKDYDVLILDEPTNDLD-IATINILE--EYLMEFKG-ALIFVSHDRYFVDKLATKLYVFENGV 525
Cdd:PRK10418 141 MSGGMLQRmmIALALL--CEAPFIIADEPTTDLDvVAQARILDllESIVQKRAlGMLLVTHDMGVVARLADDVAVMSHGR 218
|
....*
gi 1751968159 526 InIEH 530
Cdd:PRK10418 219 I-VEQ 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
15-215 |
2.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 49.80 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 15 EKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSgriirqNDKSIamlaqqvdfnTNLSLDELINKNLSEI 94
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD------NPNSK----------ITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YEALN-KYENLqaklathlDNKNLHKEINNLINF-IESKDAWNIEQKK--ERFLKEFKLFEYKNRPISSLSGGEIRKINL 170
Cdd:PRK13640 83 REKVGiVFQNP--------DNQFVGATVGDDVAFgLENRAVPRPEMIKivRDVLADVGMLDYIDSEPANLSGGQKQRVAI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 171 CILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD 203
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
2.29e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 2 ALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFG----------TL---QLDSGRIIRQNDKSI 68
Cdd:PRK10938 259 PRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTLfgrRRGSGETIWDIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 69 AMLAQQV--DFNTNLSLDELInknLSEIYEALNKYENL---QAKLATH-LDNKNLHKEInnlinfieskdawnieqkker 142
Cdd:PRK10938 339 GYVSSSLhlDYRVSTSVRNVI---LSGFFDSIGIYQAVsdrQQKLAQQwLDILGIDKRT--------------------- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 143 flkefklfeyKNRPISSLSGGEIRkinlciLVL------QNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFI 212
Cdd:PRK10938 395 ----------ADAPFHSLSWGQQR------LALivralvKHPTLLILDEPLQGLDplnrQLVRRFVDVLISEGETQLLFV 458
|
..
gi 1751968159 213 SH 214
Cdd:PRK10938 459 SH 460
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-234 |
2.43e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.62 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLkaifgtlQLDSGRIIRQNDKSIAMlaqqvdfntnlslDELINKNLSEIYEAl 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMI-------QLTNGLIISETGQTIVG-------------DYAIPANLKKIKEV- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 nkyenlqaklathldnKNLHKEINNLINF---------IESKDAWNI----EQKKERFLKEFKLF-------EYKNRPIS 158
Cdd:PRK13645 86 ----------------KRLRKEIGLVFQFpeyqlfqetIEKDIAFGPvnlgENKQEAYKKVPELLklvqlpeDYVKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCE----FLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
330-507 |
2.74e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 49.72 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK------NADI--KIGY----- 396
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgeplDPEDrrRIGYlpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 --------FDQAR--AMLN------SDKSLIELFcpnggDRVQVrghdmhiygylksflfpKEFLSQAVSVLSGGEKNRV 460
Cdd:COG4152 81 glypkmkvGEQLVylARLKglskaeAKRRADEWL-----ERLGL-----------------GDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 461 AL--ALLFtkDYDVLILDEPTNDLDIATINILEEYLMEFK--GA-LIFVSHD 507
Cdd:COG4152 139 QLiaALLH--DPELLILDEPFSGLDPVNVELLKDVIRELAakGTtVIFSSHQ 188
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
345-529 |
3.08e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.20 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI------------KNADIKIGYFDQARAM--------- 403
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIvvngqtinlvrdKDGQLKVADKNQLRLLrtrltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 404 ---LNSDKSLIE--LFCPnggdrVQVRGHDMHIYGYLKSFLFPKEFLSQAVSV-----LSGGEKNRVALALLFTKDYDVL 473
Cdd:PRK10619 100 hfnLWSHMTVLEnvMEAP-----IQVLGLSKQEARERAVKYLAKVGIDERAQGkypvhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 474 ILDEPTNDLD---IATINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIE 529
Cdd:PRK10619 175 LFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEE 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-215 |
3.11e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 50.09 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQlDSGRIIRqNDKSIamlaQQVDFNTNLSLDELINKNLSE 93
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWF-DGQPL----HNLNRRQLLPVRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 94 IYEALNKYENLQAKLATHLdnKNLHKEINnlinfieskdAWNIEQKKERFLKEFKL-FEYKNRPISSLSGGEIRKINLC- 171
Cdd:PRK15134 371 PNSSLNPRLNVLQIIEEGL--RVHQPTLS----------AAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIAr 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1751968159 172 ILVLQnPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHD 215
Cdd:PRK15134 439 ALILK-PSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-240 |
3.26e-06 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.21 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQldsgriiRQNDKSIAMLAQQVDFNTNLsldELINKNLSEIYEAl 98
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYP-------GKFEGNVFINGKPVDIRNPA---QAIRAGIAMVPED- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 NKYENLQAKLAThldNKNLHKEINNLINFIESKDAWNIEQKKERFLKEFKLFEYK-NRPISSLSGGEIRKINLCILVLQN 177
Cdd:TIGR02633 345 RKRHGIVPILGV---GKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 178 PDVLLLDEPTNHLDV---YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI--SFFNGG 240
Cdd:TIGR02633 422 PRVLILDEPTRGVDVgakYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLkgDFVNHA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-214 |
3.50e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 1 MALIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAI-----FGTLqldSGRIIRQNDKSIAmlaqqv 75
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvypHGTY---EGEIIFEGEELQA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 dfnTNLSLDEliNKNLSEIYEALNKYENLqaklaTHLDNKNLHKEI--NNLINFIEskdawnIEQKKERFLKEFKLFEYK 153
Cdd:PRK13549 74 ---SNIRDTE--RAGIAIIHQELALVKEL-----SVLENIFLGNEItpGGIMDYDA------MYLRAQKLLAQLKLDINP 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGG-----EIRK-INlcilvlQNPDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISH 214
Cdd:PRK13549 138 ATPVGNLGLGqqqlvEIAKaLN------KQARLLILDEPTASLTESETAVLLDIirdLKAHGIACIYISH 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
452-530 |
3.73e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 50.07 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 452 LSGGEKNRV----ALALlftkDYDVLILDEPTNDLDIaTI--NILEeyLM-----EFKGALIFVSHDRYFVDKLATKLYV 520
Cdd:COG4172 157 LSGGQRQRVmiamALAN----EPDLLIADEPTTALDV-TVqaQILD--LLkdlqrELGMALLLITHDLGVVRRFADRVAV 229
|
90
....*....|
gi 1751968159 521 FENGVInIEH 530
Cdd:COG4172 230 MRQGEI-VEQ 238
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-214 |
3.84e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIfgtlqldsGRIIRQNDksIAMLAQQVD-FNTNLS 82
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF--------NRLLELNE--EARVEGEVRlFGRNIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDEL----INKNLSEIYEALNKYENLqaklaTHLDNKNLHKEINNLInfiESKDawNIEQKKERFLKEFKLF-EYKNR-- 155
Cdd:PRK14267 75 SPDVdpieVRREVGMVFQYPNPFPHL-----TIYDNVAIGVKLNGLV---KSKK--ELDERVEWALKKAALWdEVKDRln 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 156 -PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK--ICVIFISH 214
Cdd:PRK14267 145 dYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKkeYTIVLVTH 206
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-234 |
4.59e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.03 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKF----GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamlaqqVDFN- 78
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVL-------------VDGQd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 79 -TNLSLDELI--NKNLSEIYEALNKyenLQAKlaTHLDNKNLHKEINNLinfieSKDAwnIEQKKERFLKEFKLFEYKNR 155
Cdd:PRK11153 69 lTALSEKELRkaRRQIGMIFQHFNL---LSSR--TVFDNVALPLELAGT-----PKAE--IKARVTELLELVGLSDKADR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 156 PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSK--ICVIFISHDRYFIDNVASRCVEIEG 231
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRElgLTIVLITHEMDVVKRICDRVAVIDA 216
|
...
