|
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: 606.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 6 DILRSEFPEIDGQVFDYVTGVLHSGSADF-ESVDDLVEAVGELLQEvSGDSKDDAGIRAVCQRM---YNTLRLAEPQNQG 81
Cdd:PLN03073 13 EVLGRRIRDVDSPIIDYIINVLADEDFDFgPEGEGAFDALGELLVA-AECVSDDAECRLVCSKLaekFGKHGLVKPKPSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 82 NSqvlLDAPIQLSKIMENYDCDTKLPGLLKREQSSTVNAKKLEkaeaRLKAKQEKrsEKETLKTSNPLVLEEASASQAGS 161
Cdd:PLN03073 92 RS---LAAPVRMSDGMDDSEVAKKKPEPDDGPLLSERDLAKIE----RRKRKEER--QREVQYQAHVAEMEAAKAGMPGV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 162 RKESRLESSGKNKSyDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLR-VPAHISLLHVE 240
Cdd:PLN03073 163 YVNHDGNGGGPAIK-DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIDgIPKNCQILHVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 241 QEVAGDDTPALQSVLESDTVREDLLRQE-------RELSLRIAAGRAEGSE---------AAQLAEIYGKLEEIEADKAP 304
Cdd:PLN03073 242 QEVVGDDTTALQCVLNTDIERTQLLEEEaqlvaqqRELEFETETGKGKGANkdgvdkdavSQRLEEIYKRLELIDAYTAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 305 ARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDR 384
Cdd:PLN03073 322 ARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 385 NFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKL 464
Cdd:PLN03073 402 EFLNTVVTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 465 PELKPVDKESEVVLKFPDGFEKFSPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP 544
Cdd:PLN03073 482 GHVDAVVNDPDYKFEFPTPDDRPGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 545 VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQM 624
Cdd:PLN03073 562 SSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKI 641
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 625 TMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRALLQ 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: 559.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEV-AGDDTPALQ 252
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAgelepdSGEVSIPKGLRIGYLPQEPpLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 SVLESDTVREDLLRQERELSLRIAAGRAEGSEaaqLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGW 332
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLER---LAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETF 412
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 413 IKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKESEVVLKFPDGfEKFSPPIL 492
Cdd:COG0488 238 LEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPP-ERLGKKVL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 493 QLDEVDFYYDPKHsIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHvEQLDLNV 572
Cdd:COG0488 317 ELEGLSKSYGDKT-LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPDK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 SAVELLARKFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQA 652
Cdd:COG0488 395 TVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 29789050 653 LNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRA 697
Cdd:COG0488 475 LDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
188-707 |
4.88e-124 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 383.37 E-value: 4.88e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAGDDTPALQSVLESDtvR 261
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEisadggSYTFPGNWQLAWVNQETPALPQPALEYVIDGD--R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 262 EdlLRQeRELSLRIAAGRAEGSeaaQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARA 341
Cdd:PRK10636 90 E--YRQ-LEAQLHDANERNDGH---AIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 342 LFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERLL 421
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 422 NQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKP--VDKESEVVLKFPdgfEKFSPPILQLDEVDF 499
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPahVDNPFHFSFRAP---ESLPNPLLKMEKVSA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 500 YYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLA 579
Cdd:PRK10636 321 GYGDR-IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQHLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 580 RKFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG 659
Cdd:PRK10636 400 RLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 29789050 660 VILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRALLQEQFRREG 707
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQEN 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
181-670 |
1.66e-90 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 292.57 E-value: 1.66e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ENFDVSFGDrvllagadvnlawGRRYGLVGRNGLGKTTLLKMLA--------TRSLRVPAHISLLHVEQeVAGDDtpalQ 252
Cdd:PRK15064 18 ENISVKFGG-------------GNRYGLIGANGCGKSTFMKILGgdlepsagNVSLDPNERLGKLRQDQ-FAFEE----F 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 SVLesDTV---REDL--LRQERElslRIAAgRAEGSEA--AQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPT 325
Cdd:PRK15064 80 TVL--DTVimgHTELweVKQERD---RIYA-LPEMSEEdgMKVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYGLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGY 405
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 406 RGDFETFIKSK---QERLLNQQREYEAQQqyrQHIQVFIDRFRYNANRASQVQSKLKMLEK--LPELKPVDKESEVVlKF 480
Cdd:PRK15064 234 PGNYDEYMTAAtqaRERLLADNAKKKAQI---AELQSFVSRFSANASKAKQATSRAKQIDKikLEEVKPSSRQNPFI-RF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 481 PDGfEKFSPPILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYF 560
Cdd:PRK15064 310 EQD-KKLHRNALEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYY 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHVEQLDLNVSAVELLAR-KFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:PRK15064 388 AQDHAYDFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTN 467
|
490 500 510
....*....|....*....|....*....|.
gi 29789050 640 HLDMETIEALGQALNNFRGGVILVSHDERFI 670
Cdd:PRK15064 468 HMDMESIESLNMALEKYEGTLIFVSHDREFV 498
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
178-692 |
5.29e-71 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 243.32 E-value: 5.29e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRslrVPAHISLLHVEQEVagddtpaLQSVLES 257
Cdd:PRK11147 4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGE---VLLDDGRIIYEQDL-------IVARLQQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVRE-----------------DLLRQERELSLRIAAgraEGSEA--AQLAEIYGKLEEIEADKAPARASVILAGLGFTP 318
Cdd:PRK11147 74 DPPRNvegtvydfvaegieeqaEYLKRYHDISHLVET---DPSEKnlNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 319 KMqqqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:PRK11147 151 DA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 399 SQRLDGYRGDFETFIKSKQERL---LNQQREYE---AQQQY--RQHIQVFIDRF--RYNANRA-----SQ---VQSKLKM 460
Cdd:PRK11147 228 RGKLVSYPGNYDQYLLEKEEALrveELQNAEFDrklAQEEVwiRQGIKARRTRNegRVRALKAlrrerSErreVMGTAKM 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 461 leklpELKPVDKESEVVlkfpdgFEkfsppilqLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMG 540
Cdd:PRK11147 308 -----QVEEASRSGKIV------FE--------MENVNYQIDGK-QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 541 DLSPVRGIRHAHRNLKIGYFSQHHvEQLDLNVSAVELLARkfpGLPEEEY----RHQLG---RYGISGELAMRPVASLSG 613
Cdd:PRK11147 368 QLQADSGRIHCGTKLEVAYFDQHR-AELDPEKTVMDNLAE---GKQEVMVngrpRHVLGylqDFLFHPKRAMTPVKALSG 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 614 GQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCE-NGSVTRVEGGF 692
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRYVGGY 523
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
197-697 |
6.59e-58 |
|
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: 205.55 E-value: 6.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAW--GRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEvagddtPALQsvlESDTVRE------ 262
Cdd:TIGR03719 23 DISLSFfpGAKIGVLGLNGAGKSTLLRIMAgvdkdfNGEARPQPGIKVGYLPQE------PQLD---PTKTVREnveegv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 263 ----DLLRQERELSLRIAAgraEGSEAAQLAEIYGKLEE-IEADKA---PARASVILAGLGFTPKmqQQPTREFSGGWRM 334
Cdd:TIGR03719 94 aeikDALDRFNEISAKYAE---PDADFDKLAAEQAELQEiIDAADAwdlDSQLEIAMDALRCPPW--DADVTKLSGGERR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIK 414
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 415 SKQERLLNQQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSKLKmLEKLPELKPVDKEsevvlKFPDGFEKFSPP---- 490
Cdd:TIGR03719 249 QKQKRLEQEEKEESARQKTLKRELEWV---RQSP-KGRQAKSKAR-LARYEELLSQEFQ-----KRNETAEIYIPPgprl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ---ILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHvEQ 567
Cdd:TIGR03719 319 gdkVIEAENLTKAFGDK-LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSR-DA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 LDLNVSAVELLA----------RKFPGlpeeeyRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:TIGR03719 397 LDPNKTVWEEISggldiiklgkREIPS------RAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 638 TNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGS-VTRVEGGFDQYRA 697
Cdd:TIGR03719 471 TNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDShVEWFEGNFSEYEE 531
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
188-697 |
3.78e-50 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 184.17 E-value: 3.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 188 GDRVLLAgaDVNLAW--GRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEvagddtPALQsvlESDT 259
Cdd:PRK11819 18 PKKQILK--DISLSFfpGAKIGVLGLNGAGKSTLLRIMAgvdkefEGEARPAPGIKVGYLPQE------PQLD---PEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 VRE----------DLLRQERELSLRIAAGRAEGSEaaqLAEIYGKLEE-IEADKA---PARASVILAGLGFTPKmqQQPT 325
Cdd:PRK11819 87 VREnveegvaevkAALDRFNEIYAAYAEPDADFDA---LAAEQGELQEiIDAADAwdlDSQLEIAMDALRCPPW--DAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGY 405
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 406 RGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIdrfRYNAnRASQVQSK--LKMLEKLpelkpVDKESEvvlKFPDG 483
Cdd:PRK11819 242 EGNYSSWLEQKAKRLAQEEKQEAARQKALKRELEWV---RQSP-KARQAKSKarLARYEEL-----LSEEYQ---KRNET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 484 FEKFSPP-------ILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLK 556
Cdd:PRK11819 310 NEIFIPPgprlgdkVIEAENLSKSFGDR-LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQHHvEQLD---------------LNVSAVELLARKFpglpeeeyrhqLGRYGISGELAMRPVASLSGGQKSRVAF 621
Cdd:PRK11819 389 LAYVDQSR-DALDpnktvweeisggldiIKVGNREIPSRAY-----------VGRFNFKGGDQQKKVGVLSGGERNRLHL 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 622 AQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCE-NGSVTRVEGGFDQYRA 697
Cdd:PRK11819 457 AKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEgDSQVEWFEGNFQEYEE 533
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
492-683 |
1.64e-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: 1.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQhhveqldln 571
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 vsavellarkfpglpeeeyrhqlgrygisgelamrpvasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQ 651
Cdd:cd03221 71 ---------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE 111
|
170 180 190
....*....|....*....|....*....|..
