|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
6-700 |
0e+00 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 599.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 6 EILRSEFPEIDGQVFDYVTGVLHSGSADF-ESVDDLVEAVGELLQEvSGDSKDDAGIRAVCQRM---YNTLRLAEPQSQG 81
Cdd:PLN03073 13 EVLGRRIRDVDSPIIDYIINVLADEDFDFgPEGEGAFDALGELLVA-AECVSDDAECRLVCSKLaekFGKHGLVKPKPSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 82 NSqvlLDAPIQLSKITENYDCGTKLPGLLKREQSSTVNAKKLEkaeaRLKAKQEKRSEKDTlkTSNPLVLEEASASQAGS 161
Cdd:PLN03073 92 RS---LAAPVRMSDGMDDSEVAKKKPEPDDGPLLSERDLAKIE----RRKRKEERQREVQY--QAHVAEMEAAKAGMPGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 162 RKESRLESSGKNKSyDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLR-VPAHISLLHVE 240
Cdd:PLN03073 163 YVNHDGNGGGPAIK-DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 241 QEVAGDDTPALQSVLESDSVREDLLRRERELTAQ-------IAAGRAEGSE---------AAELAEIYAKLEEIEADKAP 304
Cdd:PLN03073 242 QEVVGDDTTALQCVLNTDIERTQLLEEEAQLVAQqrelefeTETGKGKGANkdgvdkdavSQRLEEIYKRLELIDAYTAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 305 ARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDR 384
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 385 NFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKL 464
Cdd:PLN03073 402 EFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 465 PELKPVDKESEVVMKFPDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP 544
Cdd:PLN03073 482 GHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 545 VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQM 624
Cdd:PLN03073 562 SSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKI 641
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 625 TMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQ 700
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDYKKTLQ 717
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
180-697 |
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: 555.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEV-AGDDTPALQ 252
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgelepdSGEVSIPKGLRIGYLPQEPpLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 SVLESDSVREDLLRRERELTAQIAAGRAEGseaAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGW 332
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDL---ERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETF 412
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 413 IKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVMKFPDGfEKFSPPIL 492
Cdd:COG0488 238 LEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPP-ERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHvEQLDLNV 572
Cdd:COG0488 317 ELEGLSKSYGDK-TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 SAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA 652
Cdd:COG0488 395 TVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 148612853 653 LNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRA 697
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
188-707 |
3.06e-123 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 381.44 E-value: 3.06e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAGDDTPALQSVLESDsvr 261
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 262 edllRRERELTAQIAAGRAEGSEAAeLAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARA 341
Cdd:PRK10636 89 ----REYRQLEAQLHDANERNDGHA-IATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 342 LFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLL 421
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 422 NQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKP--VDKESEVVMKFPdgfEKFSPPILQLDEVDF 499
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPahVDNPFHFSFRAP---ESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 500 YYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLA 579
Cdd:PRK10636 321 GYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 580 RKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG 659
Cdd:PRK10636 400 RLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 148612853 660 VILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFRREG 707
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
181-695 |
1.86e-88 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 287.17 E-value: 1.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 ENFDVSFGDrvllagadvnlawGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLESDSV 260
Cdd:PRK15064 18 ENISVKFGG-------------GNRYGLIGANGCGKSTFMKILG--------------------GDLEPSAGNVSLDPNE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 261 REDLLRRE-------RELTAQIAaGRAEGSEA-AELAEIYAKLEEIEAD-----------------KAPARASVILAGLG 315
Cdd:PRK15064 65 RLGKLRQDqfafeefTVLDTVIM-GHTELWEVkQERDRIYALPEMSEEDgmkvadlevkfaemdgyTAEARAGELLLGVG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 316 FTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:PRK15064 144 IPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 396 HLHSQRLDGYRGDFETFIKSK---QERLLNQQREYEAQQqyrQHIQVFIDRFRYNANRASQVQSKLKMLEK--LPELKPV 470
Cdd:PRK15064 224 DLDYGELRVYPGNYDEYMTAAtqaRERLLADNAKKKAQI---AELQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 471 DKESEVVmKFPDGfEKFSPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRH 550
Cdd:PRK15064 301 SRQNPFI-RFEQD-KKLHRNALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHRNLKIGYFSQHHVEQLDLNVSAVELLAR-KFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCP 629
Cdd:PRK15064 378 WSENANIGYYAQDHAYDFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 630 NFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQY 695
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
178-692 |
8.12e-72 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 245.63 E-value: 8.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRslrVPAHISLLHVEQEVagddtpaLQSVLES 257
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE---VLLDDGRIIYEQDL-------IVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVRE-----------------DLLRRERELTAQIAAgraEGSEA--AELAEIYAKLEEIEADKAPARASVILAGLGFTP 318
Cdd:PRK11147 74 DPPRNvegtvydfvaegieeqaEYLKRYHDISHLVET---DPSEKnlNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 319 KMqqqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:PRK11147 151 DA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 399 SQRLDGYRGDFETFIKSKQERL---LNQQREYE---AQQQY--RQHIQVFIDRF--RYNANRA-----SQ---VQSKLKM 460
Cdd:PRK11147 228 RGKLVSYPGNYDQYLLEKEEALrveELQNAEFDrklAQEEVwiRQGIKARRTRNegRVRALKAlrrerSErreVMGTAKM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 461 leklpELKPVDKESEVVmkfpdgFEkfsppilqLDEVDFYYDPKHVI--FSRLSVSADlesRICVVGENGAGKSTMLKLL 538
Cdd:PRK11147 308 -----QVEEASRSGKIV------FE--------MENVNYQIDGKQLVkdFSAQVQRGD---KIALIGPNGCGKTTLLKLM 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 539 LGDLAPVRGIRHAHRNLKIGYFSQHHvEQLDLNVSAVELLAR-----KFPGRPeeeyRHQLG---RYGISGELAMRPLAS 610
Cdd:PRK11147 366 LGQLQADSGRIHCGTKLEVAYFDQHR-AELDPEKTVMDNLAEgkqevMVNGRP----RHVLGylqDFLFHPKRAMTPVKA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEG-GGVTRVE 689
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGnGKIGRYV 520
|
...
gi 148612853 690 GGF 692
Cdd:PRK11147 521 GGY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
197-697 |
8.36e-59 |
|
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: 208.25 E-value: 8.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNLAW--GRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEVAGDDTPALQSVLEsDSVRE--DLLR 266
Cdd:TIGR03719 23 DISLSFfpGAKIGVLGLNGAGKSTLLRIMAgvdkdfNGEARPQPGIKVGYLPQEPQLDPTKTVRENVE-EGVAEikDALD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 267 RERELTAQIAAgraEGSEAAELAEIYAKLEE-IEADKA---PARASVILAGLGFTPKmqQQPTREFSGGWRMRLALARAL 342
Cdd:TIGR03719 102 RFNEISAKYAE---PDADFDKLAAEQAELQEiIDAADAwdlDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 343 FARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLN 422
Cdd:TIGR03719 177 LSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 423 QQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSK--LKMLEKLpelkpvdkESEVVMKFPDGFEKFSPP-------ILQ 493
Cdd:TIGR03719 257 EEKEESARQKTLKRELEWV---RQSP-KGRQAKSKarLARYEEL--------LSQEFQKRNETAEIYIPPgprlgdkVIE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 494 LDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHvEQLDLNVS 573
Cdd:TIGR03719 325 AENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DALDPNKT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 AVELLA----------RKFPGRpeeEYrhqLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 643
Cdd:TIGR03719 403 VWEEISggldiiklgkREIPSR---AY---VGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 644 ETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG-VTRVEGGFDQYRA 697
Cdd:TIGR03719 477 ETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDShVEWFEGNFSEYEE 531
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
188-697 |
1.69e-50 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 184.94 E-value: 1.69e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 188 GDRVLLAgaDVNLAW--GRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEVAGDDTpalQSVLES-- 257
Cdd:PRK11819 18 PKKQILK--DISLSFfpGAKIGVLGLNGAGKSTLLRIMAgvdkefEGEARPAPGIKVGYLPQEPQLDPE---KTVRENve 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVRE--DLLRRERELTAQIAAGRAEGSE-AAELAEIYAKLEEIEADKAPARASVILAGLGFTPKmqQQPTREFSGGWRM 334
Cdd:PRK11819 93 EGVAEvkAALDRFNEIYAAYAEPDADFDAlAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPW--DAKVTKLSGGERR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 335 RLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIK 414
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 415 SKQERLLNQQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSK--LKMLEKLpelkpVDKESEvvmKFPDGFEKFSPP-- 490
Cdd:PRK11819 251 QKAKRLAQEEKQEAARQKALKRELEWV---RQSP-KARQAKSKarLARYEEL-----LSEEYQ---KRNETNEIFIPPgp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 -----ILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHv 565
Cdd:PRK11819 319 rlgdkVIEAENLSKSFGDR-LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSR- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 566 EQLDLN------VSA----VELLARKFPGRpeeEYrhqLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILD 635
Cdd:PRK11819 397 DALDPNktvweeISGgldiIKVGNREIPSR---AY---VGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 636 EPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG-VTRVEGGFDQYRA 697
Cdd:PRK11819 471 EPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGDSqVEWFEGNFQEYEE 533
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
492-684 |
1.54e-48 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 167.24 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQhhveqldln 571
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 572 vsavellarkfpgrpeeeyrhqlgrygisgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 651
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 652 ALNNFRGGVILVSHDERFIRLVCRELWVCEGGG 684
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
178-401 |
1.12e-47 |
|
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: 164.93 E-value: 1.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQevagddtpal 251
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGElepdegIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 qsvlesdsvredllrrereltaqiaagraegseaaelaeiyakleeieadkaparasvilaglgftpkmqqqptreFSGG 331
Cdd:cd03221 71 ----------------------------------------------------------------------------LSGG 74
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 332 WRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd03221 75 EKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
109-414 |
1.43e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 167.55 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 109 LLKREQS----STVNAKKLEKAEARLKAKQE-KRSEKDTLKTSNPLVLEEAsasqagsrkesrlESSGKnksyDV-RIEN 182
Cdd:COG0488 258 KIAKEEEfirrFRAKARKAKQAQSRIKALEKlEREEPPRRDKTVEIRFPPP-------------ERLGK----KVlELEG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 183 FDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAGDDtpalqsvlE 256
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepdsgTVKLGETVKIGYFDQHQEELD--------P 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 257 SDSVREdllrrereltaqiaagraegseaaELAEIYAKLEEIEadkapARAsvILAGLGFTPKMQQQPTREFSGGWRMRL 336
Cdd:COG0488 393 DKTVLD------------------------ELRDGAPGGTEQE-----VRG--YLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 337 ALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIK 414
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
503-706 |
2.00e-40 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 155.61 E-value: 2.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 503 PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNV---------S 573
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVldtvldgdaE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 AVELLARKF-----PGRPEEEYRHQ----------------------LGRYGISGELAMRPLASLSGGQKSRVAFAQMTM 626
Cdd:COG0488 89 LRALEAELEeleakLAEPDEDLERLaelqeefealggweaearaeeiLSGLGFPEEDLDRPVSELSGGWRRRVALARALL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGFDQYRALLQEQFRRE 706
Cdd:COG0488 169 SEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQE 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
178-679 |
1.19e-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: 138.50 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSF--GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPAHISllhVEQEVAGDDTPALqsvl 255
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-GLLPHGGRIS---GEVLLDGRDLLEL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 esdsvREDLLRRERELTAQIAAGRAEGSE-AAELAEIyAKLEEIEADKAPARASVILAGLGFTPKMQQQPTrEFSGGWRM 334
Cdd:COG1123 77 -----SEALRGRRIGMVFQDPMTQLNPVTvGDQIAEA-LENLGLSRAEARARVLELLEAVGLERRLDRYPH-QLSGGQRQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 335 RLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWP-STILVVSHDRNFLNAIATDIIHLHSQRLdgyrgdfe 410
Cdd:COG1123 150 RVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRI-------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 411 tfikskQErllnqqreyeaqqqyrqhiqvfidrfrynANRASQVQSKLKMLEKLPELKPVDKESEVVmkfpdgfEKFSPP 490
Cdd:COG1123 222 ------VE-----------------------------DGPPEEILAAPQALAAVPRLGAARGRAAPA-------AAAAEP 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRL--SVSADLES--RICVVGENGAGKSTMLKLLLG--------------DLAPVRGIRHAH 552
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAvdDVSLTLRRgeTLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSLRE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 553 RNLKIGYFSQHHVEQLDLNVSAVELLA---RKFPGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMT 625
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNPRMTVGDIIAeplRLHGLLSRAERRERvaelLERVGLPPDLADRYPHELSGGQRQRVAIARAL 419
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 626 MPCPNFYILDEPTNHLD-------METIEALGRALNnfrGGVILVSHDERFIRLVCRELWV 679
Cdd:COG1123 420 ALEPKLLILDEPTSALDvsvqaqiLNLLRDLQRELG---LTYLFISHDLAVVRYIADRVAV 477
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
488-682 |
2.59e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 2.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-----KIGYFS 561
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGKPPrrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 562 QHHVEQLDLNVSAVELLA------RKFPGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:COG1121 82 QRAEVDWDFPITVRDVVLmgrygrRGLFRRPSRADReavdEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 632 YILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD-----ERFIRLVC--RELwVCEG 682
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavrEYFDRVLLlnRGL-VAHG 220
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-666 |
7.65e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 120.33 E-value: 7.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIGYFSQHHVE 566
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtsgsirVFGKPLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 567 QLDLNVSAVELLA------RKFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03235 80 DRDFPISVRDVVLmglyghKGLFRRLSKADKAKvdeaLERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 637 PTNHLDMETIEALGRALNNFRG---GVILVSHD 666
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
491-685 |
1.13e-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: 115.14 E-value: 1.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 559
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLLDGRDLaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHHVEQLDLNVSAVELLAR----KFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRyphlGLFGRPSAEDREAveeaLERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 632 YILDEPTNHLDM----ETIEALgRALNNFRG-GVILVSHDerfIRLVCR---ELWVCEGGGV 685
Cdd:COG1120 159 LLLDEPTSHLDLahqlEVLELL-RRLARERGrTVVMVLHD---LNLAARyadRLVLLKDGRI 216
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
179-402 |
1.47e-28 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 114.57 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLhveqeVAGDDtpalqSVLESD 258
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKPDSGSIL-----IDGED-----VRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 SVREDL--LRRERELTaqiaagraEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQpTREFSGGWRMRL 336
Cdd:COG4555 71 EARRQIgvLPDERGLY--------DRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 337 ALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW---PSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
395-477 |
1.24e-27 |
|
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: 106.50 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 395 IHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKES 474
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
...
gi 148612853 475 EVV 477
Cdd:pfam12848 81 PKL 83
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
178-383 |
2.25e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.92 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPA--HISLLhvEQEVAGDDTPALQS-- 253
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG--LLRPTsgEVRVL--GEDVARDPAEVRRRig 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 -VLESDSVREDLlrrerelTAqiaagraegseaAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGW 332
Cdd:COG1131 77 yVPQEPALYPDL-------TV------------RENLRFFARLYGLPRKEARERIDELLELFGLTDAADR-KVGTLSGGM 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 383
Cdd:COG1131 137 KQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
179-402 |
2.58e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 109.91 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPA--HISLLhvEQEVAGDDTPAL----- 251
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA--DLDPPTsgEIYLD--GKPLSAMPPPEWrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 ----QSVLESDSVREDLlrrerELTAQIAAGRAEGSEAAELaeiyakleeieadkaparasviLAGLGFTPKMQQQPTRE 327
Cdd:COG4619 78 yvpqEPALWGGTVRDNL-----PFPFQLRERKFDRERALEL----------------------LERLGLPPDILDKPVER 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:COG4619 131 LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
178-397 |
1.99e-26 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 107.18 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDTPALQSVL-- 255
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAG--LLPPSAGEVLWNGEPIRDAREDYRRRLAyl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 -ESDSVREdllrrerELTaqiaagraegseAAELAEIYAKLEEIEADKAPARASVILAGLGftpKMQQQPTREFSGGWRM 334
Cdd:COG4133 81 gHADGLKP-------ELT------------VRENLRFWAALYGLRADREAIDEALEAVGLA---GLADLPVRQLSAGQKR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 335 RLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRnfLNAIATDIIHL 397
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQP--LELAAARVLDL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
123-420 |
2.48e-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: 110.80 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 123 LEKAEARLK--AKQEKRSEKdTLKTSNPLVLEEASASQAGSRkeSRL---------ESSGKNKSYDVRI----------- 180
Cdd:TIGR03719 247 LEQKQKRLEqeEKEESARQK-TLKRELEWVRQSPKGRQAKSK--ARLaryeellsqEFQKRNETAEIYIppgprlgdkvi 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 --ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEvaGDDTPALQ 252
Cdd:TIGR03719 324 eaENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeqpdsgTIEIGETVKLAYVDQS--RDALDPNK 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 SVLEsdsvredllrrereltaqiaagraegseaaelaEIYAKLEEIEADKA--PARASVilAGLGFTPKMQQQPTREFSG 330
Cdd:TIGR03719 402 TVWE---------------------------------EISGGLDIIKLGKReiPSRAYV--GRFNFKGSDQQKKVGQLSG 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 331 GWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ-RLDGYRGDF 409
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNF 526
|
330
....*....|.
gi 148612853 410 ETFIKSKQERL 420
Cdd:TIGR03719 527 SEYEEDKKRRL 537
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-683 |
2.86e-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: 99.63 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYdPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIrhahrnlkigyfsqhhveqldlnv 572
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 saVELLARKFPGRPEEEYRHQLGRygisgelamrpLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA 652
Cdd:cd00267 56 --ILIDGKDIAKLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....
gi 148612853 653 LNNFRGG---VILVSHDERFIRLVCRELWVCEGG 683
Cdd:cd00267 123 LRELAEEgrtVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
178-464 |
1.02e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.41 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahisllhveqevAGDDTPALQSVLES 257
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL--------------------AGELAPVSGEIGLA 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVREDLLRREreltaQIAAGRAEGSEAAELAEIYAK-LEEIEADkaparasvILAGLGFTPKMQQQPTREFSGGWRMRL 336
Cdd:PRK10636 373 KGIKLGYFAQH-----QLEFLRADESPLQHLARLAPQeLEQKLRD--------YLGGFGFQGDKVTEETRRFSGGEKARL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 337 ALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFiksk 416
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY---- 515
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148612853 417 QERLLNQQREYEAQQQYRQHI-----QVFIDRFRYNANRASQVQSKLKMLEKL 464
Cdd:PRK10636 516 QQWLSDVQKQENQTDEAPKENnansaQARKDQKRREAELRTQTQPLRKEIARL 568
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
179-401 |
1.22e-23 |
|
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: 97.70 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisllhveqevagddtpalqsVLESD 258
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG----------------------------LLKPT 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 SVredllrrereltaqiaagraegseaaelaEIYAKLEEIEADKAPARASVIlaglGFTPkmqqqptrEFSGGWRMRLAL 338
Cdd:cd00267 53 SG-----------------------------EILIDGKDIAKLPLEELRRRI----GYVP--------QLSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 339 ARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP---STILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
178-402 |
3.31e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.06 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLH-------VEQEVAGDDTPA 250
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----------GLIKpdsgeitFDGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 251 LQ---SVLESDSVREDLLRRERELTAQIAAGRAEgseaaelAEIYAKLEEIeadkaparasvilaGLGFTPKmqqQPTRE 327
Cdd:cd03268 71 LRrigALIEAPGFYPNLTARENLRLLARLLGIRK-------KRIDEVLDVV--------------GLKDSAK---KKVKG 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03268 127 FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
492-685 |
1.16e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 97.02 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgyfsqhHVEQLDLN 571
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG--------EV------LVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 572 VSAVELLARK------FP--------------------GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAF 621
Cdd:COG1122 67 KKNLRELRRKvglvfqNPddqlfaptveedvafgpenlGLPREEIRERveeaLELVGLE-HLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 622 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
493-686 |
1.17e-22 |
|
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: 95.58 E-value: 1.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFS 561
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGeilldgkdlasLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 562 QhhveqldlnvsAVELLarkfpgrpeeeyrhqlgryGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL 641
Cdd:cd03214 80 Q-----------ALELL-------------------GLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 642 D-------METIEALGRALNNfrgGVILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:cd03214 129 DiahqielLELLRRLARERGK---TVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
123-420 |
2.14e-22 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 101.73 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 123 LEKAEARLKakQEKRSEKDTLKT---------SNPlvleeaSASQAGSRkeSRL---------ESSGKNKSYDVRI---- 180
Cdd:PRK11819 249 LEQKAKRLA--QEEKQEAARQKAlkrelewvrQSP------KARQAKSK--ARLaryeellseEYQKRNETNEIFIppgp 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 ---------ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAG 245
Cdd:PRK11819 319 rlgdkvieaENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeqpdsgTIKIGETVKLAYVDQSRDA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 246 -DDTpalQSVLEsdsvredllrrereltaqiaagraegseaaelaEIYAKLEEIEADKA--PARASVilAGLGFTPKMQQ 322
Cdd:PRK11819 399 lDPN---KTVWE---------------------------------EISGGLDIIKVGNReiPSRAYV--GRFNFKGGDQQ 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 323 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAilwLENYLQTWPSTILVVSHDRNFLNAIATDIIhlhS 399
Cdd:PRK11819 441 KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVetlRA---LEEALLEFPGCAVVISHDRWFLDRIATHIL---A 514
|
330 340
....*....|....*....|....*
gi 148612853 400 QRLDG----YRGDFETFIKSKQERL 420
Cdd:PRK11819 515 FEGDSqvewFEGNFQEYEEDKKRRL 539
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
178-402 |
4.83e-22 |
|
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: 93.62 E-value: 4.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPahisllhveqevagddtpalqsvlES 257
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKP------------------------DS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVR---EDLLRRERELTAQIAAgraegseAAELAEIYAKLeeieadkaparaSVI--LaglgftpkmqqqptrEFSGGW 332
Cdd:cd03230 55 GEIKvlgKDIKKEPEEVKRRIGY-------LPEEPSLYENL------------TVRenL---------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
488-702 |
5.10e-22 |
|
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: 100.60 E-value: 5.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLK 556
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsilingvdlsdLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQH-HVEQLDL--NVsaveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQ 623
Cdd:COG4988 413 IAWVPQNpYLFAGTIreNL----RLGR--PDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 624 MTM-PCPnFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLvCRELWVCEGGGVtrVEGGfdQYRALLQ 700
Cdd:COG4988 487 ALLrDAP-LLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRI--VEQG--THEELLA 560
|
..
gi 148612853 701 EQ 702
Cdd:COG4988 561 KN 562
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
490-679 |
8.33e-22 |
|
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: 94.08 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYYDpKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIG---YFSQ--- 562
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNGEPIRDAredYRRRlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 --HHVEqLDLNVSAVELLA--RKFPGR--PEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:COG4133 80 lgHADG-LKPELTVRENLRfwAALYGLraDREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148612853 637 PTNHLDMETIEALGRALNNFR---GGVILVSHDERFIRlVCRELWV 679
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELA-AARVLDL 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
178-674 |
3.00e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 97.95 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML------ATRSLRVPAHISL----LHVE-QEVAGD 246
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyEPTSGRIIYHVALcekcGYVErPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 247 DTPALQSVLE---------SDSVREDLLRRereltAQIAAGR--AEGSEAAELAEIYAKLEEI--EADKAPARASVILAG 313
Cdd:TIGR03269 81 PCPVCGGTLEpeevdfwnlSDKLRRRIRKR-----IAIMLQRtfALYGDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 314 LGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDvrailwlenylqtwPSTilvvshdrnflnaiaTD 393
Cdd:TIGR03269 156 VQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD--------------PQT---------------AK 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 394 IIHlhsqrldgyrgdfetfikskqERLLNQQREYEAQQQYRQHIQVFIdrfrynanraSQVQSKLKMLEKlPELKPVDKE 473
Cdd:TIGR03269 206 LVH---------------------NALEEAVKASGISMVLTSHWPEVI----------EDLSDKAIWLEN-GEIKEEGTP 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 474 SEVVMKFPDGFEKFSP--------PILQLDEVDFYYDP--KHVIFSRLSVSADLESR--ICVVGENGAGKSTMLKLLLGD 541
Cdd:TIGR03269 254 DEVVAVFMEGVSEVEKecevevgePIIKVRNVSKRYISvdRGVVKAVDNVSLEVKEGeiFGIVGTSGAGKTTLSKIIAGV 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 542 LAPV-----------------RGIRHAHRNLK-IGYFSQH-----HVEQLDLNVSAVEL-----LAR-------KFPGRP 586
Cdd:TIGR03269 334 LEPTsgevnvrvgdewvdmtkPGPDGRGRAKRyIGILHQEydlypHRTVLDNLTEAIGLelpdeLARmkavitlKMVGFD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGV----IL 662
Cdd:TIGR03269 414 EEKAEEILDKYP----------DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqtfII 483
|
570
....*....|..
gi 148612853 663 VSHDERFIRLVC 674
Cdd:TIGR03269 484 VSHDMDFVLDVC 495
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
521-682 |
3.65e-21 |
|
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: 92.55 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRGI---------------RHAHRNLKIGY-FSQHH------VEQldlNVSAVELL 578
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdisklsekeLAAFRRRHIGFvFQSFNllpdltALE---NVELPLLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 579 ARKFPGRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALNN 655
Cdd:cd03255 110 AGVPKKERRERAEELLERVGLGDRLNHYP-SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNK 188
|
170 180
....*....|....*....|....*...
gi 148612853 656 FRG-GVILVSHDERFIRLVCRELWVCEG 682
Cdd:cd03255 189 EAGtTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
203-356 |
4.82e-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: 90.01 E-value: 4.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHveQEVAGDDTPALQ---SVLESDSVredLLRREReltaqiaagr 279
Cdd:pfam00005 11 GEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG--QDLTDDERKSLRkeiGYVFQDPQ---LFPRLT---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 280 aegseAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKM---QQQPTREFSGGWRMRLALARALFARPDLLLLDEPTN 356
Cdd:pfam00005 76 -----VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
520-639 |
5.06e-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: 90.01 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 520 RICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFSQHHV--------EQLDLNVSAVELLAR 580
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdltdDERKSLRKEIGYVFQDPQlfprltvrENLRLGLLLKGLSKR 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 581 KFPGRPEEeYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:pfam00005 93 EKDARAEE-ALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
184-402 |
8.66e-21 |
|
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: 91.63 E-value: 8.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 184 DVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQ---EVAGDDT--------- 248
Cdd:COG1122 5 NLSFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN----------GLLKPTSgevLVDGKDItkknlrelr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 ---------PALQSVleSDSVREDLlrrereltaqiaagrAEGSEAAELAEiyaklEEIEAdkapaRASVILAGLGFTpK 319
Cdd:COG1122 75 rkvglvfqnPDDQLF--APTVEEDV---------------AFGPENLGLPR-----EEIRE-----RVEEALELVGLE-H 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 320 MQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIH 396
Cdd:COG1122 127 LADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIV 206
|
....*.
gi 148612853 397 LHSQRL 402
Cdd:COG1122 207 LDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
179-401 |
1.09e-20 |
|
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: 90.99 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLhvEQEVAGDDT-------- 248
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIkkGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD--GKDLTKLSLkelrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 -----PALQsvLESDSVREDLlrrereltaqiaagrAEGSEAAELAEiyaklEEIEAdkapaRASVILAGLGFTPkMQQQ 323
Cdd:cd03225 79 lvfqnPDDQ--FFGPTVEEEV---------------AFGLENLGLPE-----EEIEE-----RVEEALELVGLEG-LRDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 324 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 148612853 401 R 401
Cdd:cd03225 211 K 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
500-683 |
3.00e-20 |
|
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: 89.45 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 500 YYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY--------F 560
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDLtklslkelrrKVGLvfqnpddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHVEQlDLNVSAVELlarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03225 89 FGPTVEE-EVAFGLENL------GLPEEEIEERveeaLELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 637 PTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGG 683
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
112-416 |
3.60e-20 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 94.57 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 112 REQSSTVNAKKLEK-AE-----ARL-----KAKQE----KRSEKdtlktsnpLVLEEASASqagSRKES--RLESSGKNK 174
Cdd:PRK15064 248 RERLLADNAKKKAQiAElqsfvSRFsanasKAKQAtsraKQIDK--------IKLEEVKPS---SRQNPfiRFEQDKKLH 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 175 SYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSV 254
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV--------------------GELEPDSGTV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDSVR--------EDLLRRERELTAQIAAGRAEGSeaaelaeiyakleeieaDKAPARAsvILAGLGFTPKMQQQPTR 326
Cdd:PRK15064 377 KWSENANigyyaqdhAYDFENDLTLFDWMSQWRQEGD-----------------DEQAVRG--TLGRLLFSQDDIKKSVK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYR 406
Cdd:PRK15064 438 VLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFS 517
|
330
....*....|
gi 148612853 407 GDFETFIKSK 416
Cdd:PRK15064 518 GTYEEYLRSQ 527
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
492-674 |
5.24e-20 |
|
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: 87.84 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrlsVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLK-IGY 559
Cdd:cd03230 1 IEVRNLSKRYGKKTALDD---ISLTVEkgEIYGLLGPNGAGKTTLIKIILGLLKPDSGeikvlgkdiKKEPEEVKRrIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHhvEQLDLNVSAVELLarkfpgrpeeeyrhqlgrygisgelamrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:cd03230 78 LPEE--PSLYENLTVRENL-------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 148612853 640 HLDMETIEALGRALNNFR---GGVILVSHDERFIRLVC 674
Cdd:cd03230 125 GLDPESRREFWELLRELKkegKTILLSSHILEEAERLC 162
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
178-383 |
7.04e-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: 88.97 E-value: 7.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisLLHVEQ---EVAGDDTpalqsV 254
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT----------LLKPTSgraTVAGHDV-----V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDSVREDL------LRRERELTAQiaagraegseaaELAEIYAKLEEIEADKAPARASVILAGLGFTPKmQQQPTREF 328
Cdd:cd03265 66 REPREVRRRIgivfqdLSVDDELTGW------------ENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTY 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAILW--LENYLQTWPSTILVVSHD 383
Cdd:cd03265 133 SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPqtRAHVWeyIEKLKEEFGMTILLTTHY 191
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
461-702 |
9.41e-20 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 94.13 E-value: 9.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 461 LEKLPELkpVDKESEVvmkfPDGFEKFSPPILQ----LDEVDFYYDPKHV-IFSRLSVSADLESRICVVGENGAGKSTML 535
Cdd:COG2274 445 LERLDDI--LDLPPER----EEGRSKLSLPRLKgdieLENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 536 KLLLGDLAPVRG--------IRHAHRNL---KIGYFSQHhvEQLdLNVSAVE--LLARkfPGRPEEEYRHQLGRYGISGE 602
Cdd:COG2274 519 KLLLGLYEPTSGrilidgidLRQIDPASlrrQIGVVLQD--VFL-FSGTIREniTLGD--PDATDEEIIEAARLAGLHDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 603 LAMRPL----------ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFI 670
Cdd:COG2274 594 IEALPMgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI 673
|
250 260 270
....*....|....*....|....*....|....*....
gi 148612853 671 RLvCRELWVCEGGGVTRvEGGFDQ-------YRALLQEQ 702
Cdd:COG2274 674 RL-ADRIIVLDKGRIVE-DGTHEEllarkglYAELVQQQ 710
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
178-420 |
1.41e-19 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 88.50 E-value: 1.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPA--HISLLhvEQEVAGDDTPALQSV- 254
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII--GLLRPDsgEILVD--GQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 ------------LESDSVREDL---LRRERELTAqiaagraegSEAAELAEiyAKLEEIE----ADKAPArasvilaglg 315
Cdd:COG1127 82 rrigmlfqggalFDSLTVFENVafpLREHTDLSE---------AEIRELVL--EKLELVGlpgaADKMPS---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 316 ftpkmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQ-TWPSTILVVSHDRNFLNAIA 391
Cdd:COG1127 141 -----------ELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTHDLDSAFAIA 209
|
250 260
....*....|....*....|....*....
gi 148612853 392 TDIIHLHSQRLDGYrGDFETFIKSKQERL 420
Cdd:COG1127 210 DRVAVLADGKIIAE-GTPEELLASDDPWV 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
521-685 |
1.65e-19 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 87.31 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-KFPGRPEEEYR 591
Cdd:cd03226 29 IALTGKNGAGKTTLAKILAGLIKESSGsillngkpIKAKERRKSIGYVMQDVDYQLFTDSVREELLLGlKELDAGNEQAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 592 HQLGRYGISGELAMRPLaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNNFRGGVILVSHDER 668
Cdd:cd03226 109 TVLKDLDLYALKERHPL-SLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYE 187
|
170
....*....|....*...