gi 1751968159 232 GKI 234
Cdd:PRK11153 217 GRL 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-215 |
5.51e-06 |
|
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: 49.36 E-value: 5.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI------IRQNDK-----SIAMLAQQVDFntnls 82
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadLSQWDReelgrHIGYLPQDVEL----- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 83 LDELINKNLS--------EIYEAlnkyenlqAKLAthldnkNLHKEINNLINFIESkdawnieqkkerflkefklfeykn 154
Cdd:COG4618 418 FDGTIAENIArfgdadpeKVVAA--------AKLA------GVHEMILRLPDGYDT------------------------ 459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 155 rPI----SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVymcEFLEKL------LKNSKICVIFISHD 215
Cdd:COG4618 460 -RIgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDD---EGEAALaaairaLKARGATVVVITHR 526
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
343-486 |
6.18e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 49.43 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK--NADIK----------IGYFDQARAMLN----- 405
Cdd:COG5265 372 PIL-KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILidGQDIRdvtqaslraaIGIVPQDTVLFNdtiay 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 406 ---------SDKSL--------IELF---CPNGGD-RVQVRGhdmhiygyLKsflfpkeflsqavsvLSGGEKNRVALA- 463
Cdd:COG5265 451 niaygrpdaSEEEVeaaaraaqIHDFiesLPDGYDtRVGERG--------LK---------------LSGGEKQRVAIAr 507
|
170 180
....*....|....*....|....
gi 1751968159 464 -LLftKDYDVLILDEPTNDLDIAT 486
Cdd:COG5265 508 tLL--KNPPILIFDEATSALDSRT 529
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-223 |
6.62e-06 |
|
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: 48.51 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQ---LDSGRI-----------------IRQNDksIAMLAQqvD-F 77
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEIlfdgedllklsekelrkIRGRE--IQMIFQ--DpM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 NtnlSLDEL--INKNLSEIYEALNKY--ENLQAKLATHLDNKNLHKEinnlinfieskdawnieqkkERFLKEFklfeyk 153
Cdd:COG0444 97 T---SLNPVmtVGDQIAEPLRIHGGLskAEARERAIELLERVGLPDP--------------------ERRLDRY------ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 154 nrPiSSLSGGEIRKINLCI-LVLqNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD----RYFIDNVA 223
Cdd:COG0444 148 --P-HELSGGMRQRVMIARaLAL-EPKLLIADEPTTALDVtiqaQILNLLKDLQRELGLAILFITHDlgvvAEIADRVA 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
10-73 |
6.69e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 6.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII-RQNDKSIAMLAQ 73
Cdd:PRK11701 13 TKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyRMRDGQLRDLYA 77
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
360-524 |
6.76e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.08 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 360 GIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYfdQARAMLNSDKSLIELFcPNGGDRVQVRGHDMHIYGYLKSFL 439
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLLALRQQVATVF-QDPEQQIFYTDIDSDIAFSLRNLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 440 FPKE-----------------FLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA----TINILEEYLMEFK 498
Cdd:PRK13638 108 VPEAeitrrvdealtlvdaqhFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRRIVAQGN 187
|
170 180
....*....|....*....|....*.
gi 1751968159 499 GALIfVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK13638 188 HVII-SSHDIDLIYEISDAVYVLRQG 212
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
25-220 |
7.55e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 25 SANENEKI-------AIIGKNGEGKSTLLKAIFGTLqldSGRIIRQNDKsiamlaqqvdfntNLSLDELINKNlseiyea 97
Cdd:cd03240 11 SFHERSEIeffspltLIVGQNGAGKTTIIEALKYAL---TGELPPNSKG-------------GAHDPKLIREG------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 98 lnkyENL-QAKLATHLDNKNLHKEINNLINFIESkdawnIEQKKERFlkeFKLFEyknRPISSLSGGEIRKINLCI---- 172
Cdd:cd03240 68 ----EVRaQVKLAFENANGKKYTITRSLAILENV-----IFCHQGES---NWPLL---DMRGRCSGGEKVLASLIIrlal 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 173 --LVLQNPDVLLLDEPTNHLD-----VYMCEFLEKLLKNSKICVIFISHDRYFID 220
Cdd:cd03240 133 aeTFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVITHDEELVD 187
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-214 |
7.75e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 47.33 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNdksiamlaqqvdfntnlsldELINKNLSEIYEAL 98
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSN--------------------KNESEPSFEATRSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 NKYENLQAKLATHLDNKNLHKEIN-----NLINFIESKDAWNIeQKKERFLKEFKLFEYKNRPISsLSGGEIRKINLCIL 173
Cdd:cd03290 77 NRYSVAYAAQKPWLLNATVEENITfgspfNKQRYKAVTDACSL-QPDIDLLPFGDQTEIGERGIN-LSGGQRQRICVARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1751968159 174 VLQNPDVLLLDEPTNHLDVY-----MCEFLEKLLKNSKICVIFISH 214
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTH 200
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
346-540 |
7.76e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 47.92 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 346 FKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYfdQARAMLNSDKSLIELFCPNGGDRVQVR 425
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY--SRKGLMKLRESVGMVFQDPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 426 GHDMHIYGYLKSFLfPKEFLSQAVS-----------------VLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATIN 488
Cdd:PRK13636 100 VYQDVSFGAVNLKL-PEDEVRKRVDnalkrtgiehlkdkpthCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 489 ----ILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQYLERE 540
Cdd:PRK13636 179 eimkLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKE 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
11-234 |
9.57e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 48.49 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIfgtlqldsGRIIRQNDKSIAMLAQQVDFNTNLSLDELINKN 90
Cdd:PRK10070 36 EKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLL--------NRLIEPTRGQVLIDGVDIAKISDAELREVRRKK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 91 LSEIYEALNKYENLqaklaTHLDNKNLHKEINNLinfieskDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINL 170
Cdd:PRK10070 108 IAMVFQSFALMPHM-----TVLDNTAFGMELAGI-------NAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 171 CILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:PRK10070 176 ARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-215 |
1.06e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.48 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIamlaqqvdfnTNLSLDELINKNLSEIYE-- 96
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI-RLDGEDI----------TGLSPRERRRLGVAYIPEdr 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 97 -------ALNKYENLqakLATHLDNKNLHKeinnliNFIESKDAwnIEQKKERFLKEFKLfeyknR------PISSLSGG 163
Cdd:COG3845 343 lgrglvpDMSVAENL---ILGRYRRPPFSR------GGFLDRKA--IRAFAEELIEEFDV-----RtpgpdtPARSLSGG 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 164 EIRKInlcIL---VLQNPDVLLLDEPTNHLDVYMCEFLEKLL---KNSKICVIFISHD 215
Cdd:COG3845 407 NQQKV---ILareLSRDPKLLIAAQPTRGLDVGAIEFIHQRLlelRDAGAAVLLISED 461
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-234 |
1.06e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.77 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 4 IELIKASKKF----GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGtLQL-DSGRII--------------RQN 64
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERpTSGSVLvdgvdltalserelRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 65 DKSIAMLAQQvdFNtnlsldeLINknlseiyeALNKYEN--LQAKLAtHLDNKNLHKEINNLINFIeskdawNIEQKKER 142
Cdd:COG1135 81 RRKIGMIFQH--FN-------LLS--------SRTVAENvaLPLEIA-GVPKAEIRKRVAELLELV------GLSDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 143 FlkefklfeyknrPiSSLSGGEIRKInlCI---LVLqNPDVLLLDEPTNHLD------VymcefLEkLLK--NSK--ICV 209
Cdd:COG1135 137 Y------------P-SQLSGGQKQRV--GIaraLAN-NPKVLLCDEATSALDpettrsI-----LD-LLKdiNRElgLTI 194
|
250 260
....*....|....*....|....*
gi 1751968159 210 IFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:COG1135 195 VLITHEMDVVRRICDRVAVLENGRI 219
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-225 |
1.16e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.51 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 16 KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTL-----------------------QLDSGRIIRQNdksiAMLA 72
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdvtlngeplaAIDAPRLARLR----AVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 73 QQVDFNTNLSLDELInknlseiyeALNKYENLQAKLATHLDNKNLhkeinnlinfieskdAWnieqkkeRFLKEFKLFEY 152
Cdd:PRK13547 90 QAAQPAFAFSAREIV---------LLGRYPHARRAGALTHRDGEI---------------AW-------QALALAGATAL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 153 KNRPISSLSGGEIRKINLCILVLQ---------NPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDryfi 219
Cdd:PRK13547 139 VGRDVTTLSGGELARVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHD---- 214
|
....*.