gi 29789050 652 ALNNFRGGVILVSHDERFIRLVCKELWVCENG 683
Cdd:cd03221 112 ALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
178-401 |
7.40e-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: 165.31 E-value: 7.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA--------------------GELEPDEGIVTWG 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQerelslriaagraegseaaqlaeiygkleeieadkaparasvilaglgftpkmqqqptreFSGGWRMRLA 337
Cdd:cd03221 61 STVKIGYFEQ------------------------------------------------------------LSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 338 LARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
109-414 |
2.21e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 167.16 E-value: 2.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 109 LLKREQS----STVNAKKLEKAEARLKAKQE-KRSEKETLKTSNPLVLEEAsasqagsrkesrlESSGKnksyDV-RIEN 182
Cdd:COG0488 258 KIAKEEEfirrFRAKARKAKQAQSRIKALEKlEREEPPRRDKTVEIRFPPP-------------ERLGK----KVlELEG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 183 FDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAGDDtpalqsvlE 256
Cdd:COG0488 321 LSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGElepdsgTVKLGETVKIGYFDQHQEELD--------P 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 SDTVREdllrqerelslriaagraegseaaQLAEIYGKLEEIEadkapARAsvILAGLGFTPKMQQQPTREFSGGWRMRL 336
Cdd:COG0488 393 DKTVLD------------------------ELRDGAPGGTEQE-----VRG--YLGRFLFSGDDAFKPVGVLSGGEKARL 441
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 337 ALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIK 414
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLE 519
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
507-706 |
1.42e-41 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 159.07 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 507 IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHVEQLDLNV---------SAVEL 577
Cdd:COG0488 13 LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVldtvldgdaELRAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 578 LARKF-----PGLPEEEYRHQ----------------------LGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPN 630
Cdd:COG0488 93 EAELEeleakLAEPDEDLERLaelqeefealggweaearaeeiLSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 631 FYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRALLQEQFRRE 706
Cdd:COG0488 173 LLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYLEQRAERLEQE 248
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
178-689 |
5.09e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.43 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF--GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPAHISllhVEQEVAGDDTPALQSVL 255
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALM-GLLPHGGRIS---GEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 256 ESDTVRedLLRQERELSL---RIAAGRAEGSEAAQLAeiygkleeieADKAPARASVILAGLGFTPKMQQQPTrEFSGGW 332
Cdd:COG1123 81 RGRRIG--MVFQDPMTQLnpvTVGDQIAEALENLGLS----------RAEARARVLELLEAVGLERRLDRYPH-QLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWP-STILVVSHDRNFLNAIATDIIHLHSQRLdgyrgd 408
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVttqAEILDLLRELQRERgTTVLLITHDLGVVAEIADRVVVMDDGRI------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 409 fetfikskQErllnqqreyeaqqqyrqhiqvfidrfrynANRASQVQSKLKMLEKLPELKPVDKESEVVlkfpdgfEKFS 488
Cdd:COG1123 222 --------VE-----------------------------DGPPEEILAAPQALAAVPRLGAARGRAAPA-------AAAA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 489 PPILQLDEVDFYYDPKHSIFSRL--SVSADLES--RICVVGENGAGKSTMLKLLMG--------------DLSPVRGIRH 550
Cdd:COG1123 258 EPLLEVRNLSKRYPVRGKGGVRAvdDVSLTLRRgeTLGLVGESGSGKSTLARLLLGllrptsgsilfdgkDLTKLSRRSL 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 551 AHRNLKIGYFSQHHVEQLDLNVSAVELLA---RKFPGLPEEEYRHQ----LGRYGISGELAMRPVASLSGGQKSRVAFAQ 623
Cdd:COG1123 338 RELRRRVQMVFQDPYSSLNPRMTVGDIIAeplRLHGLLSRAERRERvaelLERVGLPPDLADRYPHELSGGQRQRVAIAR 417
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 624 MTMPCPNFYILDEPTNHLD-------METIEALGQALNnfrGGVILVSHDERFIRLVCKELWVCENGSVtrVE 689
Cdd:COG1123 418 ALALEPKLLILDEPTSALDvsvqaqiLNLLRDLQRELG---LTYLFISHDLAVVRYIADRVAVMYDGRI--VE 485
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
488-674 |
2.10e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.81 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL-----KIGYFS 561
Cdd:COG1121 3 MMPAIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGtVRLFGKPPrrarrRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 562 QHHVEQLDLNVSAVELLA-------RKFPGLPEEEY---RHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:COG1121 82 QRAEVDWDFPITVRDVVLmgrygrrGLFRRPSRADReavDEALERVGLE-DLADRPIGELSGGQQQRVLLARALAQDPDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 632 YILDEPTNHLDMETIEALGQALNNFRG---GVILVSHD-----ERFIRLVC 674
Cdd:COG1121 161 LLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavrEYFDRVLL 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-666 |
1.97e-29 |
|
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: 116.09 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 493 QLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLKIGYFSQHHVE 566
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPtsgsirVFGKPLEKERKRIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 567 QLDLNVSAVELLA-------RKFPGLPEEEYR---HQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03235 80 DRDFPISVRDVVLmglyghkGLFRRLSKADKAkvdEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|...