gi 148612853 669 FIRLVC-RELWVCEGGGV 685
Cdd:cd03226 188 FLAKVCdRVLLLANGAIV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
492-683 |
2.52e-19 |
|
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: 85.90 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHV-IFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQLDL 570
Cdd:cd03228 1 IEFKNVSFSYPGRPKpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG--------EI-LIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 571 nvsavellarkfpgrpeEEYRHQLG-------------RYGIsgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03228 72 -----------------ESLRKNIAyvpqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 638 TNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLvCRELWVCEGG 683
Cdd:cd03228 124 TSALDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
489-665 |
3.96e-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: 87.45 E-value: 3.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 489 PPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHa 551
Cdd:COG1119 1 DPLLELRNVTVRRGGK-TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvweLRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 552 hrnlKIGYFSQHHVEQLDLNVSAVELLARKF------PGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAF 621
Cdd:COG1119 79 ----RIGLVSPALQLRFPRDETVLDVVLSGFfdsiglYREPTDEQRERarelLELLGLA-HLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 622 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSH 665
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
492-685 |
7.78e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 85.64 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKhVIFSrlSVSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIG 558
Cdd:COG4619 1 LELEGLSFRVGGK-PILS--PVSLTLEAgeCVAITGPSGSGKSTLLRALADLDPPTSGeIYLDGKPLsampppewrrQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 559 YFSQH------HVEQldlNVSAVELLARKFPGRpeEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:COG4619 78 YVPQEpalwggTVRD---NLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 633 ILDEPTNHLDMETIEALGRALNNFR----GGVILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLaeegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
130-393 |
7.80e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.78 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 130 LKAKQEKRSEKDTLKTSNPLVLEEASasqagsrkesrleSSGKnksYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLV 209
Cdd:PRK11147 288 LKALRRERSERREVMGTAKMQVEEAS-------------RSGK---IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 210 GRNGLGKTTLLKM----LATRSLRVPAHISLlhveqEVAgddtpalqsvlESDSVREDLlRRERELTAQIAAGRaegsea 285
Cdd:PRK11147 352 GPNGCGKTTLLKLmlgqLQADSGRIHCGTKL-----EVA-----------YFDQHRAEL-DPEKTVMDNLAEGK------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 286 aelaeiyaklEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARaLFARP-DLLLLDEPTNMLDVRAIL 364
Cdd:PRK11147 409 ----------QEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLE 477
|
250 260
....*....|....*....|....*....
gi 148612853 365 WLENYLQTWPSTILVVSHDRNFLNAIATD 393
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVDNTVTE 506
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
491-689 |
1.06e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------------K 556
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqVLVNGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQHHveQL--DLNVSavELLArkFP----GRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTM 626
Cdd:COG2884 81 IGVVFQDF--RLlpDRTVY--ENVA--LPlrvtGKSRKEIRRRvrevLDLVGLSDKAKALP-HELSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHDERFIRLVCRELWVCEGGGVTRVE 689
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEInRRGttVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
524-666 |
1.21e-18 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 85.50 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK--IGYFSQHHVeqLDLNVSAVELL-----ARKFPGRPEE 588
Cdd:COG1131 32 LGPNGAGKTTTIRMLLGLLRPTSGevrvlgedVARDPAEVRrrIGYVPQEPA--LYPDLTVRENLrffarLYGLPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 589 EYRHQ-LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVS 664
Cdd:COG1131 110 ERIDElLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVLLST 188
|
..
gi 148612853 665 HD 666
Cdd:COG1131 189 HY 190
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
523-685 |
1.69e-18 |
|
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: 85.64 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAP-----------VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-----KFPGRP 586
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPdagtvdlagvdLHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRiphrsLWAGDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEY---RHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALgRALNNFRGG 659
Cdd:TIGR03873 112 PHDAavvDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraqLETLALV-RELAATGVT 189
|
170 180
....*....|....*....|....*.
gi 148612853 660 VILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:TIGR03873 190 VVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-666 |
1.74e-18 |
|
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: 85.29 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDpKHVIFSRLSVSADlESRI-CVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL---------KIGYF 560
Cdd:COG4555 2 IEVENLSKKYG-KVPALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGsILIDGEDVrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHVeqLDLNVSA---VELLARKFPGRPE------EEYRHQLGRygisGELAMRPLASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:COG4555 80 PDERG--LYDRLTVrenIRYFAELYGLFDEelkkriEELIELLGL----EEFLDRRVGELSTGMKKKVALARALVHDPKV 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 148612853 632 YILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD 666
Cdd:COG4555 154 LLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHI 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
179-402 |
2.80e-18 |
|
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: 82.87 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPA-HISLlhveqevagDDTPalqsvLES 257
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPSSgEILL---------DGKD-----LAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVREdlLRRERELTAQiaagraegseAAELAEIyakleeieADKAparasvilaglgftpkmqQQPTREFSGGWRMRLA 337
Cdd:cd03214 66 LSPKE--LARKIAYVPQ----------ALELLGL--------AHLA------------------DRPFNELSGGERQRVL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAhqiELLeLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
178-402 |
3.17e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 84.85 E-value: 3.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-------------TRSLRVPAHISLLHVE 240
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglerpwsgevtfdGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 241 QEVAGDDTPAL---QSVLesDSVREDL-LRRERELTAQIAagraegsEAAELAEIYAKLeeieADKAParasvilaglgf 316
Cdd:COG1124 82 QMVFQDPYASLhprHTVD--RILAEPLrIHGLPDREERIA-------ELLEQVGLPPSF----LDRYP------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 317 tpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTWPSTILVVSHDRNFLNAIAT 392
Cdd:COG1124 137 ---------HQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsVQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCD 207
|
250
....*....|
gi 148612853 393 DIIHLHSQRL 402
Cdd:COG1124 208 RVAVMQNGRI 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
492-685 |
6.93e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.02 E-value: 6.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDP-KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGY 559
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtdirqLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHHV-------EQL---DLNVSAVELL-ARKFPGRPEEEYRH------QLGRYGisgelamrplASLSGGQKSRVAFA 622
Cdd:cd03245 83 VPQDVTlfygtlrDNItlgAPLADDERILrAAELAGVTDFVNKHpngldlQIGERG----------RGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 623 QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCReLWVCEGGGV 685
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLVDR-IIVMDSGRI 216
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
178-402 |
1.06e-17 |
|
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: 82.54 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGD----RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLlhveqEVAGDDTPALqs 253
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEV-----RVDGTDISKL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 vlesDSVREDLLRRER------------ELTAqiaagraegSEAAELAEIYAKLEEIEAdkaPARASVILAGLGFTPKMQ 321
Cdd:cd03255 72 ----SEKELAAFRRRHigfvfqsfnllpDLTA---------LENVELPLLLAGVPKKER---RERAEELLERVGLGDRLN 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 322 QQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENYLQTwpsTILVVSHDRNfLNAIATDI 394
Cdd:cd03255 136 HYPS-ELSGGQQQRVAIARALANDPKIILADEPTGNLDsetgkevMELLRELNKEAGT---TIVVVTHDPE-LAEYADRI 210
|
....*...
gi 148612853 395 IHLHSQRL 402
Cdd:cd03255 211 IELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
178-402 |
1.09e-17 |
|
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: 82.18 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGddTPALQS---- 253
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--GLERPDSGEILIDGRDVTG--VPPERRnigm 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESD------SVREDL---LRRERELTAQIAAgRAEgsEAAELAEIyakleEIEADKAPArasvilaglgftpkmqqqp 324
Cdd:cd03259 77 VFQDYalfphlTVAENIafgLKLRGVPKAEIRA-RVR--ELLELVGL-----EGLLNRYPH------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 325 trEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:cd03259 130 --ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVMNEG 207
|
..
gi 148612853 401 RL 402
Cdd:cd03259 208 RI 209
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
179-397 |
2.13e-17 |
|
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: 81.15 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDDTPA------- 250
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA--GLIKESSGSIL-----LNGKPIKAkerrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 251 ---LQSV---LESDSVREDLLRREREltaqiaagraegseaaelaeiyakleeieADKAPARASVILAGLGFTPKMQQQP 324
Cdd:cd03226 74 gyvMQDVdyqLFTDSVREELLLGLKE-----------------------------LDAGNEQAETVLKDLDLYALKERHP 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 325 tREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03226 125 -LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
178-402 |
2.82e-17 |
|
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: 82.01 E-value: 2.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRvPA--HISLlhveqevagDDTPalqsvL 255
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLK-PSsgEVLL---------DGRD-----L 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 ESDSVREdlLRRERELTAQiAAGRAEGSEAAELAEI----YAKL--EEIEADKAPARASVILAGLGftpKMQQQPTREFS 329
Cdd:COG1120 66 ASLSRRE--LARRIAYVPQ-EPPAPFGLTVRELVALgrypHLGLfgRPSAEDREAVEEALERTGLE---HLADRPVDELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 330 GGWRMRLALARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqlEVLeLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
203-682 |
5.13e-17 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 84.84 E-value: 5.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVlESDSVREDLLRREReltaqiaagraeG 282
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILS--------------------GELKPNLGDY-DEEPSWDEVLKRFR------------G 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 283 SEAAE-LAEIYAKleEIEA-------DKAP----ARASVILAG-------------LGFTPKMQQqPTREFSGGWRMRLA 337
Cdd:COG1245 146 TELQDyFKKLANG--EIKVahkpqyvDLIPkvfkGTVRELLEKvdergkldelaekLGLENILDR-DISELSGGELQRVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIHLhsqrLDGYRGDFETF 412
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDIYqrlnvARLIRE--LAEEGKYVLVVEHDLAILDYLA-DYVHI----LYGEPGVYGVV 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 413 IKSKQerllnqqreyeaqqqYRQHIQVFID--------RFRynanrasqvQSKLKMLEKLPelkPVDKESEVVMKFPDgF 484
Cdd:COG1245 296 SKPKS---------------VRVGINQYLDgylpeenvRIR---------DEPIEFEVHAP---RREKEEETLVEYPD-L 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 485 EKfsppilQLDEvdfyydpkhviFSrLSVSADlESR----ICVVGENGAGKSTMLKLLLGDLAPVRGIrhAHRNLKIGYF 560
Cdd:COG1245 348 TK------SYGG-----------FS-LEVEGG-EIRegevLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHVEQLDLNVSAV--ELLARKFPGRPeeeYRHQLGR-YGISgELAMRPLASLSGGQKSRVAFAQmtmpC----PNFYI 633
Cdd:COG1245 407 PQYISPDYDGTVEEFlrSANTDDFGSSY---YKTEIIKpLGLE-KLLDKNVKDLSGGELQRVAIAA----ClsrdADLYL 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 148612853 634 LDEPTNHLDMETIEALGRALNNF---RG-GVILVSHDERFIRLVCRELWVCEG 682
Cdd:COG1245 479 LDEPSAHLDVEQRLAVAKAIRRFaenRGkTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
179-397 |
5.47e-17 |
|
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: 80.27 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----TR-SLRV---PAHISLLHV----EQEVAG 245
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkpTSgSIRVfgkPLEKERKRIgyvpQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 246 DDTPAlqSVLesDSVREDLLRRERELTAQIAAGRAEGSEAAELAEIYAKLEeieadkaparasvilaglgftpkmqqQPT 325
Cdd:cd03235 81 RDFPI--SVR--DVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELAD--------------------------RQI 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKtqeDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
501-681 |
5.55e-17 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 84.79 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 501 YDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQhhvE-QLDL------NV- 572
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ---EpQLDPektvreNVe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 ----SAVELLAR------KFpGRPEEEYR----------------------HQLgrygisgELAM---R------PLASL 611
Cdd:PRK11819 93 egvaEVKAALDRfneiyaAY-AEPDADFDalaaeqgelqeiidaadawdldSQL-------EIAMdalRcppwdaKVTKL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 612 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRelWVCE 681
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
173-402 |
5.68e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 84.82 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 173 NKSYDVRIEnfDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHVE-QEVAGD 246
Cdd:COG4987 329 PGGPSLELE--DVSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLDPQSgSITLGGVDlRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 247 DTPALQSVLE------SDSVREDLLrrereltaqIAAGRAegSEAaelaEIYAKLEeieadkaparasviLAGLGftPKM 320
Cdd:COG4987 406 DLRRRIAVVPqrphlfDTTLRENLR---------LARPDA--TDE----ELWAALE--------------RVGLG--DWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 321 QQQPT----------REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWP-STILVVSHDRNF 386
Cdd:COG4987 455 AALPDgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAgRTVLLITHRLAG 532
|
250
....*....|....*.
gi 148612853 387 LnAIATDIIHLHSQRL 402
Cdd:COG4987 533 L-ERMDRILVLEDGRI 547
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
178-395 |
8.71e-17 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 79.86 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahISLLHVEQ---EVAGDDTPA 250
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI----------LGLLKPTSgsiIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 251 LQsvlesdsvREDLLRRERELT-----------------AQIAagraegsEAAELAEIYAKLEEIEAdkapaRASVILAG 313
Cdd:cd03257 72 LS--------RRLRKIRRKEIQmvfqdpmsslnprmtigEQIA-------EPLRIHGKLSKKEARKE-----AVLLLLVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 314 LGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQT-WPSTILVVSHDRNFLNA 389
Cdd:cd03257 132 VGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAK 211
|
....*.
gi 148612853 390 IATDII 395
Cdd:cd03257 212 IADRVA 217
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
488-682 |
1.01e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 84.05 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDP-KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK--------- 556
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsITLGGVDLRdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 -IGYFSQH-HV------EQLdlnvsaveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSR 618
Cdd:COG4987 410 rIAVVPQRpHLfdttlrENL--------RLAR--PDATDEELWAALERVGLGDWLAALPDgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 619 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELWVCEG 682
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMDRILVLEDG 545
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
152-416 |
1.17e-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: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 152 EEASASQAGSRKESRLESSgknksyDVRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRV 230
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPP------SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL--GFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 231 PAHISLLHVEQEVAGDDTPALQ---------SVLESDSVREDLLRrereltAQIAAGRAEGSEAAELAEIYAKLEEIEAd 301
Cdd:COG4988 389 PYSGSILINGVDLSDLDPASWRrqiawvpqnPYLFAGTIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPD- 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 302 kaparasvilaGL-------GFTpkmqqqptreFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--AILW--LENYL 370
Cdd:COG4988 462 -----------GLdtplgegGRG----------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLA 520
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148612853 371 QTwpSTILVVSHDRNFLnAIATDIIHLHSQRLDGyRGDFETFIKSK 416
Cdd:COG4988 521 KG--RTVILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKN 562
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
186-383 |
1.19e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 186 SFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEVAGDDT-PAlqSVLESD 258
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptSGTVRRAGGARVAYVPQRSEVPDSlPL--TVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 SV----REDLLRREReltaqiAAGRAEGSEAAElaeiyakleeieadkaparaSVILAGLGftpkmqQQPTREFSGGWRM 334
Cdd:NF040873 79 AMgrwaRRGLWRRLT------RDDRAAVDDALE--------------------RVGLADLA------GRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 335 RLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 383
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
178-397 |
1.26e-16 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 80.13 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAHISllHVEQEV 243
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILgllpptsgtvrlfgKPPRRARRRIG--YVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 244 AGD-DTPAlqsvlesdSVRE----------DLLRREReltaqiaagraegseAAELAEIYAKLEEIEadkaparasviLA 312
Cdd:COG1121 85 EVDwDFPI--------TVRDvvlmgrygrrGLFRRPS---------------RADREAVDEALERVG-----------LE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 313 GLgftpkmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNA 389
Cdd:COG1121 131 DL------ADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVRE 204
|
....*...
gi 148612853 390 IATDIIHL 397
Cdd:COG1121 205 YFDRVLLL 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
183-407 |
1.28e-16 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 79.33 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 183 FDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisLLHVEQ---EVAGDDTpalqsvlesds 259
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG----------LLEPDAgfaTVDGFDV----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 VREDLLRRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALA 339
Cdd:cd03266 70 VKEPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDR-RVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 340 RALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLdGYRG 407
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV-VYEG 218
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
450-675 |
2.50e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 82.99 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 450 RASQVQSKLKMLEKLPELkPVDkesevvmkFPDGFEKFSPPILQ----LDEVDFYY--DPKHVIfsrLSVSADLE--SRI 521
Cdd:TIGR03375 427 RYQQAKTALQSLDELMQL-PVE--------RPEGTRFLHRPRLQgeieFRNVSFAYpgQETPAL---DNVSLTIRpgEKV 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAH-----RNlkIGYFSQHHV-------EQLDL---NVSAVELL 578
Cdd:TIGR03375 495 AIIGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdIRQIDpadlrRN--IGYVPQDPRlfygtlrDNIALgapYADDEEIL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 579 --ARK-----FPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 651
Cdd:TIGR03375 573 raAELagvteFVRRHPDGLDMQIGERG----------RSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKD 642
|
250 260
....*....|....*....|....*.
gi 148612853 652 ALNNFRGG--VILVSHDERFIRLVCR 675
Cdd:TIGR03375 643 RLKRWLAGktLVLVTHRTSLLDLVDR 668
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
178-382 |
2.79e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTPALQSV--- 254
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLL--GLTHPDAGSISLCGEPVPSRARHARQRVgvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 -----LESD-SVREDLLrrereltaqiAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVilaglgftpkmqqqptREF 328
Cdd:PRK13537 86 pqfdnLDPDfTVRENLL----------VFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----------------GEL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTwPSTILVVSH 382
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLAR-GKTILLTTH 196
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
158-383 |
3.80e-16 |
|
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: 82.02 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 158 QAGSRKESRLESSGKNKSYDVRIENFDVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAH- 233
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPTLELRDLSAgypGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA--GLLDPLQg 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 234 -ISLLHVE-QEVAGDDTPALQSVLESD------SVREDLLrrereltaqIAAGRAEGSEAAELAEiYAKLEEIeADKAPA 305
Cdd:TIGR02868 391 eVTLDGVPvSSLDQDEVRRRVSVCAQDahlfdtTVRENLR---------LARPDATDEELWAALE-RVGLADW-LRALPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 306 RASVILAGLGftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL-WLENYLQTWPS-TILVVSHD 383
Cdd:TIGR02868 460 GLDTVLGEGG----------ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
488-672 |
5.67e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.56 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLK 556
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsiavngvpladADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQHHVeQLDLNVSAVELLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTM 626
Cdd:TIGR02857 398 IAWVPQHPF-LFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRL 672
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL 522
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
150-383 |
5.80e-16 |
|
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: 81.80 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 150 VLEEASASQAGSRKESRLESSGknksyDVRIENfdVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA- 224
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKG-----DIELEN--VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLg 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 225 --------------------TRSLRvpAHISLlhVEQEVagddtpalqsVLESDSVREDllrrereltaqIAAGRAEGS- 283
Cdd:COG2274 524 lyeptsgrilidgidlrqidPASLR--RQIGV--VLQDV----------FLFSGTIREN-----------ITLGDPDATd 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 284 ----EAAELAEIyakLEEIEADkaPAR-ASVILAGlGftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNML 358
Cdd:COG2274 579 eeiiEAARLAGL---HDFIEAL--PMGyDTVVGEG-G----------SNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
250 260 270
....*....|....*....|....*....|
gi 148612853 359 DV---RAILwleNYLQTW--PSTILVVSHD 383
Cdd:COG2274 643 DAeteAIIL---ENLRRLlkGRTVIIIAHR 669
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
203-682 |
6.03e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 6.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLESDSvREDLLRREReltaqiaagraeG 282
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILS--------------------GELIPNLGDYEEEPS-WDEVLKRFR------------G 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 283 SEAAE-LAEIYAKleEIEA-------DKAP----ARASVILAG-------------LGFTPKMQQqPTREFSGGWRMRLA 337
Cdd:PRK13409 146 TELQNyFKKLYNG--EIKVvhkpqyvDLIPkvfkGKVRELLKKvdergkldevverLGLENILDR-DISELSGGELQRVA 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 338 LARALFARPDLLLLDEPTNMLDV-------RAILWL-ENylqtwpSTILVVSHDRNFLNAIAtDIIHLhsqrLDGYRGDF 409
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIrqrlnvaRLIRELaEG------KYVLVVEHDLAVLDYLA-DNVHI----AYGEPGAY 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 410 ETFIKSKQERllnqqreyEAQQQYrqhIQVFID----RFRynanrasqvQSKLKMLEKLPElkpVDKESEVVMKFPDgFE 485
Cdd:PRK13409 292 GVVSKPKGVR--------VGINEY---LKGYLPeenmRIR---------PEPIEFEERPPR---DESERETLVEYPD-LT 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 486 KfsppilQLDevDFyydpkhvifsRLSVSADlESR----ICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFS 561
Cdd:PRK13409 348 K------KLG--DF----------SLEVEGG-EIYegevIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 562 QHHVEQLDLNVSavELLARKFPGRPEEEYRHQLGR-YGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 640
Cdd:PRK13409 407 QYIKPDYDGTVE--DLLRSITDDLGSSYYKSEIIKpLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAH 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 148612853 641 LDME----TIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEG 682
Cdd:PRK13409 484 LDVEqrlaVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
522-666 |
7.57e-16 |
|
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: 77.16 E-value: 7.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNlkIGYFSQHHVeqLDLNVSAVELL---ARkFPGRP 586
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGtayingysirtdRKAARQS--LGYCPQFDA--LFDELTVREHLrfyAR-LKGLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEYRHQLGRYGISGEL---AMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VI 661
Cdd:cd03263 107 KSEIKEEVELLLRVLGLtdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGrsII 186
|
....*
gi 148612853 662 LVSHD 666
Cdd:cd03263 187 LTTHS 191
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
504-683 |
9.58e-16 |
|
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: 76.56 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 504 KHVIFSRLSVSADL-ESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQHHveQ 567
Cdd:cd03297 8 KRLPDFTLKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtIVLNGTVLfdsrkkinlppqqrKIGLVFQQY--A 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 568 LDLNVSAVELLA----RKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 643
Cdd:cd03297 86 LFPHLNVRENLAfglkRKRNREDRISVDELLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148612853 644 ET----IEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGG 683
Cdd:cd03297 165 ALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
178-383 |
1.02e-15 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 76.84 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslRVPAHISLLHVEQEV--AGDDTPALQsvl 255
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLN----RLNDLIPGAPDEGEVllDGKDIYDLD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 esdsVREDLLRRERELTAQ------------IAAG-RAEGS-EAAELAEIYAK------LEEIEADKAPArasvilaglg 315
Cdd:cd03260 74 ----VDVLELRRRVGMVFQkpnpfpgsiydnVAYGlRLHGIkLKEELDERVEEalrkaaLWDEVKDRLHA---------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 316 ftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWpsTILVVSHD 383
Cdd:cd03260 140 ----------LGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIaelkKEY--TIVIVTHN 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
490-667 |
1.10e-15 |
|
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: 80.48 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIG 558
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 559 YFSQH-HVeqLDLNVSAVELLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMP 627
Cdd:TIGR02868 413 VCAQDaHL--FDTTVRENLRLAR--PDATDEELWAALERVGLADWLRALPDgldtvlgeggARLSGGERQRLALARALLA 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 628 CPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDE 667
Cdd:TIGR02868 489 DAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHHL 530
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
178-402 |
1.16e-15 |
|
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: 76.77 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahISLLHVEQ---EVAGDDTPAL--- 251
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI----------VGLLRPDSgevLIDGEDISGLsea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 --------------QSVLESD-SVREDL---LRRERELTAqiaagraegseaaelaeiyaklEEIEAdkapaRASVILAG 313
Cdd:cd03261 71 elyrlrrrmgmlfqSGALFDSlTVFENVafpLREHTRLSE----------------------EEIRE-----IVLEKLEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 314 LGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENYLQTwpsTILVVSHDRNF 386
Cdd:cd03261 124 VGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDT 199
|
250
....*....|....*.
gi 148612853 387 LNAIATDIIHLHSQRL 402
Cdd:cd03261 200 AFAIADRIAVLYDGKI 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
506-664 |
2.06e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.68 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 506 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIG-YFSQ-H---HVEQLDLNVSAVELLA 579
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDIDDPdVAEAcHylgHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 580 --RKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA----L 653
Cdd:PRK13539 96 fwAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELirahL 174
|
170
....*....|.
gi 148612853 654 NnfRGGVILVS 664
Cdd:PRK13539 175 A--QGGIVIAA 183
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
173-402 |
2.64e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 173 NKSYDVRIENFDVsfgdrvlLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLhveqeVAGDDTPALq 252
Cdd:COG1136 11 TKSYGTGEGEVTA-------LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEVL-----IDGQDISSL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 svleSDSVReDLLRRER------------ELTAQiaagraegsEAAELAEIYAKleeIEADKAPARASVILAGLGFTPKM 320
Cdd:COG1136 76 ----SEREL-ARLRRRHigfvfqffnllpELTAL---------ENVALPLLLAG---VSRKERRERARELLERVGLGDRL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 321 QQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTWPSTILVVSHDRNFLnAIATDI 394
Cdd:COG1136 139 DHRPS-QLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeeVLEL--LRELNRELGTTIVMVTHDPELA-ARADRV 214
|
....*...
gi 148612853 395 IHLHSQRL 402
Cdd:COG1136 215 IRLRDGRI 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
489-668 |
2.69e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.47 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 489 PPILQLDEVDFYYDPKHVIFSRLS-VSADLES--RICVVGENGAGKSTMLKLLLGDLAP------VRGI---------RH 550
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRgVSLSIEAgeFVAIVGPSGSGKSTLLNILGGLDRPtsgevlIDGQdisslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHRNLKIGY-FSQHH------VEQldlNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQ 623
Cdd:COG1136 82 RLRRRHIGFvFQFFNllpeltALE---NVALPLLLAGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 624 MTMPCPNFYILDEPTNHLDMET----IEALgRALNNFRG-GVILVSHDER 668
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgeevLELL-RELNRELGtTIVMVTHDPE 206
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
193-402 |
3.20e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.83 E-value: 3.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHV---EQEVAGddtpalqsvlesdsvrEDLLRRER 269
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILS----------GLLQPtsgEVRVAG----------------LVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 270 ELTAQIAAGRAEGSE------AAE----LAEIYakleEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALA 339
Cdd:cd03267 91 KFLRRIGVVFGQKTQlwwdlpVIDsfylLAAIY----DLPPARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 340 RALFARPDLLLLDEPTNMLDVRAILWLENYLQTW----PSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
179-402 |
8.76e-15 |
|
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: 74.40 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRvPAHISLLHVEQEVAGddTPALQ------ 252
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLI-SGFLR-PTSGSVLFDGEDITG--LPPHEiarlgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 -------SVLESDSVREDLLrrereLTAQIAAGRAEGSEAAELAEiyakleeieaDKAPARASVILAGLGFTPKMQQqPT 325
Cdd:cd03219 78 grtfqipRLFPELTVLENVM-----VAAQARTGSGLLLARARREE----------REARERAEELLERVGLADLADR-PA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
523-666 |
1.20e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 74.38 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGYFSQHHVEQLDLNVSAVELLAR----KFPGRPE 587
Cdd:COG4559 32 IIGPNGAGKSTLLKLLTGELTPSSGeVRLNGRPLaawspwelarRRAVLPQHSSLAFPFTVEEVVALGRaphgSSAAQDR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 588 EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFA-------QMTMPCPNFYILDEPTNHLD-------MEtieaLGRAL 653
Cdd:COG4559 112 QIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALDlahqhavLR----LARQL 186
|
170
....*....|...
gi 148612853 654 NNFRGGVILVSHD 666
Cdd:COG4559 187 ARRGGGVVAVLHD 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
496-670 |
2.35e-14 |
|
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: 72.44 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 496 EVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL------KIGYFS 561
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqdVSDLRGRAipylrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 562 QHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 148612853 638 TNHLDMETIEALGRALN--NFRGGVILVS-HDERFI 670
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELV 199
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
520-683 |
2.39e-14 |
|
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: 73.30 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 520 RICVVGENGAGKSTMLKLLLG-----------DLAPVRGIRHAHRNLKIGYFSQHHVEQLD--LNVSAV--ELLARKFPG 584
Cdd:COG1124 33 SFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAFRRRVQMVFQDPYASLHprHTVDRIlaEPLRIHGLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 585 RPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALNNFRG-GV 660
Cdd:COG1124 113 DREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeILNLLKDLREERGlTY 192
|
170 180
....*....|....*....|...
gi 148612853 661 ILVSHDERFIRLVCRELWVCEGG 683
Cdd:COG1124 193 LFVSHDLAVVAHLCDRVAVMQNG 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
178-401 |
3.19e-14 |
|
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: 70.87 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLA---------------------TRSLRvpAHI 234
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIkpGEKVAIVGPSGSGKSTLLKLLLrlydptsgeilidgvdlrdldLESLR--KNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 235 SLlhVEQEvagddtpalqSVLESDSVREDLLrrereltaqiaagraegseaaelaeiyakleeieadkaparasvilagl 314
Cdd:cd03228 79 AY--VPQD----------PFLFSGTIRENIL------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 315 gftpkmqqqptrefSGGWRMRLALARALFARPDLLLLDEPTNMLDVR-AILWLENyLQTWP--STILVVSHDRNfLNAIA 391
Cdd:cd03228 98 --------------SGGQRQRIAIARALLRDPPILILDEATSALDPEtEALILEA-LRALAkgKTVIVIAHRLS-TIRDA 161
|
250
....*....|
gi 148612853 392 TDIIHLHSQR 401
Cdd:cd03228 162 DRIIVLDDGR 171
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
150-397 |
3.47e-14 |
|
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: 75.79 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 150 VLEEASASQAGSRKESRLESSGknksydVRIENFDVSFGDR-VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSL 228
Cdd:TIGR02857 300 VLDAAPRPLAGKAPVTAAPASS------LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL--GF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 229 RVPAHISLLHVEQEVAGDDTPALQS---------VLESDSVREDLLRREREltaqiaAGRAEGSEAAELAEiyakLEEIE 299
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDqiawvpqhpFLFAGTIAENIRLARPD------ASDAEIREALERAG----LDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 300 ADkaparasvilAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTw 373
Cdd:TIGR02857 442 AA----------LPQGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDaeteaeVLEA--LRALAQG- 507
|
250 260
....*....|....*....|....
gi 148612853 374 pSTILVVSHDRNfLNAIATDIIHL 397
Cdd:TIGR02857 508 -RTVLLVTHRLA-LAALADRIVVL 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
523-666 |
5.36e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNLKIGYFSQ--HHVEQLDLNVSAVELLArkfPGRPEEEYRHQLGRYGiS 600
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTLPLTVNRFLRLR---PGTKKEDILPALKRVQ-A 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 601 GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG----GVILVSHD 666
Cdd:PRK09544 111 GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHD 180
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
523-666 |
6.96e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.11 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK----------IGYFSQHHVEQLDLNVSAVELLAR----KFPGRPE 587
Cdd:PRK13548 33 ILGPNGAGKSTLLRALSGELSPDSGeVRLNGRPLAdwspaelarrRAVLPQHSSLSFPFTVEEVVAMGRaphgLSRAEDD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 588 EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFA----QMTMPC--PNFYILDEPTNHLDM---ETIEALGRALNNFRG 658
Cdd:PRK13548 113 ALVAAALAQVDLAH-LAGRDYPQLSGGEQQRVQLArvlaQLWEPDgpPRWLLLDEPTSALDLahqHHVLRLARQLAHERG 191
|
....*....
gi 148612853 659 -GVILVSHD 666
Cdd:PRK13548 192 lAVIVVLHD 200
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
178-383 |
1.03e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 71.66 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDT----- 248
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA--GLEKPTSGEVLVDGKPVTGPGPdrgvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 ---PAL---QSVLESdsvredllrrereltaqIAAGraegseaaelaeiyAKLEEIEADKAPARASVILAGLGFTPKMQQ 322
Cdd:COG1116 86 fqePALlpwLTVLDN-----------------VALG--------------LELRGVPKAERRERARELLELVGLAGFEDA 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 323 QPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 383
Cdd:COG1116 135 YP-HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltRERLqdELLRLWQETGKTVLFVTHD 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
179-355 |
1.06e-13 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 70.93 E-value: 1.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLK----MLATRSLRVpahisllhveqEVAGDDTPALQS- 253
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtimgLLPPRSGSI-----------RFDGRDITGLPPh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 ---------VLESD------SVREDLLrrereLTAQIaagRAEGSEAAELAEIYA---KLEEieadkaparasvilaglg 315
Cdd:cd03224 71 eraragigyVPEGRrifpelTVEENLL-----LGAYA---RRRAKRKARLERVYElfpRLKE------------------ 124
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 316 ftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPT 355
Cdd:cd03224 125 ----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
179-404 |
1.10e-13 |
|
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: 70.70 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHveqevagDDTPALQsv 254
Cdd:cd03245 2 RIEFRNVSFSypnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPTSGSVLL-------DGTDIRQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDSVREDL--LRRERELTAqiaagraeGS--EAAELAEIYAKLEEIEAdkaparaSVILAGLgfTPKMQQQPT----- 325
Cdd:cd03245 71 LDPADLRRNIgyVPQDVTLFY--------GTlrDNITLGAPLADDERILR-------AAELAGV--TDFVNKHPNgldlq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 326 -----REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHdRNFLNAIATDIIHLH 398
Cdd:cd03245 134 igergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMD 212
|
....*...