gi 1751968159 220 DNVASR 225
Cdd:PRK13547 215 PNLAAR 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
349-506 |
1.52e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.50 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 349 FSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQAR---AMLNSDKSL---------IEL-FC 415
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRrpvSMLFQENNLfshltvaqnIGLgLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 416 P----NGGDRVQVR--GHDMHIygylksflfpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA---- 485
Cdd:PRK10771 98 PglklNAAQREKLHaiARQMGI----------EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAlrqe 167
|
170 180
....*....|....*....|.
gi 1751968159 486 TINILEEYLMEFKGALIFVSH 506
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSH 188
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-229 |
1.55e-05 |
|
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: 47.90 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 3 LIELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDS--GRIIRQNDKSIAMlaqqvdfntn 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKAS---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 lSLDELINKNLSEIYEALNKYENLQAKLATHLDNKNLHKeiNNLINFIEskdawnIEQKKERFLKEFKLFEYKN-RPISS 159
Cdd:TIGR02633 71 -NIRDTERAGIVIIHQELTLVPELSVAENIFLGNEITLP--GGRMAYNA------MYLRAKNLLRELQLDADNVtRPVGD 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 160 LSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNSK---ICVIFISHDryfIDNVASRCVEI 229
Cdd:TIGR02633 142 YGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKahgVACVYISHK---LNEVKAVCDTI 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
361-524 |
1.86e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 361 IVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIG--YFDQARAMLNSDKSLIELFC-PNG-----GDRV--QVRGHDM- 429
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGgrSIFNYRDVLEFRRRVGMLFQrPNPfpmsiMDNVlaGVRAHKLv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 430 ---HIYGYLKSFLFP-------KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG 499
Cdd:PRK14271 132 prkEFRGVAQARLTEvglwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLAD 211
|
170 180
....*....|....*....|....*..
gi 1751968159 500 AL--IFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK14271 212 RLtvIIVTHNLAQAARISDRAALFFDG 238
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
347-526 |
2.06e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.65 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADI------------KIGYF-----DQARAMLNSDKS 409
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRevnaenekwvrsKVGLVfqdpdDQVFSSTVWDDV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 410 LielFCPN----GGDRVQVRGHDMhiygyLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:PRK13647 102 A---FGPVnmglDKDEVERRVEEA-----LKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 486 TINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13647 173 GQETLMEILDRLHNQgktVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-187 |
2.15e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.81 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII------------RQNDKSIAMLAQQvdfntn 80
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvlggdmadarhrRAVCPRIAYMPQG------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 81 lsldelINKNLseiYEALNKYENLQ--AKLATHldnknlhkeinnlinfieskDAWNIEQKKERFLKEFKLFEYKNRPIS 158
Cdd:NF033858 85 ------LGKNL---YPTLSVFENLDffGRLFGQ--------------------DAAERRRRIDELLRATGLAPFADRPAG 135
|
170 180
....*....|....*....|....*....
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPT 187
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
348-532 |
2.44e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 46.75 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIG-------------------YFDQARAMLNSDK 408
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnknlkklrkkvslvfQFPEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 409 SLIELFCPNGG---DRVQVRGHDmhiygYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIA 485
Cdd:PRK13641 105 KDVEFGPKNFGfseDEAKEKALK-----WLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1751968159 486 TINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENGVInIEHMS 532
Cdd:PRK13641 180 GRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL-IKHAS 228
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
152-231 |
2.45e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.26 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 152 YKNRPISsLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCV 227
Cdd:cd03222 65 YKPQYID-LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIH 143
|
....
gi 1751968159 228 EIEG 231
Cdd:cd03222 144 VFEG 147
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
316-540 |
2.47e-05 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 47.41 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 316 NSSIQKPNFNKQKMIFELVNASKIIN-NKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADI 392
Cdd:TIGR00958 466 LTGTLAPLNLEGLIEFQDVSFSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQvlLDGVPL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 393 ----------KIGYFDQARAMLN-SDKSLIEL---FCPNGGDRVQVRGHDMHiygylkSFL--FPKEF---LSQAVSVLS 453
Cdd:TIGR00958 546 vqydhhylhrQVALVGQEPVLFSgSVRENIAYgltDTPDEEIMAAAKAANAH------DFImeFPNGYdteVGEKGSQLS 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 454 GGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEyLMEFKG-ALIFVSHDRYFVDKlATKLYVFENGVInIEHMS 532
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE-SRSRASrTVLLIAHRLSTVER-ADQILVLKKGSV-VEMGT 696
|
....*...