gi 29789050 637 PTNHLDMETIEALGQALNNFRG---GVILVSHD 666
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRRegmTILVVTHD 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
179-402 |
2.25e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 116.88 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLhveqeVAGDDtpalqSVLESD 258
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAG--LLKPDSGSIL-----IDGED-----VRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 TVREDL--LRQERELSLRIAAgraegseaAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQpTREFSGGWRMRL 336
Cdd:COG4555 71 EARRQIgvLPDERGLYDRLTV--------RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRR-VGELSTGMKKKV 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 337 ALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW---PSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
491-666 |
4.49e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 113.60 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGY 559
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGeVLLDGRDLaslsrrelarRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHVEQLDLNVSAVELLARK-----FPGLPEEEYR---HQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGRYphlglFGRPSAEDREaveEALERTGLE-HLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 632 YILDEPTNHLDM----ETIEALgQALNNFRG-GVILVSHD 666
Cdd:COG1120 159 LLLDEPTSHLDLahqlEVLELL-RRLARERGrTVVMVLHD 197
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
179-402 |
8.11e-28 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.45 E-value: 8.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPA--HISLLhvEQEVAGDDTPAL----- 251
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALA--DLDPPTsgEIYLD--GKPLSAMPPPEWrrqva 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 ----QSVLESDTVREDLlrqerelslriaagraegSEAAQLAEIYGKLEEIEADkaparasviLAGLGFTPKMQQQPTRE 327
Cdd:COG4619 78 yvpqEPALWGGTVRDNL------------------PFPFQLRERKFDRERALEL---------LERLGLPPDILDKPVER 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:COG4619 131 LSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
395-477 |
9.98e-28 |
|
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: 106.89 E-value: 9.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 395 IHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFRYNANRASQVQSKLKMLEKLPELKPVDKES 474
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
...
gi 29789050 475 EVV 477
Cdd:pfam12848 81 PKL 83
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
178-397 |
3.83e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.49 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRV---------PAHISLLHVEQEVA--GD 246
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSagevlwngePIRDAREDYRRRLAylGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DtPALQSVLesdTVREDLlrqerELSLRIAAGRAEGSEAAQLAEIYGkleeieadkaparasviLAGLgftpkmQQQPTR 326
Cdd:COG4133 83 A-DGLKPEL---TVRENL-----RFWAALYGLRADREAIDEALEAVG-----------------LAGL------ADLPVR 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRnfLNAIATDIIHL 397
Cdd:COG4133 131 QLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQP--LELAAARVLDL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
123-420 |
5.29e-27 |
|
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: 115.80 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 123 LEKAEARLKakQEKRSEKETLKT-SNPL--VLEEASASQAGSRkeSRL---------ESSGKNKSYDVRI---------- 180
Cdd:TIGR03719 247 LEQKQKRLE--QEEKEESARQKTlKRELewVRQSPKGRQAKSK--ARLaryeellsqEFQKRNETAEIYIppgprlgdkv 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ---ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:TIGR03719 323 ieaENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT--------------------GQEQPDSGTIEIG 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQERElslriaagrAEGSEAAQLAEIYGKLEEIEADKA--PARASVilAGLGFTPKMQQQPTREFSGGWRMR 335
Cdd:TIGR03719 383 ETVKLAYVDQSRD---------ALDPNKTVWEEISGGLDIIKLGKReiPSRAYV--GRFNFKGSDQQKKVGQLSGGERNR 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 336 LALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ-RLDGYRGDFETFIK 414
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEYEE 531
|
....*.
gi 29789050 415 SKQERL 420
Cdd:TIGR03719 532 DKKRRL 537
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
178-383 |
8.80e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 109.38 E-value: 8.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisLLHVEQ---EVAGDDTPAlqsv 254
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLG----------LLRPTSgevRVLGEDVAR---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 lESDTVREDL--LRQE----RELSLRiaagraegseaaQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQqPTREF 328
Cdd:COG1131 67 -DPAEVRRRIgyVPQEpalyPDLTVR------------ENLRFFARLYGLPRKEARERIDELLELFGLTDAADR-KVGTL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 383
Cdd:COG1131 133 SGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
492-685 |
2.47e-25 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 104.72 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgyfsqhHVEQLDLN 571
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSG--------EV------LVDGKDIT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 VSAVELLARK------FP--------------------GLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAF 621
Cdd:COG1122 67 KKNLRELRRKvglvfqNPddqlfaptveedvafgpenlGLPREEIRERveeaLELVGLE-HLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 622 AQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:COG1122 146 AGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
493-683 |
8.37e-25 |
|
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: 101.17 E-value: 8.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 493 QLDEVDFYYdPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIrhahrnlkigyfsqhhveqldlnv 572
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGE------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 saVELLARKFPGLPEEEYRHQLGRygisgelamrpVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQA 652
Cdd:cd00267 56 --ILIDGKDIAKLPLEELRRRIGY-----------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|....
gi 29789050 653 LNNFRGG---VILVSHDERFIRLVCKELWVCENG 683
Cdd:cd00267 123 LRELAEEgrtVIIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
123-420 |
3.63e-24 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 107.13 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 123 LEKAEARLKakQEKRSEKETLKT---------SNPlvleeaSASQAGSRkeSRL---------ESSGKNKSYDVRI---- 180
Cdd:PRK11819 249 LEQKAKRLA--QEEKQEAARQKAlkrelewvrQSP------KARQAKSK--ARLaryeellseEYQKRNETNEIFIppgp 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ---------ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------SLRVPAHISLLHVEQEVAG 245
Cdd:PRK11819 319 rlgdkvieaENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQeqpdsgTIKIGETVKLAYVDQSRDA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 246 DDtpalqsvlESDTVREdllrqerelslriaagraegseaaqlaEIYGKLEEIEADKA--PARASVilAGLGFTPKMQQQ 323
Cdd:PRK11819 399 LD--------PNKTVWE---------------------------EISGGLDIIKVGNReiPSRAYV--GRFNFKGGDQQK 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 324 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAilwLENYLQTWPSTILVVSHDRNFLNAIATDIIhlhSQ 400
Cdd:PRK11819 442 KVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVetlRA---LEEALLEFPGCAVVISHDRWFLDRIATHIL---AF 515
|
330 340
....*....|....*....|....
gi 29789050 401 RLDG----YRGDFETFIKSKQERL 420
Cdd:PRK11819 516 EGDSqvewFEGNFQEYEEDKKRRL 539
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
179-401 |
3.82e-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: 99.24 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqsvlesd 258
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 tvredllrqereLSLRIAAGRAEgseaaqlaeIYGKleeieaDKAPARASVILAGLGFTPkmqqqptrEFSGGWRMRLAL 338
Cdd:cd00267 47 ------------GLLKPTSGEIL---------IDGK------DIAKLPLEELRRRIGYVP--------QLSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 339 ARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP---STILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
178-464 |
9.45e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 106.41 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahisllhveqevAGDDTPalqsvles 257
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLL--------------------AGELAP-------- 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvredllrQERELSLriaagrAEGSEAAQLAEiyGKLEEIEADKAPARASVILA-------------GLGFTPKMQQQP 324
Cdd:PRK10636 365 ---------VSGEIGL------AKGIKLGYFAQ--HQLEFLRADESPLQHLARLApqeleqklrdylgGFGFQGDKVTEE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 325 TREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDG 404
Cdd:PRK10636 428 TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEP 507
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 405 YRGDFETFikskQERLLNQQREYEAQQQYRQHI-----QVFIDRFRYNANRASQVQSKLKMLEKL 464
Cdd:PRK10636 508 FDGDLEDY----QQWLSDVQKQENQTDEAPKENnansaQARKDQKRREAELRTQTQPLRKEIARL 568
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
178-402 |
5.01e-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: 97.67 E-value: 5.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLH-------VEQEVAGDDTPA 250
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----------GLIKpdsgeitFDGKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 LQ---SVLESDTVREDLLRQErelSLRIaagraegseaaqLAEIYGKLEEieadkapaRASVILA--GLGFTPKmqqQPT 325
Cdd:cd03268 71 LRrigALIEAPGFYPNLTARE---NLRL------------LARLLGIRKK--------RIDEVLDvvGLKDSAK---KKV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03268 125 KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDqgiTVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
178-402 |
6.62e-23 |
|
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: 95.93 E-value: 6.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPahisllhveqevagddtpalqsvlES 257
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILG--LLKP------------------------DS 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVR---EDLLRQERELSLRIAAgraegseAAQLAEIYGKLeeieadkaparaSVI--LaglgftpkmqqqptrEFSGGW 332
Cdd:cd03230 55 GEIKvlgKDIKKEPEEVKRRIGY-------LPEEPSLYENL------------TVRenL---------------KLSGGM 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03230 101 KQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKegkTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
493-686 |
1.21e-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: 1.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 493 QLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgYFSQHHVEQLdlnv 572
Cdd:cd03214 1 EVENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSG--------EI-LLDGKDLASL---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 SAVElLARKFPGLPeeeyrhQ-LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------ME 644
Cdd:cd03214 67 SPKE-LARKIAYVP------QaLELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahqielLE 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 645 TIEALGQALNNfrgGVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:cd03214 139 LLRRLARERGK---TVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
488-702 |
2.32e-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: 101.76 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLK 556
Cdd:COG4988 333 GPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGsilingvdlsdLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQH-HVEQLDL--NVsaveLLARkfPGLPEEEYRHQLGRYGISGELAMRPV----------ASLSGGQKSRVAFAQ 623
Cdd:COG4988 413 IAWVPQNpYLFAGTIreNL----RLGR--PDASDEELEAALEAAGLDEFVAALPDgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 624 MTM-PCPnFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLvCKELWVCENGSVtrVEGGfdQYRALLQ 700
Cdd:COG4988 487 ALLrDAP-LLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALLAQ-ADRILVLDDGRI--VEQG--THEELLA 560
|
..