gi 148612853 399 SQRL--DG 404
Cdd:cd03245 213 SGRIvaDG 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
492-674 |
1.29e-13 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 70.99 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVifsrLS-VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNL- 555
Cdd:cd03261 1 IELRGLTKSFGGRTV----LKgVDLDVRrgEILAIIGPSGSGKSTLLRLIVGLLRPDSGevlidgedisglSEAELYRLr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 556 -KIGYFSQHHVEQLDLNVSA-VELLARKFPGRPEEEYR----HQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCP 629
Cdd:cd03261 77 rRMGMLFQSGALFDSLTVFEnVAFPLREHTRLSEEEIReivlEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 630 NFYILDEPTNHLD---METIEALGRALNNFRG-GVILVSHDERFIRLVC 674
Cdd:cd03261 156 ELLLYDEPTAGLDpiaSGVIDDLIRSLKKELGlTSIMVTHDLDTAFAIA 204
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
179-397 |
1.38e-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: 70.54 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSF-----GDRVL--LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHVEQEVagdDtpa 250
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCI-YGNYLPDSgSILVRHDGGWV---D--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 251 lqsvLESDSVREDL-LRRE-----------------RELTAQiaAGRAEGSEAAElaeiyakleeieadkAPARASVILA 312
Cdd:COG4778 79 ----LAQASPREILaLRRRtigyvsqflrviprvsaLDVVAE--PLLERGVDREE---------------ARARARELLA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 313 GLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWPSTILVVSHDRNF 386
Cdd:COG4778 138 RLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravVVELI---EEAKARGTAIIGIFHDEEV 214
|
250
....*....|.
gi 148612853 387 LNAIATDIIHL 397
Cdd:COG4778 215 REAVADRVVDV 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
492-685 |
1.41e-13 |
|
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: 69.17 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK---IGY 559
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGrvrldgadISQWDPNELgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHhveqldlnvsaVELLarkfpgrpeeeyrhqlgrygiSGELAMrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:cd03246 81 LPQD-----------DELF---------------------SGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 640 HLDMETIEALGRALNNFRGG---VILVSHDERFIRLVCRELwVCEGGGV 685
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAgatRIVIAHRPETLASADRIL-VLEDGRV 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
180-367 |
1.68e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.95 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKmlATRSLRVPAHISLLhveqeVAGDDTPALQSvlesds 259
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLR--AINGTLTPTAGTVL-----VAGDDVEALSA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 vredllrreRELTAQIAAGRAEGSEAAELaEIYAKLE------------EIEADKAPARASVILAGlgfTPKMQQQPTRE 327
Cdd:PRK09536 73 ---------RAASRRVASVPQDTSLSFEF-DVRQVVEmgrtphrsrfdtWTETDRAAVERAMERTG---VAQFADRPVTS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV-RAILWLE 367
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLE 180
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
490-691 |
2.43e-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: 73.01 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYYdPKHVIFSRLSVSADLE--SRICVVGENGAGKSTMLKLLLGDLAP--------------VRGIRHAHR 553
Cdd:COG1123 3 PLLEVRDLSVRY-PGGDVPAVDGVSLTIApgETVALVGESGSGKSTLALALMGLLPHggrisgevlldgrdLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 554 NLKIGYFSQHHVEQLD-LNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPC 628
Cdd:COG1123 82 GRRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARvlelLEAVGLERRLDRYP-HQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 629 PNFYILDEPTNHLDMET---IEALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 691
Cdd:COG1123 161 PDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI--VEDG 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
178-404 |
2.43e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.12 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQEVAGDDTPALQSVLeS 257
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-----------INKL--EEITSGDLIVDGLKVN-D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVREDLLRRER-----------ELTA--QIAAG--RAEGSEAAElaeiyakleeieadkAPARASVILAGLGFTPKMQQ 322
Cdd:PRK09493 68 PKVDERLIRQEAgmvfqqfylfpHLTAleNVMFGplRVRGASKEE---------------AEKQARELLAKVGLAERAHH 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 323 QPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VR-AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHS 399
Cdd:PRK09493 133 YPS-ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDK 211
|
....*..
gi 148612853 400 QRL--DG 404
Cdd:PRK09493 212 GRIaeDG 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
492-666 |
2.72e-13 |
|
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: 69.81 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLS-VSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRnlKIGYF 560
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEdISLSVEEGefVALVGPSGCGKSTLLRIIAGLERPTSGevlvdgepVTGPGP--DRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHH-------VEQldlNVsaveLLARKFPGRP----EEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCP 629
Cdd:cd03293 79 FQQDallpwltVLD---NV----ALGLELQGVPkaeaRERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 630 NFYILDEPTNHLDMETIEALGRAL----NNFRGGVILVSHD 666
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
492-666 |
3.55e-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: 69.52 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrlsVSADLESRIC--VVGENGAGKSTMLKLL-----LGDLAPVRG-IRHAHRNLkigYFSQH 563
Cdd:cd03260 1 IELRDLNVYYGDKHALKD---ISLDIPKGEItaLIGPSGCGKSTLLRLLnrlndLIPGAPDEGeVLLDGKDI---YDLDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 564 HVEQLDLNVSAVELLARKFPG-------------------RPEEEYRHQLGRYGISGELAMRPLA-SLSGGQKSRVAFAQ 623
Cdd:cd03260 75 DVLELRRRVGMVFQKPNPFPGsiydnvayglrlhgiklkeELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQRLCLAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148612853 624 MTMPCPNFYILDEPTNHLD---METIEALGRALNNfRGGVILVSHD 666
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDpisTAKIEELIAELKK-EYTIVIVTHN 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
178-382 |
3.70e-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: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----TRSlrvpAHISLLhvEQEVAGDD----- 247
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgdlppTYG----NDVRLF--GERRGGEDvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 248 ------TPALQ-SVLESDSVREDLLrrerelTAqiaagrAEGSeaaelAEIYAKLEEIEAdkapARASVILAGLGFTPKM 320
Cdd:COG1119 78 kriglvSPALQlRFPRDETVLDVVL------SG------FFDS-----IGLYREPTDEQR----ERARELLELLGLAHLA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 321 QQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW----PSTILVVSH 382
Cdd:COG1119 137 DR-PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTH 201
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
153-382 |
3.75e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 71.40 E-value: 3.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 153 EASASQAGSRKESRLESSGKNKSYdvrienfdvsfGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML--------- 223
Cdd:PRK13536 28 EAKASIPGSMSTVAIDLAGVSKSY-----------GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMIlgmtspdag 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 224 --ATRSLRVPAHISLLHVEQEVagddTPALQSVLESDSVREDLLrrereltaqiAAGRAEGSEAAELAEI------YAKL 295
Cdd:PRK13536 97 kiTVLGVPVPARARLARARIGV----VPQFDNLDLEFTVRENLL----------VFGRYFGMSTREIEAVipslleFARL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 296 EeieaDKAPARASvilaglgftpkmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE-NYLQT 372
Cdd:PRK13536 163 E----SKADARVS------------------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDphARHLIWERlRSLLA 220
|
250
....*....|
gi 148612853 373 WPSTILVVSH 382
Cdd:PRK13536 221 RGKTILLTTH 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
172-382 |
3.93e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 72.50 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 172 KNKSYDVRIENfdVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA---------------------TRS 227
Cdd:COG1132 334 PPVRGEIEFEN--VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidgvdirdltLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 228 LRvpAHISLlhVEQEVagddtpalqsVLESDSVREDllrrereltaqIAAGRAEGS-----EAAELAEIY---AKLEEie 299
Cdd:COG1132 412 LR--RQIGV--VPQDT----------FLFSGTIREN-----------IRYGRPDATdeeveEAAKAAQAHefiEALPD-- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 300 adkaparasvilaGLGftpkmqqqpTR------EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILW-LENY 369
Cdd:COG1132 465 -------------GYD---------TVvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTeteALIQEaLERL 522
|
250
....*....|...
gi 148612853 370 LQTwpSTILVVSH 382
Cdd:COG1132 523 MKG--RTTIVIAH 533
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
207-394 |
5.11e-13 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 68.69 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 207 GLVGRNGLGKTTLLKMLAtrSLRVP----AHISllhvEQEVAGDDTPALQSVlesdSV--REDLLrrERELTAQiaagra 280
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLT--GELRPtsgtAYIN----GYSIRTDRKAARQSL----GYcpQFDAL--FDELTVR------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 281 egseaaELAEIYAKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:cd03263 94 ------EHLRFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 148612853 361 RA--ILWleNYLQTWP--STILVVSHDRNFLNAIATDI 394
Cdd:cd03263 167 ASrrAIW--DLILEVRkgRSIILTTHSMDEAEALCDRI 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
519-666 |
5.59e-13 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 69.13 E-value: 5.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 519 SRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNL--KIGYFSQHH--VEQLDL--NV-------- 572
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgtdinklKGKALRQLrrQIGMIFQQFnlIERLSVleNVlsgrlgrr 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 SAVELLARKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG-- 650
Cdd:cd03256 108 STWRSLFGLFPKEEKQRALAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMdl 186
|
170
....*....|....*...
gi 148612853 651 -RALNNFRGGVILVS-HD 666
Cdd:cd03256 187 lKRINREEGITVIVSlHQ 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
178-399 |
7.30e-13 |
|
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: 67.21 E-value: 7.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--------------------GLEEPDSGSILID 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVREDLLRRERELTAQIAAGRAEGSeaaelaeIYAKLEEIEAdkaparasvILAGLgftpkmqqqptrefSGGWRMRLA 337
Cdd:cd03229 61 GEDLTDLEDELPPLRRRIGMVFQDFA-------LFPHLTVLEN---------IALGL--------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHDRNFLNAIATDIIHLHS 399
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
492-665 |
7.40e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.73 E-value: 7.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK----------IGYF 560
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILIDGVDIRdltleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHVeqldL-------NVsaveLLARkfPGRPEEE--------------------YRHQLGRYGisgelamrplASLSG 613
Cdd:COG1132 420 PQDTF----LfsgtireNI----RYGR--PDATDEEveeaakaaqahefiealpdgYDTVVGERG----------VNLSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 614 GQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 665
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
506-668 |
7.65e-13 |
|
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: 67.77 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 506 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVEL 577
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGTPLAEQRDEPHenilylgHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 578 LA--RKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNN 655
Cdd:TIGR01189 94 LHfwAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|....*.
gi 148612853 656 F--RGG-VILVSHDER 668
Cdd:TIGR01189 173 HlaRGGiVLLTTHQDL 188
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
506-665 |
9.46e-13 |
|
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: 67.52 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 506 VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVEL 577
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDFQRDSIArgllylgHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 578 LARKFPGRPEEEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF- 656
Cdd:cd03231 94 LRFWHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHc 172
|
170
....*....|.
gi 148612853 657 -RGG-VILVSH 665
Cdd:cd03231 173 aRGGmVVLTTH 183
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
180-402 |
9.68e-13 |
|
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: 67.99 E-value: 9.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAgaDVNLAWGR-RYGLVGRNGLGKTTLLKMLATrsLRVPahisllhVEQEVAGDDtpalQSVLESd 258
Cdd:cd03264 3 LENLTKRYGKKRALD--GVSLTLGPgMYGLLGPNGAGKTTLMRILAT--LTPP-------SSGTIRIDG----QDVLKQ- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 svREDLLRRERELTAQIaaGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMRLAL 338
Cdd:cd03264 67 --PQKLRRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 339 ARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEdrIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
521-706 |
1.01e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 68.59 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNlKIGYFSQHhvEQLDLNVSAVELLARKFPGRpeeeYRHQLGRYGIS 600
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQY--IKADYEGTVRDLLSSITKDF----YTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 601 GELAM-----RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHDERFIR 671
Cdd:cd03237 101 KPLQIeqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMID 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 672 LVCRELWVCEG-GGVTRV-------EGGFDQYRALLQEQFRRE 706
Cdd:cd03237 181 YLADRLIVFEGePSVNGVanppqslRSGMNRFLKNLDITFRRD 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
197-398 |
1.02e-12 |
|
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: 67.94 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNL--AWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQ---EVAGDDTP--ALQSVLESD-SVREDLLRRE 268
Cdd:cd03220 40 DVSFevPRGERIGLIGRNGAGKSTLLRLLA----------GIYPPDSgtvTVRGRVSSllGLGGGFNPElTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 269 RELTAQIAagraegseaaelaEIYAKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDL 348
Cdd:cd03220 110 RLLGLSRK-------------EIDEKIDEIIE----------FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 349 LLLDEPTNMLDV----RAILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:cd03220 164 LLIDEVLAVGDAafqeKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
178-384 |
1.37e-12 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 69.79 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVP--AHISLlhveqevAGDDTPALQSVL 255
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIA--GLETPdsGRIVL-------NGRDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 ESD--------------SVREDL---LRRERELTAQIAAgraegsEAAELAEIYaKLEEIeADKAPArasvilaglgftp 318
Cdd:COG1118 74 ERRvgfvfqhyalfphmTVAENIafgLRVRPPSKAEIRA------RVEELLELV-QLEGL-ADRYPS------------- 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 319 kmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 384
Cdd:COG1118 133 --------QLSGGQRQRVALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
178-398 |
1.49e-12 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 67.17 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllHVEQEVAG----DDTpalqs 253
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-------------LLEEPDSGtiiiDGL----- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESDSVREDLLRRE-----------RELTAQiaagraegsEAAELAEIYA-KLEEIEADkapARASVILAGLGFTPKMQ 321
Cdd:cd03262 63 KLTDDKKNINELRQKvgmvfqqfnlfPHLTVL---------ENITLAPIKVkGMSKAEAE---ERALELLEKVGLADKAD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 322 QQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:cd03262 131 AYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
151-398 |
1.72e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 151 LEEASASQAGSRKESRLESSGknksydVRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA----- 224
Cdd:COG4178 342 LEAADALPEAASRIETSEDGA------LALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpy 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 225 -TRSLRVPAHISLLHVEQevagddtpalQSVLESDSVREDLLRrereltaqiaAGRAEGSEAAELAEIyakLEEieadka 303
Cdd:COG4178 416 gSGRIARPAGARVLFLPQ----------RPYLPLGTLREALLY----------PATAEAFSDAELREA---LEA------ 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 304 parasvilAGLG-FTPKM-QQQP-TREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL-QTWPSTILV 379
Cdd:COG4178 467 --------VGLGhLAERLdEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTVI 538
|
250 260
....*....|....*....|
gi 148612853 380 -VSHdRNFLNAIATDIIHLH 398
Cdd:COG4178 539 sVGH-RSTLAAFHDRVLELT 557
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
178-383 |
1.85e-12 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 67.11 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDR----VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDtPALQS 253
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG--LERPTSGEVLVDGEPVTGPG-PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESD------SVREDllrrereltaqIAAG-RAEGSEAAELAEIyakleeieadkapARASVILAGL-GFTPKMqqqPt 325
Cdd:cd03293 78 VFQQDallpwlTVLDN-----------VALGlELQGVPKAEARER-------------AEELLELVGLsGFENAY---P- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 383
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltREQLqeELLDIWRETGKTVLLVTHD 191
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
179-398 |
2.21e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHveQEVAGDDTPAL------ 251
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLI-TGFYRPTSgRILFDG--RDITGLPPHRIarlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 ---Q--SVLESDSVREDLL------RRERELTAQIAAGRAEGSEAAELAEIYAKLEEIE-ADKAparasvilaglgftpk 319
Cdd:COG0411 83 rtfQnpRLFPELTVLENVLvaaharLGRGLLAALLRLPRARREEREARERAEELLERVGlADRA---------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 320 mqQQPTREFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAIL-WLENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:COG0411 147 --DEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
...
gi 148612853 396 HLH 398
Cdd:COG0411 225 VLD 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
195-360 |
2.32e-12 |
|
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: 70.10 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 195 GADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLR-VPAHISLLHVEQEVAGDDTPALQSvlesdsvredlLRRE----- 268
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLAL----LRlIPSEGEIRFDGQDLDGLSRRALRP-----------LRRRmqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 269 ---------RELTAQIAAgraEGseaaeLAeiyakLEEIEADKAPARASVI--LAGLGFTPKMQQQPTREFSGGWRMRLA 337
Cdd:COG4172 369 qdpfgslspRMTVGQIIA---EG-----LR-----VHGPGLSAAERRARVAeaLEEVGLDPAARHRYPHEFSGGQRQRIA 435
|
170 180
....*....|....*....|...
gi 148612853 338 LARALFARPDLLLLDEPTNMLDV 360
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALDV 458
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
488-666 |
2.35e-12 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 67.81 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPK---HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIG 558
Cdd:COG1116 4 AAPALELRGVSKRFPTGgggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 559 Y-FSQHH------VEQldlNVsaveLLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 627
Cdd:COG1116 84 VvFQEPAllpwltVLD---NV----ALGLELRGVPKAERRERarelLELVGLAGFEDAYP-HQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 628 CPNFYILDEPTNHLDMETIEALG----RALNNFRGGVILVSHD 666
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQdellRLWQETGKTVLFVTHD 198
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
492-665 |
2.51e-12 |
|
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: 67.26 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLL-------G----DLAPVRGIRHAHRNLKIGYF 560
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFrfydvssGsiliDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQ----------HHVEQLDLNVSAVELLA-----------RKFPgrpeEEYRHQLGRYGISgelamrplasLSGGQKSRV 619
Cdd:cd03253 81 PQdtvlfndtigYNIRYGRPDATDEEVIEaakaaqihdkiMRFP----DGYDTIVGERGLK----------LSGGEKQRV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 620 AFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 665
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAH 194
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
203-398 |
2.55e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLA----------TRSLRVPAhisLLhveqEVAGddtpALQSVLesdSVREDLlrrerelt 272
Cdd:COG1134 52 GESVGIIGRNGAGKSTLLKLIAgileptsgrvEVNGRVSA---LL----ELGA----GFHPEL---TGRENI-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 273 aqIAAGRAEGseaAELAEIYAKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLD 352
Cdd:COG1134 110 --YLNGRLLG---LSRKEIDEKFDEIVE----------FAELG---DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148612853 353 EptnMLDV-------RAILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:COG1134 172 E---VLAVgdaafqkKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
179-355 |
3.24e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.93 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLK----MLATRS----------LRVPAH------ISllH 238
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLPPRSgsirfdgediTGLPPHriarlgIG--Y 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 239 VEQEvagddtpalQSVLESDSVREDLlrrerELTAQIAAGRAEGSEAaeLAEIYA---KLEEieadkaparasvilaglg 315
Cdd:COG0410 83 VPEG---------RRIFPSLTVEENL-----LLGAYARRDRAEVRAD--LERVYElfpRLKE------------------ 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 316 ftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPT 355
Cdd:COG0410 129 ----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
494-702 |
3.83e-12 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 66.79 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 494 LDEVDFYYD--PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IR----HAHRNlKIGY 559
Cdd:cd03249 3 FKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeilldgvdIRdlnlRWLRS-QIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQhhvEQLDLNVSAVELLARKFPGRPEEE--------------------YRHQLGRYGisgelamrplASLSGGQKSRV 619
Cdd:cd03249 82 VSQ---EPVLFDGTIAENIRYGKPDATDEEveeaakkanihdfimslpdgYDTLVGERG----------SQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 620 AFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIR---LVCrelwVCEGGGVtrVE-GGFD 693
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAHRLSTIRnadLIA----VLQNGQV--VEqGTHD 222
|
250
....*....|....*.
gi 148612853 694 Q-------YRALLQEQ 702
Cdd:cd03249 223 ElmaqkgvYAKLVKAQ 238
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
192-402 |
3.93e-12 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 67.14 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 192 LLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahislLHVEQEVAGDDTPALQSVLESDSVREDLLRREREL 271
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-------------LGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 272 TAQ--IAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLL 349
Cdd:TIGR02769 93 VFQdsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 350 LLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:TIGR02769 173 VLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
178-383 |
4.04e-12 |
|
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: 66.56 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslRVPAHISllhveqevaGDDTPALQSVLE 256
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN----RLIEPTS---------GEIFIDGEDIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 257 SDSVRedlLRRERELTAQiAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPK--MQQQPtREFSGGWRM 334
Cdd:cd03295 68 QDPVE---LRRKIGYVIQ-QIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYP-HELSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148612853 335 RLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHD 383
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDpiTRDQLQEEfkRLQQELGKTIVFVTHD 195
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
512-674 |
4.04e-12 |
|
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: 66.38 E-value: 4.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 512 SVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------------KIGYFSQHHVEQLD--LNVS 573
Cdd:cd03257 23 DVSFSIKkgETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLlklsrrlrkirrkEIQMVFQDPMSSLNprMTIG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 A--VELLARKFPGRPEEEYRHQLGRYGISGELA-----MRPlASLSGGQKSRVAFAqMTMPC-PNFYILDEPTNHLDMET 645
Cdd:cd03257 103 EqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnRYP-HELSGGQRQRVAIA-RALALnPKLLIADEPTSALDVSV 180
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 646 ---IEALGRALNNFRG-GVILVSHDERFIRLVC 674
Cdd:cd03257 181 qaqILDLLKKLQEELGlTLLFITHDLGVVAKIA 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
180-691 |
6.40e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.58 E-value: 6.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKT-TLLKMLatRSLRVPAHISLlhveqevAGDDTPALQSV 254
Cdd:PRK15134 8 IENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYP-------SGDIRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDsvrEDLLRR-----------------------ERELTAQIAAGRAEGSEAAElAEIYAKLEEIEADKAPARasvil 311
Cdd:PRK15134 79 LHAS---EQTLRGvrgnkiamifqepmvslnplhtlEKQLYEVLSLHRGMRREAAR-GEILNCLDRVGIRQAAKR----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 312 agLGFTPkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHDRNFL 387
Cdd:PRK15134 150 --LTDYP-------HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELqQELNMGLLFITHNLSIV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 388 NAIATDIIHLHSQRLdgyrgdFETfikSKQERLLNQqreyeAQQQYRQhiqvfidrfrynanrasqvqsklKMLEKLPEL 467
Cdd:PRK15134 221 RKLADRVAVMQNGRC------VEQ---NRAATLFSA-----PTHPYTQ-----------------------KLLNSEPSG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 468 KPVDKESEvvmkfpdgfekfSPPILQLDEVDFYYDPKHVIFSRL--------SVSADL---ESrICVVGENGAGKSTM-L 535
Cdd:PRK15134 264 DPVPLPEP------------ASPLLDVEQLQVAFPIRKGILKRTvdhnvvvkNISFTLrpgET-LGLVGESGSGKSTTgL 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 536 KLLlgDLAPVRG--------IRHAHRNLKIGYFSQHHVEQLD--------LNVSAV--ELLARKFP----GRPEEEYRHQ 593
Cdd:PRK15134 331 ALL--RLINSQGeiwfdgqpLHNLNRRQLLPVRHRIQVVFQDpnsslnprLNVLQIieEGLRVHQPtlsaAQREQQVIAV 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 594 LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNN-FRGGVILVSHDERF 669
Cdd:PRK15134 409 MEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQkHQLAYLFISHDLHV 488
|
570 580
....*....|....*....|..
gi 148612853 670 IRLVCRELWVCEGGGVtrVEGG 691
Cdd:PRK15134 489 VRALCHQVIVLRQGEV--VEQG 508
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
522-665 |
7.75e-12 |
|
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: 64.93 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAPVRGI---------RHAHRNLKIGYFSQHHVeqLDLNVSAVE--LLARKFPGRPEEEY 590
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqKNIEALRRIGALIEAPG--FYPNLTAREnlRLLARLLGIRKKRI 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 591 RHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI---EALGRALNNFRGGVILVSH 665
Cdd:cd03268 108 DEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIkelRELILSLRDQGITVLISSH 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
188-363 |
9.52e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTP----------ALQSVLes 257
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA--GLLPPAAGTIKLDGGDIDDPDVAeachylghrnAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 dSVREDLlrrerELTAQIAAGRaegseaaelaeiyakleeiEADKAPARASVILAGLGFTpkmqqqPTREFSGGWRMRLA 337
Cdd:PRK13539 89 -TVAENL-----EFWAAFLGGE-------------------ELDIAAALEAVGLAPLAHL------PFGYLSAGQKRRVA 137
|
170 180
....*....|....*....|....*.
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
492-644 |
1.03e-11 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.91 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIfsrLSVSADLESRICV-VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL--KIGYF 560
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPGMYGlLGPNGAGKTTLMRILATLTPPSSGtiridgqdVLKQPQKLrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHveQLDLNVSAVELLA------RKFPGRPEEEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:cd03264 78 PQEF--GVYPNFTVREFLDyiawlkGIPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170
....*....|
gi 148612853 635 DEPTNHLDME 644
Cdd:cd03264 155 DEPTAGLDPE 164
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
490-666 |
1.06e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KI 557
Cdd:PRK13635 4 EIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGMVLseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHVEQLdlnVSA-VE------LLARKFPgRPE--EEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPC 628
Cdd:PRK13635 84 GMVFQNPDNQF---VGAtVQddvafgLENIGVP-REEmvERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148612853 629 PNFYILDEPTNHLD-------METIealgRALNNFRG-GVILVSHD 666
Cdd:PRK13635 159 PDIIILDEATSMLDprgrrevLETV----RQLKEQKGiTVLSITHD 200
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
492-666 |
1.08e-11 |
|
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: 64.85 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------KIGYFSQ 562
Cdd:cd03259 1 LELKGLSKTYGSVRAL-DDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGRDVtgvpperrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 HH-------VEQldlNVsAVELLARKFPgRPEEEYRHQ--LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYI 633
Cdd:cd03259 80 DYalfphltVAE---NI-AFGLKLRGVP-KAEIRARVRelLELVGLEGLLNRYP-HELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 634 LDEPTNHLD----METIEALGRALNNFRGGVILVSHD 666
Cdd:cd03259 154 LDEPLSALDaklrEELREELKELQRELGITTIYVTHD 190
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
187-420 |
1.22e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 187 FGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVA-GDDTPALQSVLESDSVRedLL 265
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI--NFLEKPSEGSIVVNGQTINlVRDKDGQLKVADKNQLR--LL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 266 RRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFAR 345
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 346 PDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERL 420
Cdd:PRK10619 171 PEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
491-691 |
1.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 66.02 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYY-DPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----K 556
Cdd:PRK13636 5 ILKVEELNYNYsDGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfdgkpIDYSRKGLmklreS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQHHVEQL-------DLNVSAVELlarkfpGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMT 625
Cdd:PRK13636 84 VGMVFQDPDNQLfsasvyqDVSFGAVNL------KLPEDEVRkrvdNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 626 MPCPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTrVEGG 691
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
523-682 |
1.23e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG---------------IRHAHRNLKIGYFSQHHVEQLDL----NVSAVELLARKFP 583
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaAKAELRNQKLGFIYQFHHLLPDFtaleNVAMPLLIGKKKP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 584 GRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRGGV 660
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTA 198
|
170 180
....*....|....*....|...
gi 148612853 661 IL-VSHDERFIRLVCRELWVCEG 682
Cdd:PRK11629 199 FLvVTHDLQLAKRMSRQLEMRDG 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
193-395 |
1.27e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 66.53 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisllhVEQEVAGDDTPALQSVLESDSVREDLLRRERELT 272
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTM-------------IETPTGGELYYQGQDLLKADPEAQKLLRQKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 273 AQIAAG-----RAEGSEAAELAEIYAKLEEieADKApARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:PRK11308 98 FQNPYGslnprKKVGQILEEPLLINTSLSA--AERR-EKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 348 LLLLDEPTNMLDV--RA-ILWLENYLQTWPSTILV-VSHDRNFLNAIATDII 395
Cdd:PRK11308 175 VVVADEPVSALDVsvQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIADEVM 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
180-395 |
1.29e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 65.47 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqevAGDdTPAlqsvlesDS 259
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA--GLETPSAGELL------AGT-APL-------AE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 VRED--LLRRERELTA------QIAAG-RAEGSEAAELAeiyakleeieadkaparasviLAGLGFTPKMQQQPTrEFSG 330
Cdd:PRK11247 79 AREDtrLMFQDARLLPwkkvidNVGLGlKGQWRDAALQA---------------------LAAVGLADRANEWPA-ALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 331 GWRMRLALARALFARPDLLLLDEPTNMLDvrAI-----------LWLENYLqtwpsTILVVSHDRNFLNAIATDII 395
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALD--ALtriemqdliesLWQQHGF-----TVLLVTHDVSEAVAMADRVL 205
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
492-686 |
1.49e-11 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 64.85 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IR-----------HAHRNLKIGY 559
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRG-VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsIRldgeditklppHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 -------FSQHHVEQlDLNVSAvELLARKFPGRPEEEYrhqlGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR03410 80 vpqgreiFPRLTVEE-NLLTGL-AALPRRSRKIPDEIY----ELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 633 ILDEPTNHLDMETIEALGRALNNFRG----GVILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAeggmAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
188-402 |
1.53e-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: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHIsllhveqEVAGDDTPALQSVlesdsvREDLLRR 267
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-------RVNGQDVSDLRGR------AIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 268 ERELTAQ----IAAGRAEGSEAAELAEIYAKLEEIeadkaPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALF 343
Cdd:cd03292 79 KIGVVFQdfrlLPDRNVYENVAFALEVTGVPPREI-----RKRVPAALELVGLSHKHRALPA-ELSGGEQQRVAIARAIV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 344 ARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03292 153 NSPTILIADEPTGNLDpdtTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
492-674 |
1.56e-11 |
|
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: 63.36 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYdPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG--------------DLAPVRGIRHAHRNlKI 557
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsilidgeDLTDLEDELPPLRR-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHveQLDLNVSAVELLArkfpgrpeeeyrhqlgrYGisgelamrplasLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03229 79 GMVFQDF--ALFPHLTVLENIA-----------------LG------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 638 TNHLDMET---IEALGRALN-NFRGGVILVSHDERFIRLVC 674
Cdd:cd03229 128 TSALDPITrreVRALLKSLQaQLGITVVLVTHDLDEAARLA 168
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
513-702 |
1.58e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFsqhhveqLDLNV------SAVE---LLARk 581
Cdd:COG1134 45 VSFEVERgeSVGIIGRNGAGKSTLLKLIAGILEPTSG--RVEVNGRVSAL-------LELGAgfhpelTGREniyLNGR- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 582 FPGRPEEEYRH---------QLGRYgisgelAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDeptnhldmetiEALG-- 650
Cdd:COG1134 115 LLGLSRKEIDEkfdeivefaELGDF------IDQPVKTYSSGMRARLAFAVATAVDPDILLVD-----------EVLAvg 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 651 ---------RALNNFR---GGVILVSHDERFIRLVC-RELWVcEGGGVT---RVEGGFDQYRALLQEQ 702
Cdd:COG1134 178 daafqkkclARIRELResgRTVIFVSHSMGAVRRLCdRAIWL-EKGRLVmdgDPEEVIAAYEALLAGR 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-674 |
1.58e-11 |
|
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: 63.22 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKigyfsqhhvEQLDLNVSAVellarkfpgrpeeeyrHQLg 595
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPdsgeilVDGKEVSFASPR---------DARRAGIAMV----------------YQL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 596 rygisgelamrplaslSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRL 672
Cdd:cd03216 84 ----------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFE 147
|
..