gi 1751968159 533 YTQYLERE 540
Cdd:TIGR00958 697 HKQLMEDQ 704
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-215 |
2.71e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 46.24 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 13 FGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKaifgTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDelINKNLS 92
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLR----TLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLE--FRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 93 EIYEALNKY-----ENLQAKLATHldnknlhkeinnliNFIESKDAWNIEQKKerfLKEFKLFE-YKNRPISS---LSGG 163
Cdd:PRK14271 105 MLFQRPNPFpmsimDNVLAGVRAH--------------KLVPRKEFRGVAQAR---LTEVGLWDaVKDRLSDSpfrLSGG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 164 EIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKN--SKICVIFISHD 215
Cdd:PRK14271 168 QQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSlaDRLTVIIVTHN 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
347-507 |
2.81e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 46.26 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI---------KNA-DI--KIGYF---------------DQ 399
Cdd:PRK13650 24 NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteENVwDIrhKIGMVfqnpdnqfvgatvedDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 400 ARAMLNSDKSLIELFcpnggDRVQvrgHDMHIYGYLksflfpkEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPT 479
Cdd:PRK13650 104 AFGLENKGIPHEEMK-----ERVN---EALELVGMQ-------DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 1751968159 480 NDLD-------IATI-NILEEYLMefkgALIFVSHD 507
Cdd:PRK13650 169 SMLDpegrlelIKTIkGIRDDYQM----TVISITHD 200
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
567-624 |
2.93e-05 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 42.45 E-value: 2.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 567 KLSYKQNEILNLYPEKIELLEKKIKKLNLELSK---TSDYENTNKLFEELKTLQNELNNLE 624
Cdd:pfam16326 1 KLSYKEQRELEELEAEIEKLEEEIAELEAQLADpelYSDYEKLQELSAELEELEAELEELY 61
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
361-594 |
3.11e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 361 IVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNSD---------------------------KSLIE- 412
Cdd:PRK13631 57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPyskkiknfkelrrrvsmvfqfpeyqlfKDTIEk 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 413 --LFCPNGGDRVQVRGHDMHIYgYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINIL 490
Cdd:PRK13631 137 diMFGPVALGVKKSEAKKLAKF-YLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEM 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 491 EEYLMEFKG---ALIFVSHDRYFVDKLATKLYVFENGVINIEHMSYTQYLEREFelreFDDFVLNLEKEKGAIKEKQNKK 567
Cdd:PRK13631 216 MQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI----INSTSIQVPRVIQVINDLIKKD 291
|
250 260
....*....|....*....|....*..
gi 1751968159 568 LSYKqnEILNLYPEKIELLEKKIKKLN 594
Cdd:PRK13631 292 PKYK--KLYQKQPRTIEQLADAINEFI 316
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
20-215 |
3.52e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.39 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 20 DEINFSANENekiAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQ----VDFNTN----------LSLDE 85
Cdd:COG0419 17 ETIDFDDGLN---LIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEasveLEFEHGgkryrierrqGEFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 86 LINKNLSEIYEALNK------YENLQAKLathldnKNLHKEINNLInfiesKDAWNIEQKKERFLKEFKLFEyknrPISS 159
Cdd:COG0419 94 FLEAKPSERKEALKRllgleiYEELKERL------KELEEALESAL-----EELAELQKLKQEILAQLSGLD----PIET 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 160 LSGGEIRKINLCILVlqnpdVLLLDepTNHLDVYMCEFLEKLLKNSKIcvifISHD 215
Cdd:COG0419 159 LSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELAI----ITHV 203
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
331-507 |
4.19e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.17 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKIL---LNLDKLSSGEIK--NADI--------KIGYF 397
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIagtLSPAFSASGEVLlnGRRLtalpaeqrRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQaRAMLNSDKSLIE--LFC-PNGGDRVQVRGHDMhiygylksflfpkEFLSQA---------VSVLSGGEKNRVAL--A 463
Cdd:COG4136 82 FQ-DDLLFPHLSVGEnlAFAlPPTIGRAQRRARVE-------------QALEEAglagfadrdPATLSGGQRARVALlrA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1751968159 464 LLftKDYDVLILDEPTNDLDIA-TINILE---EYLMEFKGALIFVSHD 507
Cdd:COG4136 148 LL--AEPRALLLDEPFSKLDAAlRAQFREfvfEQIRQRGIPALLVTHD 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-192 |
4.92e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIiRQNDKSIAMLAQQVDFNTN------------LSLDEL 86
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYV-TLDGHEVVTRSPQDGLANGivyisedrkrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 87 INKNLSeiYEALNKYenlqAKLATHLDNKNLHKEINNLInfieskdawnieqkkerflkefKLFEYK----NRPISSLSG 162
Cdd:PRK10762 347 VKENMS--LTALRYF----SRAGGSLKHADEQQAVSDFI----------------------RLFNIKtpsmEQAIGLLSG 398
|
170 180 190
....*....|....*....|....*....|
gi 1751968159 163 GEIRKINLCILVLQNPDVLLLDEPTNHLDV 192
Cdd:PRK10762 399 GNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
353-483 |
6.73e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 45.01 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 353 ILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-----------KNADIK-----IG-YFDQARAMLNSDKSLIEL-F 414
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkKNKKLKplrkkVGiVFQFPEHQLFEETVEKDIcF 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 415 CP-NGG---DRVQVRGHDMhiygyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD 483
Cdd:PRK13634 110 GPmNFGvseEDAKQKAREM-----IELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-191 |
6.74e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 16 KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQ-----LDSGRIIRQND-----KSIAMLAQqvdfNTNLsLDE 85
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPyqgslKINGIELRELDpeswrKHLSWVGQ----NPQL-PHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 86 LINKNLSeiyealnkyenlqaklathLDNKNLHKE-INNLInfiesKDAWnieqkkerfLKEF--KLFEYKNRPIS---- 158
Cdd:PRK11174 438 TLRDNVL-------------------LGNPDASDEqLQQAL-----ENAW---------VSEFlpLLPQGLDTPIGdqaa 484
|
170 180 190
....*....|....*....|....*....|...
gi 1751968159 159 SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:PRK11174 485 GLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
19-225 |
6.87e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.56 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQlDSGRI----IRQNDKSIAMLaqqvdfnTNLSLDELINKNLSEI 94
Cdd:PRK15093 23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVtadrMRFDDIDLLRL-------SPRERRKLVGHNVSMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 95 YE----ALNKYENLQAKLathldnknlhkeinnlinfIESKDAWNIeqkKERFLKEFKLfeYKNRPIS------------ 158
Cdd:PRK15093 95 FQepqsCLDPSERVGRQL-------------------MQNIPGWTY---KGRWWQRFGW--RKRRAIEllhrvgikdhkd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 159 -------SLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD----VYMCEFLEKLLKNSKICVIFISHDRYFIDNVASR 225
Cdd:PRK15093 151 amrsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADK 228
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
331-489 |
7.37e-05 |
|
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: 44.46 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 331 FELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI--KNADIK-----------IGYF 397
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIllDGQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 398 DQA----RAMLNSD--KSLIELFCPNGGDRVQVrghdmhiygyLKSFLfpKEF-----LSQAVSVLSGGEKNRVALALLF 466
Cdd:cd03218 81 PQEasifRKLTVEEniLAVLEIRGLSKKEREEK----------LEELL--EEFhithlRKSKASSLSGGERRRVEIARAL 148
|
170 180
....*....|....*....|....
gi 1751968159 467 TKDYDVLILDEPTNDLD-IATINI 489
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDpIAVQDI 172
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-234 |
7.49e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 43.96 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRqNDKSIamlaqqvdfnTNLSLDELINKNLSEIYEal 98
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL-DGKPV----------TRRSPRDAIRAGIAYVPE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 99 nkyenlqaklathldnknlhkeinnlinfieskdawniEQKKERFLKEFKLFEykNRPISS-LSGGEIRKINLCILVLQN 177
Cdd:cd03215 83 --------------------------------------DRKREGLVLDLSVAE--NIALSSlLSGGNQQKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 178 PDVLLLDEPTNHLDVYMCEFLEKL---LKNSKICVIFISHDRYFIDNVASRCVEIEGGKI 234
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLireLADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
453-507 |
7.73e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.34 E-value: 7.73e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 453 SGGEKNRVALALLFTKDYDVLILDEPTNDLDIA----TINILEEYLMEFKGALIFVSHD 507
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSvqaqVLNLMMDLQQELGLSYVFISHD 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
18-191 |
7.83e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 7.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqQVDFNTNLSLDElinknlSEIYEA 97
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI-------------QIDGKTATRGDR------SRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 98 LNKYENLQAKLATHldnKNLHkeinnlinFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQN 177
Cdd:PRK13543 87 LGHLPGLKADLSTL---ENLH--------FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSP 155
|
170
....*....|....