gi 29789050 701 EQ 702
Cdd:COG4988 561 KN 562
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
179-401 |
3.95e-22 |
|
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: 95.23 E-value: 3.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLhvEQEVAGDDT-------- 248
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIkkGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD--GKDLTKLSLkelrrkvg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 -----PALQsvLESDTVREDLlrqerelslriaagrAEGSEAAQLAEiygklEEIEAdkapaRASVILAGLGFTPkMQQQ 323
Cdd:cd03225 79 lvfqnPDDQ--FFGPTVEEEV---------------AFGLENLGLPE-----EEIEE-----RVEEALELVGLEG-LRDR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 324 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:cd03225 131 SPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
.
gi 29789050 401 R 401
Cdd:cd03225 211 K 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
490-679 |
3.98e-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: 94.85 E-value: 3.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIG---YFSQ--- 562
Cdd:COG4133 1 MMLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGeVLWNGEPIRDAredYRRRlay 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 --HHVEqLDLNVSAVELLA--RKFPGL--PEEEYRHQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:COG4133 80 lgHADG-LKPELTVRENLRfwAALYGLraDREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29789050 637 PTNHLDMETIEALGQALNNFR---GGVILVSHDERFIRlVCKELWV 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 ... |
178-688 |
4.65e-22 |
|
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: 100.26 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML------ATRSLRVPAHISL----LHVE-QEVAGD 246
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgmdqyEPTSGRIIYHVALcekcGYVErPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DTPALQSVLE---------SDTVREDLLRQ-----ERELSLRiaagraegSEAAQLAEIYGKLEEI--EADKAPARASVI 310
Cdd:TIGR03269 81 PCPVCGGTLEpeevdfwnlSDKLRRRIRKRiaimlQRTFALY--------GDDTVLDNVLEALEEIgyEGKEAVGRAVDL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 311 LAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDvrailwlenylqtwPSTilvvshdrnflnai 390
Cdd:TIGR03269 153 IEMVQLSHRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD--------------PQT-------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 391 aTDIIHlhsqrldgyrgdfetfikskqERLLNQQREYEAQQQYRQHIQVFIdrfrynanraSQVQSKLKMLEKlPELKPV 470
Cdd:TIGR03269 204 -AKLVH---------------------NALEEAVKASGISMVLTSHWPEVI----------EDLSDKAIWLEN-GEIKEE 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 471 DKESEVVLKFPDGFEKFSP--------PILQLDEVDFYYdpkHSIfSRLSVSA----DLESR----ICVVGENGAGKSTM 534
Cdd:TIGR03269 251 GTPDEVVAVFMEGVSEVEKecevevgePIIKVRNVSKRY---ISV-DRGVVKAvdnvSLEVKegeiFGIVGTSGAGKTTL 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 535 LKLLMGDLSPV-----------------RGIRHAHRNLK-IGYFSQH-----HVEQLDLNVSAVEL-----LAR------ 580
Cdd:TIGR03269 327 SKIIAGVLEPTsgevnvrvgdewvdmtkPGPDGRGRAKRyIGILHQEydlypHRTVLDNLTEAIGLelpdeLARmkavit 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 581 -KFPGLPEEEYRHQLGRYgisgelamrpVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG 659
Cdd:TIGR03269 407 lKMVGFDEEKAEEILDKY----------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREE 476
|
570 580 590
....*....|....*....|....*....|...
gi 29789050 660 V----ILVSHDERFIRLVCKELWVCENGSVTRV 688
Cdd:TIGR03269 477 MeqtfIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
500-683 |
5.79e-22 |
|
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: 94.46 E-value: 5.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 500 YYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGY--------F 560
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGeVLVDGKDLtklslkelrrKVGLvfqnpddqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHVEQlDLNVSAVELlarkfpGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03225 89 FGPTVEE-EVAFGLENL------GLPEEEIEERveeaLELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 637 PTNHLDMETIEALGQALNNFRG---GVILVSHDERFIRLVCKELWVCENG 683
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
184-402 |
7.17e-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: 94.71 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 184 DVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQ---EVAGDDT--------- 248
Cdd:COG1122 5 NLSFsypGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN----------GLLKPTSgevLVDGKDItkknlrelr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 ---------PALQSVleSDTVREDLlrqerelslriaagrAEGSEAAQLAEiygklEEIEAdkapaRASVILAGLGFTpK 319
Cdd:COG1122 75 rkvglvfqnPDDQLF--APTVEEDV---------------AFGPENLGLPR-----EEIRE-----RVEEALELVGLE-H 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 320 MQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIH 396
Cdd:COG1122 127 LADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIV 206
|
....*.
gi 29789050 397 LHSQRL 402
Cdd:COG1122 207 LDDGRI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
520-639 |
1.83e-21 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 91.17 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 520 RICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLKIGYFSQHHveQLDLNVSAVE--LLARKFPGLP 586
Cdd:pfam00005 13 ILALVGPNGAGKSTLLKLIAGLLSPTEGtilldgqdltdDERKSLRKEIGYVFQDP--QLFPRLTVREnlRLGLLLKGLS 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 E-------EEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:pfam00005 91 KrekdaraEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
491-681 |
2.59e-21 |
|
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: 98.47 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHhvEQLDL 570
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQE--PQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 571 ------NV-----SAVELLAR-------------KFPGLPEEEYR----------HQLGRygiSGELAM---------RP 607
Cdd:TIGR03719 82 tktvreNVeegvaEIKDALDRfneisakyaepdaDFDKLAAEQAElqeiidaadaWDLDS---QLEIAMdalrcppwdAD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 608 VASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKelWVCE 681
Cdd:TIGR03719 159 VTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAG--WILE 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
521-685 |
3.33e-21 |
|
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: 91.31 E-value: 3.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlkigyfsqhHVEQLDLNVSAVELLARKFPG-LPEEEYrhqlgrygI 599
Cdd:cd03230 29 YGLLGPNGAGKTTLIKIILGLLKPDSG----------------EIKVLGKDIKKEPEEVKRRIGyLPEEPS--------L 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 600 SGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR---GGVILVSHDERFIRLVCKE 676
Cdd:cd03230 85 YENLTVRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDR 164
|
....*....