gi 148612853 673 VC 674
Cdd:cd03216 148 IA 149
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
180-407 |
1.60e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 64.30 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPA-HISllhveqeVAGDDTPALQsvl 255
Cdd:COG2884 2 IRFENVSKrypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-GEERPTSgQVL-------VNGQDLSRLK--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 esdsvREDL--LRRE-----------RELTAqiaagraegSEAAELAeiyakLEEIEADKAPARASV--ILAGLGFTPKM 320
Cdd:COG2884 71 -----RREIpyLRRRigvvfqdfrllPDRTV---------YENVALP-----LRVTGKSRKEIRRRVreVLDLVGLSDKA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 321 QQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL--E-NYLQTwpsTILVVSHDRNFLNAIATDI 394
Cdd:COG2884 132 KALP-HELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetSWEIMELleEiNRRGT---TVLIATHDLELVDRMPKRV 207
|
250
....*....|....*
gi 148612853 395 IHLHSQRL--DGYRG 407
Cdd:COG2884 208 LELEDGRLvrDEARG 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
513-679 |
1.76e-11 |
|
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: 64.77 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRH--AHR-----------------------NLKI 557
Cdd:cd03219 19 VSFSVRpgEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgedITGlpPHEiarlgigrtfqiprlfpeltvleNVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHVEQLDLNVSAVELLARkfpgrpeEEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03219 99 AAQARTGSGLLLARARREEREAR-------ERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 638 T---NHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWV 679
Cdd:cd03219 171 AaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTV 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
178-383 |
1.85e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML------ATRSLRVPAHISLLHVEQEVAGDDTPAL 251
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlglvapDEGVIKRNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 qsvlesdSVREDLLRREreltaqiaagraegseAAELAEIYAKLEEIEADKaparasvilaglgftpkMQQQPTREFSGG 331
Cdd:PRK09544 85 -------TVNRFLRLRP----------------GTKKEDILPALKRVQAGH-----------------LIDAPMQKLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 332 WRMRLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYLQTWPSTILVVSHD 383
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
488-668 |
2.03e-11 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 64.38 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYY-DPKH--VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI---------------R 549
Cdd:COG4181 5 SAPIIELRGLTKTVgTGAGelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedaR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 550 HAHRNLKIGYFSQHhvEQLDLNVSAVE--LLARKFPGRPE--EEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMT 625
Cdd:COG4181 85 ARLRARHVGFVFQS--FQLLPTLTALEnvMLPLELAGRRDarARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 626 MPCPNFYILDEPTNHLDMET---IEALGRALNNFRGG-VILVSHDER 668
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATgeqIIDLLFELNRERGTtLVLVTHDPA 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
523-683 |
3.05e-11 |
|
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: 63.31 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLG--DLAPVRG-IRHAHRNLkigyfsqhhveqLDLNvsavellarkfpgrPEEeyRHQLGRY-- 597
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpKYEVTEGeILFKGEDI------------TDLP--------------PEE--RARLGIFla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 598 --------GISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSH 665
Cdd:cd03217 83 fqyppeipGVKNADFLRYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
170 180
....*....|....*....|....*.
gi 148612853 666 DER--------FIRLVCRELWVCEGG 683
Cdd:cd03217 163 YQRlldyikpdRVHVLYDGRIVKSGD 188
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
177-385 |
3.36e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 64.26 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 177 DVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHveqevagDDTPalqsvLE 256
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RLLTPQSGTVFL-------GDKP-----IS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 257 SDSVREdlLRRERELTAQIAAgRAEGSEAAELAE--------IYAKLeeieADKAPARASVILAGLGfTPKMQQQPTREF 328
Cdd:PRK11231 68 MLSSRQ--LARRLALLPQHHL-TPEGITVRELVAygrspwlsLWGRL----SAEDNARVNQAMEQTR-INHLADRRLTDL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK11231 140 SGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDLN 199
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
207-383 |
3.52e-11 |
|
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: 63.47 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 207 GLVGRNGLGKTTLLKMLATrSLRVPA-HISLlhveqevagDDTpalqsVLESDSVREDLLRRERE--LTAQIAAGRAEGS 283
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAG-LEKPDGgTIVL---------NGT-----VLFDSRKKINLPPQQRKigLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 284 EAAELAEIYAKLEEIEaDKAPARASVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:cd03297 92 VRENLAFGLKRKRNRE-DRISVDELLDLLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180
....*....|....*....|....
gi 148612853 364 LWLENYLQTWPS----TILVVSHD 383
Cdd:cd03297 168 LQLLPELKQIKKnlniPVIFVTHD 191
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
524-679 |
3.65e-11 |
|
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: 63.89 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLGDLAPVRG-------------IRHAHRnlkIGY-FSQHhvEQLDLNVSAVE---LLARKFpGRP 586
Cdd:cd03267 53 IGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrrKKFLRR---IGVvFGQK--TQLWWDLPVIDsfyLLAAIY-DLP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEYRHQLGRygIS-----GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRG 658
Cdd:cd03267 127 PARFKKRLDE--LSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNRERG 204
|
170 180
....*....|....*....|..
gi 148612853 659 G-VILVSHDERFIRLVCRELWV 679
Cdd:cd03267 205 TtVLLTSHYMKDIEALARRVLV 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
523-672 |
3.67e-11 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 63.01 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLL----GDLAPvRGIRHAHRNLKIGyfSQHHVEQLDLNVSAVE----LLARKFPGRPEEEYRHQl 594
Cdd:cd03240 27 IVGQNGAGKTTIIEALKyaltGELPP-NSKGGAHDPKLIR--EGEVRAQVKLAFENANgkkyTITRSLAILENVIFCHQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 595 gryGISGELAMRPLASLSGGQKS------RVAFAQ-MTMPCPnFYILDEPTNHLDMETIE-ALGRALNNFRGG----VIL 662
Cdd:cd03240 103 ---GESNWPLLDMRGRCSGGEKVlasliiRLALAEtFGSNCG-ILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIV 178
|
170
....*....|
gi 148612853 663 VSHDERFIRL 672
Cdd:cd03240 179 ITHDEELVDA 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
488-665 |
3.98e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGY 559
Cdd:PRK13543 8 APPLLAAHALAFSRNEE-PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqiqidgktATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSqhHVEQLDLNVSAVELL----------ARKFPGrpeeeyrHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTM-PC 628
Cdd:PRK13543 87 LG--HLPGLKADLSTLENLhflcglhgrrAKQMPG-------SALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLsPA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 629 PnFYILDEPTNHLDMETIEALGRALN---NFRGGVILVSH 665
Cdd:PRK13543 157 P-LWLLDEPYANLDLEGITLVNRMISahlRGGGAALVTTH 195
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
150-382 |
4.62e-11 |
|
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: 65.89 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 150 VLEEASASQAGSRKESRLESsgknksyDVRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKML---- 223
Cdd:TIGR02203 310 LLDSPPEKDTGTRAIERARG-------DVEFRNVTFRYPGRDRPALDSISLviEPGETVALVGRSGSGKSTLVNLIprfy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 224 -----------------ATRSLRvpAHISLlhVEQEVagddtpalqsVLESDSVredllrrerelTAQIAAGRAEGseaa 286
Cdd:TIGR02203 383 epdsgqilldghdladyTLASLR--RQVAL--VSQDV----------VLFNDTI-----------ANNIAYGRTEQ---- 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 287 elaeiyAKLEEIEADKAPARASVILAGLgftPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV-- 360
Cdd:TIGR02203 434 ------ADRAEIERALAAAYAQDFVDKL---PLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNes 504
|
250 260
....*....|....*....|....
gi 148612853 361 -RAI-LWLENYLQTwpSTILVVSH 382
Cdd:TIGR02203 505 eRLVqAALERLMQG--RTTLVIAH 526
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
492-685 |
4.94e-11 |
|
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: 62.84 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHA--HR--NLKIGY 559
Cdd:cd03224 1 LEVENLNAGYGKSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrdITGLppHEraRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 -------FSQHHVEQlDLNVSAVELLARKFPGRPEE---------EYRHQLGrygisgelamrplASLSGGQKSRVAFAQ 623
Cdd:cd03224 80 vpegrriFPELTVEE-NLLLGAYARRRAKRKARLERvyelfprlkERRKQLA-------------GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 624 MTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLERGRV 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
488-674 |
5.34e-11 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 63.46 E-value: 5.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVifsrLS-VSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL-------- 555
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVV----LDgVSLDVPrgEILAIIGGSGSGKSVLLKLIIGLLRPDSGeILVDGQDItglsekel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 556 -----KIGY-------FSqhhveqlDLNVSA-VELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSR 618
Cdd:COG1127 78 yelrrRIGMlfqggalFD-------SLTVFEnVAFPLREHTDLSEAEIRELvlekLELVGLPGAADKMP-SELSGGMRKR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 619 VAFAQMTMPCPNFYILDEPTNHLD---METIEALGRALNNFRGG-VILVSHDERFIRLVC 674
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRDELGLtSVVVTHDLDSAFAIA 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
179-402 |
5.61e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 63.64 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHveQEVAGDDTPAL------ 251
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELSPDSgEVRLNG--RPLADWSPAELarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 ---QSVLESD-SVREdllrrereltaQIAAGRAEGSEAAElaeiyakleeiEADKAPARA--SVILAGLGftpkmqQQPT 325
Cdd:PRK13548 81 lpqHSSLSFPfTVEE-----------VVAMGRAPHGLSRA-----------EDDALVAAAlaQVDLAHLA------GRDY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 326 REFSGGWRMRLALARAL------FARPDLLLLDEPTNMLDVR---AILWL-ENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:PRK13548 133 PQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAhqhHVLRLaRQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
....*..
gi 148612853 396 HLHSQRL 402
Cdd:PRK13548 213 LLHQGRL 219
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
328-402 |
5.73e-11 |
|
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: 61.85 E-value: 5.73e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLnAIATDIIHLHSQRL 402
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
491-686 |
6.14e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 559
Cdd:PRK11231 2 TLRTENLTVGYGTKRIL-NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPIsmlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHHVEQLDLNVSavELLAR------KFPGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRvAFAQMTMPC- 628
Cdd:PRK11231 81 LPQHHLTPEGITVR--ELVAYgrspwlSLWGRLSAEDNARvnqaMEQTRIN-HLADRRLTDLSGGQRQR-AFLAMVLAQd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 629 PNFYILDEPTNHLDM-ETIEALG--RALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:PRK11231 157 TPVVLLDEPTTYLDInHQVELMRlmRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
497-665 |
7.22e-11 |
|
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: 62.63 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 497 VDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG-----------DLAPVRGI-RHAHRNlKIGY----- 559
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqiliDGIDIRDIsRKSLRS-MIGVvlqdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 --FSQHHVEQLDLN----------VSAVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMP 627
Cdd:cd03254 87 flFSGTIMENIRLGrpnatdeeviEAAKEAGAHDFIMKLPNGYDTVLGENG----------GNLSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 628 CPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 665
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
521-666 |
7.89e-11 |
|
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: 63.22 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSAV-------- 575
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGkvtvdgldtldeenlweIRK-----KVGMVFQNPDNQF---VGATveddvafg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 576 -ELLarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLD------- 642
Cdd:TIGR04520 103 lENL-----GVPREEMRKRvdeaLKLVGME-DFRDREPHLLSGGQKQRVAIAGvLAMR-PDIIILDEATSMLDpkgrkev 175
|
170 180
....*....|....*....|....*
gi 148612853 643 METIealgRALNNFRG-GVILVSHD 666
Cdd:TIGR04520 176 LETI----RKLNKEEGiTVISITHD 196
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
524-665 |
8.16e-11 |
|
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: 62.30 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLGDLAPVRGIRH--------AHRNlKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ-- 593
Cdd:cd03269 32 LGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARN-RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRid 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 594 --LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSH 665
Cdd:cd03269 111 ewLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
180-397 |
8.54e-11 |
|
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: 62.66 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR-SLRVPA-HISLlhveqevAGDDTPAL------ 251
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpSYEVTSgTILF-------KGQDLLELepdera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 --------QSVLESDSVR-EDLLRrerelTAQIAAGRAEGSEAAELAEIYAKLEEIeadkaparasviLAGLGFTPKMQQ 322
Cdd:TIGR01978 76 raglflafQYPEEIPGVSnLEFLR-----SALNARRSARGEEPLDLLDFEKLLKEK------------LALLDMDEEFLN 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 323 QPTRE-FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:TIGR01978 139 RSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIdalKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
521-645 |
1.02e-10 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 62.70 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLK--------------LLLGDLAPVRG--IRHAHRnlKIGYFSQHH--VEQLDL--NV-------- 572
Cdd:TIGR02315 31 VAIIGPSGAGKSTLLRcinrlvepssgsilLEGTDITKLRGkkLRKLRR--RIGMIFQHYnlIERLTVleNVlhgrlgyk 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 573 SAVELLARKFPGRPEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 645
Cdd:TIGR02315 109 PTWRSLLGRFSEEDKERALSALERVGLA-DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
492-682 |
1.40e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.69 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrLSVSADleSRICVVGENGAGKSTMLKLLLGDLAPVRG-IR-----HAHR------------ 553
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD-LTIAAG--ERVAILGPSGAGKSTLLNLIAGFLPPDSGrILwngqdLTALppaerpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 554 --NLkigyFSQHHVEQldlNVSavelLARKfPG-RPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTM 626
Cdd:COG3840 79 enNL----FPHLTVAQ---NIG----LGLR-PGlKLTAEQRAQveqaLERVGLAGLLDRLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 627 ---PCpnfYILDEPTNHLD-------METIEALGRALNNfrgGVILVSHD-ERFIRLVCRELWVCEG 682
Cdd:COG3840 146 rkrPI---LLLDEPFSALDpalrqemLDLVDELCRERGL---TVLMVTHDpEDAARIADRVLLVADG 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
504-670 |
1.76e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.51 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 504 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGdlapvrgirhAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFP 583
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----------ALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 584 GRPEEEYrhqLGRYGISGELAM-RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----NNFRG 658
Cdd:COG2401 112 FKDAVEL---LNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLqklaRRAGI 188
|
170
....*....|..
gi 148612853 659 GVILVSHDERFI 670
Cdd:COG2401 189 TLVVATHHYDVI 200
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-672 |
1.88e-10 |
|
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: 60.07 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 506 VIFSRLSVSADLESRICVVGENGAGKSTMLKlllgDLAPVRGIRHAHRNlkigyfsQHHVEQLDLNVSAVELLARKFpgr 585
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILD----AIGLALGGAQSATR-------RRSGVKAGCIVAAVSAELIFT--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 peeeyRHQlgrygisgelamrplasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGRALNNFRGG- 659
Cdd:cd03227 75 -----RLQ-----------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKg 131
|
170
....*....|....*
gi 148612853 660 --VILVSHDERFIRL 672
Cdd:cd03227 132 aqVIVITHLPELAEL 146
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
178-416 |
1.92e-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: 61.44 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDR----VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhveqevagdDTPALQS 253
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRC-----------INGL---------ERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VL----ESDSVREDLLRRERELTAQI-------AAGRAEGSEAAELaeiyaKLEEIEADKAPARASVILAGLGFTPKMQQ 322
Cdd:cd03258 62 VLvdgtDLTLLSGKELRKARRRIGMIfqhfnllSSRTVFENVALPL-----EIAGVPKAEIEERVLELLELVGLEDKADA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 323 QPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:cd03258 137 YPA-QLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILaLLRDINRELGLTIVLITHEMEVVKRICDRVAVME 215
|
250
....*....|....*...
gi 148612853 399 SQRLDGYRGDFETFIKSK 416
Cdd:cd03258 216 KGEVVEEGTVEEVFANPQ 233
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
197-642 |
2.00e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNLAWGRRYGLVGRNGLGKTTLLKMLA----------TRSLRVPAHISLlhvEQevagddtpaLQSVLESDSVRE--DL 264
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAgelpllsgerQSQFSHITRLSF---EQ---------LQKLVSDEWQRNntDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 265 LRRERELTaqiaagraeGSEAAELAeiyakLEEIeadKAPARASVILAGLGFTPKMqqqpTREF---SGGWRMRLALARA 341
Cdd:PRK10938 91 LSPGEDDT---------GRTTAEII-----QDEV---KDPARCEQLAQQFGITALL----DRRFkylSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 342 LFARPDLLLLDEPTNMLDVRAILWLENYLQTWPST----ILVVshdrNFLNAIAtdiihlhsqrldgyrgDFETFIKSKQ 417
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgitlVLVL----NRFDEIP----------------DFVQFAGVLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 418 ERLLNQQREyeaqqqyRQHIQvfidrfrynanrASQVQSKLKMLEKLPELK-PVDKESEVVMKFPDGfekfSPPILQLDE 496
Cdd:PRK10938 210 DCTLAETGE-------REEIL------------QQALVAQLAHSEQLEGVQlPEPDEPSARHALPAN----EPRIVLNNG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 497 VDFYYDpkHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGD-----------LAPVRG-------IRHahrnlKIG 558
Cdd:PRK10938 267 VVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlFGRRRGsgetiwdIKK-----HIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 559 YFS-QHHVE-QLDLNVSAVEL--------LARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPC 628
Cdd:PRK10938 340 YVSsSLHLDyRVSTSVRNVILsgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKH 419
|
490
....*....|....
gi 148612853 629 PNFYILDEPTNHLD 642
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
178-383 |
2.00e-10 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 61.48 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGddTPA----LQS 253
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA--GFETPTSGEILLDGKDITN--LPPhkrpVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESD------SVREDL---LRRERELTAQIaagRAEGSEAAELAeiyaKLEEIEaDKAPArasvilaglgftpkmqqqp 324
Cdd:cd03300 77 VFQNYalfphlTVFENIafgLRLKKLPKAEI---KERVAEALDLV----QLEGYA-NRKPS------------------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 325 trEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR----AILWLENYLQTWPSTILVVSHD 383
Cdd:cd03300 130 --QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlrkdMQLELKRLQKELGITFVFVTHD 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
181-389 |
2.02e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLH-VEQEVAGDDTPalqsvlesds 259
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA----------GLLRpDSGEVRWNGTP---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 vredLLRRERELTAQIA-AGRAEGSEAAELAEiyAKLEEIEADKAPARASV--ILAGLGFTpKMQQQPTREFSGGWRMRL 336
Cdd:TIGR01189 64 ----LAEQRDEPHENILyLGHLPGLKPELSAL--ENLHFWAAIHGGAQRTIedALAAVGLT-GFEDLPAAQLSAGQQRRL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 337 ALARALFARPDLLLLDEPTNMLDVRAILWL----ENYLQTWPSTILVVSHDRNFLNA 389
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVALLagllRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
523-691 |
2.32e-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: 61.44 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLL-----------------LGDLAPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 581
Cdd:cd03258 36 IIGRSGAGKSTLIRCInglerptsgsvlvdgtdLTLLSG-KELRKARR--RIGMIFQH-----------FNLLSSRtvfe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 582 ---FP----GRP----EEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IE 647
Cdd:cd03258 102 nvaLPleiaGVPkaeiEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 648 ALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 691
Cdd:cd03258 181 ALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEV--VEEG 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
513-678 |
2.46e-10 |
|
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: 61.01 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFsqhhveqLDLNVSavelLARKFPGRpeeEY 590
Cdd:cd03220 41 VSFEVPRgeRIGLIGRNGAGKSTLLRLLAGIYPPDSG--TVTVRGRVSSL-------LGLGGG----FNPELTGR---EN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 591 RHQLGR-YGIS-----------------GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRA 652
Cdd:cd03220 105 IYLNGRlLGLSrkeidekideiiefselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRR 184
|
170 180 190
....*....|....*....|....*....|
gi 148612853 653 LNNFR---GGVILVSHDERFIRLVC-RELW 678
Cdd:cd03220 185 LRELLkqgKTVILVSHDPSSIKRLCdRALV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
197-402 |
2.46e-10 |
|
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: 60.97 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtPALQSVleSDSVREDLLRRERELTAQIA 276
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIA--GFETPQSGRVLINGVDVTAAP-PADRPV--SMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 277 AGRAEGseaaelaeiyAKLEEIEADkapaRASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTN 356
Cdd:cd03298 93 LGLSPG----------LKLTAEDRQ----AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148612853 357 MLD--VRA---ILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03298 158 ALDpaLRAemlDLVLDLHAET-KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
522-674 |
2.89e-10 |
|
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: 60.91 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVV--GENGAGKSTMLKLLLGDLAPVRG---IRHAHRNL----------------KIGYFSQHhveqldLN----VSAVE 576
Cdd:COG4778 39 CVAltGPSGAGKSTLLKCIYGNYLPDSGsilVRHDGGWVdlaqaspreilalrrrTIGYVSQF------LRviprVSALD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 577 -----LLARkfpGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-- 645
Cdd:COG4778 113 vvaepLLER---GVDREEARARarelLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANra 189
|
170 180 190
....*....|....*....|....*....|..
gi 148612853 646 --IEALGRALNnfRG-GVILVSHDERFIRLVC 674
Cdd:COG4778 190 vvVELIEEAKA--RGtAIIGIFHDEEVREAVA 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-382 |
3.00e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.08 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLlkmlatrsLRVPAHISLLHVEQEVAGDDTPALQSVLES 257
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTL--------LRVFNRLIELYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVredLLRRERELTAQIAAGRAEGSEAAELAeIYAKLEEIEADKAPARASVILAglgfTPKMQ---------QQPTREF 328
Cdd:PRK14247 76 DVI---ELRRRVQMVFQIPNPIPNLSIFENVA-LGLKLNRLVKSKKELQERVRWA----LEKAQlwdevkdrlDAPAGKL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:PRK14247 148 SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
167-360 |
3.28e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.10 E-value: 3.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 167 LESSGKNKSYDVRIENFDVSFgdrvllagadvNLAWGRRYGLVGRNGLGKTTLLKMLATRSlrVPAHISLLHVEQEVAGD 246
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSF-----------DLYPGEVLGIVGESGSGKTTLLNALSARL--APDAGEVHYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 247 DTPALqsvleSDSVREDLLRRE--------RE-LTAQIAAG-----RAEGSEAAELAEIYAK----LEEIEADkaPARas 308
Cdd:PRK11701 74 DLYAL-----SEAERRRLLRTEwgfvhqhpRDgLRMQVSAGgnigeRLMAVGARHYGDIRATagdwLERVEID--AAR-- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 309 vilaglgftpkMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK11701 145 -----------IDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
492-666 |
3.33e-10 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 61.31 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPK----HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-------------------I 548
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGtvtidgrditakkkkklkdL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 549 RHahrnlKIGY---FSQHhveQL--------------DLNVSAVELLARKFpgrpeeEYRHQLGrygISGELAMRPLASL 611
Cdd:TIGR04521 81 RK-----KVGLvfqFPEH---QLfeetvykdiafgpkNLGLSEEEAEERVK------EALELVG---LDEEYLERSPFEL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 612 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEALGRALNNfrgGVILVSHD 666
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgrkeiLDLFKRLHKEKGL---TVILVTHS 202
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
493-666 |
3.95e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.87 E-value: 3.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYDPKHVIFSrlsVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgyfsqhHVEQLDL 570
Cdd:COG4604 3 EIKNVSKRYGGKVVLDD---VSLTIPKGgiTALIGPNGAGKSTLLSMISRLLPPDSG--------EV------LVDGLDV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 571 NVSAVELLARK------------------------FP---GRPEEEYRHQLGRYgIS----GELAMRPLASLSGGQKSR- 618
Cdd:COG4604 66 ATTPSRELAKRlailrqenhinsrltvrelvafgrFPyskGRLTAEDREIIDEA-IAyldlEDLADRYLDELSGGQRQRa 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 619 -VA--FAQMTMpcpnfYI-LDEPTNHLDM----ETIEALGRALNNFRGGVILVSHD 666
Cdd:COG4604 145 fIAmvLAQDTD-----YVlLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
179-383 |
3.96e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.80 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSF-----------GDRVLLAGADVNLAWGRRYGLVGRNGLGKTT----LLKMLATR-----------SLRVPA 232
Cdd:PRK15134 277 DVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgqplhNLNRRQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 233 HISLLHVEQEVAGDDTPALQSVLESDSVREDLLR-RERELTAqiaagraegseAAELAEIYAKLEEIeadkaparasvil 311
Cdd:PRK15134 357 LLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTLSA-----------AQREQQVIAVMEEV------------- 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 312 aglGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-ILWLENYLQ-TWPSTILVVSHD 383
Cdd:PRK15134 413 ---GLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAqILALLKSLQqKHQLAYLFISHD 485
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
184-382 |
4.29e-10 |
|
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: 60.56 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 184 DVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVAGDDTPALQSVLESD 258
Cdd:cd03248 16 NVTFAyptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 SVREDLLrrERELTAQIAAGRAEGSeaaelaeiyakLEEIEADKAPARASvilaglGFTPKMQQQPTRE-------FSGG 331
Cdd:cd03248 94 GQEPVLF--ARSLQDNIAYGLQSCS-----------FECVKEAAQKAHAH------SFISELASGYDTEvgekgsqLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148612853 332 WRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
207-383 |
5.74e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.26 E-value: 5.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 207 GLVGRNGLGKTTLLKMLAtrslrvpahiSLLHV---EQEVAGDDtPAlqsvlesdsvredllRRERELTAQIAA--G-Ra 280
Cdd:COG4586 52 GFIGPNGAGKSTTIKMLT----------GILVPtsgEVRVLGYV-PF---------------KRRKEFARRIGVvfGqR- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 281 egSE------AAE----LAEIYakleEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLL 350
Cdd:COG4586 105 --SQlwwdlpAIDsfrlLKAIY----RIPDAEYKKRLDELVELLDLGELLDT-PVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 351 LDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 383
Cdd:COG4586 178 LDEPTIGLDVvskEAIReFLKEYNRERGTTILLTSHD 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
178-402 |
6.25e-10 |
|
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: 59.58 E-value: 6.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPA----LQS 253
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTSGRIYIGGRDVT--DLPPkdrdIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLES------DSVREDL---LRRERELTAQIAAGRaegSEAAELAEIYAKLeeieaDKAParasvilaglgftpkmqqqp 324
Cdd:cd03301 77 VFQNyalyphMTVYDNIafgLKLRKVPKDEIDERV---REVAELLQIEHLL-----DRKP-------------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 325 tREFSGGWRMRLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:cd03301 129 -KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
..
gi 148612853 401 RL 402
Cdd:cd03301 208 QI 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
492-665 |
7.35e-10 |
|
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: 58.48 E-value: 7.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQLDL 570
Cdd:cd03247 1 LSINNVSFSYPEQEqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG--------EI-TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 571 NVS-AVELLARKfPGRPEEEYRHQLGRygisgelamrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEAL 649
Cdd:cd03247 72 ALSsLISVLNQR-PYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170
....*....|....*...
gi 148612853 650 GRALNNFRGG--VILVSH 665
Cdd:cd03247 138 LSLIFEVLKDktLIWITH 155
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
301-419 |
7.55e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 60.03 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWP 374
Cdd:COG4161 116 EQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqVVEII---RELSQTG 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 148612853 375 STILVVSHDRNFLNAIATDIIHLHSQRLDGYrGDFETFIKSKQER 419
Cdd:COG4161 192 ITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
503-673 |
8.33e-10 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 61.98 E-value: 8.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 503 PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL---KIGYFSQ--------- 562
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGsvrldgadLKQWDRETfgkHIGYLPQdvelfpgtv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 -HHVEQLDLNVSAVELL-ARKFPG------RPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:TIGR01842 409 aENIARFGENADPEKIIeAAKLAGvhelilRLPDGYDTVIGPGG----------ATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 635 DEPTNHLDMETIEALGRALNNF--RGG-VILVSHDERFIRLV 673
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALkaRGItVVVITHRPSLLGCV 520
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
179-361 |
8.62e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.13 E-value: 8.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPAlqsvleSD 258
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT--------------------GELTPS------SG 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 SVREDllrrERELTA----QIAAGRAEGSEAAELA------EI-----YAKLEEIEADKAPARASVILAGLGftpKMQQQ 323
Cdd:COG4559 57 EVRLN----GRPLAAwspwELARRRAVLPQHSSLAfpftveEVvalgrAPHGSSAAQDRQIVREALALVGLA---HLAGR 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 324 PTREFSGGWRMRLALARAL-------FARPDLLLLDEPTNMLDVR 361
Cdd:COG4559 130 SYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLA 174
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
492-671 |
8.88e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.02 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPK----HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFSQ----- 562
Cdd:cd03250 1 ISVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG--SVSVPGSIAYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 -------------HHVEQLDLNVSAVELLA--RKFPGRPEEEyrhqLGRYGIsgelamrplaSLSGGQKSRVAFAQMTMP 627
Cdd:cd03250 79 ngtirenilfgkpFDEERYEKVIKACALEPdlEILPDGDLTE----IGEKGI----------NLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 628 CPNFYILDEPTNHLDMET---I--EALGRALNNFRgGVILVSHDERFIR 671
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgrhIfeNCILGLLLNNK-TRILVTHQLQLLP 192
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
507-698 |
9.78e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.01 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 507 IFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNlkIGYFSQHHVEQLDLNVSAVELLARKFPGR 585
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtVLVAGDD--VEALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 PEEEY-RH-QLGRYGISGE-----------------LAMRPLASLSGGQKSRV----AFAQMTmpcPNFyILDEPTNHLD 642
Cdd:PRK09536 96 QVVEMgRTpHRSRFDTWTEtdraaveramertgvaqFADRPVTSLSGGERQRVllarALAQAT---PVL-LLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 643 M----ETIEALGRALNNFRGGVILVsHDERFIRLVCRELWVCEGGGVT------------RVEGGFDQYRAL 698
Cdd:PRK09536 172 InhqvRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRaagppadvltadTLRAAFDARTAV 242
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
492-683 |
1.22e-09 |
|
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: 58.70 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIfsrLSVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----K 556
Cdd:cd03262 1 IEIKNLHKSFGDFHVL---KGIDLTVKkgEVVVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglkLTDDKKNInelrqK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQH-----HVEQLDlNVSaveLLARKFPGRPEEEY----RHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 627
Cdd:cd03262 78 VGMVFQQfnlfpHLTVLE-NIT---LAPIKVKGMSKAEAeeraLELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 628 CPNFYILDEPTNHLDMETI-EALGRALNNFRGG--VILVSHDERFIRLVCRELWVCEGG 683
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVgEVLDVMKDLAEEGmtMVVVTHEMGFAREVADRVIFMDDG 211
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
167-461 |
1.26e-09 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 61.28 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 167 LESSGKNKSYDVRIENFDVsfgdrvlLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHisllhVEQEVAGD 246
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEV-------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGC--LDKPTS-----GTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 247 DTpalqSVLESDSVREdlLRRER--------ELTAQIAAgraegSEAAELAEIYAKLEEieaDKAPARASVILAGLGFTP 318
Cdd:PRK10535 71 DV----ATLDADALAQ--LRREHfgfifqryHLLSHLTA-----AQNVEVPAVYAGLER---KQRLLRAQELLQRLGLED 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 319 KMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWPSTILVVSHDRNfLNAIAT 392
Cdd:PRK10535 137 RVEYQPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VAAQAE 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 393 DIIHLHsqrldgyrgDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFR------YNANRASQVQSKLKML 461
Cdd:PRK10535 212 RVIEIR---------DGEIVRNPPAQEKVNVAGGTEPVVNTASGWRQFVSGFRealtmaWRAMAANKMRTLLTML 277
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
203-383 |
1.31e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPAlqsvlesdsvREDLLRRERELTAQIAAGRAEg 282
Cdd:PRK11629 35 GEMMAIVGSSGSGKSTLLHLLG--------------------GLDTPT----------SGDVIFNGQPMSKLSSAAKAE- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 283 SEAAELAEIY---------AKLEEIE-----ADKAPA----RASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFA 344
Cdd:PRK11629 84 LRNQKLGFIYqfhhllpdfTALENVAmplliGKKKPAeinsRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 345 RPDLLLLDEPTNMLDVR---AILWLENYLQTWPST-ILVVSHD 383
Cdd:PRK11629 163 NPRLVLADEPTGNLDARnadSIFQLLGELNRLQGTaFLVVTHD 205
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
491-666 |
1.39e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.81 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYY-DPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP---------VRGIRHAHRNL----- 555
Cdd:PRK13640 5 IVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 556 KIGYFSQHHVEQ-LDLNVS---AVELLARKFPgRPEEE--YRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCP 629
Cdd:PRK13640 85 KVGIVFQNPDNQfVGATVGddvAFGLENRAVP-RPEMIkiVRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 630 NFYILDEPTNHLD---METIEALGRALNNFRG-GVILVSHD 666
Cdd:PRK13640 163 KIIILDESTSMLDpagKEQILKLIRKLKKKNNlTVISITHD 203
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
207-383 |
1.76e-09 |
|
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: 60.11 E-value: 1.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 207 GLVGRNGLGKTTLLKMLA--------------------TRSLRVPAH---ISLlhVEQEvagddtPALQSVLesdSVRED 263
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAglerpdsgrirlggevlqdsARGIFLPPHrrrIGY--VFQE------ARLFPHL---SVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 264 LL---RREREltaqiAAGRAEGSEAAELaeiyakleeieadkaparasvilagLGFTPKMQQQPTReFSGGWRMRLALAR 340
Cdd:COG4148 98 LLygrKRAPR-----AERRISFDEVVEL-------------------------LGIGHLLDRRPAT-LSGGERQRVAIGR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 341 ALFARPDLLLLDEPTNMLDV---RAILwleNYLQTWPST----ILVVSHD 383
Cdd:COG4148 147 ALLSSPRLLLMDEPLAALDLarkAEIL---PYLERLRDEldipILYVSHS 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
178-361 |
1.96e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.40 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAHI 234
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLdiPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghdvrdyTLASLR--RQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 235 SLlhVEQEVagddtpalqsVLESDSVREDLLRREREltaqiaAGRAEGSEAAELAEIYAKLEEIEadkaparasvilagL 314
Cdd:cd03251 79 GL--VSQDV----------FLFNDTVAENIAYGRPG------ATREEVEEAARAANAHEFIMELP--------------E 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 315 GFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:cd03251 127 GYDTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
487-693 |
2.04e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 59.25 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 487 FSPPILqLDEVDFYYDPKHVIFSRLSVSADLESR----ICVVGENGAGKSTMLKL------------LLGDL---APVRG 547
Cdd:PRK13645 3 FSKDII-LDNVSYTYAKKTPFEFKALNNTSLTFKknkvTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYaipANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 548 IRHAHRNLK-IGYFSQHHVEQL-------DLNVSAVELLARKfpgrpEEEYR---HQLGRYGISGELAMRPLASLSGGQK 616
Cdd:PRK13645 82 IKEVKRLRKeIGLVFQFPEYQLfqetiekDIAFGPVNLGENK-----QEAYKkvpELLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 617 SRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVTRVEGGF 692
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
.