gi 1751968159 178 PDVLLLDEPTNHLD 191
Cdd:PRK13543 156 APLWLLDEPYANLD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
452-524 |
7.97e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 45.25 E-value: 7.97e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 452 LSGGEKNRVAL--ALLfTKDyDVLILDEPTNDLDIA----TINILEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK11144 129 LSGGEKQRVAIgrALL-TAP-ELLLMDEPLASLDLPrkreLLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
337-494 |
9.08e-05 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.62 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 337 SKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNL---DKLS-----------------SGEIKNADIKIGY 396
Cdd:PRK09984 11 AKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAgshiellgrtvqregrlARDIRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 FDQARAMLNSDKSLIELFCPNGGD--------RVQVRGHDMHIYGYLKSFLFpKEFLSQAVSVLSGGEKNRVALALLFTK 468
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGALGStpfwrtcfSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180
....*....|....*....|....*.
gi 1751968159 469 DYDVLILDEPTNDLDIATINILEEYL 494
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTL 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
345-569 |
1.04e-04 |
|
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: 45.67 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADiKIGYFDQAR-AMLNSDKSLIeLFcpnggdrvq 423
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-RISFSPQTSwIMPGTIKDNI-IF--------- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 424 vrGHDMHIYGYLKSF----------LFP---KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT-INI 489
Cdd:TIGR01271 510 --GLSYDEYRYTSVIkacqleediaLFPekdKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTeKEI 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 490 LEE---YLMEFKGALIFVSHDRYFvdKLATKLYVFENGVINIehmsYTQYLEREFELREFDDFVLNLEKEKGAIKEKQNK 566
Cdd:TIGR01271 588 FESclcKLMSNKTRILVTSKLEHL--KKADKILLLHEGVCYF----YGTFSELQAKRPDFSSLLLGLEAFDNFSAERRNS 661
|
...
gi 1751968159 567 KLS 569
Cdd:TIGR01271 662 ILT 664
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-237 |
1.06e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.87 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 33 AIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamLAQQVDFNTNlsldelinknlSEIYEALNK----YENLQAKL 108
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIV---------LNGRVLFDAE-----------KGICLPPEKrrigYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 109 ATHLDNK-NLHKEINnlinfieskdawniEQKKERFLKEFKLFEYK---NRPISSLSGGEIRKINLCILVLQNPDVLLLD 184
Cdd:PRK11144 88 FPHYKVRgNLRYGMA--------------KSMVAQFDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 185 EPTNHLDV----YMCEFLEKLLKNSKICVIFISHDRYFIDNVASRCVEIEGGKISFF 237
Cdd:PRK11144 154 EPLASLDLprkrELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAF 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-191 |
1.13e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.77 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGriirqnDKSIA---MLAQQVDFNTNL-------SLDELIN 88
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG------DATVAgksILTNISDVHQNMgycpqfdAIDDLLT 2028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 89 KNlseiyEALNKYENLQAKLAthldnknlhKEINNLINfieskdaWNIeqkkerflKEFKLFEYKNRPISSLSGGEIRKI 168
Cdd:TIGR01257 2029 GR-----EHLYLYARLRGVPA---------EEIEKVAN-------WSI--------QSLGLSLYADRLAGTYSGGNKRKL 2079
|
170 180
....*....|....*....|...
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLD 191
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMD 2102
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
325-526 |
1.56e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 325 NKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLD--KLSSGEIKNADIKIGYFD-QAR 401
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEpEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AMLN---SDKSLIELFCPNGGDRVQVRGHDMHIYgYLKSFLFPKEFLSQAVSVL------------------SGGEKNR- 459
Cdd:CHL00131 82 AHLGiflAFQYPIEIPGVSNADFLRLAYNSKRKF-QGLPELDPLEFLEIINEKLklvgmdpsflsrnvnegfSGGEKKRn 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 460 --VALALLftkDYDVLILDEPTNDLDIATINILEE---YLMEFKGALIFVSHDRYFVDKLA-TKLYVFENGVI 526
Cdd:CHL00131 161 eiLQMALL---DSELAILDETDSGLDIDALKIIAEginKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
14-51 |
1.64e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.64e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1751968159 14 GEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFG 51
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
347-520 |
1.65e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 43.70 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADIKIGYFDQARAMLNSDKSLIelfcP--NGGDRV-- 422
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALL----PwlNVLDNVaf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 423 --QVRGHDMH----IYGYLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLME 496
Cdd:COG4525 100 glRLRGVPKAerraRAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLD 179
|
170 180 190
....*....|....*....|....*....|..
gi 1751968159 497 F-----KGALiFVSHDryfVDK---LATKLYV 520
Cdd:COG4525 180 VwqrtgKGVF-LITHS---VEEalfLATRLVV 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
154-234 |
1.65e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 44.32 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVY----MCEFLEKLLKNSKICVIFISHDryfIDNV---ASRC 226
Cdd:COG4148 128 DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLArkaeILPYLERLRDELDIPILYVSHS---LDEVarlADHV 204
|
....*...
gi 1751968159 227 VEIEGGKI 234
Cdd:COG4148 205 VLLEQGRV 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
345-526 |
1.69e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.96 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFkNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-----------KNADIK-----IGY-FDQARAMLNSD 407
Cdd:PRK13649 23 LF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVrvddtlitstsKNKDIKqirkkVGLvFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 408 KSLIEL-FCP-NGG----DRVQVRGHDMHIYGylksflFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:PRK13649 102 TVLKDVaFGPqNFGvsqeEAEALAREKLALVG------ISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 482 LDIATinilEEYLME-FKG------ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK13649 176 LDPKG----RKELMTlFKKlhqsgmTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-235 |
1.83e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 22 INFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIrqndksiamlaqqVDfntnlsldeliNKNLSEiyEALNKY 101
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL-------------LD-----------GKPVTA--EQPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 102 ENLQAKLAT--HLDNKNLHKEInnlinfiESKDAWNIEQKKERFLKEFKLfEYKNRPIS--SLSGGEIRKINLCILVLQN 177
Cdd:PRK10522 396 RKLFSAVFTdfHLFDQLLGPEG-------KPANPALVEKWLERLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 178 PDVLLLDEPTNHLD-VYMCEFLEKLL---KNSKICVIFISH-DRYFIDnvASRCVEIEGGKIS 235
Cdd:PRK10522 468 RDILLLDEWAADQDpHFRREFYQVLLpllQEMGKTIFAISHdDHYFIH--ADRLLEMRNGQLS 528
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
5-220 |
1.84e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.92 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 5 ELIKASKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLD 84
Cdd:pfam13304 85 EKLSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 ELINKNLSEIYEALNKYENLQAKLATHLDNKNLHKEinnLINFIESKDAWNIEQKKERFLKEFKLFEYKNRPISSLSGGE 164
Cdd:pfam13304 165 DWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLS---DLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGT 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 165 IRKINLCILVL---QNPDVLLLDEPTNHLDVYMCEFLEKLLK---NSKICVIFISHDRYFID 220
Cdd:pfam13304 242 KRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKelsRNGAQLILTTHSPLLLD 303
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
33-223 |
2.05e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 43.88 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 33 AIIGKNGEGKSTLLKAI-----FGTLQLDSGRIIRQNDKSIAMLAQQ-----VDFNTN-------LSLD----------- 84
Cdd:COG1106 33 LIYGANASGKSNLLEALyflrnLVLNSSQPGDKLVEPFLLDSESKNEpsefeILFLLDgvryeygFELDkeriisewlyf 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 85 -----ELINKNLSEIYEALNKYENLQAKLATHL----DNKNLHKEINNLINFIES--KDAWNIEQKKERFLKEFKLFEYK 153
Cdd:COG1106 113 lstaaQLNVPLLSPLYDWFDNNISLDTSSDGLTlllkEDESLKEELLELLKIADPgiEDIEVEEEEIEDLVERKLIFKHK 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 154 NR----PISSLSGGeIRKI----NLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLL----KNSKICVIFISHDRYFIDN 221
Cdd:COG1106 193 GGnvplPLSEESDG-TKRLlalaGALLDALAKGGVLLIDEIEASLHPSLLRKLLKLFldlaNKNNAQLIFTTHSTELLDA 271
|
..