gi 29789050 677 LWVCENGSV 685
Cdd:cd03230 165 VAILNNGRI 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
99-416 |
3.55e-21 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 97.65 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 99 NYDcDTKLPGLLKREQSSTVNAKKLEK-AE-----ARL-----KAKQ----EKRSEKetlktsnpLVLEEASASqagSRK 163
Cdd:PRK15064 236 NYD-EYMTAATQARERLLADNAKKKAQiAElqsfvSRFsanasKAKQatsrAKQIDK--------IKLEEVKPS---SRQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 164 ES--RLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveq 241
Cdd:PRK15064 304 NPfiRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV----------------- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 242 evaGDDTPALQSVLESDTVREDLLRQERElslriaagrAEGSEAAQLAEIYGKLEEIEADKAPARAsvILAGLGFTPKMQ 321
Cdd:PRK15064 367 ---GELEPDSGTVKWSENANIGYYAQDHA---------YDFENDLTLFDWMSQWRQEGDDEQAVRG--TLGRLLFSQDDI 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 322 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:PRK15064 433 KKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
330
....*....|....*
gi 29789050 402 LDGYRGDFETFIKSK 416
Cdd:PRK15064 513 VVDFSGTYEEYLRSQ 527
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
513-683 |
3.62e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 92.19 E-value: 3.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGYFSQH------HVEQldlNVS 573
Cdd:COG4619 19 VSLTLEAgeCVAITGPSGSGKSTLLRALADLDPPTSGeIYLDGKPLsampppewrrQVAYVPQEpalwggTVRD---NLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 574 AVELLARKFPglPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQAL 653
Cdd:COG4619 96 FPFQLRERKF--DRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
|
170 180 190
....*....|....*....|....*....|....
gi 29789050 654 NNFR----GGVILVSHDERFIRLVCKELWVCENG 683
Cdd:COG4619 174 REYLaeegRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
521-672 |
4.78e-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: 92.17 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGI---------------RHAHRNLKIGY-FSQHH------VEQldlNVSAVELL 578
Cdd:cd03255 33 VAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgtdisklsekeLAAFRRRHIGFvFQSFNllpdltALE---NVELPLLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 579 ARKFPGLPEEEYRHQLGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGQALNN 655
Cdd:cd03255 110 AGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkeVMELLRELNK 188
|
170
....*....|....*...
gi 29789050 656 FRG-GVILVSHDERFIRL 672
Cdd:cd03255 189 EAGtTIVVVTHDPELAEY 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
203-356 |
1.13e-20 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 88.86 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHveQEVAGDDTPALQ---SVLESD-------TVREDLLrqerels 272
Cdd:pfam00005 11 GEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG--QDLTDDERKSLRkeiGYVFQDpqlfprlTVRENLR------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 lriaagraegseaaqlaeIYGKLEEIEADKAPARASVILAGLGFTPKM---QQQPTREFSGGWRMRLALARALFARPDLL 349
Cdd:pfam00005 82 ------------------LGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLL 143
|
....*..
gi 29789050 350 LLDEPTN 356
Cdd:pfam00005 144 LLDEPTA 150
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
461-702 |
4.01e-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: 95.29 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 461 LEKLPELkpVDKESEVvlkfPDGFEKFSPPILQ----LDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTML 535
Cdd:COG2274 445 LERLDDI--LDLPPER----EEGRSKLSLPRLKgdieLENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 536 KLLMGDLSPVRG--------IRHAHRNL---KIGYFSQHhvEQLdLNVSAVE--LLARkfPGLPEEEYRHQLGRYGISGE 602
Cdd:COG2274 519 KLLLGLYEPTSGrilidgidLRQIDPASlrrQIGVVLQD--VFL-FSGTIREniTLGD--PDATDEEIIEAARLAGLHDF 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 603 LAMRP----------VASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFI 670
Cdd:COG2274 594 IEALPmgydtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGrtVIIIAHRLSTI 673
|
250 260 270
....*....|....*....|....*....|....*....
gi 29789050 671 RLvCKELWVCENGSVTRvEGGFDQ-------YRALLQEQ 702
Cdd:COG2274 674 RL-ADRIIVLDKGRIVE-DGTHEEllarkglYAELVQQQ 710
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
492-683 |
5.76e-20 |
|
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: 87.44 E-value: 5.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPK-HSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgYFSQHHVEQLDL 570
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSG--------EI-LIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 571 nvsavellarkfpglpeEEYRHQLG-------------RYGIsgelamrpvasLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03228 72 -----------------ESLRKNIAyvpqdpflfsgtiRENI-----------LSGGQRQRIAIARALLRDPPILILDEA 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 638 TNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLvCKELWVCENG 683
Cdd:cd03228 124 TSALDPETEALILEALRALAKGktVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
498-686 |
6.97e-20 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 88.47 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 498 DFYYDPKHSIFSRLSVSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLKIGYFSQHHVEQ 567
Cdd:cd03226 4 NISFSYKKGTEILDDLSLDLYAGeiIALTGKNGAGKTTLAKILAGLIKESSGsillngkpIKAKERRKSIGYVMQDVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 LDLNVSAVELLAR-KFPGLPEEEYRHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI 646
Cdd:cd03226 84 LFTDSVREELLLGlKELDAGNEQAETVLKDLDLY-ALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29789050 647 EALGQALNNFRG---GVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:cd03226 163 ERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
492-685 |
8.42e-20 |
|
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: 89.15 E-value: 8.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHsIFSRLSVSADlESRI-CVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL---------KIGYF 560
Cdd:COG4555 2 IEVENLSKKYGKVP-ALKDVSFTAK-DGEItGLLGPNGAGKTTLLRMLAGLLKPDSGsILIDGEDVrkeprearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHVeqLDLNVSAVELLAR--KFPGLPEEEYRHQ----LGRYGISGELAMRpVASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:COG4555 80 PDERG--LYDRLTVRENIRYfaELYGLFDEELKKRieelIELLGLEEFLDRR-VGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 635 DEPTNHLDMETIEALGQALNNFRG---GVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
520-706 |
9.26e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 93.86 E-value: 9.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 520 RICVVGENGAGKSTMLKLLMGDLS--------------------PVR------------GIRHAHRNLKIGYFSQHHVEQ 567
Cdd:PRK11147 31 RVCLVGRNGAGKSTLMKILNGEVLlddgriiyeqdlivarlqqdPPRnvegtvydfvaeGIEEQAEYLKRYHDISHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 lDLNVSAVELLARKfpglpEEEYRHQ------------LGRYGISGElamRPVASLSGGQKSRVAFAQMTMPCPNFYILD 635
Cdd:PRK11147 111 -DPSEKNLNELAKL-----QEQLDHHnlwqlenrinevLAQLGLDPD---AALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 636 EPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGFDQYRALLQEQFRRE 706
Cdd:PRK11147 182 EPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVE 252
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
492-673 |
1.20e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 88.03 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDP-KHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLKIGY 559
Cdd:cd03245 3 IEFRNVSFSYPNqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGsvlldgtdirqLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHV-------EQL---DLNVSAVELL-ARKFPGLPEEEYRH------QLGRYGisgelamrpvASLSGGQKSRVAFA 622
Cdd:cd03245 83 VPQDVTlfygtlrDNItlgAPLADDERILrAAELAGVTDFVNKHpngldlQIGERG----------RGLSGGQRQAVALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 623 QMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLV 673
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDktLIIITHRPSLLDLV 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
524-666 |
1.30e-19 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 88.58 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLK--IGYFSQHHVeqLDLNVSAVELLA--RKFPGLPEEEYR 591
Cdd:COG1131 32 LGPNGAGKTTTIRMLLGLLRPTSGevrvlgedVARDPAEVRrrIGYVPQEPA--LYPDLTVRENLRffARLYGLPRKEAR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 592 HQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVS 664
Cdd:COG1131 110 ERidelLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEgktVLLST 188
|
..
gi 29789050 665 HD 666
Cdd:COG1131 189 HY 190
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
178-420 |
1.52e-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: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPA--HISLLhvEQEVAGDDTPALQSV- 254
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII--GLLRPDsgEILVD--GQDITGLSEKELYELr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 ------------LESDTVREDL---LRQERELSLriaagraegSEAAQLAEIygKLEEIE----ADKAPArasvilaglg 315
Cdd:COG1127 82 rrigmlfqggalFDSLTVFENVafpLREHTDLSE---------AEIRELVLE--KLELVGlpgaADKMPS---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 316 ftpkmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQ-TWPSTILVVSHDRNFLNAIA 391
Cdd:COG1127 141 -----------ELSGGMRKRVALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRdELGLTSVVVTHDLDSAFAIA 209
|
250 260
....*....|....*....|....*....