gi 148612853 693 D 693
Cdd:PRK13645 237 E 237
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
193-383 |
2.15e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 58.25 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEV---AGDDTPALQ--SVLESDSVREDLlrr 267
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQItepGPDRMVVFQnySLLPWLTVRENI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 268 ereltaqiaagraegseAAELAEIYAKLEEIEaDKAPARASVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:TIGR01184 76 -----------------ALAVDRVLPDLSKSE-RRAIVEEHIALVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 348 LLLLDEPTNMLD--VRAILWlENYLQTWPS---TILVVSHD 383
Cdd:TIGR01184 135 VLLLDEPFGALDalTRGNLQ-EELMQIWEEhrvTVLMVTHD 174
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
178-395 |
2.22e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDTPALQSVLes 257
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINL--LEQPEAGTIRVGDITIDTARSLSQQKGL-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 dsVREdlLRRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLA 337
Cdd:PRK11264 80 --IRQ--LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 338 LARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
178-382 |
2.38e-09 |
|
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: 56.67 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqsvles 257
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 dsvredllrrereltaqiaagraeGSEAAELAEIYAKLEEIEAdKAPARAsvILAGLGFTPKMqqqptrefSGGWRMRLA 337
Cdd:cd03216 48 ------------------------GLYKPDSGEILVDGKEVSF-ASPRDA--RRAGIAMVYQL--------SVGERQMVE 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSH 382
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
486-642 |
2.45e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 58.85 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 486 KFSPPILQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrNLKI-GY-FSQ 562
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG------EIKIdGItISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 HHVEQLDLNV-------------SAVE------LLARKFPgrPEE------EYRHQLgryGISGELAMRPLaSLSGGQKS 617
Cdd:PRK13632 76 ENLKEIRKKIgiifqnpdnqfigATVEddiafgLENKKVP--PKKmkdiidDLAKKV---GMEDYLDKEPQ-NLSGGQKQ 149
|
170 180
....*....|....*....|....*
gi 148612853 618 RVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
505-665 |
2.55e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.51 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 505 HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGdLA------------PVRGIRHA-HRNLK-IGyfsqhHVEQLDL 570
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LArpdagevlwqgePIRRQRDEyHQDLLyLG-----HQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 571 NVSAVELL--ARKFPGRPEEEYRHQ-LGRYGISG-ELAmrPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI 646
Cdd:PRK13538 88 ELTALENLrfYQRLHGPGDDEALWEaLAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|..
gi 148612853 647 EALGRALNNF--RGG-VILVSH 665
Cdd:PRK13538 166 ARLEALLAQHaeQGGmVILTTH 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
492-684 |
2.73e-09 |
|
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: 56.78 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLlGDLAPVRG---IRHAHRNLkigYFsqhhveql 568
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGSgriGMPEGEDL---LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 569 dlnvsavellarkFPGRPeeeyrhqlgrYGISGELA---MRPLAS-LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME 644
Cdd:cd03223 69 -------------LPQRP----------YLPLGTLReqlIYPWDDvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 645 TIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGG 684
Cdd:cd03223 126 SEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
178-401 |
2.85e-09 |
|
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: 57.68 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRVpahisLLHVEQEVAGDDTPalqsvlES 257
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI----LGI-----ILPDSGEVLFDGKP------LD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVREDL--LRRERELTAQIaagraegsEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMR 335
Cdd:cd03269 66 IAARNRIgyLPEERGLYPKM--------KVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEY-ANKRVEELSKGNQQK 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 336 LALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd03269 137 VQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
508-666 |
3.02e-09 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 58.12 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 508 FSRLSVSADLE-SRICVV-GENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNlkIGYFSQHHVEQLDLNVS- 573
Cdd:cd03299 13 FKLKNVSLEVErGDYFVIlGPTGSGKSVLLETIAGFIKPDSGkillngkditnLPPEKRD--ISYVPQNYALFPHMTVYk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 --AVELLARKFPgRPEEEYR-HQLGRY-GISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---- 645
Cdd:cd03299 91 niAYGLKKRKVD-KKEIERKvLEIAEMlGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkekl 168
|
170 180
....*....|....*....|.
gi 148612853 646 IEALGRALNNFRGGVILVSHD 666
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHD 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
504-643 |
3.73e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 504 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNL--KIGYFSQHHVEQLDLNV 572
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 SavELLAR-KFPGRP---------EEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK10253 99 Q--ELVARgRYPHQPlftrwrkedEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
.
gi 148612853 643 M 643
Cdd:PRK10253 176 I 176
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
511-686 |
3.75e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 58.28 E-value: 3.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 511 LSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK-----IGYFSQHHVEQL-------DLNV 572
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPtsgsvlIRGEPITKENIRevrkfVGLVFQNPDDQIfsptveqDIAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 SAVELlarkfpGRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 648
Cdd:PRK13652 103 GPINL------GLDEETVAHRvssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 649 LGRALNNF--RGG--VILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:PRK13652 176 LIDFLNDLpeTYGmtVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
523-666 |
4.20e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 57.76 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGYFSQHHVEQLDLNVSA--VELLARKFPGRPEE- 588
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPqyVDLIPKAVKGKVGEl 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 589 ----EYRHQLGRYGISGELAM---RPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME---TIEALGRALNNFRG 658
Cdd:cd03236 111 lkkkDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDN 190
|
....*...
gi 148612853 659 GVILVSHD 666
Cdd:cd03236 191 YVLVVEHD 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
178-384 |
4.50e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.94 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISL-------LHVEQEVAGD--DT 248
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrLHARDRKVGFvfQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 PAL---QSVLESDSVREDLL-RRERELTAQIAAGRAEGSEAAELAEIyakleeieADKAPArasvilaglgftpkmqqqp 324
Cdd:PRK10851 83 YALfrhMTVFDNIAFGLTVLpRRERPNAAAIKAKVTQLLEMVQLAHL--------ADRYPA------------------- 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148612853 325 trEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 384
Cdd:PRK10851 136 --QLSGGQKQRVALARALAVEPQILLLDEPFGALDaqVRKELrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
197-384 |
4.68e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNLAW--GRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPALQSVLESdSVREDLLRRERELTAQ 274
Cdd:PRK11607 37 DVSLTIykGEIFALLGASGCGKSTLLRMLA--GFEQPTAGQIMLDGVDLS--HVPPYQRPINM-MFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 275 IAAGRAEGSEAAelAEIYAKLEEIeadkaparasvilagLGFTpKMQQQPTR---EFSGGWRMRLALARALFARPDLLLL 351
Cdd:PRK11607 112 IAFGLKQDKLPK--AEIASRVNEM---------------LGLV-HMQEFAKRkphQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 352 DEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 384
Cdd:PRK11607 174 DEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
178-382 |
4.83e-09 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 57.74 E-value: 4.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAgaDVNLAWGRR--YGLVGRNGLGKTTLLkmlatRSL-RVPAHISLLHVEQEVAGDDtpalQSV 254
Cdd:COG1117 12 IEVRNLNVYYGDKQALK--DINLDIPENkvTALIGPSGCGKSTLL-----RCLnRMNDLIPGARVEGEILLDG----EDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDsVREDLLRRERELTAQ------------IAAG--------RAEGSEAAELA--------EIYAKLeeieadKAPAR 306
Cdd:COG1117 81 YDPD-VDVVELRRRVGMVFQkpnpfpksiydnVAYGlrlhgiksKSELDEIVEESlrkaalwdEVKDRL------KKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 307 AsviLAGlGftpkmQQQptrefsggwrmRLALARALFARPDLLLLDEPTNMLDVRA-------ILWL-ENYlqtwpsTIL 378
Cdd:COG1117 154 G---LSG-G-----QQQ-----------RLCIARALAVEPEVLLMDEPTSALDPIStakieelILELkKDY------TIV 207
|
....
gi 148612853 379 VVSH 382
Cdd:COG1117 208 IVTH 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
492-668 |
6.68e-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: 56.73 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYdpkHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAH------------- 552
Cdd:cd03298 1 VRLDKIRFSY---GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPqsgrvlINGVDVTAappadrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 553 -RNLkigyFSQHHVEQ-LDLNVSavellarkfPG---RPEEEYRHQ--LGRYGISGELAMRPlASLSGGQKSRVAFAQMT 625
Cdd:cd03298 78 eNNL----FAHLTVEQnVGLGLS---------PGlklTAEDRQAIEvaLARVGLAGLEKRLP-GELSGGERQRVALARVL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 626 MPCPNFYILDEPtnhldmetIEALGRALNNFRGGVILVSHDER 668
Cdd:cd03298 144 VRDKPVLLLDEP--------FAALDPALRAEMLDLVLDLHAET 178
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-420 |
7.07e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpaHISLLHVEQEVAGDDTPALQSVLES 257
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--------RMNELESEVRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 dSVREDLLRRERELT--------AQIAAGRAEGseaaelAEIYAKLEEIEADKApARASVILAGLGFTPKMQ-QQPTREF 328
Cdd:PRK14258 80 -RVNLNRLRRQVSMVhpkpnlfpMSVYDNVAYG------VKIVGWRPKLEIDDI-VESALKDADLWDEIKHKiHKSALDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP----STILVVSHDRNFLNAIAtdiihlhsqrldg 404
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLS------------- 218
|
250
....*....|....*.
gi 148612853 405 yrgDFETFIKSKQERL 420
Cdd:PRK14258 219 ---DFTAFFKGNENRI 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
491-665 |
7.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.82 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRLSVSADLE----SRICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IR 549
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsstskqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 550 HAHRnlKIGYFSQHHVEQL--DLNVSAVELLARKFPGRPEEEYR---HQLGRYGISGELAMRPLASLSGGQKSRVAFAQM 624
Cdd:PRK13643 81 PVRK--KVGVVFQFPESQLfeETVLKDVAFGPQNFGIPKEKAEKiaaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148612853 625 TMPCPNFYILDEPTNHLDMET---IEALGRALNNFRGGVILVSH 665
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
177-359 |
7.22e-09 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 58.16 E-value: 7.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 177 DVRIENFDVSFGDRVLLAgaDVNLAW--GRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAH---ISLl 237
Cdd:COG3839 3 SLELENVSKSYGGVEALK--DIDLDIedGEFLVLLGPSGCGKSTLLRMIAgledptsgeiliggRDVTDLPPKdrnIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 238 hVEQevagddTPALqsvLESDSVREDL---LRRERELTAQIAAgRAEgsEAAELAEIYAKLeeieaDKAParasvilagl 314
Cdd:COG3839 80 -VFQ------SYAL---YPHMTVYENIafpLKLRKVPKAEIDR-RVR--EAAELLGLEDLL-----DRKP---------- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 315 gftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG3839 132 -----------KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
492-691 |
7.34e-09 |
|
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: 56.73 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKH-VIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNLKIGY 559
Cdd:cd03252 1 ITFEHVRFRYKPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQhhvEQLDLNVSAVELLARKFPGRPEEEY--------RHQ------LGRYGISGELAmrplASLSGGQKSRVAFAQMT 625
Cdd:cd03252 81 VLQ---ENVLFNRSIRDNIALADPGMSMERVieaaklagAHDfiselpEGYDTIVGEQG----AGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 626 MPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELwVCEGGGVtrVEGG 691
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAHRLSTVKNADRII-VMEKGRI--VEQG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
191-359 |
7.85e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 56.67 E-value: 7.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 191 VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPAlqsvleSDSVREDllrrERE 270
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLA--------------------GLDRPT------SGTVRLA----GQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 271 LTA----QIAAGRAEG------SE-------AAE---LAeiyakLEEIEADKAPARASVILAGLGFTPKMQQQPtREFSG 330
Cdd:COG4181 76 LFAldedARARLRARHvgfvfqSFqllptltALEnvmLP-----LELAGRRDARARARALLERVGLGHRLDHYP-AQLSG 149
|
170 180
....*....|....*....|....*....
gi 148612853 331 GWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
497-699 |
8.58e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.97 E-value: 8.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 497 VDFYYD--PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIGYFSQH 563
Cdd:TIGR00958 484 VSFSYPnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptggqvLLDGVPLVQYDHHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 564 HV-----------------EQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVAFAQMTM 626
Cdd:TIGR00958 564 PVlfsgsvreniaygltdtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG----------SQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 627 PCPNFYILDEPTNHLDMEtIEALGRALNNFRG-GVILVSHDERFIR-----LVCRELWVCEGGGVTRVEGGFDQYRALL 699
Cdd:TIGR00958 634 RKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVEradqiLVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
492-645 |
1.05e-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: 58.60 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI------------RHAHRNLkIGY 559
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdidRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQhhvEQLDLNVSAVE-LLARKFPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMPC 628
Cdd:TIGR01193 553 LPQ---EPYIFSGSILEnLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTD 629
|
170
....*....|....*..
gi 148612853 629 PNFYILDEPTNHLDMET 645
Cdd:TIGR01193 630 SKVLILDESTSNLDTIT 646
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
301-397 |
1.10e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.56 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAIlwleNYLQTW 373
Cdd:PRK11124 116 DQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSII----RELAET 190
|
90 100
....*....|....*....|....
gi 148612853 374 PSTILVVSHDRNFLNAIATDIIHL 397
Cdd:PRK11124 191 GITQVIVTHEVEVARKTASRVVYM 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
190-383 |
1.19e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 56.62 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 190 RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHisllhveQEVAGDDTPalqsVLESDSVREDLLRRER 269
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLV--GLESPSQ-------GNVSWRGEP----LAKLNRAQRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 270 ELTAQ--IAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:PRK10419 92 QMVFQdsISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 348 LLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK10419 172 LLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
177-384 |
1.21e-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: 57.42 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 177 DVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAH---ISLL-- 237
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfetpdsgrilldgRDVTGLPPEkrnVGMVfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 238 ------H--VEQEVA-GddtpalqsvlesdsvredlLRRERELTAQIAAgRAEgsEAAELAEIyAKLeeieADKAParas 308
Cdd:COG3842 85 dyalfpHltVAENVAfG-------------------LRMRGVPKAEIRA-RVA--ELLELVGL-EGL----ADRYP---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 309 vilaglgftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 384
Cdd:COG3842 134 -----------------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDakLREEMREElrRLQRELGITFIYVTHDQ 196
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
488-694 |
1.26e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIFSrlsVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRGI----------------- 548
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRD---VSFDLYPGevLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdgqlrdlyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 549 ----RHAHRNlKIGYFSQHHVEQLDLNVSA----VELL----ARKFpGRPEEEYRHQLGRYGI-SGELAMRPlASLSGGQ 615
Cdd:PRK11701 80 eaerRRLLRT-EWGFVHQHPRDGLRMQVSAggniGERLmavgARHY-GDIRATAGDWLERVEIdAARIDDLP-TTFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 616 KSRVAFAQMTMPCPNFYILDEPTNHLDMeTIEAlgRALNNFRG-------GVILVSHDERFIRLVCRELWVCEGGGVtrV 688
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQA--RLLDLLRGlvrelglAVVIVTHDLAVARLLAHRLLVMKQGRV--V 231
|
....*..
gi 148612853 689 EGGF-DQ 694
Cdd:PRK11701 232 ESGLtDQ 238
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
161-382 |
1.54e-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: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 161 SRKESRLESSGKNKSYDVRIENFDVSFGDRVLlagADVNLA--WGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLH 238
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSYGYGSNIL---SDISLTikMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 239 VEqeVAGDDTPAL---------QSVLESDSVREDLLRRERELTAQiaagrAEGSEAAELAEIYAKLEEIEadkaparasv 309
Cdd:TIGR01193 536 FS--LKDIDRHTLrqfinylpqEPYIFSGSILENLLLGAKENVSQ-----DEIWAACEIAEIKDDIENMP---------- 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 310 ilagLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWPSTILVVSH 382
Cdd:TIGR01193 599 ----LGYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNLDTiteKKI--VNNLLNLQDKTIIFVAH 667
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
319-383 |
1.56e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.04 E-value: 1.56e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 319 KMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHD 383
Cdd:PRK09473 154 RMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
294-383 |
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: 55.80 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 294 KLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW 373
Cdd:cd03299 97 KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKI 175
|
90
....*....|....
gi 148612853 374 PS----TILVVSHD 383
Cdd:cd03299 176 RKefgvTVLHVTHD 189
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
179-409 |
2.03e-08 |
|
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: 55.65 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDTPALQSV--- 254
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 ----------LESDSVREDLL--RRERELTAQIAAGR---AEGSEAAELaeiyakLEEIE-ADKAPARASvilaglgftp 318
Cdd:cd03256 80 igmifqqfnlIERLSVLENVLsgRLGRRSTWRSLFGLfpkEEKQRALAA------LERVGlLDKAYQRAD---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 319 kmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWPSTILVVSHDRNFLNAIATDI 394
Cdd:cd03256 144 --------QLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRI 215
|
250
....*....|....*..
gi 148612853 395 IHLHSQRL--DGYRGDF 409
Cdd:cd03256 216 VGLKDGRIvfDGPPAEL 232
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
193-392 |
2.15e-08 |
|
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.
Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 55.47 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVagDDTPAlqsvlesdSVREDLLRREREL- 271
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWV--DLAQA--------SPREVLEVRRKTIg 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 272 -TAQI--AAGRAEgseAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDL 348
Cdd:TIGR02324 94 yVSQFlrVIPRVS---ALEVVAEPLLERGVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 349 LLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIAT 392
Cdd:TIGR02324 171 LLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVAD 217
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
523-666 |
2.77e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 56.31 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL---------KIGYFSQH-----H--VEQldlNVSAVelLARKFPGR 585
Cdd:COG1118 33 LLGPSGSGKTTLLRIIAGLETPDSGrIVLNGRDLftnlpprerRVGFVFQHyalfpHmtVAE---NIAFG--LRVRPPSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 PE--EEYRHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------METIeaLGRALNNFR 657
Cdd:COG1118 108 AEirARVEELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRRW--LRRLHDELG 184
|
....*....
gi 148612853 658 GGVILVSHD 666
Cdd:COG1118 185 GTTVFVTHD 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
525-665 |
2.93e-08 |
|
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: 54.68 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 525 GENGAGKSTMLKLLLGDLAP------VRGIRhAHRN-----LKIGYFSQHhvEQLDLNVSAVELLArkFPGRPEEEYRHQ 593
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPdagfatVDGFD-VVKEpaearRRLGFVSDS--TGLYDRLTARENLE--YFAGLYGLKGDE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 594 L--------GRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VIL 662
Cdd:cd03266 113 LtarleelaDRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILF 191
|
...
gi 148612853 663 VSH 665
Cdd:cd03266 192 STH 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
327-360 |
3.01e-08 |
|
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: 55.83 E-value: 3.01e-08
10 20 30
....*....|....*....|....*....|....
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
179-382 |
3.27e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVAGDDTPALQS 253
Cdd:TIGR00958 478 LIEFQDVSFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQPTGGQVLLDGVPLVQYDHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 ---------VLESDSVREDLlrrereltaqiaagrAEGSEAAELAEIYAKLEEIEADKaparasvilaglgFTPKMQQQP 324
Cdd:TIGR00958 556 qvalvgqepVLFSGSVRENI---------------AYGLTDTPDEEIMAAAKAANAHD-------------FIMEFPNGY 607
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 325 TRE-------FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAilwlENYLQTWPS----TILVVSH 382
Cdd:TIGR00958 608 DTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
492-666 |
3.28e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 55.61 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVI----FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI----------RHAHRNLK- 556
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhitpETGNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 ----IGYFSQHHVEQLDLN--VSAVELLARKFpGRPEEEYRHQ----LGRYGISGELAMRPLASLSGGQKSRVAFAQMTM 626
Cdd:PRK13641 83 lrkkVSLVFQFPEAQLFENtvLKDVEFGPKNF-GFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHD 666
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGhtVILVTHN 204
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
513-683 |
3.32e-08 |
|
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: 55.20 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLESRICV--VGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQHHVEQLDLNV------SAV--ELLARK 581
Cdd:TIGR02769 30 VSLSIEEGETVglLGRSGCGKSTLARLLLGLEKPAQGtVSFRGQDLYQLDRKQRRAFRRDVQLvfqdspSAVnpRMTVRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 582 FPGRPEEEY------------RHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETI 646
Cdd:TIGR02769 110 IIGEPLRHLtsldeseqkariAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqAVI 189
|
170 180 190
....*....|....*....|....*....|....*....
gi 148612853 647 EALGRALNNfRGGV--ILVSHDERFIRLVCRELWVCEGG 683
Cdd:TIGR02769 190 LELLRKLQQ-AFGTayLFITHDLRLVQSFCQRVAVMDKG 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
182-383 |
3.38e-08 |
|
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: 55.89 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 182 NFDVSFGDRVLlaGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhveqevagDDTpalqsVLESDSVR 261
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL---------NGR-----TLFDSRKG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 262 EDLLRREREL--TAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARasvILAGLGFTPkMQQQPTREFSGGWRMRLALA 339
Cdd:TIGR02142 68 IFLPPEKRRIgyVFQEARLFPHLSVRGNLRYGMKRARPSERRISFER---VIELLGIGH-LLGRLPGRLSGGEKQRVAIG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 340 RALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 383
Cdd:TIGR02142 144 RALLSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
176-383 |
3.40e-08 |
|
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: 55.04 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 176 YDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlatrslrvpahisllhveqeVAGDDTPALQSVL 255
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRL--------------------IAGLERPDSGTIL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 256 --ESDSVREDLLRRE-----------RELTA--QIAAG-----RAEGSEAAELAEIYAKLEEIeadkaparasVILAGLG 315
Cdd:cd03296 61 fgGEDATDVPVQERNvgfvfqhyalfRHMTVfdNVAFGlrvkpRSERPPEAEIRAKVHELLKL----------VQLDWLA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 316 ftpkmQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHD 383
Cdd:cd03296 131 -----DRYPA-QLSGGQRQRVALARALAVEPKVLLLDEPFGALDakVRKELrrWLRRLHDELHVTTVFVTHD 196
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
491-666 |
3.61e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGY 559
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGREVnaenekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHHVEQL-------DLNVSAVEL-LARKFPGRPEEEYRHQLGRYgisgELAMRPLASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:PRK13647 84 VFQDPDDQVfsstvwdDVAFGPVNMgLDKDEVERRVEEALKAVRMW----DFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 148612853 632 YILDEPTNHLD---METIEALGRALNNFRGGVILVSHD 666
Cdd:PRK13647 160 IVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
523-673 |
3.78e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLG-------------------DLAPvrgirhAHR-NLKIGYFSQHHVE----------QLDLN- 571
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSP------DERaRAGIFLAFQYPVEipgvsvsnflRTALNa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 572 VSAVELLARKFpgrpEEEYRHQLGRYGISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG 650
Cdd:COG0396 105 RRGEELSAREF----LKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVA 180
|
170 180
....*....|....*....|....*.
gi 148612853 651 RALNNFRG---GVILVSHDERFIRLV 673
Cdd:COG0396 181 EGVNKLRSpdrGILIITHYQRILDYI 206
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
329-389 |
3.82e-08 |
|
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: 56.68 E-value: 3.82e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILwlenYLQTWPSTILVVSHDRNFLNA 389
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLLAA 532
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
491-666 |
4.07e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 55.08 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNL-----KI 557
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgepIKYDKKSLlevrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHVEQL-------DLNVSAVELlarkfpGRPEEEY----RHQLGRYGISGeLAMRPLASLSGGQKSRVAFAQMTM 626
Cdd:PRK13639 81 GIVFQNPDDQLfaptveeDVAFGPLNL------GLSKEEVekrvKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALN--NFRGGVILVS-HD 666
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHD 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
492-642 |
5.21e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.20 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVifsRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG------IRHAH------------- 552
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGsltlngQDHTTtppsrrpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 553 -RNLkigyFSQHHVEQ---LDLNvsavellarkfPG-RPEEEYRHQL----GRYGISGELAMRPlASLSGGQKSRVAFAQ 623
Cdd:PRK10771 79 eNNL----FSHLTVAQnigLGLN-----------PGlKLNAAQREKLhaiaRQMGIEDLLARLP-GQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 148612853 624 MTMPCPNFYILDEPTNHLD 642
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
207-383 |
5.26e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.34 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 207 GLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqSVLESDSVREDLLRRERELTAQIAAGRAEGSeaa 286
Cdd:cd03237 29 GILGPNGIGKTTFIKMLA----------------------------GVLKPDEGDIEIELDTVSYKPQYIKADYEGT--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 287 elaeIYAKLEEIEADK--APARASVILAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---- 360
Cdd:cd03237 78 ----VRDLLSSITKDFytHPYFKTEIAKPLQIEQILDRE-VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrl 152
|
170 180
....*....|....*....|....*.
gi 148612853 361 ---RAIlwlENYLQTWPSTILVVSHD 383
Cdd:cd03237 153 masKVI---RRFAENNEKTAFVVEHD 175
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
606-671 |
5.50e-08 |
|
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: 53.10 E-value: 5.50e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148612853 606 RPLASLSGGQKSRVAFAQM--TMPCPNFYILDEPTNHLDMETIEALgraLNNFRG------GVILVSHDERFIR 671
Cdd:cd03238 83 QKLSTLSGGELQRVKLASElfSEPPGTLFILDEPSTGLHQQDINQL---LEVIKGlidlgnTVILIEHNLDVLS 153
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
178-359 |
5.65e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 54.63 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKmlatrslrvpaHISLLhveqeVAGDDTPALQSVLES 257
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR-----------HLSGL-----ITGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVRedllrRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEadkaparaSVILAGLG-----------FTPKMQQ---- 322
Cdd:PRK09984 69 RTVQ-----REGRLARDIRKSRANTGYIFQQFNLVNRLSVLE--------NVLIGALGstpfwrtcfswFTREQKQralq 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 323 ------------QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK09984 136 altrvgmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
509-666 |
6.74e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.08 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 509 SRLS-VSADLES--RICVVGENGAGKSTMLKLLLG-------------DLAPVRGIRHAHRNlkiGYFSQHHVEQLDLNV 572
Cdd:COG4138 10 GRLGpISAQVNAgeLIHLIGPNGAGKSTLLARMAGllpgqgeillngrPLSDWSAAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 saVELLARKFPGRPEEEYRHQL-----GRYGISGELaMRPLASLSGGQKSRVAFAQMTM-------PCPNFYILDEPTNH 640
Cdd:COG4138 87 --FQYLALHQPAGASSEAVEQLlaqlaEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 148612853 641 LDMETIEALGRALNNFR---GGVILVSHD 666
Cdd:COG4138 164 LDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
172-400 |
7.91e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.56 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 172 KNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDDTPAL 251
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA--SLISPTSGTLL-----FEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 ------QSV--------LESDSVREDLLrrereLTAQIAAGRAEgseaaelaeiyakleeieadkaPARASVILAGLGFT 317
Cdd:PRK10247 75 kpeiyrQQVsycaqtptLFGDTVYDNLI-----FPWQIRNQQPD----------------------PAIFLDDLERFALP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 318 PKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTWPSTILVVSHDRNFLNAiA 391
Cdd:PRK10247 128 DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEI--IHRYVREQNIAVLWVTHDKDEINH-A 204
|
....*....
gi 148612853 392 TDIIHLHSQ 400
Cdd:PRK10247 205 DKVITLQPH 213
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
170-418 |
8.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 170 SGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVpaHISLLHVEQEVA--GDD 247
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEI--YDSKIKVDGKVLyfGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 248 tpalqsVLESDSVRedlLRRERELTAQIAAGRAEGSEAAELAeiYAKLEEIEADKAPARASV--ILAGLGFTPKMQQQ-- 323
Cdd:PRK14246 80 ------IFQIDAIK---LRKEVGMVFQQPNPFPHLSIYDNIA--YPLKSHGIKEKREIKKIVeeCLRKVGLWKEVYDRln 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 324 -PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:PRK14246 149 sPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNG 228
|
250
....*....|....*...
gi 148612853 401 RLDGYRGDFETFIKSKQE 418
Cdd:PRK14246 229 ELVEWGSSNEIFTSPKNE 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
181-360 |
8.30e-08 |
|
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: 53.27 E-value: 8.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAhisllhvEQEVAGDDTPALQsvlESDSV 260
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILA--GLSPPL-------AGRVLLNGGPLDF---QRDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 261 REDLLRrereltaqiaAGRAEGSEAAELAEiyAKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALAR 340
Cdd:cd03231 72 ARGLLY----------LGHAPGIKTTLSVL--ENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALAR 138
|
170 180
....*....|....*....|
gi 148612853 341 ALFARPDLLLLDEPTNMLDV 360
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDK 158
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
494-665 |
8.37e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 494 LDEVDFYYDPKhVIFSRL-----SVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYfSQHHVEQ 567
Cdd:PRK13634 5 FQKVEHRYQYK-TPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtVTIGERVITAGK-KNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 568 LDLNVSAVellaRKFP--------------------GRPEEE----YRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQ 623
Cdd:PRK13634 83 LRKKVGIV----FQFPehqlfeetvekdicfgpmnfGVSEEDakqkAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148612853 624 MTMPCPNFYILDEPTNHLD-------METIEALGRalnnfRGG--VILVSH 665
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHK-----EKGltTVLVTH 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
600-706 |
8.58e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 600 SGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGVILVSHDERFIRLVCRELWV 679
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
90 100
....*....|....*....|....*..
gi 148612853 680 CEGGGVTRVEGGFDQYRALLQEQFRRE 706
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQ 440
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
179-385 |
9.52e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRslRVPAHISLLHVEQEVAGDDTPALQsvlesd 258
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH--QPPSEGEILLDAQPLESWSSKAFA------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 259 svredllRRERELTAQIAAgrAEGSEAAELAEI-----YAKLEEI-EADKAPARASVILAGLgfTPkMQQQPTREFSGGW 332
Cdd:PRK10575 85 -------RKVAYLPQQLPA--AEGMTVRELVAIgrypwHGALGRFgAADREKVEEAISLVGL--KP-LAHRLVDSLSGGE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 333 RMRLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHDIN 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
488-683 |
9.74e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 54.43 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI----------RHAHRNLKI 557
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVV-DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSislcgepvpsRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQhhVEQLDLNVSAVELL---ARKFpGRPEEEYRHQ---LGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:PRK13537 83 GVVPQ--FDNLDPDFTVRENLlvfGRYF-GLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 632 YILDEPTNHLDMETIEALGRALNNF--RGGVILVSHD--ERFIRLvCRELWVCEGG 683
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLTTHfmEEAERL-CDRLCVIEEG 214
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
197-359 |
1.14e-07 |
|
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: 53.26 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 197 DVNL--AWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVAGDDTPAL---------QSVLESDSVREDLL 265
Cdd:cd03252 20 NISLriKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLALADPAWLrrqvgvvlqENVLFNRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 266 rrerelTAQIAAGRAEGSEAAELAEIYAKLEEIeadkaPARASVILAGLGFTpkmqqqptreFSGGWRMRLALARALFAR 345
Cdd:cd03252 98 ------LADPGMSMERVIEAAKLAGAHDFISEL-----PEGYDTIVGEQGAG----------LSGGQRQRIAIARALIHN 156
|
170
....*....|....
gi 148612853 346 PDLLLLDEPTNMLD 359
Cdd:cd03252 157 PRILIFDEATSALD 170
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
519-702 |
1.35e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.85 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 519 SRICVVGENGAGKSTMLKLLLGDLaPVRGirhahrNLKIGyfsqhHVE--QLDL-----------------------NVs 573
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQG------SLKIN-----GIElrELDPeswrkhlswvgqnpqlphgtlrdNV- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 aveLLARkfPGRPEEEYRHQLGRYGISGELAMRPL----------ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 643
Cdd:PRK11174 444 ---LLGN--PDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 644 ETIEALGRALNNFRGG--VILVSHDERFIRlVCRELWVCEGGGVtrVEGGfdQYRALLQEQ 702
Cdd:PRK11174 519 HSEQLVMQALNAASRRqtTLMVTHQLEDLA-QWDQIWVMQDGQI--VQQG--DYAELSQAG 574
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-666 |
1.44e-07 |
|
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: 52.85 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL------KIGYFSQHHV-------EQLDLNVSAVellarkFPGRP 586
Cdd:TIGR01184 14 ISLIGHSGCGKSTLLNLISGLAQPTSGgVILEGKQItepgpdRMVVFQNYSLlpwltvrENIALAVDRV------LPDLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEYR----HQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----NNFRG 658
Cdd:TIGR01184 88 KSERRaiveEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRV 166
|
....*...
gi 148612853 659 GVILVSHD 666
Cdd:TIGR01184 167 TVLMVTHD 174
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
327-360 |
1.48e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 53.97 E-value: 1.48e-07
10 20 30
....*....|....*....|....*....|....