gi 1751968159 222 VA 223
Cdd:COG1106 272 FL 273
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
345-486 |
2.49e-04 |
|
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: 43.31 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 345 LFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIKNADiKIGYFDQ-ARAMLNSDKSLIelfcpnggdrvq 423
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RISFSSQfSWIMPGTIKENI------------ 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 424 VRGHDMHIYGYlKSFL-----------FPKE---FLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIAT 486
Cdd:cd03291 119 IFGVSYDEYRY-KSVVkacqleeditkFPEKdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
325-572 |
2.52e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 325 NKQKMIFELVNASKiinNKILF--KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI-KNADIKIGYFDqar 401
Cdd:PRK13546 20 NKERMKDALIPKHK---NKTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAIS--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 402 AMLNSDKSLIE-----LFCpNGGDRVQVRGHDMHIYgylkSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILD 476
Cdd:PRK13546 94 AGLSGQLTGIEniefkMLC-MGFKRKEIKAMTPKII----EFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVID 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 477 EPTNDLDIATINILEEYLMEFKGA---LIFVSHDRYFVDKLATKLYVFENGVINiehmsytQYLEREFELREFDDFVLNL 553
Cdd:PRK13546 169 EALSVGDQTFAQKCLDKIYEFKEQnktIFFVSHNLGQVRQFCTKIAWIEGGKLK-------DYGELDDVLPKYEAFLNDF 241
|
250
....*....|....*....
gi 1751968159 554 EKEKGAIKEKQNKKLSYKQ 572
Cdd:PRK13546 242 KKKSKAEQKEFRNKLDESR 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
156-213 |
3.39e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.76 E-value: 3.39e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1751968159 156 PISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV---YMCEFLEKLLKNSKICVIFIS 213
Cdd:PRK13549 402 AIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakYEIYKLINQLVQQGVAIIVIS 462
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-213 |
3.53e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.47 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 19 LDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRI--------IRQNDKSIA---------------MLAQQV 75
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIrldgkpvrIRSPRDAIRagiayvpedrkgeglVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 76 DFNTNL-SLDELINK---NLSEIYEALNKY-ENLQAKLAthldnknlhkeinnlinfieskdawNIEQkkerflkefklf 150
Cdd:COG1129 348 RENITLaSLDRLSRGgllDRRRERALAEEYiKRLRIKTP-------------------------SPEQ------------ 390
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 151 eyknrPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDV------YmcEFLEKLLKNSKiCVIFIS 213
Cdd:COG1129 391 -----PVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaeiY--RLIRELAAEGK-AVIVIS 451
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-216 |
3.65e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQN------------------DKSIAMLAQQVDFNt 79
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDcdvakfgltdlrrvlsiiPQSPVLFSGTVRFN- 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 80 nlsLDELINKNLSEIYEALNKyenlqaklaTHLdnknlhkeinnlinfiesKDAwnieQKKERFLKEFKLFEYKnrpiSS 159
Cdd:PLN03232 1330 ---IDPFSEHNDADLWEALER---------AHI------------------KDV----IDRNPFGLDAEVSEGG----EN 1371
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1751968159 160 LSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLKNS-KICVIFISHDR 216
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEfKSCTMLVIAHR 1429
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
341-483 |
3.66e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 43.50 E-value: 3.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 341 NNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDK---LSSGEIKNADIKIGYfDQARAM---LNSDksliELF 414
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDA-KEMRAIsayVQQD----DLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 415 CPNggdrVQVRGHDM---HI-----YGYLKSFLFPKEFLSQ---------------AVSVLSGGEKNRVALALLFTKDYD 471
Cdd:TIGR00955 111 IPT----LTVREHLMfqaHLrmprrVTKKEKRERVDEVLQAlglrkcantrigvpgRVKGLSGGERKRLAFASELLTDPP 186
|
170
....*....|..
gi 1751968159 472 VLILDEPTNDLD 483
Cdd:TIGR00955 187 LLFCDEPTSGLD 198
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
353-387 |
3.68e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.29 E-value: 3.68e-04
10 20 30
....*....|....*....|....*....|....*
gi 1751968159 353 ILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEI 387
Cdd:PRK11650 27 VADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
10-234 |
4.72e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 42.53 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 10 SKKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaQQVDFNTNLSLDELINK 89
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI------------QVGDIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 90 NlseiyealnkyENLQAKLAthlDNKNLHKEINNLINFIE--------SKDAW----NIEQKKERFLKEFKLF------- 150
Cdd:PRK13631 101 T-----------NPYSKKIK---NFKELRRRVSMVFQFPEyqlfkdtiEKDIMfgpvALGVKKSEAKKLAKFYlnkmgld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 151 -EYKNRPISSLSGGEIRKINLC-ILVLQnPDVLLLDEPTNHLDVYMCEFLEKLLKNSKI---CVIFISHDRYFIDNVASR 225
Cdd:PRK13631 167 dSYLERSPFGLSGGQKRRVAIAgILAIQ-PEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADE 245
|
....*....
gi 1751968159 226 CVEIEGGKI 234
Cdd:PRK13631 246 VIVMDKGKI 254
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-61 |
5.03e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 5.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII 61
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRIL 1297
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
348-546 |
5.86e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.42 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKS-TFLKILLNLD---KLSSG--EIKNADIKIGYFDQARAMLNSDKSLI---------- 411
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEklEFNGQDLQRISEKERRNLVGAEVAMIfqdpmtslnp 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 412 ----------ELFCPNGGDRVQVRGHDMHIYGyLKSFLFPKEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTND 481
Cdd:PRK11022 105 cytvgfqimeAIKVHQGGNKKTRRQRAIDLLN-QVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 482 LDIATINILEEYLMEFKG----ALIFVSHDRYFVDKLATKLYVFENGVINIEHMS----------YTQYLERefELREF 546
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQkenmALVLITHDLALVAEAAHKIIVMYAGQVVETGKAhdifraprhpYTQALLR--ALPEF 260
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-506 |
7.26e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.82 E-value: 7.26e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 442 KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG--ALIFVSH 506
Cdd:PRK14247 137 KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
155-241 |
7.37e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 155 RPISSLSGGEIRKINLCILVL---QNPDVLLLDEPTNHL---DVY-MCEFLEKLLKNSKICVIfISHDRYFIdNVASRCV 227
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKaLIYVLQSLTHQGHTVVI-IEHNMHVV-KVADYVL 882
|
90
....*....|....*.