gi 29789050 392 TDIIHLHSQRLDGYrGDFETFIKSKQERL 420
Cdd:COG1127 210 DRVAVLADGKIIAE-GTPEELLASDDPWV 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
178-383 |
1.53e-19 |
|
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: 87.81 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisLLHVEQ---EVAGDDTpalqsV 254
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTT----------LLKPTSgraTVAGHDV-----V 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESDTVREDLLRQERELSL-RIAAGRaegseaaQLAEIYGKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWR 333
Cdd:cd03265 66 REPREVRRRIGIVFQDLSVdDELTGW-------ENLYIHARLYGVPGAERRERIDELLDFVGLLEA-ADRLVKTYSGGMR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLDV--RAILW--LENYLQTWPSTILVVSHD 383
Cdd:cd03265 138 RRLEIARSLVHRPEVLFLDEPTIGLDPqtRAHVWeyIEKLKEEFGMTILLTTHY 191
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
491-689 |
3.62e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.64 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL-------------K 556
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGqVLVNGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQHHveQL--DLNVSavELLArkFP----GLPEEEYRHQ----LGRYGISGELAMRPVAsLSGGQKSRVAFAQMTM 626
Cdd:COG2884 81 IGVVFQDF--RLlpDRTVY--ENVA--LPlrvtGKSRKEIRRRvrevLDLVGLSDKAKALPHE-LSGGEQQRVAIARALV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 627 PCPNFYILDEPTNHLDMETIEALGQALNNF-RGG--VILVSHDERFIRLVCKELWVCENGSVTRVE 689
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEInRRGttVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
178-402 |
4.94e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 87.17 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-------------TRSLRVPAHISLLHVE 240
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAglerpwsgevtfdGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 241 QEVAGDDTPAL---QSVLesDTVREdllrqerelSLRIAAGRAEGSEAAQLAEIYGkLEEIEADKAParasvilaglgft 317
Cdd:COG1124 82 QMVFQDPYASLhprHTVD--RILAE---------PLRIHGLPDREERIAELLEQVG-LPPSFLDRYP------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 318 pkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTWPSTILVVSHDRNFLNAIATD 393
Cdd:COG1124 137 --------HQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsVQAEILnlLKDLREERGLTYLFVSHDLAVVAHLCDR 208
|
....*....
gi 29789050 394 IIHLHSQRL 402
Cdd:COG1124 209 VAVMQNGRI 217
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
130-393 |
5.64e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.17 E-value: 5.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 130 LKAKQEKRSEKETLKTSNPLVLEEASasqagsrkesrleSSGKnksYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLV 209
Cdd:PRK11147 288 LKALRRERSERREVMGTAKMQVEEAS-------------RSGK---IVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALI 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 210 GRNGLGKTTLLKM----LATRSLRVPAHISLlhveqEVAgddtpalqsvlESDTVREDLlrqerelslriaagRAEGSEA 285
Cdd:PRK11147 352 GPNGCGKTTLLKLmlgqLQADSGRIHCGTKL-----EVA-----------YFDQHRAEL--------------DPEKTVM 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 286 AQLAEiyGKlEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARaLFARP-DLLLLDEPTNMLDVRAIL 364
Cdd:PRK11147 402 DNLAE--GK-QEVMVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLAR-LFLKPsNLLILDEPTNDLDVETLE 477
|
250 260
....*....|....*....|....*....
gi 29789050 365 WLENYLQTWPSTILVVSHDRNFLNAIATD 393
Cdd:PRK11147 478 LLEELLDSYQGTVLLVSHDRQFVDNTVTE 506
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
489-665 |
6.31e-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: 86.68 E-value: 6.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 489 PPILQLDEVDFYYDPKHsIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------------IRHa 551
Cdd:COG1119 1 DPLLELRNVTVRRGGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvweLRK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 552 hrnlKIGYFSQHHVEQLDLNVSAVELLARKF---PGL---PEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAF 621
Cdd:COG1119 79 ----RIGLVSPALQLRFPRDETVLDVVLSGFfdsIGLyrePTDEQRERarelLELLGLA-HLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 622 AQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG----VILVSH 665
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaptLVLVTH 201
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
501-681 |
1.86e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 89.41 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 501 YDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQhhvE-QLDL------NV- 572
Cdd:PRK11819 16 VPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ---EpQLDPektvreNVe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 ----SAVELLAR-------------KFPGLPEEEYR--------------HQLgrygisgELAM---R------PVASLS 612
Cdd:PRK11819 93 egvaEVKAALDRfneiyaayaepdaDFDALAAEQGElqeiidaadawdldSQL-------EIAMdalRcppwdaKVTKLS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 613 GGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKelWVCE 681
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG--WILE 232
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
522-666 |
2.21e-18 |
|
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: 84.48 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSPVRG------------IRHAHRNlkIGYFSQHHVeqLDLNVSAVELL---ARkFPGLP 586
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGtayingysirtdRKAARQS--LGYCPQFDA--LFDELTVREHLrfyAR-LKGLP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYRHQLGRYGISGEL---AMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VI 661
Cdd:cd03263 107 KSEIKEEVELLLRVLGLtdkANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGrsII 186
|
....*
gi 29789050 662 LVSHD 666
Cdd:cd03263 187 LTTHS 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
178-402 |
3.75e-18 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 83.72 E-value: 3.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIA--------------------GLERPDSGEILID 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQERELSL---------------RIAagraegseaaqlaeiYG-KLEEIEADKAPARASVILAGLGFTPKMQ 321
Cdd:cd03259 61 GRDVTGVPPERRNIGMvfqdyalfphltvaeNIA---------------FGlKLRGVPKAEIRARVRELLELVGLEGLLN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 322 QQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03259 126 RYP-HELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKElqreLGITTIYVTHDQEEALALADRIAVM 204
|
....*
gi 29789050 398 HSQRL 402
Cdd:cd03259 205 NEGRI 209
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
179-402 |
4.44e-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: 82.48 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPA-HISLlhveqevAGDDTPALQSvles 257
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLA-GLLKPSSgEILL-------DGKDLASLSP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvredllrqeRELSLRIAAgraegseAAQLaeiygkLEEIEADKaparasviLAglgftpkmqQQPTREFSGGWRMRLA 337
Cdd:cd03214 69 -----------KELARKIAY-------VPQA------LELLGLAH--------LA---------DRPFNELSGGERQRVL 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 338 LARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03214 108 LARALAQEPPILLLDEPTSHLDIAhqiELLeLLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
496-685 |
4.60e-18 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 83.50 E-value: 4.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 496 EVDFYYdpKHSIFSrLSVSADL-ESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL--------------KIGY 559
Cdd:cd03297 3 CVDIEK--RLPDFT-LKIDFDLnEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtIVLNGTVLfdsrkkinlppqqrKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHveQLDLNVSAVELLARKFPGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILD 635
Cdd:cd03297 80 VFQQY--ALFPHLNVRENLAFGLKRKRNREDRISvdelLDLLGLD-HLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 636 EPTNHLDMET----IEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:cd03297 157 EPFSALDRALrlqlLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
488-702 |
8.87e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 87.13 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDP-KHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLK--------- 556
Cdd:COG4987 330 GGPSLELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGsITLGGVDLRdldeddlrr 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 -IGYFSQH-HV------EQLdlnvsaveLLARkfPGLPEEEYRHQLGRYGISGELAMRPV----------ASLSGGQKSR 618
Cdd:COG4987 410 rIAVVPQRpHLfdttlrENL--------RLAR--PDATDEELWAALERVGLGDWLAALPDgldtwlgeggRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 619 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLVCkELWVCENGSVtrVEGGfdQYR 696
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGrtVLLITHRLAGLERMD-RILVLEDGRI--VEQG--THE 554
|
....*.