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
327-691 |
1.49e-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: 54.69 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTwpST---ILVVSHDRNFLNAIATDIIHLHsq 400
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDLLKDLQR--ELgmaLLLITHDLGVVRRFADRVAVMR-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 401 rlDGY---RGDFETFIKSkqerllnqqreyeAQQQYRQHiqvfidrfrynanrasqvqsklkMLEKLPELKPVDKESEvv 477
Cdd:COG4172 232 --QGEiveQGPTAELFAA-------------PQHPYTRK-----------------------LLAAEPRGDPRPVPPD-- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 478 mkfpdgfekfSPPILQLDEVDFYYDPKHVIFSRL--------SVSADL---ESrICVVGENGAGKSTMLKLLLGdLAPVR 546
Cdd:COG4172 272 ----------APPLLEARDLKVWFPIKRGLFRRTvghvkavdGVSLTLrrgET-LGLVGESGSGKSTLGLALLR-LIPSE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 547 G----------------IRHAHRNLKI------GYFS-QHHVEQLdlnVSavELLARKFPGRPEEEYRHQ----LGRYGI 599
Cdd:COG4172 340 GeirfdgqdldglsrraLRPLRRRMQVvfqdpfGSLSpRMTVGQI---IA--EGLRVHGPGLSAAERRARvaeaLEEVGL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 600 SGELAMRPLASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHDERFIRLV 673
Cdd:COG4172 415 DPAARHRYPHEFSGGQRQRIAIARaLILE-PKLLVLDEPTSALDV-SVQAqildLLRDLQREHGlAYLFISHDLAVVRAL 492
|
410
....*....|....*...
gi 148612853 674 CRELWVCEGGGVtrVEGG 691
Cdd:COG4172 493 AHRVMVMKDGKV--VEQG 508
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
178-404 |
1.52e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.57 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSF-GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhveqevAGDDTPALQSvle 256
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-------SGHDITRLKN--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 257 sdsvRE-DLLRRERELTAQ----IAAGRAEGSEAAELAEIYAKLEEIEAdkapaRASVILAGLGFTPKMQQQPTrEFSGG 331
Cdd:PRK10908 72 ----REvPFLRRQIGMIFQdhhlLMDRTVYDNVAIPLIIAGASGDDIRR-----RVSAALDKVGLLDKAKNFPI-QLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 332 WRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDG 404
Cdd:PRK10908 142 EQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
203-421 |
1.53e-07 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 55.02 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLATRSlrvpahisllhveQEVAGDDTPALQSVLESDSVREDLLRRERELTA--QIAAGRa 280
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDT-------------TVTSGDATVAGKSILTNISDVHQNMGYCPQFDAidDLLTGR- 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 281 egseaaELAEIYAKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:TIGR01257 2031 ------EHLYLYARLRGVPAEEIEKVANWSIQSLGLS-LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 361 RAILWLENYLQTW---PSTILVVSHDRNFLNAIAT--------------DIIHLHSQRLDGYRGDFEtfIKSKQERLL 421
Cdd:TIGR01257 2104 QARRMLWNTIVSIireGRAVVLTSHSMEECEALCTrlaimvkgafqclgTIQHLKSKFGDGYIVTMK--IKSPKDDLL 2179
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
521-678 |
1.60e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.86 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLG----DLAPVRGI-----------RHAHRNLKIGYFSQHHVEQLDLN-VSAVELLARkFPG 584
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGlddgSSGEVSLVgqplhqmdeeaRAKLRAKHVGFVFQSFMLIPTLNaLENVELPAL-LRG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 585 RPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALN-NF 656
Cdd:PRK10584 118 ESSRQSRNGakalLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNrEH 196
|
170 180
....*....|....*....|....*....
gi 148612853 657 RGGVILVSHDE-------RFIRLVCRELW 678
Cdd:PRK10584 197 GTTLILVTHDLqlaarcdRRLRLVNGQLQ 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
328-397 |
1.61e-07 |
|
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: 52.14 E-value: 1.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHV 177
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
523-666 |
1.64e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.01 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDL----------APVRGIRHAHRNLKIGYFSQH-------HVEQ-LDLNVSAvellarkfpG 584
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLpgsgsiqfagQPLEAWSAAELARHRAYLSQQqtppfamPVFQyLTLHQPD---------K 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 585 RPEEEYRHQL----GRYGISGELAmRPLASLSGGQKSRVAFAQMTM-------PCPNFYILDEPTNHLDMETIEALGRAL 653
Cdd:PRK03695 98 TRTEAVASALnevaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDRLL 176
|
170
....*....|....*.
gi 148612853 654 NNF--RGGVILVS-HD 666
Cdd:PRK03695 177 SELcqQGIAVVMSsHD 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
522-674 |
1.97e-07 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 54.25 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAP-------------VRGIRHAHRnLKIGYFSQHhveqLDL--NVSAVE--LLARkFPG 584
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPdsgeilldgepvrFRSPRDAQA-AGIAIIHQE----LNLvpNLSVAEniFLGR-EPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 585 RP--------EEEYRHQLGRYGISGELAmRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF 656
Cdd:COG1129 108 RGglidwramRRRARELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL 186
|
170 180
....*....|....*....|...
gi 148612853 657 RG---GVILVSH--DErfIRLVC 674
Cdd:COG1129 187 KAqgvAIIYISHrlDE--VFEIA 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
523-667 |
2.12e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.10 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAP---VRG-IRHAHRNL--------KIGYFSQ------HhveqldLNVsaVELLARKFPG 584
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPafsASGeVLLNGRRLtalpaeqrRIGILFQddllfpH------LSV--GENLAFALPP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 585 RPEEEYRHQ-----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETiealgRAlnNFR-- 657
Cdd:COG4136 104 TIGRAQRRArveqaLEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL-----RA--QFRef 175
|
170
....*....|....*....
gi 148612853 658 ---------GGVILVSHDE 667
Cdd:COG4136 176 vfeqirqrgIPALLVTHDE 194
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
523-666 |
2.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 52.81 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG----------------IRHahrnlKIGYFSQHHVEQLdlnVSA-VEL-----LAR 580
Cdd:PRK13650 38 IIGHNGSGKSTTVRLIDGLLEAESGqiiidgdllteenvwdIRH-----KIGMVFQNPDNQF---VGAtVEDdvafgLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 581 KfpGRPEEEYR----HQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGRA 652
Cdd:PRK13650 110 K--GIPHEEMKervnEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGI 186
|
170
....*....|....
gi 148612853 653 LNNFRGGVILVSHD 666
Cdd:PRK13650 187 RDDYQMTVISITHD 200
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
489-638 |
2.32e-07 |
|
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: 52.29 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 489 PPILQLDEVDFYYDPKHVIFSrlsVSADLE--SRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLK--------- 556
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHG---VSLEVEegEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRFDGEDITglpphriar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 --IGY-------FSQHHVEQ-LDLnVSAVELLARKFPGRPEE---------EYRHQLGrygisgelamrplASLSGGQKS 617
Cdd:COG0410 78 lgIGYvpegrriFPSLTVEEnLLL-GAYARRDRAEVRADLERvyelfprlkERRRQRA-------------GTLSGGEQQ 143
|
170 180
....*....|....*....|.
gi 148612853 618 RVAFAQMTMPCPNFYILDEPT 638
Cdd:COG0410 144 MLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
188-370 |
2.50e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 51.73 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAhisllhvEQEVAGDDTPALQsvlesdsVREDLLRR 267
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA--GLARPD-------AGEVLWQGEPIRR-------QRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 268 ----------ERELTA----QIAAGRAEGSEAAELAEIYAKleeieadkaparasVILAGlgftpkMQQQPTREFSGGWR 333
Cdd:PRK13538 76 llylghqpgiKTELTAlenlRFYQRLHGPGDDEALWEALAQ--------------VGLAG------FEDVPVRQLSAGQQ 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 334 MRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL 370
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
179-359 |
2.59e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 52.56 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSF--GDRVLLAGADVNLAWGRRYGLV--GRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtpALQSV 254
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVValGASGCGKTTLLNLIA--GFLAPSSGEITLDGVPVTGPG--ADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESD-------SVREDLlrrerELTAQIAA-GRAEGSEAAElaeiyAKLeeieadkaparASVILAGLGftpkmqQQPTR 326
Cdd:COG4525 81 VFQKdallpwlNVLDNV-----AFGLRLRGvPKAERRARAE-----ELL-----------ALVGLADFA------RRRIW 133
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4525 134 QLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
505-666 |
2.70e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 52.52 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 505 HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDL--------APVRG--------------IRHAHRNlkiGYFSQ 562
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGdvtlngeplaaidaPRLARLR---AVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 HHVEQLDLNVSAVELLARKFPGRPEEEYRHQ--------LGRYGISGeLAMRPLASLSGGQKSRVAFAQM---------T 625
Cdd:PRK13547 91 AAQPAFAFSAREIVLLGRYPHARRAGALTHRdgeiawqaLALAGATA-LVGRDVTTLSGGELARVQFARVlaqlwpphdA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 626 MPCPNFYILDEPTNHLD-------METIEALGRalnNFRGGVILVSHD 666
Cdd:PRK13547 170 AQPPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
482-683 |
2.92e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 2.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 482 DGFEKFSPPILQLDEVDF--YYDPKHVIfsrlsvsadlesricvVGENGAGKSTMLKLLLGDLAPVRGI---------RH 550
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLtvYPGEIHAL----------------LGENGAGKSTLMKVLSGIHEPTKGTitinninynKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHR---NLKIGYFSQHH--VEQLDL--NVSAVELLARKFPGRPEEEYRHQ-------LGRYGISGELAMRpLASLSGGQK 616
Cdd:PRK09700 73 DHKlaaQLGIGIIYQELsvIDELTVleNLYIGRHLTKKVCGVNIIDWREMrvraammLLRVGLKVDLDEK-VANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 617 SRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHDERFIRLVCRELWVCEGG 683
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
326-397 |
2.98e-07 |
|
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: 50.62 E-value: 2.98e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHdRNFLNAIATDIIHL 397
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDL 160
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
521-666 |
3.08e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrNLKIGYFSQHHV-EQLDLNVSAVELLARK---------FPGRPEEEY 590
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPLAEArEDTRLMFQDARLLPWKkvidnvglgLKGQWRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 591 RHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-------IEALGRAlNNFRggVILV 663
Cdd:PRK11247 115 LQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemqdlIESLWQQ-HGFT--VLLV 190
|
...
gi 148612853 664 SHD 666
Cdd:PRK11247 191 THD 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
523-702 |
3.67e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 52.91 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRnlKIGYFSQhhVEQLDLNVSAVELL---ARKF--PGR 585
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGkitvlgvpvparARLARA--RIGVVPQ--FDNLDLEFTVRENLlvfGRYFgmSTR 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 PEEEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF--RGGVILV 663
Cdd:PRK13536 148 EIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 664 SHD--ERFIRLvCRELWVCEgGGVTRVEGGFDqyrALLQEQ 702
Cdd:PRK13536 228 TTHfmEEAERL-CDRLCVLE-AGRKIAEGRPH---ALIDEH 263
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
524-666 |
3.68e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLGDLAP------VRGI---RHAHRNLK-IGY-FSQHhvEQLDLNVSAVE--LLARKFPGRPEEEY 590
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPtsgevrVLGYvpfKRRKEFARrIGVvFGQR--SQLWWDLPAIDsfRLLKAIYRIPDAEY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 591 RHQLGRY----GIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRALNNFRGG-VIL 662
Cdd:COG4586 132 KKRLDELvellDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvskEAIREFLKEYNRERGTtILL 210
|
....
gi 148612853 663 VSHD 666
Cdd:COG4586 211 TSHD 214
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
492-682 |
4.30e-07 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 51.40 E-value: 4.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYdpKHVIFsRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLKIGYFSQ 562
Cdd:TIGR01277 1 LALDKVRYEY--EHLPM-EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsikvndqshTGLAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 HHVEQLDLNVSAVELLARKfPGRP----EEEYRHQLGR-YGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLH-PGLKlnaeQQEKVVDAAQqVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 638 TNHLD----METIEALGRALNNFRGGVILVSHD-ERFIRLVCRELWVCEG 682
Cdd:TIGR01277 156 FSALDpllrEEMLALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQG 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
492-667 |
4.31e-07 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 51.10 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-----------IRHAHRNlkIGYF 560
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrdvtdLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQHHVEQLDLNVS---AVELLARKFPGRPEEEYRHQLGR-YGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03301 78 FQNYALYPHMTVYdniAFGLKLRKVPKDEIDERVREVAElLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 148612853 637 PTNHLD----METIEALGRALNNFRGGVILVSHDE 667
Cdd:cd03301 157 PLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQ 191
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
491-677 |
4.31e-07 |
|
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: 53.86 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEV-DFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG------------IRHAHRNLki 557
Cdd:TIGR01257 1937 ILRLNELtKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksiltnISDVHQNM-- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHH-VEQLDLNVSAVELLARkFPGRPEEEYRhQLGRYGISG----ELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR01257 2015 GYCPQFDaIDDLLTGREHLYLYAR-LRGVPAEEIE-KVANWSIQSlglsLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 633 ILDEPTNHLDMETIEALGRALNN-FRGG--VILVSHDERFIRLVCREL 677
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSiIREGraVVLTSHSMEECEALCTRL 2140
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
184-382 |
4.88e-07 |
|
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: 50.39 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 184 DVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLESds 259
Cdd:cd03247 5 NVSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT--------------------GDLKPQQGEITLD-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 vredllrrereltaqiaagraeGSEAAELAEIYAKLEEIEADKAPARASVILAGLGftpkmqqqptREFSGGWRMRLALA 339
Cdd:cd03247 63 ----------------------GVPVSDLEKALSSLISVLNQRPYLFDTTLRNNLG----------RRFSGGERQRLALA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 340 RALFARPDLLLLDEPTNMLDVRAILWLENYL--QTWPSTILVVSH 382
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIfeVLKDKTLIWITH 155
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
484-670 |
5.61e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.03 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 484 FEKFSPPIL----QLDEVDFYYDPKHVIFsrlsvsadlesricVVGENGAGKSTMLKLLLGDLAPVRG---------IRH 550
Cdd:PRK10908 4 FEHVSKAYLggrqALQGVTFHMRPGEMAF--------------LTGHSGAGKSTLLKLICGIERPSAGkiwfsghdiTRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHRNL-----KIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGELAMRPLaSLSGGQKSRVAF 621
Cdd:PRK10908 70 KNREVpflrrQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRvsaaLDKVGLLDKAKNFPI-QLSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 622 AQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF-RGG--VILVSHDERFI 670
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnRVGvtVLMATHDIGLI 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-669 |
6.54e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 6.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 525 GENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK--------IGYFSQHHVEQLDLnvsAVELLARKFPGRP---- 586
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPdagsilIDGQEMRFASTTaalaagvaIIYQELHLVPEMTV---AENLYLGQLPHKGgivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 ----EEEYRHQLGRYGISGELAMrPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR--GGV 660
Cdd:PRK11288 114 rrllNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaeGRV 192
|
170
....*....|..
gi 148612853 661 IL-VSH--DERF 669
Cdd:PRK11288 193 ILyVSHrmEEIF 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
180-364 |
8.25e-07 |
|
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: 50.69 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRV--PAHISLLHVEQEVAGDDTPALQ-- 252
Cdd:cd03253 1 IEFENVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL----FRFydVSSGSILIDGQDIREVTLDSLRra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 -------SVLESDSVREDllrrereltaqIAAGRAEGS-----EAAELAEIYAKLEEIEAdkaparasvilaglGFTPKM 320
Cdd:cd03253 77 igvvpqdTVLFNDTIGYN-----------IRYGRPDATdeeviEAAKAAQIHDKIMRFPD--------------GYDTIV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 321 QQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 364
Cdd:cd03253 132 GERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALDThteREIQ 177
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
488-666 |
8.60e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 51.64 E-value: 8.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIfsrLSVSADLESR--ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------K 556
Cdd:COG3842 2 AMPALELENVSKRYGDVTAL---DDVSLSIEPGefVALLGPSGCGKTTLLRMIAGFETPDSGrILLDGRDVtglppekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQH-----H--VEQldlNVsAVELLARKFPgRPEEEYR--HQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMP 627
Cdd:COG3842 79 VGMVFQDyalfpHltVAE---NV-AFGLRMRGVP-KAEIRARvaELLELVGLEGLADRYP-HQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 148612853 628 CPNFYILDEPTNHLD----METIEALGRALNNFRGGVILVSHD 666
Cdd:COG3842 153 EPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
497-686 |
9.26e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 9.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 497 VDFYYDPKHviFSRLSVSADLESRIC------VVGENGAGKSTMLK------------LLLGDL------APVRGIRhah 552
Cdd:PRK09493 2 IEFKNVSKH--FGPTQVLHNIDLNIDqgevvvIIGPSGSGKSTLLRcinkleeitsgdLIVDGLkvndpkVDERLIR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 553 rnLKIGY-FSQHHveqLDLNVSAVELLA---RKFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQM 624
Cdd:PRK09493 77 --QEAGMvFQQFY---LFPHLTALENVMfgpLRVRGASKEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 625 TMPCPNFYILDEPTNHLDMETI-EALG--RALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
491-685 |
9.87e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 50.94 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYdPKHVIFSRLSVSADLeSRIC-VVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIG 558
Cdd:PRK10575 11 TFALRNVSFRV-PGRTLLHPLSLTFPA-GKVTgLIGHNGSGKSTLLKMLgrhqppsegeiLLDAQPLESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 559 YFSQHHVEQLDLNVSavELLA-RKFPgrpeeeYRHQLGRYGISGE---------LAMRPLA-----SLSGGQKSRVAFAQ 623
Cdd:PRK10575 89 YLPQQLPAAEGMTVR--ELVAiGRYP------WHGALGRFGAADRekveeaislVGLKPLAhrlvdSLSGGERQRAWIAM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 624 MTMPCPNFYILDEPTNHLDME---TIEALGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDIAhqvDVLALVHRLSQERGlTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
168-437 |
1.00e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 168 ESSGKNKSYDVRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMLaTRSlRVPAHISLLHVEQEVAG 245
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLqiKAGEKVALLGRTGCGKSTLLQLL-TRA-WDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 246 DDTPAL--------QSV-LESDSVREDLLrrereltaqIAAGRAEGseaAELAEIYAK--LEEIEADKAPARAsvILAGL 314
Cdd:PRK11160 407 YSEAALrqaisvvsQRVhLFSATLRDNLL---------LAAPNASD---EALIEVLQQvgLEKLLEDDKGLNA--WLGEG 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 315 GftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWL-----ENylqtwpSTILVVSHdRnf 386
Cdd:PRK11160 473 G----------RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeteRQILELlaehaQN------KTVLMITH-R-- 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 387 LNAIAT-DIIHLhsqrLDGYR----GDFETfikskqerLLNQQREYeaqQQYRQHI 437
Cdd:PRK11160 534 LTGLEQfDRICV----MDNGQiieqGTHQE--------LLAQQGRY---YQLKQRL 574
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
179-359 |
1.04e-06 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 50.17 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpAHISLLHVEQEVAGDDT-----PALQ- 252
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG------TLSPAFSASGEVLLNGRrltalPAEQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 253 --SVLESD-------SVREDLLRrerELTAQIaaGRAEGSEAAELAeiyakLEEIEadkaparasviLAGLGF-TPKmqq 322
Cdd:COG4136 77 riGILFQDdllfphlSVGENLAF---ALPPTI--GRAQRRARVEQA-----LEEAG-----------LAGFADrDPA--- 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 323 qptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4136 133 ----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
180-397 |
1.14e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtpALQSVLESDs 259
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIA--GFVPYQHGSITLDGKPVEGPG--AERGVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 vreDLLRRERELTAQIAAGraegseaAELAEIYAKLEEIEADKAPARasVILAGLGftpkmqQQPTREFSGGWRMRLALA 339
Cdd:PRK11248 79 ---EGLLPWRNVQDNVAFG-------LQLAGVEKMQRLEIAHQMLKK--VGLEGAE------KRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 340 RALFARPDLLLLDEPTNMLDV--RAILWlENYLQTWPST---ILVVSHDRNFLNAIATDIIHL 397
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAftREQMQ-TLLLKLWQETgkqVLLITHDIEEAVFMATELVLL 202
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
605-691 |
1.23e-06 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 49.39 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 605 MRPLASLSGGQKSRVA----FA-QMTMPCPnFYILDEPTNHLDMETIEALGRALNNFRGGV--ILVSHDERFIRlVCREL 677
Cdd:cd03278 108 VQRLSLLSGGEKALTAlallFAiFRVRPSP-FCVLDEVDAALDDANVERFARLLKEFSKETqfIVITHRKGTME-AADRL 185
|
90
....*....|....
gi 148612853 678 WvceggGVTRVEGG 691
Cdd:cd03278 186 Y-----GVTMQESG 194
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
492-665 |
1.32e-06 |
|
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: 49.92 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHV-IFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKIGY 559
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIprfydvdsgriLIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQ-----------------HHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISgelamrplasLSGGQKSRVAFA 622
Cdd:cd03251 81 VSQdvflfndtvaeniaygrPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVK----------LSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 148612853 623 QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSH 665
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAH 195
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
513-667 |
1.32e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.24 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLES--RICVVGENGAGKSTMLKLLLG--------------DLAPVrgirHAhRNLKIGYFSQH-----HVEQLDlN 571
Cdd:PRK10851 21 ISLDIPSgqMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRL----HA-RDRKVGFVFQHyalfrHMTVFD-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 572 VS-AVELLARKfpGRPEEEYRH----------QLGRygisgeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 640
Cdd:PRK10851 95 IAfGLTVLPRR--ERPNAAAIKakvtqllemvQLAH------LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190
....*....|....*....|....*....|.
gi 148612853 641 LDMETIEALGRALNN----FRGGVILVSHDE 667
Cdd:PRK10851 167 LDAQVRKELRRWLRQlheeLKFTSVFVTHDQ 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
513-667 |
1.47e-06 |
|
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: 50.03 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRG---------IRHAHRNLKIGYFSQH-----HVEQLDlNVsAVE 576
Cdd:cd03296 21 VSLDIPSgeLVALLGPSGSGKTTLLRLIAGLERPDSGtilfggedaTDVPVQERNVGFVFQHyalfrHMTVFD-NV-AFG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 577 LLARKFPGRP-EEEYRHQ----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGR 651
Cdd:cd03296 99 LRVKPRSERPpEAEIRAKvhelLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRR 177
|
170 180
....*....|....*....|
gi 148612853 652 ALNNFRGGV----ILVSHDE 667
Cdd:cd03296 178 WLRRLHDELhvttVFVTHDQ 197
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
525-667 |
1.48e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 525 GENGAGKSTMLKLLLGDLAPVRGirhahrnlKIGYFSQHHVEQLDLNVSAVELLARKFPGRPEEEYRHQL--------GR 596
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKG--------EILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENClydihfspGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 597 YGIS--------GELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR---GGVILVSH 665
Cdd:PRK13540 106 VGITelcrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSH 185
|
..
gi 148612853 666 DE 667
Cdd:PRK13540 186 QD 187
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
178-385 |
1.54e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.21 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------TRSLRVPAHISLlhVEQEVAGDDTP 249
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaPRGARVTGDVTL--NGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 250 AL---QSVLESDSVRE-DLLRRERELTAQIAAGRAEGSEAAELAEIyakleeieADKAPARA-SVILAGLGFTpkmqqqp 324
Cdd:PRK13547 80 RLarlRAVLPQAAQPAfAFSAREIVLLGRYPHARRAGALTHRDGEI--------AWQALALAgATALVGRDVT------- 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148612853 325 trEFSGGWRMRLALARAL---------FARPDLLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK13547 145 --TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPN 216
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
178-354 |
1.66e-06 |
|
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: 49.85 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVP--------------------AHISLL 237
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIV--GLVKPdsgkilldgqditklpmhkrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 238 HVEQEvagddtpalQSVLESDSVREDLLrrereltaqiaagraegseaaELAEIYAKLEEIEADKAPArasvILAGLGFT 317
Cdd:cd03218 79 YLPQE---------ASIFRKLTVEENIL---------------------AVLEIRGLSKKEREEKLEE----LLEEFHIT 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 318 pKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 354
Cdd:cd03218 125 -HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
523-645 |
1.77e-06 |
|
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: 49.68 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLK--IGYFSQHhvEQLDLNVSA---VELLARKF--PGRPE 587
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRrrIGIVFQD--LSVDDELTGwenLYIHARLYgvPGAER 108
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 588 EEYRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 645
Cdd:cd03265 109 RERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
208-361 |
1.80e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.01 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 208 LVGRNGLGKTTLLKMLatrslrvpahISLLHVEQ---EVAGddtpalqSVLESDSVREdlLRRERELTAQIAAGRAEGSE 284
Cdd:PRK13635 38 IVGHNGSGKSTLAKLL----------NGLLLPEAgtiTVGG-------MVLSEETVWD--VRRQVGMVFQNPDNQFVGAT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 285 AAElaEIYAKLEE--IEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK13635 99 VQD--DVAFGLENigVPREEMVERVDQALRQVGMEDFLNREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
490-666 |
1.86e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 50.13 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYYDPKHVI-FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlKIgYFSQHHVEQL 568
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EI-FYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 569 DLNvsavELlaRKFPG----RPEEEYRHQLGRYGIS---------------------GELAMRPLA-----SLSGGQKSR 618
Cdd:PRK13648 77 NFE----KL--RKHIGivfqNPDNQFVGSIVKYDVAfglenhavpydemhrrvsealKQVDMLERAdyepnALSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 619 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSHD 666
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhnitIISITHD 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
511-686 |
1.89e-06 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 50.50 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 511 LSVSADLES--RICVVGENGAGKSTMLKLLLGDLAPVRGIRH----------------AHRNlKIGYFSQHhveqldlnv 572
Cdd:TIGR02142 14 LDADFTLPGqgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgiflpPEKR-RIGYVFQE--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 savellARKFPgrpEEEYRHQLgRYGIS--------------------GELAMRPLASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR02142 84 ------ARLFP---HLSVRGNL-RYGMKrarpserrisferviellgiGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 633 ILDEPTNHLDM----ETIEALGRALNNFRGGVILVSHDERFIRLVCRELWVCEGGGVT 686
Cdd:TIGR02142 154 LMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
317-421 |
1.91e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 317 TPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATD 393
Cdd:PRK10762 386 TPSMEQ-AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkkeIYQLINQFKAEGLSIILVSSEMPEVLGMSDR 464
|
90 100
....*....|....*....|....*...
gi 148612853 394 IIHLHSQRLdgyRGDFETfIKSKQERLL 421
Cdd:PRK10762 465 ILVMHEGRI---SGEFTR-EQATQEKLM 488
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
491-665 |
1.98e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLlGDLAPVR-GIRHAHRNLKIGYFSQHHV---- 565
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYgGRLTKPAKGKLFYVPQRPYmtlg 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 566 ---EQLDLNVSAVELLARKFPGRPEEEY------RHQLGRYGisGELAMRPLAS-LSGGQKSRVAFAQMTMPCPNFYILD 635
Cdd:TIGR00954 530 tlrDQIIYPDSSEDMKRRGLSDKDLEQIldnvqlTHILEREG--GWSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|
gi 148612853 636 EPTNHLDMETIEALGRALNNFRGGVILVSH 665
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
178-364 |
2.19e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 50.97 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENfdVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAH 233
Cdd:COG5265 358 VRFEN--VSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtsgrilidgqdirdvTQASLR--AA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 234 ISLlhVEQevagdDTpalqsVLESDSVREDllrrereltaqIAAGRAEGSEaaelaeiyaklEEIEAdkaPARASVILAG 313
Cdd:COG5265 434 IGI--VPQ-----DT-----VLFNDTIAYN-----------IAYGRPDASE-----------EEVEA---AARAAQIHDF 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 314 LGFTPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 364
Cdd:COG5265 477 IESLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSrteRAIQ 534
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-665 |
2.39e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAP------VRG----IRHAH--RNLKIGYFSQHH--VEQLdlnvSAVE--LLA---RKF 582
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPdsgeilIDGkpvrIRSPRdaIALGIGMVHQHFmlVPNL----TVAEniVLGlepTKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 583 PGRPEEEYRHQL----GRYGISGELAmRPLASLSGGQKSRV----AFAQmtmpCPNFYILDEPTNHLDMETIEALGRALN 654
Cdd:COG3845 111 GRLDRKAARARIrelsERYGLDVDPD-AKVEDLSVGEQQRVeilkALYR----GARILILDEPTAVLTPQEADELFEILR 185
|
170
....*....|....
gi 148612853 655 NFRG---GVILVSH 665
Cdd:COG3845 186 RLAAegkSIIFITH 199
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
521-682 |
2.54e-06 |
|
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: 48.34 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRGirhahrnlkigyfsqhhVEQLDLNVSAVellarkfpgRPEEeyrhqlgrygis 600
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGD-----------------NDEWDGITPVY---------KPQY------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 601 gelamrplASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHDERFIRLVCRE 676
Cdd:cd03222 70 --------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDR 141
|
....*.
gi 148612853 677 LWVCEG 682
Cdd:cd03222 142 IHVFEG 147
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
169-361 |
2.73e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 169 SSGKNKSYDVRieNFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLgkttllkmlATRSLRVPAHisllhveqeVAGDDT 248
Cdd:NF000106 7 SNGARNAVEVR--GLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAH---------V*GPDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 PALQSVLESDSVREDLLRRERELTAQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTReF 328
Cdd:NF000106 67 GRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK-Y 145
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
488-664 |
2.88e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 2.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 488 SPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRNLKIGY 559
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisilgqpTRQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 FSQHhvEQLDLN----VSAVELLAR----KFPGRPEEEYRH----QLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMP 627
Cdd:PRK15056 83 VPQS--EEVDWSfpvlVEDVVMMGRyghmGWLRRAKKRDRQivtaALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 628 CPNFYILDEPTNHLDMET---IEALGRALNNfRGGVILVS 664
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTearIISLLRELRD-EGKTMLVS 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
490-694 |
3.04e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 490 PILQLDEVDFYYDPK--HVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP-------VRG----------IRH 550
Cdd:PLN03232 613 PAISIKNGYFSWDSKtsKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetssvvIRGsvayvpqvswIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHRNLKIGYFSQHHVEQL--DLNVSAVELLARKFPGRPeeeyRHQLGRYGISgelamrplasLSGGQKSRVAFAQMTMPC 628
Cdd:PLN03232 693 ATVRENILFGSDFESERYwrAIDVTALQHDLDLLPGRD----LTEIGERGVN----------ISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 629 PNFYILDEPTNHLDMETIEALGRAL--NNFRGGV-ILVSHDERFIRLVCRELWVCEggGVTRVEGGFDQ 694
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCmkDELKGKTrVLVTNQLHFLPLMDRIILVSE--GMIKEEGTFAE 825
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
523-691 |
3.32e-06 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 49.80 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLG--------------DLA--PVRGIRHAHRnlKIGYFSQHhveqldLNvsaveLLARK----- 581
Cdd:PRK11153 36 VIGASGAGKSTLIRCINLlerptsgrvlvdgqDLTalSEKELRKARR--QIGMIFQH------FN-----LLSSRtvfdn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 582 --FP----GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEA 648
Cdd:PRK11153 103 vaLPlelaGTPKAEIKARvtelLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATtrsILE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148612853 649 LGRALNNFRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVEGG 691
Cdd:PRK11153 182 LLKDINRELGlTIVLITHEMDVVKRICDRVAVIDAGRL--VEQG 223
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
306-383 |
3.60e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 306 RASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILWLENylQTWPSTILV 379
Cdd:PRK10584 126 GAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdkIADLLFSLN--REHGTTLIL 202
|
....