gi 1751968159 228 EI--EGGKIsffnGGY 241
Cdd:PRK00635 883 ELgpEGGNL----GGY 894
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-483 |
7.43e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 42.52 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 343 KILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILL-------NLdKLSSGEIKNADIKigyfdQARAML-----NSdksl 410
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLgflpyqgSL-KINGIELRELDPE-----SWRKHLswvgqNP---- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 411 iELFCPNGGDRVQVRGHDM---HIYGYLKSfLFPKEFLSQ-----------AVSVLSGGEKNRVALALLFTKDYDVLILD 476
Cdd:PRK11174 433 -QLPHGTLRDNVLLGNPDAsdeQLQQALEN-AWVSEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQPCQLLLLD 510
|
....*..
gi 1751968159 477 EPTNDLD 483
Cdd:PRK11174 511 EPTASLD 517
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
328-506 |
7.55e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 42.31 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 328 KMIFELVNASKIIN-NKILfKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknadikigYFDQARAMLNS 406
Cdd:COG1129 2 EPLLEMRGISKSFGgVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEI--------LLDGEPVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 407 DK-------SLI--EL-FCPN---------------GG--DRVQVR----------GHDMHiygylksflfpkefLSQAV 449
Cdd:COG1129 73 PRdaqaagiAIIhqELnLVPNlsvaeniflgreprrGGliDWRAMRrrarellarlGLDID--------------PDTPV 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 450 SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG---ALIFVSH 506
Cdd:COG1129 139 GDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAqgvAIIYISH 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-235 |
7.59e-04 |
|
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: 42.48 E-value: 7.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 22 INFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIirqndksiamlaqQVDfntnlslDELINKNLSEIYEALnky 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-------------LLD-------GQPVTADNREAYRQL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 102 enlqakLAT-----HLDNKNLHKEINNLinfieskdawniEQKKERFLKEFKL---FEYKNRPISS--LSGGEiRK-INL 170
Cdd:COG4615 408 ------FSAvfsdfHLFDRLLGLDGEAD------------PARARELLERLELdhkVSVEDGRFSTtdLSQGQ-RKrLAL 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 171 CILVLQNPDVLLLDE------PTNHlDVYMCEFLEKLLKNSKIcVIFISHD-RYFidNVASRCVEIEGGKIS 235
Cdd:COG4615 469 LVALLEDRPILVFDEwaadqdPEFR-RVFYTELLPELKARGKT-VIAISHDdRYF--DLADRVLKMDYGKLV 536
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-221 |
7.85e-04 |
|
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: 41.77 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 18 ILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSiamLAQQVDFNTNLSLDELINKNLSeiyea 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS---FSSQFSWIMPGTIKENIIFGVS----- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 98 LNKYENLQAKLATHLDnknlhkeinnlinfiesKDAWNIEQKKERFLKEFKLfeyknrpisSLSGGEIRKINLCILVLQN 177
Cdd:cd03291 124 YDEYRYKSVVKACQLE-----------------EDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1751968159 178 PDVLLLDEPTNHLDVymceFLEKLLKNSKICVIFISHDRYFIDN 221
Cdd:cd03291 178 ADLYLLDSPFGYLDV----FTEKEIFESCVCKLMANKTRILVTS 217
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
442-506 |
8.04e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.75 E-value: 8.04e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1751968159 442 KEFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG--ALIFVSH 506
Cdd:PRK14267 140 KDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-61 |
8.64e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 8.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1751968159 21 EINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRII 61
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL 71
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
335-540 |
1.00e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.42 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 335 NASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADIK-----------IGY----- 396
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiIDDEDISllplhararrgIGYlpqea 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 397 --------FDQARAMLNSDKSLIElfcPNGGDRVQVRGHDMHIygylkSFLfpKEFLSQAvsvLSGGEKNRVALALLFTK 468
Cdd:PRK10895 88 sifrrlsvYDNLMAVLQIRDDLSA---EQREDRANELMEEFHI-----EHL--RDSMGQS---LSGGERRRVEIARALAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 469 DYDVLILDEPTNDLD-IATINI--LEEYLMEFKGALIFVSHDRYFVDKLATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:PRK10895 155 NPKFILLDEPFAGVDpISVIDIkrIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL-IAHGTPTEILQDE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
330-524 |
1.02e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 41.30 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 330 IFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKIL-----LNLDKLSSGEIknadikigyfdqaraML 404
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSI---------------VY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSDksliELFCPNGgDRVQVRG----------------HDMHIYGYLKSFLFPKEFLSQAVSV----------------- 451
Cdd:PRK14239 70 NGH----NIYSPRT-DTVDLRKeigmvfqqpnpfpmsiYENVVYGLRLKGIKDKQVLDEAVEKslkgasiwdevkdrlhd 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 452 ----LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG--ALIFVSHDRYFVDKLATKLYVFENG 524
Cdd:PRK14239 145 salgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDdyTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
158-234 |
1.39e-03 |
|
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: 40.53 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1751968159 158 SSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLDVYMCEFLEKLLK--NSKICVIFISHDRYFIDNvASRCVEIEGGKI 234
Cdd:cd03248 149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYdwPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
348-538 |
1.47e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.41 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIknaDIK-IGYFDQARAMLNSDKSLIElfcpnggdRVQVRG 426
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV---DIKgSAALIAISSGLNGQLTGIE--------NIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 427 HDMHIYGYLKSFLFPK--------EFLSQAVSVLSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFK 498
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEiiefadigKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFK 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1751968159 499 ---GALIFVSHDRYFVDKLATKL------YVFENGVINIEHMSYTQYLE 538
Cdd:PRK13545 191 eqgKTIFFISHSLSQVKSFCTKAlwlhygQVKEYGDIKEVVDHYDEFLK 239
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-191 |
1.55e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 41.26 E-value: 1.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1751968159 128 IESKDAwniEQKKERFLKEFKLFEYKNRPISSLSGGEIRKINLCILVLQNPDVLLLDEPTNHLD 191
Cdd:NF000106 116 LSRKDA---RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
154-220 |
1.68e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 1.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 154 NRPISSLSGGEIRKINLCILVLQNPD--VLLLDEPTNHLDVYMCE-FLEKL--LKNSKICVIFISHDRYFID 220
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINqLLEVIkgLIDLGNTVILIEHNLDVLS 153
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
348-574 |
1.78e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 348 NFSTRILQGEKIGIVGQNGCGKSTFLKILLNldKLSSGEIKNADIK--IGYFDQARAMLNSDKSLIELFcpnGGD----- 420