gi 29789050 697 ALLQEQ 702
Cdd:COG4987 555 ELLAQN 560
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
178-397 |
1.09e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAHISllHVEQEV 243
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILgllpptsgtvrlfgKPPRRARRRIG--YVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 244 AGD-DTPAlqsvlesdTVReDLlrqerelslrIAAGRAEGSeaaQLAEIYGKleeieADKAPARASVILAGLGftpKMQQ 322
Cdd:COG1121 85 EVDwDFPI--------TVR-DV----------VLMGRYGRR---GLFRRPSR-----ADREAVDEALERVGLE---DLAD 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 323 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHL 397
Cdd:COG1121 135 RPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL 212
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
450-673 |
1.31e-17 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 87.23 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 450 RASQVQSKLKMLEKLPELkPVDkesevvlkFPDGFEKFSPPILQ----LDEVDFYYdPKHSIFSRLSVSADLE--SRICV 523
Cdd:TIGR03375 427 RYQQAKTALQSLDELMQL-PVE--------RPEGTRFLHRPRLQgeieFRNVSFAY-PGQETPALDNVSLTIRpgEKVAI 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRG--------IRHAH-----RNlkIGYFSQHHV-------EQLDLNVSAVE----LLA 579
Cdd:TIGR03375 497 IGRIGSGKSTLLKLLLGLYQPTEGsvlldgvdIRQIDpadlrRN--IGYVPQDPRlfygtlrDNIALGAPYADdeeiLRA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 580 RKFPGLPEEEYRHQLGrygisgeLAMrPV----ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNN 655
Cdd:TIGR03375 575 AELAGVTEFVRRHPDG-------LDM-QIgergRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKR 646
|
250 260
....*....|....*....|
gi 29789050 656 FRGG--VILVSHDERFIRLV 673
Cdd:TIGR03375 647 WLAGktLVLVTHRTSLLDLV 666
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
173-402 |
1.34e-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: 86.74 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 173 NKSYDVRIEnfDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHVE-QEVAGD 246
Cdd:COG4987 329 PGGPSLELE--DVSFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALL-LRFLDPQSgSITLGGVDlRDLDED 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DTPALQSVLE------SDTVREDLlrqerelslRIAAGRAEGSEAAQLAEiygkleeieadkaparasviLAGLGftPKM 320
Cdd:COG4987 406 DLRRRIAVVPqrphlfDTTLRENL---------RLARPDATDEELWAALE--------------------RVGLG--DWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 321 QQQPT----------REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWP-STILVVSHDRNF 386
Cdd:COG4987 455 AALPDgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAateQAL--LADLLEALAgRTVLLITHRLAG 532
|
250
....*....|....*.
gi 29789050 387 LnAIATDIIHLHSQRL 402
Cdd:COG4987 533 L-ERMDRILVLEDGRI 547
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
183-407 |
2.23e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 81.65 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 183 FDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisLLHVEQ---EVAGDDTpalqsvlesdt 259
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAG----------LLEPDAgfaTVDGFDV----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 vredlLRQERELSLRIA---AGRA--EGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRM 334
Cdd:cd03266 70 -----VKEPAEARRRLGfvsDSTGlyDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDR-RVGGFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLdGYRG 407
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVmatRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV-VYEG 218
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
523-685 |
2.77e-17 |
|
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: 82.17 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSP-----------VRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLAR-----KFPGLP 586
Cdd:TIGR03873 32 LLGPNGSGKSTLLRLLAGALRPdagtvdlagvdLHGLSRRARARRVALVEQDSDTAVPLTVRDVVALGRiphrsLWAGDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEY---RHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGQaLNNFRGG 659
Cdd:TIGR03873 112 PHDAavvDRALARTELS-HLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDvraqLETLALVRE-LAATGVT 189
|
170 180
....*....|....*....|....*.
gi 29789050 660 VILVSHDERFIRLVCKELWVCENGSV 685
Cdd:TIGR03873 190 VVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
179-397 |
3.21e-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: 80.76 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDDTPA------- 250
Cdd:cd03226 1 RIENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA--GLIKESSGSIL-----LNGKPIKAkerrksi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 ---LQSV---LESDTVREDLLrqereLSLRiaagraegseaaqlaeiygkleeiEADKAPARASVILAGLGFTPKMQQQP 324
Cdd:cd03226 74 gyvMQDVdyqLFTDSVREELL-----LGLK------------------------ELDAGNEQAETVLKDLDLYALKERHP 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 325 tREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03226 125 -LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
158-383 |
3.87e-17 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 85.10 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 158 QAGSRKESRLESSGKNKSYDVRIENFDVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAH- 233
Cdd:TIGR02868 313 AAGPVAEGSAPAAGAVGLGKPTLELRDLSAgypGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLA--GLLDPLQg 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 234 -ISLLHVE-QEVAGDDTPALQSVLESD------TVREDLlrqerelslRIAAGRAEGSEAAQLAEIYGKLEEIEAdkAPA 305
Cdd:TIGR02868 391 eVTLDGVPvSSLDQDEVRRRVSVCAQDahlfdtTVRENL---------RLARPDATDEELWAALERVGLADWLRA--LPD 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 306 RASVILAGLGftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL-WLENYLQTWPS-TILVVSHD 383
Cdd:TIGR02868 460 GLDTVLGEGG----------ARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADeLLEDLLAALSGrTVVLITHH 529
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
186-383 |
4.30e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 79.97 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 186 SFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA------TRSLRVPAHISLLHVEQEVAGDDT-PAlqsvlesd 258
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptSGTVRRAGGARVAYVPQRSEVPDSlPL-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 TVREDL---LRQERELSLRI-AAGRAEGSEAaqlaeiygkLEeieadkaparaSVILAGLGftpkmqQQPTREFSGGWRM 334
Cdd:NF040873 73 TVRDLVamgRWARRGLWRRLtRDDRAAVDDA---------LE-----------RVGLADLA------GRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHD 383
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
178-402 |
4.65e-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: 81.24 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRvPA--HISLlhveqevAGDDTPALQSvl 255
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALA-GLLK-PSsgEVLL-------DGRDLASLSR-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 256 esdtvredllrqeRELSLRIA-----AGRAEGSEAAQLAEI----YGKL--EEIEADKAPARASVILAGLGftpKMQQQP 324
Cdd:COG1120 71 -------------RELARRIAyvpqePPAPFGLTVRELVALgrypHLGLfgRPSAEDREAVEEALERTGLE---HLADRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 325 TREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:COG1120 135 VDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAhqlEVLeLLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
..