gi 148612853 380 VSHD 383
Cdd:PRK10584 203 VTHD 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
493-703 |
3.67e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.34 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 493 QLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGI-----RHAhrnlk 556
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrvfdpqsgriLIDGTDIRTVtraslRRN----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 557 IGYFSQhhvEQLDLNVSAVELLARKFPGRPEEEYRHQLGRYGISGELAMRPLA----------SLSGGQKSRVAFAQMTM 626
Cdd:PRK13657 411 IAVVFQ---DAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 627 PCPNFYILDEPTNHLDMETIEALGRALNNFRGG--VILVSHDERFIRLVCRELwVCEGGGVtrVE-GGFDQ-------YR 696
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGrtTFIIAHRLSTVRNADRIL-VFDNGRV--VEsGSFDElvarggrFA 564
|
....*..
gi 148612853 697 ALLQEQF 703
Cdd:PRK13657 565 ALLRAQG 571
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
180-359 |
3.93e-06 |
|
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: 48.69 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAH 233
Cdd:cd03249 1 IEFKNVSFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptsgeilldgvdirdlNLRWLR--SQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 234 ISLlhVEQEvagddtPalqsVLESDSVREDllrrereltaqIAAGRAEgseaaelaeiyAKLEEIEADKAPARASVILAG 313
Cdd:cd03249 79 IGL--VSQE------P----VLFDGTIAEN-----------IRYGKPD-----------ATDEEVEEAAKKANIHDFIMS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 314 L--GFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03249 125 LpdGYDTLVGERGS-QLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
301-395 |
4.24e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPS-T 376
Cdd:PRK13646 119 DEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSkrqVMRLLKSLQTDENkT 198
|
90
....*....|....*....
gi 148612853 377 ILVVSHDRNFLNAIATDII 395
Cdd:PRK13646 199 IILVSHDMNEVARYADEVI 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
305-385 |
4.33e-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: 48.79 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 305 ARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-----ILWLENYLQtwpSTI 377
Cdd:cd03294 139 ERAAEALELVGLEGWEHKYP-DELSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRRemqdeLLRLQAELQ---KTI 214
|
....*...
gi 148612853 378 LVVSHDRN 385
Cdd:cd03294 215 VFITHDLD 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
491-669 |
4.38e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 48.95 E-value: 4.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIFSrlsVSADLES-RIC-VVGENGAGKSTMLKLLLGDLAP------VRG--IRHAHRNlKIGY- 559
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDD---VSFTVPKgEIFgLLGPNGAGKTTTIRIILGILAPdsgevlWDGepLDPEDRR-RIGYl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 560 ------FSQHHV-EQLdlnvsaVELLARKfpGRPEEEYRHQ----LGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPC 628
Cdd:COG4152 77 peerglYPKMKVgEQL------VYLARLK--GLSKAEAKRRadewLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 629 PNFYILDEPTNHLD---METIEALGRALNNfRG-GVILVSHD----ERF 669
Cdd:COG4152 148 PELLILDEPFSGLDpvnVELLKDVIRELAA-KGtTVIFSSHQmelvEEL 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
193-383 |
4.62e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHV-EQEVAGDDTPALQSVLESDSVREDLLRRERel 271
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHL--NALLLPDTGTIEWIfKDEKNKKKTKEKEKVLEKLVIQKTRFKKIK-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 272 taQIAAGRAEGSEAAELAEiYAKLEE-IEAD-------------KAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLA 337
Cdd:PRK13651 99 --KIKEIRRRVGVVFQFAE-YQLFEQtIEKDiifgpvsmgvskeEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 148612853 338 LARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
524-642 |
4.71e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLGDLAPVRG--------IRHAHRN-------LKIGYFSQHHVEQL--DLNVSAVELLARKFPGRP 586
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlITSTSKNkdikqirKKVGLVFQFPESQLfeETVLKDVAFGPQNFGVSQ 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 587 EEE---YRHQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK13649 119 EEAealAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
611-666 |
5.05e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.93 E-value: 5.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME-TIEALG--RALNNFRGGVILVSHD 666
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
491-665 |
5.19e-06 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 48.24 E-value: 5.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYD--PKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLL-----------LGDLAPVRGIRHAHRNLKI 557
Cdd:cd03248 11 IVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqggqvLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHV---EQLDLNVS--------------AVELLARKFPGRPEEEYRHQLGRYGisgelamrplASLSGGQKSRVA 620
Cdd:cd03248 91 SLVGQEPVlfaRSLQDNIAyglqscsfecvkeaAQKAHAHSFISELASGYDTEVGEKG----------SQLSGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 621 FAQMTMPCPNFYILDEPTNHLDMETIEALGRAL--NNFRGGVILVSH 665
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALydWPERRTVLVIAH 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
182-383 |
5.25e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 48.55 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 182 NFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHisllhveqEVAGDDTPALQSVLESDSVR 261
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY--------RYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 262 EdlLRRERELTAQIAAGRAEGSEAAELAEIYA-KLEEIEADKAPARASVILAGL--GFTPKMQQQPTReFSGGWRMRLAL 338
Cdd:PRK14271 98 E--FRRRVGMLFQRPNPFPMSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLwdAVKDRLSDSPFR-LSGGQQQLLCL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 339 ARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 383
Cdd:PRK14271 175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
180-383 |
5.66e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 5.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSF--GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpAHISLLHVEQEVAGDDTPALQsvles 257
Cdd:PRK11831 8 VDMRGVSFtrGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG-------GQIAPDHGEILFDGENIPAMS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 dsvREDLLRRERELTAQIAAGrAEGSEAAELAEIYAKLEEIEADKAPARASVILAGL---GFTPKMQQQPTrEFSGGWRM 334
Cdd:PRK11831 76 ---RSRLYTVRKRMSMLFQSG-ALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLeavGLRGAAKLMPS-ELSGGMAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 335 RLALARALFARPDLLLLDEP-------TNMLDVRAILWLENYLQTwpsTILVVSHD 383
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHD 203
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
521-673 |
6.12e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 48.21 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLL------------LGDLA-----PVRGIRHAHRNLK--IGYFSQH-----HVEQLDlNVSAVE 576
Cdd:PRK11264 32 VAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarSLSQQKGLIRQLRqhVGFVFQNfnlfpHRTVLE-NIIEGP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 577 LLARKFP-GRPEEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI-EALG--RA 652
Cdd:PRK11264 111 VIVKGEPkEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVgEVLNtiRQ 189
|
170 180
....*....|....*....|.
gi 148612853 653 LNNFRGGVILVSHDERFIRLV 673
Cdd:PRK11264 190 LAQEKRTMVIVTHEMSFARDV 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
521-700 |
6.32e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.94 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRGirHAHRNLKIGYFSQHHVEQLDlnvsavELLARKFPGRPEEE--YRHQLGRYG 598
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEG--HVHMKGSVAYVPQQAWIQND------SLRENILFGKALNEkyYQQVLEACA 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 599 ISGELAMRPLA----------SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM--------ETIEALGRALNNFRggv 660
Cdd:TIGR00957 739 LLPDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhvgkhifeHVIGPEGVLKNKTR--- 815
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148612853 661 ILVSHDERFIRLVcRELWVCEGGGVTrvEGGfdQYRALLQ 700
Cdd:TIGR00957 816 ILVTHGISYLPQV-DVIIVMSGGKIS--EMG--SYQELLQ 850
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
513-664 |
6.72e-06 |
|
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: 47.65 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 513 VSADLES--RICVVGENGAGKSTMLKLLLG---DLAPVRG-IRHAHRNLKIGYFSQH--HVEQLDLNVS----------- 573
Cdd:cd03234 26 VSLHVESgqVMAILGSSGSGKTTLLDAISGrveGGGTTSGqILFNGQPRKPDQFQKCvaYVRQDDILLPgltvretltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 574 AVELLARKFPgrpeEEYRHQLGRYGISGELAMRPLA-----SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 648
Cdd:cd03234 106 AILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170
....*....|....*...
gi 148612853 649 LGRALNNF--RGGVILVS 664
Cdd:cd03234 182 LVSTLSQLarRNRIVILT 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
178-383 |
7.10e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 48.16 E-value: 7.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSfGDRVLLAGADVNLAWGRRYGLVGRNGLGKTtlLKMLATRSLrVPAHISLLHveQEVAGDDTPALQSVLES 257
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGI-LPAGVRQTA--GRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 258 DSVrEDLLRRERELTAQIAAGRAEGSEAAelaeiyaKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLA 337
Cdd:PRK10418 79 RKI-ATIMQNPRSAFNPLHTMHTHARETC-------LALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 338 LARALFARPDLLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHD 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
327-666 |
9.40e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPST-ILVVSHDRNFLNAIATDIIHLHsQRL 402
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY-QGE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 403 DGYRGDFETFIKSkqerllnqqreyeAQQQYRQHIQVFIDRFryNANRASQVQSKLKMLEkLPELKPVDKESEVVMKFPd 482
Cdd:PRK10261 247 AVETGSVEQIFHA-------------PQHPYTRALLAAVPQL--GAMKGLDYPRRFPLIS-LEHPAKQEPPIEQDTVVD- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 483 gfekfSPPILQLDEVDFYYDPKHVIFSRLS--------VSADL--ESRICVVGENGAGKSTMLKLLLG------------ 540
Cdd:PRK10261 310 -----GEPILQVRNLVTRFPLRSGLLNRVTrevhavekVSFDLwpGETLSLVGESGSGKSTTGRALLRlvesqggeiifn 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 541 ----DLAPVRGIRHAHRNlkIGYFSQHHVEQLD----LNVSAVELLARKFPGRPEEEYRH---QLGRYGISGELAMRPLA 609
Cdd:PRK10261 385 gqriDTLSPGKLQALRRD--IQFIFQDPYASLDprqtVGDSIMEPLRVHGLLPGKAAAARvawLLERVGLLPEHAWRYPH 462
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 610 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGRALNNFRGGVILVSHD 666
Cdd:PRK10261 463 EFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
521-685 |
9.49e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.76 E-value: 9.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKIGYFSQHHVEQLDLN------VSAVEllARKFPGRP-EEEYRH 592
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGnVSWRGEPLAKLNRAQRKAFRRDIQmvfqdsISAVN--PRKTVREIiREPLRH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 593 --------QLGR-------YGISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGRAL 653
Cdd:PRK10419 119 llsldkaeRLARasemlraVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQ 198
|
170 180 190
....*....|....*....|....*....|..
gi 148612853 654 NNFRGGVILVSHDERFIRLVCRELWVCEGGGV 685
Cdd:PRK10419 199 QQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
329-382 |
1.08e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSH 382
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRELLpYLERLAREINIPILYVSH 187
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
523-669 |
1.13e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNlKIGYFS----QHHVEQ------LDL----------NVSAVELLARKF 582
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFS-HITRLSfeqlQKLVSDewqrnnTDMlspgeddtgrTTAEIIQDEVKD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 583 PGRPEEeYRHQLGrygISGELAmRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF-RGGVI 661
Cdd:PRK10938 113 PARCEQ-LAQQFG---ITALLD-RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLhQSGIT 187
|
....*...
gi 148612853 662 LVSHDERF 669
Cdd:PRK10938 188 LVLVLNRF 195
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
485-642 |
1.13e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 485 EKFSPPILQLDEVDFY-YDPKhVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGIRHAHRNL-------- 555
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFeLEPK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIayvpqqaw 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 556 --------KIGYFSQHHVEQLD--LNVSAVELLARKFPGRPEEEyrhqLGRYGISgelamrplasLSGGQKSRVAFAQMT 625
Cdd:PTZ00243 732 imnatvrgNILFFDEEDAARLAdaVRVSQLEADLAQLGGGLETE----IGEKGVN----------LSGGQKARVSLARAV 797
|
170
....*....|....*..
gi 148612853 626 MPCPNFYILDEPTNHLD 642
Cdd:PTZ00243 798 YANRDVYLLDDPLSALD 814
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
187-355 |
1.19e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 187 FGDRVllAGADVNLAWGRR--YGLVGRNGLGKTTLLKMLaTRSLrvPA---HISLLhvEQEVAGDDTPALQSV------- 254
Cdd:NF033858 276 FGDFT--AVDHVSFRIRRGeiFGFLGSNGCGKSTTMKML-TGLL--PAsegEAWLF--GQPVDAGDIATRRRVgymsqaf 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 -LESD-SVREDLlrrereltaqiaagraegseaaelaEIYAKLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGW 332
Cdd:NF033858 349 sLYGElTVRQNL-------------------------ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDS-LPLGI 402
|
170 180
....*....|....*....|...
gi 148612853 333 RMRLALARALFARPDLLLLDEPT 355
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPT 425
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
491-689 |
1.20e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 47.30 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVifsrL-SVSADLE--SRICVVGENGAGKSTMLKLL--L-----GDLApVRGIR--HAHRNL--- 555
Cdd:COG1126 1 MIEIENLHKSFGDLEV----LkGISLDVEkgEVVVIIGPSGSGKSTLLRCInlLeepdsGTIT-VDGEDltDSKKDInkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 556 --KIGYFSQH-----H--VEQldlNVsaveLLA-RKFPGRP----EEEYRHQLGRYGISGELAMRPlASLSGGQKSRVAF 621
Cdd:COG1126 76 rrKVGMVFQQfnlfpHltVLE---NV----TLApIKVKKMSkaeaEERAMELLERVGLADKADAYP-AQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 622 AQMTMPCPNFYILDEPTNHLD-------METIEALGRalnnfRG-GVILVSHDERFIRLVCRELWVCEGGGVtrVE 689
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDpelvgevLDVMRDLAK-----EGmTMVVVTHEMGFAREVADRVVFMDGGRI--VE 216
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
329-390 |
1.26e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.83 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 329 SGGWRM------RLALARALFARPDLLLLDEPTNMLD---VRAIL--WLENYLQTWPSTILVVSHDRNFLNAI 390
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenIEESLaeIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
491-666 |
1.38e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.40 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVI--FSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRGI------RHAHRNL-----KI 557
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKvkidgeLLTAENVwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 558 GYFSQHHVEQ-LDLNVSAVELLARKFPGRPEEEYRHQLGRYGISG---ELAMRPLASLSGGQKSRVAFAQMTMPCPNFYI 633
Cdd:PRK13642 84 GMVFQNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 148612853 634 LDEPTNHLD----METIEALGRALNNFRGGVILVSHD 666
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
173-395 |
1.44e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.88 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 173 NKSYDVRI--ENFDVSFGD--RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPahisllhveqevagddt 248
Cdd:COG2401 22 DLSERVAIvlEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 palqsVLESDSVREDLLRRERELTAQIAAgraegseaaeLAEIYAKLEEIEAdkaparasvilAGLGFTPKMQQQPtREF 328
Cdd:COG2401 85 -----VAGCVDVPDNQFGREASLIDAIGR----------KGDFKDAVELLNA-----------VGLSDAVLWLRRF-KEL 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR---------AILWLENYLqtwpsTILVVSHDRNFLNAIATDII 395
Cdd:COG2401 138 STGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvarnlQKLARRAGI-----TLVVATHHYDVIDDLQPDLL 208
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
522-651 |
1.49e-05 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 46.15 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGdlapVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKfpgrpeeeyRHQLGRYGISG 601
Cdd:cd03239 26 AIVGPNGSGKSNIVDAICF----VLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITFDK---------SYFLVLQGKVE 92
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 602 ELamrplasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGR 651
Cdd:cd03239 93 QI-------LSGGEKSLSALAlifalQEIKPSP-FYVLDEIDAALDPTNRRRVSD 139
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
327-404 |
1.62e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHDRNFLNAIATDIIHLHSQR- 401
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKc 223
|
....
gi 148612853 402 -LDG 404
Cdd:PRK13637 224 eLQG 227
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
301-359 |
2.06e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 46.53 E-value: 2.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG1126 111 AEAEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
521-665 |
2.19e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.00 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSA-VELLARKF 582
Cdd:PRK13633 39 LVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwdIRN-----KAGMVFQNPDNQI---VATiVEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 583 P---GRPEEEYRHQ----LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 648
Cdd:PRK13633 111 PenlGIPPEEIRERvdesLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIKE 189
|
170
....*....|....*..
gi 148612853 649 LGRalnNFRGGVILVSH 665
Cdd:PRK13633 190 LNK---KYGITIILITH 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
183-360 |
2.50e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 47.65 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 183 FDVSFgdrVLLAGADVnlawgrryGLVGRNGLGKTTLLKMLAtrslRV--PA--HISllhveqeVAGDD--TPALQSVLE 256
Cdd:PRK13657 352 EDVSF---EAKPGQTV--------AIVGPTGAGKSTLINLLQ----RVfdPQsgRIL-------IDGTDirTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 257 S-DSVREDLLRRERELTAQIAAGRAEGSEAaelaEIYakleeiEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMR 335
Cdd:PRK13657 410 NiAVVFQDAGLFNRSIEDNIRVGRPDATDE----EMR------AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
170 180
....*....|....*....|....*
gi 148612853 336 LALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDV 504
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
281-363 |
2.56e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.50 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 281 EGSEAAELAEIYAKLEEIEA------DKAPARASV---ILAGLGFTPK-------MQQQPTRE-------FSGGWRMRLA 337
Cdd:cd03215 35 VGNGQTELAEALFGLRPPASgeitldGKPVTRRSPrdaIRAGIAYVPEdrkreglVLDLSVAEnialsslLSGGNQQKVV 114
|
90 100
....*....|....*....|....*.
gi 148612853 338 LARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:cd03215 115 LARWLARDPRVLILDEPTRGVDVGAK 140
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
299-383 |
2.64e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.29 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 299 EADKApaRASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEP---------TNMLD-VRAIlwlen 368
Cdd:COG3840 104 AEQRA--QVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPILLLDEPfsaldpalrQEMLDlVDEL----- 175
|
90
....*....|....*
gi 148612853 369 yLQTWPSTILVVSHD 383
Cdd:COG3840 176 -CRERGLTVLMVTHD 189
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
195-360 |
3.02e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.62 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 195 GADVNLAWGRRYGLVGRNGLGKTTLLKmlatrslrvpAHISLLHV-EQEVA--GDDTPALQSVlESDSVREDLLRREREL 271
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFAR----------AIIGLVKAtDGEVAwlGKDLLGMKDD-EWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 272 TAQIAAGRAEGSEAAELAEIYAKleEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLL 351
Cdd:PRK15079 108 LASLNPRMTIGEIIAEPLRTYHP--KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIIC 185
|
....*....
gi 148612853 352 DEPTNMLDV 360
Cdd:PRK15079 186 DEPVSALDV 194
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
492-666 |
3.23e-05 |
|
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: 46.14 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL----------KIGYF 560
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGeIFIDGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 561 SQH-----H--VEQldlNVSAVEllarKFPGRPEEEYRHQ----LGRYGI-SGELAMRPLASLSGGQKSRVAFAQMTMPC 628
Cdd:cd03295 81 IQQiglfpHmtVEE---NIALVP----KLLKWPKEKIRERadelLALVGLdPAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 629 PNFYILDEPTNHLDMETIEALGRALNNF----RGGVILVSHD 666
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLqqelGKTIVFVTHD 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
521-665 |
3.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 46.19 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLK-------IGYFSQHHVEQL-------DLNVSAVELlar 580
Cdd:PRK13637 36 VGLIGHTGSGKSTLIQHLNGLLKPtsgkiiIDGVDITDKKVKlsdirkkVGLVFQYPEYQLfeetiekDIAFGPINL--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 581 kfpGRPEEEYRHQLGR----YGISGE-LAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 648
Cdd:PRK13637 113 ---GLSEEEIENRVKRamniVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKE 189
|
170
....*....|....*..
gi 148612853 649 LGRALNNfrgGVILVSH 665
Cdd:PRK13637 190 LHKEYNM---TIILVSH 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
609-671 |
3.78e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.33 E-value: 3.78e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 609 ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG----VILVSHDERFIR 671
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTIR 644
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
304-362 |
3.89e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 3.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 304 PARASVIL----AGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:PRK15439 376 PARENAVLeryrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
329-383 |
4.01e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.93 E-value: 4.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 383
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
293-383 |
4.12e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.56 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 293 AKLEEIEADKAPARASVIL--AGLgftpkMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRA-I 363
Cdd:PRK11000 103 AGAKKEEINQRVNQVAEVLqlAHL-----LDRKP-KALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeI 176
|
90 100
....*....|....*....|
gi 148612853 364 LWLENYLQtwpSTILVVSHD 383
Cdd:PRK11000 177 SRLHKRLG---RTMIYVTHD 193
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
179-354 |
4.56e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 45.41 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----------------TRslrVPAH------IS 235
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVglvkpdsgrifldgediTH---LPMHkrarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 236 LLhvEQEvagddtpalQSVLESDSVREDLL--RRERELTAqiaagraegseaaelAEIYAKLEEIeadkaparasviLAG 313
Cdd:COG1137 82 YL--PQE---------ASIFRKLTVEDNILavLELRKLSK---------------KEREERLEEL------------LEE 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 314 LGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 354
Cdd:COG1137 124 FGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
518-665 |
4.71e-05 |
|
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: 46.93 E-value: 4.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 518 ESRICV-VGENGAGKSTMLKLLLGDLAPVRGI-----RHAHRNL-----KIGYFSQHHVEQLDLNVSAVELLARKFPGRP 586
Cdd:TIGR01257 955 ENQITAfLGHNGAGKTTTLSILTGLLPPTSGTvlvggKDIETNLdavrqSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 587 EEEYRHQL-------GRYGISGELAMrplaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG 659
Cdd:TIGR01257 1035 WEEAQLEMeamledtGLHHKRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
....*...
gi 148612853 660 --VILVSH 665
Cdd:TIGR01257 1111 rtIIMSTH 1118
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
203-395 |
5.08e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 43.90 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqsvlesdsvredllrrereltaqiaagraeg 282
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA---------------------------------------------------------- 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 283 seaAELAEIYAKLEEIEADKAPARASVILAGLGFTPKMqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:smart00382 24 ---RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK-----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 363 ---------ILWLENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:smart00382 96 eallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
326-359 |
5.24e-05 |
|
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: 44.85 E-value: 5.24e-05
10 20 30
....*....|....*....|....*....|....
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03213 110 RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
177-382 |
5.49e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.55 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 177 DVRIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLaTRslrvpahisLLHVEQEvagddtpalQSV 254
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIpaGKTVALVGRSGSGKSTIANLL-TR---------FYDIDEG---------EIL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 255 LESDSVREDLLRRERE---LTAQ--------IAAGRAEGSEaaelaEIYAKlEEIEADKAPARAsvilagLGFTPKMQQ- 322
Cdd:PRK11176 402 LDGHDLRDYTLASLRNqvaLVSQnvhlfndtIANNIAYART-----EQYSR-EQIEEAARMAYA------MDFINKMDNg 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 323 ------QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTwPSTILVVSH 382
Cdd:PRK11176 470 ldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTeseRAIQAALDELQK-NRTSLVIAH 537
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-383 |
6.42e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.49 E-value: 6.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 320 MQQQPTRE---FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHD 383
Cdd:PRK13650 130 MQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
322-362 |
6.70e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 6.70e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 148612853 322 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
385-666 |
6.97e-05 |
|
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: 45.46 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 385 NFLNAIAtdiiHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFID---RFRYNANRASQVQSklkml 461
Cdd:pfam13304 14 NLLEALR----FLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEdgvRYRYGLDLEREDVE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 462 EKLPELKPVDKESEVVMKF-PDGFEKFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLG 540
Cdd:pfam13304 85 EKLSSKPTLLEKRLLLREDsEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 541 DLAPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELL--ARKFPGRPEEEYRHQLGRYGISGELAMRPLASLSGGQKSR 618
Cdd:pfam13304 165 DWAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLgeGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRL 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 619 VAFA---QMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGG---VILVSHD 666
Cdd:pfam13304 245 LALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHS 298
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
173-366 |
7.10e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.56 E-value: 7.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 173 NKSYDVrienfdvsfGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQ------EVA 244
Cdd:PRK11153 8 SKVFPQ---------GGRTIHALNNVSLhiPAGEIFGVIGASGAGKSTLIRC-----------INLL--ERptsgrvLVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 245 GDDTPALqsvlesdSVREdlLRRERE-----------LTAQIAAG------RAEGSEAAElaeIYAKLEEIeadkapara 307
Cdd:PRK11153 66 GQDLTAL-------SEKE--LRKARRqigmifqhfnlLSSRTVFDnvalplELAGTPKAE---IKARVTEL--------- 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 308 sviLAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL 366
Cdd:PRK11153 125 ---LELVGLSDKADRYPA-QLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILEL 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
174-382 |
7.37e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 44.83 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 174 KSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRvpahislLHVEQEVAGDDTPALQS 253
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRLLE-------LNEEARVEGEVRLFGRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESDsVREDLLRRERELTAQ---------IAAGRAEGSEAAELAEIYAKLEEI---EADKAPARASVilaglgfTPKMQ 321
Cdd:PRK14267 73 IYSPD-VDPIEVRREVGMVFQypnpfphltIYDNVAIGVKLNGLVKSKKELDERvewALKKAALWDEV-------KDRLN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 322 QQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:PRK14267 145 DYPS-NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-666 |
7.55e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 45.43 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 522 CVVGENGAGKSTMLKLLLGDLAP---VRG-IRHAHRNL-------------------------------KIGyfsqhhvE 566
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPpgiTSGeILFDGEDLlklsekelrkirgreiqmifqdpmtslnpvmTVG-------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 567 QLD------LNVS-------AVELLAR-KFPgRPEE---EYRHQLgrygisgelamrplaslSGGQKSRVAFAQMTMPCP 629
Cdd:COG0444 108 QIAeplrihGGLSkaearerAIELLERvGLP-DPERrldRYPHEL-----------------SGGMRQRVMIARALALEP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 630 NFYILDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHD 666
Cdd:COG0444 170 KLLIADEPTTALDV-TIQAqilnLLKDLQRELGlAILFITHD 210
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
178-359 |
8.91e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 45.32 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPALQ----S 253
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA--GFETPDSGRIMLDGQDIT--HVPAENrhvnT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 254 VLESD------SVREDllrrereltaqIAAG-RAEGSEAAELAEiyaKLEEieadkapARASVILAGLGftpkmQQQPTR 326
Cdd:PRK09452 91 VFQSYalfphmTVFEN-----------VAFGlRMQKTPAAEITP---RVME-------ALRMVQLEEFA-----QRKPHQ 144
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 327 eFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK09452 145 -LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
296-359 |
9.37e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 45.10 E-value: 9.37e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148612853 296 EEIEADKAPARASVILAGlgftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK11432 111 EERKQRVKEALELVDLAG------FEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
178-364 |
9.42e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 45.07 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSF--GDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQ------EVAGDD 247
Cdd:COG1135 2 IELENLSKTFptKGGPVTALDDVSLtiEKGEIFGIIGYSGAGKSTLIRC-----------INLL--ERptsgsvLVDGVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 248 TPALqsvlesdsvREDLLRRERE-----------LTAQIAAG------RAEGseaaelaeiYAKlEEIEAdkapaRASVI 310
Cdd:COG1135 69 LTAL---------SERELRAARRkigmifqhfnlLSSRTVAEnvalplEIAG---------VPK-AEIRK-----RVAEL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 311 LAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL 364
Cdd:COG1135 125 LELVGLSDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSIL 180
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
329-361 |
9.65e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.61 E-value: 9.65e-05
10 20 30
....*....|....*....|....*....|...
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK11174 487 SVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
525-637 |
9.81e-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: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 525 GENGAGKSTMLKLLLGDLAPVRG--------IRHAH----RNLKIGYFSQHH-------VEQldlNVSAVELLARKFPGR 585
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGkilldgqdITKLPmhkrARLGIGYLPQEAsifrkltVEE---NILAVLEIRGLSKKE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 148612853 586 PEEEYRHQLGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03218 110 REEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
187-382 |
1.04e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 44.72 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 187 FGDRVLLaGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLhveqevAGDdtpalqSVLESDSVREDLLR 266
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHL--NGLLQPTEGKVT------VGD------IVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 267 RERELTAQIAAGRAEGSEAAELAEIYAKLEE--IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFA 344
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 345 RPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSH 382
Cdd:PRK13643 162 EPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
492-644 |
1.09e-04 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 44.23 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrlsVSADLESRICVV--GENGAGKSTMLKLL-------LGDL------------APVRGIRH 550
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD---ITLDCPQGETLVllGPSGAGKSSLLRVLnllemprSGTLniagnhfdfsktPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 551 AHRNLKIgYFSQHHveqLDLNVSAVELLAR---KFPGRPEEEYRHQ----LGRYGISgELAMR-PLaSLSGGQKSRVAFA 622
Cdd:PRK11124 80 LRRNVGM-VFQQYN---LWPHLTVQQNLIEapcRVLGLSKDQALARaeklLERLRLK-PYADRfPL-HLSGGQQQRVAIA 153
|
170 180
....*....|....*....|..
gi 148612853 623 QMTMPCPNFYILDEPTNHLDME 644
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPE 175
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
485-644 |
1.11e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.84 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 485 EKFSPPILQLDEVDFYYDpKHVIFsrlsvsadlesriCVVGENGAGKSTMLKLLLGDLAPVRG----------------- 547
Cdd:PRK13631 33 EKQENELVALNNISYTFE-KNKIY-------------FIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 548 --IRHAHRNLK--------IGYFSQHHVEQL-------DLNVSAVELLARKFPGRPEEEYrhQLGRYGISGELAMRPLAS 610
Cdd:PRK13631 99 liTNPYSKKIKnfkelrrrVSMVFQFPEYQLfkdtiekDIMFGPVALGVKKSEAKKLAKF--YLNKMGLDDSYLERSPFG 176
|
170 180 190
....*....|....*....|....*....|....
gi 148612853 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME 644
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
178-361 |
1.12e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.39 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA---------------TRSLRVPAH-----ISLL 237
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyqpdsgeilldgePVRFRSPRDaqaagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 238 HveQEVagddtpalqSVLESDSVREDL-LRRE---------RELTAqiaagraegsEAAELaeiyakLEEIEADKAPARa 307
Cdd:COG1129 85 H--QEL---------NLVPNLSVAENIfLGREprrgglidwRAMRR----------RAREL------LARLGLDIDPDT- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 308 svILAGLGFTpkmQQQptrefsggwrMrLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:COG1129 137 --PVGDLSVA---QQQ----------L-VEIARALSRDARVLILDEPTASLTER 174
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
486-654 |
1.14e-04 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 45.58 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 486 KFSPPILQLDEVDFYYDPKHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKigyfsqhH 564
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGrILIDGQDIR-------D 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 565 VEQLDL--------------NVSAVELLARkfpGRP---EEEYRH-----QLGRYGIS---------GElamRPLaSLSG 613
Cdd:COG5265 425 VTQASLraaigivpqdtvlfNDTIAYNIAY---GRPdasEEEVEAaaraaQIHDFIESlpdgydtrvGE---RGL-KLSG 497
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148612853 614 GQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALN 654
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
504-673 |
1.21e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 44.19 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 504 KHVIFSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNLKI-----GYFSQHHVEQLDLNVSAVEL 577
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsIVVNGQTINLvrdkdGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 578 LARKFP-------------------GRPEEEYRHQLGRY----GISGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:PRK10619 97 VFQHFNlwshmtvlenvmeapiqvlGLSKQEARERAVKYlakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 635 DEPTNHLDMETIEALGRALNNFR---GGVILVSHDERFIRLV 673
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHV 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
492-644 |
1.21e-04 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 44.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIFSrlsVSADLESRICVV--GENGAGKSTMLKLL-LGDLaPVRGIRH---------------AHR 553
Cdd:COG4161 3 IQLKNINCFYGSHQALFD---INLECPSGETLVllGPSGAGKSSLLRVLnLLET-PDSGQLNiaghqfdfsqkpsekAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 554 NL--KIGY-FSQHH------VEQlDLNVSAVELLarkfpGRPEEEYRHQ----LGRYGISGELAMRPLAsLSGGQKSRVA 620
Cdd:COG4161 79 LLrqKVGMvFQQYNlwphltVME-NLIEAPCKVL-----GLSKEQAREKamklLARLRLTDKADRFPLH-LSGGQQQRVA 151
|
170 180
....*....|....*....|....