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG--ELSHAETSSVVIRgsVAYVPQVSWIFNATVRENILF---GSDfeser 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 421 -----RVQVRGHDMHiygylksfLFP----KEFLSQAVSVlSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILE 491
Cdd:PLN03232 710 ywraiDVTALQHDLD--------LLPgrdlTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 492 EYLM--EFKGAL-IFVSHDRYF---VDKL-----------ATKLYVFENGVINIEHMSYTQYLEREFELREFDDFVLNL- 553
Cdd:PLN03232 781 DSCMkdELKGKTrVLVTNQLHFlplMDRIilvsegmikeeGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILKLg 860
|
250 260 270
....*....|....*....|....*....|
gi 1751968159 554 --------EKEKGAIKE-KQNKKLSYKQNE 574
Cdd:PLN03232 861 ptvtidvsERNLGSTKQgKRGRSVLVKQEE 890
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
350-400 |
2.07e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 41.26 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1751968159 350 STRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE-------IKNADI----KIGYFDQA 400
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpVDAGDIatrrRVGYMSQA 347
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
323-507 |
2.25e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 40.15 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 323 NFNKQKMIFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGeiKNADIKIGYFDQara 402
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG--FRVEGKVTFHGK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 403 mlnsdksliELFCPnGGDRVQVRGHDMHIYGylKSFLFPKEF------------------------LSQAV--------- 449
Cdd:PRK14243 78 ---------NLYAP-DVDPVEVRRRIGMVFQ--KPNPFPKSIydniaygaringykgdmdelversLRQAAlwdevkdkl 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1751968159 450 ----SVLSGGEKNRVALALLFTKDYDVLILDEPTNDLD-IATINIlEEYLMEFKG--ALIFVSHD 507
Cdd:PRK14243 146 kqsgLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDpISTLRI-EELMHELKEqyTIIIVTHN 209
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
297-540 |
2.30e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.16 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 297 EAKKNPGeikrlKLELLRANSSIQkpnfnkqkmiFELVNASKIINNKILFKNFSTRILQGEKIGIVGQNGCGKSTFLKIL 376
Cdd:PRK11176 325 EQEKDEG-----KRVIERAKGDIE----------FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 377 LNLDKLSSGEI--KNADIKigyfdqaramlnsDKSLIELfcpngGDRVQVRGHDMHIY--------GYLKSFLFPKEFLS 446
Cdd:PRK11176 390 TRFYDIDEGEIllDGHDLR-------------DYTLASL-----RNQVALVSQNVHLFndtianniAYARTEQYSREQIE 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 447 QAVSV------------------------LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEF---KG 499
Cdd:PRK11176 452 EAARMayamdfinkmdngldtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELqknRT 531
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1751968159 500 ALIfVSHDRYFVDKlATKLYVFENGVInIEHMSYTQYLERE 540
Cdd:PRK11176 532 SLV-IAHRLSTIEK-ADEILVVEDGEI-VERGTHAELLAQN 569
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-215 |
2.47e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.82 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 11 KKFGEKIILDEINFSANENEKIAIIGKNGEGKSTLLKAIF------GTLQLDSGRIIRQNDKsiAMLAQ----QVDF--- 77
Cdd:COG4172 294 RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLrlipseGEIRFDGQDLDGLSRR--ALRPLrrrmQVVFqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 78 ----NTNLSLDELInknlSEiyealnkyenlqaKLATHldnknlhkeinnlinFIESKDAwNIEQKKERFLKEFKL-FEY 152
Cdd:COG4172 372 fgslSPRMTVGQII----AE-------------GLRVH---------------GPGLSAA-ERRARVAEALEEVGLdPAA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 153 KNRPISSLSGGEIRKInlCI---LVLQnPDVLLLDEPTNHLDV----YMCEFLEKLLKNSKICVIFISHD 215
Cdd:COG4172 419 RHRYPHEFSGGQRQRI--AIaraLILE-PKLLVLDEPTSALDVsvqaQILDLLRDLQREHGLAYLFISHD 485
|
|
| cmk |
TIGR00017 |
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the ... |
32-154 |
2.69e-03 |
|
cytidylate kinase; This family consists of cytidylate kinase, which catalyzes the phosphorylation of cytidine 5-monophosphate (dCMP) to cytidine 5 -diphosphate (dCDP) in the presence of ATP or GTP. UMP and dCMP can also act as acceptors. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 129128 [Multi-domain] Cd Length: 217 Bit Score: 39.72 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 32 IAIIGKNGEGKSTLLKAIFGTLQ---LDSGRIIRQndKSIAMLAQQVDFNTNLSLDELINKNlsEIyealnKYENLQAKL 108
Cdd:TIGR00017 5 IAIDGPSGAGKSTVAKAVAEKLGyayLDSGAMYRA--IALAALQNRVDLTSEDALAELISHL--DI-----RFIPTNGEV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1751968159 109 ATHLDNKNLHKEI-NNLINFIESKDAWNIEQKKERFLKEFKLFEYKN 154
Cdd:TIGR00017 76 EVFLNGEDVSEAIrTQEVANAASKVAVFPKVREALLKRQQALAKNDG 122
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
452-523 |
2.80e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.17 E-value: 2.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1751968159 452 LSGGEKNRVALALLFTKDYDVLILDEPTNDLDIATINILEEYLMEFKG----ALIFVSHdRYFVDKLATKLYVFEN 523
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH-RIASIKRSDKIVVFNN 1433
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-196 |
3.16e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 16 KIILDEINFSANENEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQndKSIAMLAQQ-------VDFNTnLSLDElin 88
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE--RSIAYVPQQawimnatVRGNI-LFFDE--- 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 89 knlseiyealnkyENlQAKLATHLDNKNLHKEINNLINFIESKdawnIEQKKerflkefklfeyknrpiSSLSGGEIRKI 168
Cdd:PTZ00243 747 -------------ED-AARLADAVRVSQLEADLAQLGGGLETE----IGEKG-----------------VNLSGGQKARV 791
|
170 180
....*....|....*....|....*...
gi 1751968159 169 NLCILVLQNPDVLLLDEPTNHLDVYMCE 196
Cdd:PTZ00243 792 SLARAVYANRDVYLLDDPLSALDAHVGE 819
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
347-526 |
3.89e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 347 KNFSTRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGE--IKNADI--------------KIGYFDQARAM------L 404
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQvlIDGVDIakisdaelrevrrkKIAMVFQSFALmphmtvL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 405 NSDKSLIELFCPNGGDR-------VQVRGHDMHIYGYlksflfPKEflsqavsvLSGGEKNRVALALLFTKDYDVLILDE 477
Cdd:PRK10070 125 DNTAFGMELAGINAEERrekaldaLRQVGLENYAHSY------PDE--------LSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1751968159 478 PTNDLDIATINILEEYLMEFKG----ALIFVSHDRYFVDKLATKLYVFENGVI 526
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAkhqrTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
350-388 |
5.74e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.15 E-value: 5.74e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1751968159 350 STRILQGEKIGIVGQNGCGKSTFLKILLNLDKLSSGEIK 388
Cdd:PTZ00243 1330 SFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-125 |
6.08e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1751968159 29 NEKIAIIGKNGEGKSTLLKAIFGTLQLDSGRIIRQNDKSIAMLAQQVDFNTNLSLDELINKNLSEIYEALNKYENLQAKL 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDV 81
|
90 100
....*....|....*....|..
gi 1751968159 109 -----ATHLDNKNLHKEINNLI 125
Cdd:smart00382 82 lildeITSLLDAEQEALLLLLE 103
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
447-484 |
6.80e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.39 E-value: 6.80e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1751968159 447 QAVSVLSGGEKNRVALA-LLFTkDYDVLILDEPTNDLDI 484
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSkWLFT-DPDVLILDEPTRGIDV 437
|
|
| |