gi 148612853 621 FAQMTMPCPNFYILDEPTNHLDME 644
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPE 175
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
92-359 |
1.26e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.54 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 92 QLSKITENYDCGTKLPglLKREQSSTVNAKKLEKAEARLKAKQEKrsekDTLKTSNPLVL---EEASASQAGSRKESRLE 168
Cdd:PTZ00243 569 QLAAVLENVDVTAFVP--VKLPRAPKVKTSLLSRALRMLCCEQCR----PTKRHPSPSVVvedTDYGSPSSASRHIVEGG 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 169 SSGKNKSYDVRIENFDVSFGD---------RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR----SLRVPAHIS 235
Cdd:PTZ00243 643 TGGGHEATPTSERSAKTPKMKtddffelepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfeisEGRVWAERS 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 236 LLHVEQevagddtpalQSVLESDSVREDLLRRERELTAQIA-AGRAEGSEaAELAEIYAKLE-EIeadkapARASVILag 313
Cdd:PTZ00243 723 IAYVPQ----------QAWIMNATVRGNILFFDEEDAARLAdAVRVSQLE-ADLAQLGGGLEtEI------GEKGVNL-- 783
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148612853 314 lgftpkmqqqptrefSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PTZ00243 784 ---------------SGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
208-385 |
1.30e-04 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.15 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 208 LVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQEVAGDDTPalqsvLESDSVREdlLRRERELTAQiaagraeGSEAAE 287
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA----------GLLPGSGSIQFAGQP-----LEAWSAAE--LARHRAYLSQ-------QQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 288 LAEIYAKLEEIEADKAPARAS-----VILAGLGFTPKMQQqPTREFSGG-W-RMRLALA-----RALFARPDLLLLDEPT 355
Cdd:PRK03695 83 AMPVFQYLTLHQPDKTRTEAVasalnEVAEALGLDDKLGR-SVNQLSGGeWqRVRLAAVvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 356 NMLDVRAILWLENYLQTWPS---TILVVSHDRN 385
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQqgiAVVMSSHDLN 194
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
329-354 |
1.57e-04 |
|
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: 43.23 E-value: 1.57e-04
10 20
....*....|....*....|....*.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEP 354
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
329-359 |
1.70e-04 |
|
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: 43.96 E-value: 1.70e-04
10 20 30
....*....|....*....|....*....|.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
301-361 |
1.72e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.24 E-value: 1.72e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK13634 119 EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
440-664 |
1.90e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.80 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 440 FID------RFRYNANRASQVQSKLKMLEKLPELKPVDKESEvvmkfpdgfekfsPPILQLDEVDFYYDPKHVIFSRLSV 513
Cdd:COG4178 318 FVDnyqslaEWRATVDRLAGFEEALEAADALPEAASRIETSE-------------DGALALEDLTLRTPDGRPLLEDLSL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 514 SADLESRICVVGENGAGKSTMLKLLLGdLAP-VRGIRHAHRNLKIGYFSQH-HVEQLDLnvsaVELLArkFPGRPE---- 587
Cdd:COG4178 385 SLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARVLFLPQRpYLPLGTL----REALL--YPATAEafsd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 588 EEYRHQLGRYGIsGELAMRpLAS-------LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRGGV 660
Cdd:COG4178 458 AELREALEAVGL-GHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGT 535
|
....
gi 148612853 661 ILVS 664
Cdd:COG4178 536 TVIS 539
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
523-691 |
2.10e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLL-----------------LGDLAPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 581
Cdd:COG1135 36 IIGYSGAGKSTLIRCInllerptsgsvlvdgvdLTALSE-RELRAARR--KIGMIFQH-----------FNLLSSRtvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 582 ---FP----GRPEEEyRHQ-----LGRYGISGELAMRPlASLSGGQKSRVAFAQ--MTMPcpnfYIL--DEPTNHLDMET 645
Cdd:COG1135 102 nvaLPleiaGVPKAE-IRKrvaelLELVGLSDKADAYP-SQLSGGQKQRVGIARalANNP----KVLlcDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148612853 646 ---IEALGRALNNfRGG--VILVSHDERFIRLVCRELWVCEGGGVtrVEGG 691
Cdd:COG1135 176 trsILDLLKDINR-ELGltIVLITHEMDVVRRICDRVAVLENGRI--VEQG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
298-360 |
2.12e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 2.12e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 298 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
172-362 |
2.19e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 43.00 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 172 KNKSYDVrienfDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSlrvpaHISLLHVEQEVAGddtpal 251
Cdd:cd03232 7 KNLNYTV-----PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK-----TAGVITGEILING------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 qsvlesdsvredllrRERELTAQIAAGRAEGSEAAElaeiyAKLEEIEAdkapARASVILAGLGftpkmQQQptrefsgg 331
Cdd:cd03232 71 ---------------RPLDKNFQRSTGYVEQQDVHS-----PNLTVREA----LRFSALLRGLS-----VEQ-------- 113
|
170 180 190
....*....|....*....|....*....|.
gi 148612853 332 wRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:cd03232 114 -RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
193-382 |
2.19e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.58 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAhisllhvEQEVAGDDTpalqsVLESDSVREDL--LRRERE 270
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL--NGLHVPT-------QGSVRVDDT-----LITSTSKNKDIkqIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 271 LTAQIAagraegsEAAELAEIYAKLEE-------IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALF 343
Cdd:PRK13649 89 LVFQFP-------ESQLFEETVLKDVAfgpqnfgVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 148612853 344 ARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSH 382
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPkgrKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
606-685 |
2.22e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.82 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 606 RPLASLSGGQKSRVAFAQ--------MTmpcpnfYILDEPTNHL---DMETIEALGRALNNFRGGVILVSHDERFIRLVC 674
Cdd:PRK00635 472 RALATLSGGEQERTALAKhlgaeligIT------YILDEPSIGLhpqDTHKLINVIKKLRDQGNTVLLVEHDEQMISLAD 545
|
90
....*....|.
gi 148612853 675 RELWVCEGGGV 685
Cdd:PRK00635 546 RIIDIGPGAGI 556
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
181-383 |
2.22e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 43.34 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML-------ATRSLRVPAHISLL--HVEQEVAGDDTPAL 251
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVvgivprdAGNIIIDDEDISLLplHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 252 QSVLESDSVREDL---LRRERELTAQIAAGRAEgseaaELAEiyakleeiEADKAPARASvilagLGftpkmqqqptREF 328
Cdd:PRK10895 87 ASIFRRLSVYDNLmavLQIRDDLSAEQREDRAN-----ELME--------EFHIEHLRDS-----MG----------QSL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDE------PTNMLDVRAILwleNYLQTWPSTILVVSHD 383
Cdd:PRK10895 139 SGGERRRVEIARALAANPKFILLDEpfagvdPISVIDIKRII---EHLRDSGLGVLITDHN 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
521-666 |
2.27e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLlGDL-APVRGI-RHAHRNLK--------------IGY-FSQHHveqLDLNVSA---VELLAr 580
Cdd:PRK10535 37 VAIVGASGSGKSTLMNIL-GCLdKPTSGTyRVAGQDVAtldadalaqlrrehFGFiFQRYH---LLSHLTAaqnVEVPA- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 581 KFPGRPEEEYRHQ----LGRYGISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGRAL 653
Cdd:PRK10535 112 VYAGLERKQRLLRaqelLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQL 190
|
170
....*....|...
gi 148612853 654 NNFRGGVILVSHD 666
Cdd:PRK10535 191 RDRGHTVIIVTHD 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
193-401 |
2.43e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.57 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLkmlatrslrvpAHISLLHVEQEvaGDDTPALQSVLESDsvrEDLLRRERELT 272
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLL-----------LHLNGIYLPQR--GRVKVMGREVNAEN---EKWVRSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 273 AQIAAGRAEGSEAAELAEIYAKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLD 352
Cdd:PRK13647 85 FQDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 353 EPTNMLD------VRAILWLenyLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:PRK13647 164 EPMAYLDprgqetLMEILDR---LHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
521-642 |
2.65e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.15 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 521 ICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNlkIGYFSQH-------HVEQldlNVSA-------VE---LLA--- 579
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGsILIDGKD--VTKLPEYkrakyigRVFQ---DPMMgtapsmtIEenlALAyrr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 580 -RKFPGRP------EEEYRHQLGRYGISGELAMR-PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:COG1101 110 gKRRGLRRgltkkrRELFRELLATLGLGLENRLDtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
180-424 |
2.84e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.24 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR--------SLRVPAHISLLHVEQEVAGDDT-PA 250
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevtggTVEFKGKDLLELSPEDRAGEGIfMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 251 LQSVLESDSVREDLLRRerelTAQIAAGRAEGSEAAELAEIYAKLEE-IEADKAPARASVILAGLGFtpkmqqqptrefS 329
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQ----TALNAVRSYRGQEPLDRFDFQDLMEEkIALLKMPEDLLTRSVNVGF------------S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 330 GGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLE---NYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYR 406
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKS 227
|
250 260
....*....|....*....|..
gi 148612853 407 GDFeTFIKSKQER----LLNQQ 424
Cdd:PRK09580 228 GDF-TLVKQLEEQgygwLTEQQ 248
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
485-667 |
2.89e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 43.67 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 485 EKFSPPILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG--------IRHA---HR 553
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGqimldgvdLSHVppyQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 554 NLKIGY-----FSQHHVEQldlNVsAVELLARKFPgRPEEEYR-HQLGRYGISGELAMRPLASLSGGQKSRVAFAQMTMP 627
Cdd:PRK11607 92 PINMMFqsyalFPHMTVEQ---NI-AFGLKQDKLP-KAEIASRvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 148612853 628 CPNFYILDEPTNHLD--------METIEALGRAlnnfrgGV--ILVSHDE 667
Cdd:PRK11607 167 RPKLLLLDEPMGALDkklrdrmqLEVVDILERV------GVtcVMVTHDQ 210
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
175-420 |
2.97e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.46 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 175 SYDVRIENFDVSFGDRV-----LLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlaTRSLRVPahisllHVEQEVAGD-DT 248
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL--TNGLIIS------ETGQTIVGDyAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 249 PA-LQSVLEsdsVREdlLRRERELTAQ--------------IAAGRAEGSEAAElaEIYAKLEEIeadkaparasviLAG 313
Cdd:PRK13645 76 PAnLKKIKE---VKR--LRKEIGLVFQfpeyqlfqetiekdIAFGPVNLGENKQ--EAYKKVPEL------------LKL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 314 LGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVSHDRNFLNA 389
Cdd:PRK13645 137 VQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLR 216
|
250 260 270
....*....|....*....|....*....|.
gi 148612853 390 IATDIIHLHSQRLDGYRGDFETFikSKQERL 420
Cdd:PRK13645 217 IADEVIVMHEGKVISIGSPFEIF--SNQELL 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
189-359 |
3.62e-04 |
|
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: 42.64 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 189 DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLR-------------------VPAHISllHVEQevagDDTp 249
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilfngqprkpdqFQKCVA--YVRQ----DDI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 250 alqsVLESDSVREDLLrrereLTAQIAAGRAEGSEaaelaeIYAKLEEIEADKAPARASVilAGlgftPKMQQqptreFS 329
Cdd:cd03234 92 ----LLPGLTVRETLT-----YTAILRLPRKSSDA------IRKKRVEDVLLRDLALTRI--GG----NLVKG-----IS 145
|
170 180 190
....*....|....*....|....*....|
gi 148612853 330 GGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03234 146 GGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
327-382 |
3.85e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 42.65 E-value: 3.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-ILWL-ENYLQTWPSTILVVSH 382
Cdd:PRK10771 129 QLSGGQRQRVALARCLVREQPILLLDEPFSALDpaLRQeMLTLvSQVCQERQLTLLMVSH 188
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
491-666 |
4.28e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 42.76 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 491 ILQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAP------VRGIRHAHRNLKIGYFSQHH 564
Cdd:PRK11248 1 MLQISHLYADYGGKPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqhgsitLDGKPVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 565 VEQLDLNVSAVELLARKFPGRPEEEYRHQ----LGRYGISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 640
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIahqmLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|
gi 148612853 641 LDMETIEA----LGRALNNFRGGVILVSHD 666
Cdd:PRK11248 159 LDAFTREQmqtlLLKLWQETGKQVLLITHD 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
179-366 |
4.80e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.33 E-value: 4.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------------SLRVPAHiSLLHVEQEVAGD 246
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqgnnftgtilaNNRKPTK-QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 247 DT--PALqsvlesdSVRE-----DLLRRERELTAQIAAGRAEgSEAAELAeiYAKLEEIeadkaparasviLAGLGFTpk 319
Cdd:PLN03211 149 DIlyPHL-------TVREtlvfcSLLRLPKSLTKQEKILVAE-SVISELG--LTKCENT------------IIGNSFI-- 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148612853 320 mqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL 366
Cdd:PLN03211 205 ------RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
610-642 |
4.92e-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: 4.92e-04
10 20 30
....*....|....*....|....*....|...
gi 148612853 610 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:TIGR00955 166 GLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
326-359 |
5.79e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 5.79e-04
10 20 30
....*....|....*....|....*....|....
gi 148612853 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
296-394 |
5.92e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 296 EEIEADKAPARASVILAGLgftpkmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQT 372
Cdd:PRK13639 112 EEVEKRVKEALKAVGMEGF------ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNK 185
|
90 100
....*....|....*....|..
gi 148612853 373 WPSTILVVSHDRNFLNAIATDI 394
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKV 207
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
510-666 |
6.24e-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: 42.78 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 510 RLSVSADLESR-ICVV-GENGAGKSTMLKLLLGDLAPVRG-IR---------HAHRNLK-----IGYFSQH-----Hveq 567
Cdd:COG4148 15 TLDVDFTLPGRgVTALfGPSGSGKTTLLRAIAGLERPDSGrIRlggevlqdsARGIFLPphrrrIGYVFQEarlfpH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 568 ldLNVSAVELLARKFPGRPEEEYRHQ-----LGrygISGELAMRPlASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:COG4148 92 --LSVRGNLLYGRKRAPRAERRISFDevvelLG---IGHLLDRRP-ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
|
170 180
....*....|....*....|....*...
gi 148612853 643 M----ETIEALGRALNNFRGGVILVSHD 666
Cdd:COG4148 166 LarkaEILPYLERLRDELDIPILYVSHS 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-362 |
6.24e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 6.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 148612853 323 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
523-649 |
6.50e-04 |
|
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: 41.38 E-value: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVR--------GIRHAHRNLK--IGYFSQHhvEQLDLNVSAVELLArkfpgrpeeeyrh 592
Cdd:cd03213 40 IMGPSGAGKSTLLNALAGRRTGLGvsgevlinGRPLDKRSFRkiIGYVPQD--DILHPTLTVRETLM------------- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 593 qlgrygISGElamrpLASLSGGQKSRVAFA-QMTMPcPNFYILDEPTNHLD-------METIEAL 649
Cdd:cd03213 105 ------FAAK-----LRGLSGGERKRVSIAlELVSN-PSLLFLDEPTSGLDsssalqvMSLLRRL 157
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
492-667 |
6.51e-04 |
|
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: 41.84 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 492 LQLDEVDFYYDPKHVIfSRLSVSADLESRICVVGENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------KIGYFSQ 562
Cdd:cd03300 1 IELENVSKFYGGFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGeILLDGKDItnlpphkrPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 563 HHVEQLDLNVSAVELLARKFPGRPEEEYRHQLGRY----GISGeLAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPT 638
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEAldlvQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|...
gi 148612853 639 NHLDMETIEALGRALNNFRGGV----ILVSHDE 667
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELgitfVFVTHDQ 191
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
184-385 |
7.77e-04 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 41.75 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 184 DVSFGDRVLLAGADVNLawGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQEVAGDDTPalqsvLESDSVREd 263
Cdd:COG4138 5 DVAVAGRLGPISAQVNA--GELIHLIGPNGAGKSTLLARMA----------GLLPGQGEILLNGRP-----LSDWSAAE- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 264 lLRRERELTAQ-------------IAAGRAEGSEAAELAEIYAKLeeieadkapARAsvilagLGFTPKMQQqPTREFSG 330
Cdd:COG4138 67 -LARHRAYLSQqqsppfampvfqyLALHQPAGASSEAVEQLLAQL---------AEA------LGLEDKLSR-PLTQLSG 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 331 G-W-RMRLALA-----RALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRN 385
Cdd:COG4138 130 GeWqRVRLAAVllqvwPTINPEGQLLLLDEPMNSLDVAqqaALDRLLRELCQQGITVVMSSHDLN 194
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
606-649 |
8.00e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 8.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148612853 606 RPLASLSGGQKSRVAFA-QMTMPC--PNFYILDEPTNHLDMETIEAL 649
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAyELLAPSkkPTLYVLDEPTTGLHTHDIKAL 851
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
203-396 |
8.32e-04 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 41.58 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 203 GRRYGLVGRNGLGKTTLLKMLATRslRVPahiSLLHVEQEVAGDDT------PALQSVLESdsVREDLLR--RERELTAQ 274
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGK--LKP---NLGKFDDPPDWDEIldefrgSELQNYFTK--LLEGDVKviVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 275 I-AAGRAEGSEAAELAEIYAKLEEIeadkaparasviLAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDE 353
Cdd:cd03236 99 IpKAVKGKVGELLKKKDERGKLDEL------------VDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFFDE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 148612853 354 PTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIH 396
Cdd:cd03236 166 PSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLS-DYIH 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
310-402 |
9.08e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.71 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 310 ILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPS-TILVVSHDRN 385
Cdd:PRK13640 127 VLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqILKLIRKLKKKNNlTVISITHDID 205
|
90
....*....|....*..
gi 148612853 386 FLNaIATDIIHLHSQRL 402
Cdd:PRK13640 206 EAN-MADQVLVLDDGKL 221
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
177-361 |
9.24e-04 |
|
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: 41.44 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 177 DVRIENfdVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTR----------------------SLRvp 231
Cdd:cd03254 2 EIEFEN--VNFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MRfydpqkgqilidgidirdisrkSLR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 232 AHISLlhVEQEvagddtpalqSVLESDSVREDllrrereltaqIAAGRAEGSEAaelaeiyaklEEIEADKApARASVIL 311
Cdd:cd03254 77 SMIGV--VLQD----------TFLFSGTIMEN-----------IRLGRPNATDE----------EVIEAAKE-AGAHDFI 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 148612853 312 AGLgftPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:cd03254 123 MKL---PNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
180-223 |
1.05e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 41.63 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML 223
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII 47
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
520-666 |
1.12e-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: 41.98 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 520 RICVVGENGAGKS----TMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQ---------HHVEQ---- 567
Cdd:COG4172 38 TLALVGESGSGKSvtalSILRLLPDPAAHPSGsILFDGQDLlglserelrrirgnRIAMIFQepmtslnplHTIGKqiae 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 568 ---LDLNVS-------AVELLAR---KFPGRPEEEYRHQLgrygisgelamrplaslSGGQKSRVAFAqMTMPC-PNFYI 633
Cdd:COG4172 118 vlrLHRGLSgaaararALELLERvgiPDPERRLDAYPHQL-----------------SGGQRQRVMIA-MALANePDLLI 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 148612853 634 LDEPTNHLDMeTIEA----LGRALNNFRG-GVILVSHD 666
Cdd:COG4172 180 ADEPTTALDV-TVQAqildLLKDLQRELGmALLLITHD 216
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
327-419 |
1.13e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 40.63 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL----WLENYLQTWPSTILVVSHDRNFLNAIAtDIIHLhsqrL 402
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDLAVLDYLS-DRIHV----F 145
|
90
....*....|....*..
gi 148612853 403 DGYRGDFETFIKSKQER 419
Cdd:cd03222 146 EGEPGVYGIASQPKGTR 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
301-402 |
1.20e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 41.35 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 301 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYlQTWPST 376
Cdd:PRK13641 119 DEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmqlfKDY-QKAGHT 197
|
90 100
....*....|....*....|....*.
gi 148612853 377 ILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:PRK13641 198 VILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
605-642 |
1.25e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.84 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....*...
gi 148612853 605 MRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
301-383 |
1.49e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 40.99 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 301 DKAPARASVILAGLGFTPkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL----WLENYLQTWPST 376
Cdd:PRK13636 116 DEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLT 194
|
....*..
gi 148612853 377 ILVVSHD 383
Cdd:PRK13636 195 IIIATHD 201
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
523-668 |
1.66e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.78 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLG-------------------DLAPVRgirHAHRNLKIGYfsQHHVEQLdlNVSAVELL----- 578
Cdd:CHL00131 38 IMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPEE---RAHLGIFLAF--QYPIEIP--GVSNADFLrlayn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 579 -ARKFPGRPE-------EEYRHQLGRYGISGELAMRPL-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEAL 649
Cdd:CHL00131 111 sKRKFQGLPEldpleflEIINEKLKLVGMDPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKII 190
|
170 180
....*....|....*....|..
gi 148612853 650 GRALNNFRG---GVILVSHDER 668
Cdd:CHL00131 191 AEGINKLMTsenSIILITHYQR 212
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-359 |
1.73e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 40.84 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
608-667 |
1.77e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 40.74 E-value: 1.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 608 LASLSGGQKSRVAFAQ-MTM----PCPnFYILDEPTNHLDMETIEALGRAL-NNFRGG-VILVSHDE 667
Cdd:cd03273 164 LTELSGGQRSLVALSLiLALllfkPAP-MYILDEVDAALDLSHTQNIGRMIkTHFKGSqFIVVSLKE 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
524-674 |
1.82e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLL-------------LGDLAPVRGIRHAhRNLKIGYFSQhhveQLDL--NVSAVE--LLARKFPGR- 585
Cdd:PRK10762 36 VGENGAGKSTMMKVLtgiytrdagsilyLGKEVTFNGPKSS-QEAGIGIIHQ----ELNLipQLTIAEniFLGREFVNRf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 -------PEEEYRHQLGRYGISGElAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL-DMETiEALGRALNNFR 657
Cdd:PRK10762 111 gridwkkMYAEADKLLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFRVIRELK 188
|
170 180
....*....|....*....|
gi 148612853 658 G---GVILVSHDERFIRLVC 674
Cdd:PRK10762 189 SqgrGIVYISHRLKEIFEIC 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
329-359 |
1.84e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.53 E-value: 1.84e-03
10 20 30
....*....|....*....|....*....|.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
328-387 |
1.89e-03 |
|
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: 40.39 E-value: 1.89e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--------AILwleNYLQTWPSTILVVSHDRNFL 387
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlmqeGIL---KFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
607-666 |
1.93e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.93e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148612853 607 PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG---GVILVSHD 666
Cdd:PRK10762 392 AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
523-547 |
1.96e-03 |
|
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: 41.32 E-value: 1.96e-03
10 20
....*....|....*....|....*
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG 547
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESG 387
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
328-385 |
2.21e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 2.21e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT--WPSTILVVSHDRN 385
Cdd:PLN03232 1372 FSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREefKSCTMLVIAHRLN 1431
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
328-360 |
2.33e-03 |
|
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: 41.43 E-value: 2.33e-03
10 20 30
....*....|....*....|....*....|...
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
510-672 |
2.33e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 40.63 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 510 RLSVSADLESR-ICVV-GENGAGKSTMLKLLLGDLAPVRG-IRHAHRNL--------------KIGYFSQHhveqldlnv 572
Cdd:PRK11144 14 CLTVNLTLPAQgITAIfGRSGAGKTSLINAISGLTRPQKGrIVLNGRVLfdaekgiclppekrRIGYVFQD--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 573 savellARKFPgrpeeEYRHQlG--RYGISGE-----------LAMRPL-----ASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:PRK11144 85 ------ARLFP-----HYKVR-GnlRYGMAKSmvaqfdkivalLGIEPLldrypGSLSGGEKQRVAIGRALLTAPELLLM 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 148612853 635 DEPTNHLDM----ETIEALGRALNNFRGGVILVSH--DErFIRL 672
Cdd:PRK11144 153 DEPLASLDLprkrELLPYLERLAREINIPILYVSHslDE-ILRL 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
611-703 |
2.63e-03 |
|
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: 40.94 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI----EALGRALNNFRGGVILVSH-DERFIRLVCRELWVcEGGGV 685
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHwPEVIEDLSDKAIWL-ENGEI 247
|
90
....*....|....*...
gi 148612853 686 TRvEGGFDQYRALLQEQF 703
Cdd:TIGR03269 248 KE-EGTPDEVVAVFMEGV 264
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
329-383 |
2.77e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.12 E-value: 2.77e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHD 383
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnLLDLVRKVKsEHNITIISITHD 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
180-355 |
2.84e-03 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.86 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLhveqevaGDDTPALQSVlesds 259
Cdd:PRK11614 8 FDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD-------GKDITDWQTA----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 260 vredllRRERELTAQIAAGRAEGS-----EAAELAEIYAKLEEIEADkaparasvILAGLGFTPKMQQ---QPTREFSGG 331
Cdd:PRK11614 76 ------KIMREAVAIVPEGRRVFSrmtveENLAMGGFFAERDQFQER--------IKWVYELFPRLHErriQRAGTMSGG 141
|
170 180
....*....|....*....|....
gi 148612853 332 WRMRLALARALFARPDLLLLDEPT 355
Cdd:PRK11614 142 EQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
329-359 |
2.95e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 2.95e-03
10 20 30
....*....|....*....|....*....|.
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
524-688 |
3.26e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.40 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 524 VGENGAGKSTMLKLLLG-----------------DLAPV-RGI--------RHAHRN--------LKIGYFSQHHVEQLD 569
Cdd:PRK11000 35 VGPSGCGKSTLLRMIAGleditsgdlfigekrmnDVPPAeRGVgmvfqsyaLYPHLSvaenmsfgLKLAGAKKEEINQRV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 570 LNVSAVELLArkfpgrpeeeyrHQLGRygisgelamRPLAsLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------M 643
Cdd:PRK11000 115 NQVAEVLQLA------------HLLDR---------KPKA-LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqM 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 148612853 644 ET-IEALGRALNNfrgGVILVSHDERFIRLVCRELWVCEGGGVTRV 688
Cdd:PRK11000 173 RIeISRLHKRLGR---TMIYVTHDQVEAMTLADKIVVLDAGRVAQV 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
607-666 |
3.40e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.03 E-value: 3.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148612853 607 PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG--GVILVSHD 666
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
324-404 |
3.47e-03 |
|
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: 40.58 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 324 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
....
gi 148612853 401 RLDG 404
Cdd:TIGR02633 480 KLKG 483
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
609-654 |
3.51e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.77 E-value: 3.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 148612853 609 ASLSGGQKSRVAFAQMTM-PCPnFYILDEPTNHLDMETIEALGRALN 654
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLrDSP-ILILDEATSALDTESERAIQAALD 524
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
308-387 |
3.60e-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: 38.84 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 308 SVILAGLGFTPKMQQQPTreFSGGWRMRLALARALFARPD--LLLLDEPTNMLDVRAILWLENYLQTW---PSTILVVSH 382
Cdd:cd03238 70 FLIDVGLGYLTLGQKLST--LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEH 147
|
....*
gi 148612853 383 DRNFL 387
Cdd:cd03238 148 NLDVL 152
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
328-361 |
4.45e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.49 E-value: 4.45e-03
10 20 30
....*....|....*....|....*....|....
gi 148612853 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
329-360 |
4.46e-03 |
|
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: 39.84 E-value: 4.46e-03
10 20 30
....*....|....*....|....*....|..
gi 148612853 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-383 |
4.54e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 262 EDLLRRERELTAQIAAGRAEGSEAA-----ELA-EIYAKLEE-------IEADKAPARASVILAGlgftpkmQQQPTREF 328
Cdd:PRK03918 717 EKALERVEELREKVKKYKALLKERAlskvgEIAsEIFEELTEgkysgvrVKAEENKVKLFVVYQG-------KERPLTFL 789
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148612853 329 SGGWRM------RLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTIlVVSHD 383
Cdd:PRK03918 790 SGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQVI-IVSHD 853
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
327-383 |
4.69e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 4.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHD 383
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
523-683 |
4.81e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.49 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLG----------------DLAPVrgirHAHRNLKIGYFSQHH--VEQLDL--NVSAVeLLARKF 582
Cdd:PRK10895 34 LLGPNGAGKTTTFYMVVGivprdagniiiddediSLLPL----HARARRGIGYLPQEAsiFRRLSVydNLMAV-LQIRDD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 583 PGRPEEEYRHQ--LGRYGISgELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFRG-- 658
Cdd:PRK10895 109 LSAEQREDRANelMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDsg 187
|
170 180
....*....|....*....|....*.
gi 148612853 659 -GVILVSHDERFIRLVCRELWVCEGG 683
Cdd:PRK10895 188 lGVLITDHNVRETLAVCERAYIVSQG 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
523-668 |
5.00e-03 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 39.78 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLLLGDLAPVRG----------IRHAHRNlKIGYFSQHH-------VEQldlNVsAVELLARKFPgR 585
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGsimldgedvtNVPPHLR-HINMVFQSYalfphmtVEE---NV-AFGLKMRKVP-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 586 PE--EEYRHQLGRYGIsGELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNF--RGGV- 660
Cdd:TIGR01187 75 AEikPRVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqeQLGIt 153
|
....*....
gi 148612853 661 -ILVSHDER 668
Cdd:TIGR01187 154 fVFVTHDQE 162
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
523-665 |
5.44e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.13 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 523 VVGENGAGKSTMLKLL--LGDLAP---VRG-------------IRHAHRNLKIGYFSQHHVEQLDL--NVSAVELLARKF 582
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFnrLIELYPearVSGevyldgqdifkmdVIELRRRVQMVFQIPNPIPNLSIfeNVALGLKLNRLV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 583 PGRPE--EEYRHQLGRYGISGELAMR---PLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGRALN 654
Cdd:PRK14247 114 KSKKElqERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELK 193
|
170
....*....|.
gi 148612853 655 NfRGGVILVSH 665
Cdd:PRK14247 194 K-DMTIVLVTH 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
306-425 |
6.66e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.02 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 306 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVS 381
Cdd:PRK13652 117 RVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFST 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 148612853 382 HDRNFLNAIATDIIHLHSQRLDGYRGDFETFIkskQERLLNQQR 425
Cdd:PRK13652 196 HQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL---QPDLLARVH 236
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
606-672 |
7.11e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 7.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148612853 606 RPLASLSGGQKSRVAFA-QMTMPCPN-FYILDEPT-------NHLDMETIEALgRALNNfrgGVILVSHDERFIRL 672
Cdd:cd03270 133 RSAPTLSGGEAQRIRLAtQIGSGLTGvLYVLDEPSiglhprdNDRLIETLKRL-RDLGN---TVLVVEHDEDTIRA 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
602-667 |
7.37e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.16 E-value: 7.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 148612853 602 ELAMRPLASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------MET-IEALGRALN-NFrggvILVSHDE 667
Cdd:PRK09452 136 EFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDyklrkqMQNeLKALQRKLGiTF----VFVTHDQ 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
528-666 |
7.68e-03 |
|
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: 38.18 E-value: 7.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 528 GAGKSTMLKLLLGDLAPVRG-IR-----------HAHRNLKIGYFsqhhveqldlnvsavellarkfpgrPEEeyRHQLG 595
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGeITldgkpvtrrspRDAIRAGIAYV-------------------------PED--RKREG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 148612853 596 ---RYGISGELAMRPLasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRALNNFR---GGVILVSHD 666
Cdd:cd03215 89 lvlDLSVAENIALSSL--LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
606-672 |
8.41e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 606 RPLASLSGGQKSRVAFA-----QMT--MpcpnfYILDEPT-------NHLDMETIEALgRALNNfrgGVILVSHDERFIR 671
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLAtqigsGLTgvL-----YVLDEPSiglhqrdNRRLINTLKRL-RDLGN---TLIVVEHDEDTIR 554
|
.
gi 148612853 672 L 672
Cdd:TIGR00630 555 A 555
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
208-359 |
8.48e-03 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 39.26 E-value: 8.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 208 LVGRNGLGKTTLLKMLATRSLR------------VPAHISLLH-----VEQevagDD--TPALqsvlesdSVREDL---- 264
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKgvkgsgsvllngMPIDAKEMRaisayVQQ----DDlfIPTL-------TVREHLmfqa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 265 -LRRERELTAqiaagraegseaaelaeiyakleeieaDKAPARASVILAGLGFTPKMQ---QQPTRE--FSGGWRMRLAL 338
Cdd:TIGR00955 125 hLRMPRRVTK---------------------------KEKRERVDEVLQALGLRKCANtriGVPGRVkgLSGGERKRLAF 177
|
170 180
....*....|....*....|.
gi 148612853 339 ARALFARPDLLLLDEPTNMLD 359
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
327-383 |
8.81e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 38.71 E-value: 8.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHD 383
Cdd:PRK15056 142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
602-679 |
9.23e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148612853 602 ELAMRplASLSGGQKS------RVAFAQMTMPCPNFYILDEPTNHLDMETIEALGRAL----------NNFRggVILVSH 665
Cdd:TIGR00606 1193 ALDMR--GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALveiiksrsqqRNFQ--LLVITH 1268
|
90
....*....|....
gi 148612853 666 DERFIRLVCRELWV 679
Cdd:TIGR00606 1269 DEDFVELLGRSEYV 1282
|
|
| |