gi 29789050 401 RL 402
Cdd:COG1120 215 RI 216
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
178-395 |
5.63e-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: 80.63 E-value: 5.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahISLLHVEQ---EVAGDDTPA 250
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAI----------LGLLKPTSgsiIFDGKDLLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 LQsvlesdtvREDLLRQERELS-------------LRIAAgraegseaaQLAE---IYGKLEEIEADKApaRASVILAGL 314
Cdd:cd03257 72 LS--------RRLRKIRRKEIQmvfqdpmsslnprMTIGE---------QIAEplrIHGKLSKKEARKE--AVLLLLVGV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 315 GFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQT-WPSTILVVSHDRNFLNAI 390
Cdd:cd03257 133 GLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVsvqAQILDLLKKLQEeLGLTLLFITHDLGVVAKI 212
|
....*
gi 29789050 391 ATDII 395
Cdd:cd03257 213 ADRVA 217
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
203-679 |
7.53e-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: 84.45 E-value: 7.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLAtrSLRVPahiSLLHVEQEVAGDDtpalqsVLE--SDTVREDLLRQERELSLRIA---- 276
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILS--GELKP---NLGDYDEEPSWDE------VLKrfRGTELQDYFKKLANGEIKVAhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 277 ----AGRAEGSEAAQLAEIY---GKLEEIeADKaparasvilagLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLL 349
Cdd:COG1245 168 yvdlIPKVFKGTVRELLEKVderGKLDEL-AEK-----------LGLENILDR-DISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 350 LLDEPTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIHLhsqrLDGYRGDFETFIKSKQerllnqq 424
Cdd:COG1245 235 FFDEPSSYLDIYqrlnvARLIRE--LAEEGKYVLVVEHDLAILDYLA-DYVHI----LYGEPGVYGVVSKPKS------- 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 425 reyeaqqqYRQHIQVFID--------RFRynanrasqvQSKLKMLEKLPelkPVDKESEVVLKFPDgFEKfsppilQLDE 496
Cdd:COG1245 301 --------VRVGINQYLDgylpeenvRIR---------DEPIEFEVHAP---RREKEEETLVEYPD-LTK------SYGG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 497 vdfyydpkhsiFSrLSVSADlESR----ICVVGENGAGKSTMLKLLMGDLSPVRGIrhAHRNLKIGYFSQHHVEQLDLNV 572
Cdd:COG1245 354 -----------FS-LEVEGG-EIRegevLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISPDYDGTV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 SAVeLLARKFPGLPEEEYRHQLGR-YGISgELAMRPVASLSGGQKSRVAFAQmtmpC----PNFYILDEPTNHLDMETIE 647
Cdd:COG1245 419 EEF-LRSANTDDFGSSYYKTEIIKpLGLE-KLLDKNVKDLSGGELQRVAIAA----ClsrdADLYLLDEPSAHLDVEQRL 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 29789050 648 ALGQALNNF---RG-GVILVSHDERFIRLVCKELWV 679
Cdd:COG1245 493 AVAKAIRRFaenRGkTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
178-382 |
8.34e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 81.78 E-value: 8.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTPALQSV--- 254
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLL--GLTHPDAGSISLCGEPVPSRARHARQRVgvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 -----LESD-TVREDLLrqerelslriAAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVilaglgftpkmqqqptREF 328
Cdd:PRK13537 86 pqfdnLDPDfTVRENLL----------VFGRYFGLSAAAARALVPPLLEFAKLENKADAKV----------------GEL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILW--LENYLQTwPSTILVVSH 382
Cdd:PRK13537 140 SGGMKRRLTLARALVNDPDVLVLDEPTTGLDpqARHLMWerLRSLLAR-GKTILLTTH 196
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
178-402 |
1.10e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 79.85 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahISLLHVEQ---EVAGDDTPAL--- 251
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLI----------VGLLRPDSgevLIDGEDISGLsea 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 --------------QSVLESD-TVREDL---LRQERELSLriaagraegseaaqlaeiygklEEIEAdkapaRASVILAG 313
Cdd:cd03261 71 elyrlrrrmgmlfqSGALFDSlTVFENVafpLREHTRLSE----------------------EEIRE-----IVLEKLEA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 314 LGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENYLQTwpsTILVVSHDRNF 386
Cdd:cd03261 124 VGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELGL---TSIMVTHDLDT 199
|
250
....*....|....*.
gi 29789050 387 LNAIATDIIHLHSQRL 402
Cdd:cd03261 200 AFAIADRIAVLYDGKI 215
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
152-416 |
1.51e-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: 83.27 E-value: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 152 EEASASQAGSRKESRLESSgknksyDVRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRV 230
Cdd:COG4988 317 APEPAAPAGTAPLPAAGPP------SIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLL--GFLP 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 231 PAHISLLHVEQEVAGDDTPALQ---------SVLESDTVREDLLRQERElslriaAGRAEGSEAAQLAEIygkLEEIEAd 301
Cdd:COG4988 389 PYSGSILINGVDLSDLDPASWRrqiawvpqnPYLFAGTIRENLRLGRPD------ASDEELEAALEAAGL---DEFVAA- 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 302 kAPARASVILAGLGFTpkmqqqptreFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--AILW--LENYLQTwpSTI 377
Cdd:COG4988 459 -LPDGLDTPLGEGGRG----------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAEteAEILqaLRRLAKG--RTV 525
|
250 260 270
....*....|....*....|....*....|....*....
gi 29789050 378 LVVSHDRNFLnAIATDIIHLHSQRLDGyRGDFETFIKSK 416
Cdd:COG4988 526 ILITHRLALL-AQADRILVLDDGRIVE-QGTHEELLAKN 562
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
203-673 |
1.83e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 83.32 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVlESDTVREDLLRQERELSL-----RIAA 277
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILS--------------------GELIPNLGDY-EEEPSWDEVLKRFRGTELqnyfkKLYN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 278 GRAEGSEAAQLAE-----IYGKLEEI--EADKAPARASVILAgLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLL 350
Cdd:PRK13409 158 GEIKVVHKPQYVDlipkvFKGKVRELlkKVDERGKLDEVVER-LGLENILDR-DISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 351 LDEPTNMLDV-------RAILWL-ENylqtwpSTILVVSHDRNFLNAIAtDIIHLhsqrLDGYRGDFETFIKSKQERlln 422
Cdd:PRK13409 236 FDEPTSYLDIrqrlnvaRLIRELaEG------KYVLVVEHDLAVLDYLA-DNVHI----AYGEPGAYGVVSKPKGVR--- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 423 qqreyEAQQQYrqhIQVFID----RFRynanrasqvQSKLKMLEKLPElkpVDKESEVVLKFPDgFEKfsppilQLDevD 498
Cdd:PRK13409 302 -----VGINEY---LKGYLPeenmRIR---------PEPIEFEERPPR---DESERETLVEYPD-LTK------KLG--D 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 499 FyydpkhsifsRLSVSADlESR----ICVVGENGAGKSTMLKLLMGDLSPVRGirHAHRNLKIGYFSQHHVEQLDLNVSa 574
Cdd:PRK13409 353 F----------SLEVEGG-EIYegevIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKPQYIKPDYDGTVE- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 575 vELLARKFPGLPEEEYRHQLGR-YGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQAL 653
Cdd:PRK13409 419 -DLLRSITDDLGSSYYKSEIIKpLQLE-RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496
|
490 500
....*....|....*....|....
gi 29789050 654 N----NFRGGVILVSHDERFIRLV 673
Cdd:PRK13409 497 RriaeEREATALVVDHDIYMIDYI 520
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
179-397 |
2.12e-16 |
|
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: 78.34 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----TR-SLRV---PAHISLLHV----EQEVAG 245
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgllkpTSgSIRVfgkPLEKERKRIgyvpQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 246 DDTPAlqsvlesdTVREDLLrqereLSLRIAAGraegseaaqLAEIYGKLEEIEADKAPARasVILAGLGftpkmqQQPT 325
Cdd:cd03235 81 RDFPI--------SVRDVVL-----MGLYGHKG---------LFRRLSKADKAKVDEALER--VGLSELA------DRQI 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03235 131 GELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKtqeDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
178-383 |
2.31e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 78.76 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslRVPAHISLLHVEQEV--AGDDTPALQSVL 255
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLN----RLNDLIPGAPDEGEVllDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 256 ESDTVREDLLRQER---ELSLR--IAAGraegseaaqlAEIYGKLEEIEADkapARASVILAGLGFTPKM-QQQPTREFS 329
Cdd:cd03260 77 LELRRRVGMVFQKPnpfPGSIYdnVAYG----------LRLHGIKLKEELD---ERVEEALRKAALWDEVkDRLHALGLS 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 330 GGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWpsTILVVSHD 383
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIaelkKEY--TIVIVTHN 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
150-383 |
2.44e-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: 82.96 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 150 VLEEASASQAGSRKESRLESSGknksyDVRIENfdVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA- 224
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKG-----DIELEN--VSFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLg 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 225 --------------------TRSLRvpAHISLlhVEQEVagddtpalqsVLESDTVREDllrqerelslrIAAGRAEGS- 283
Cdd:COG2274 524 lyeptsgrilidgidlrqidPASLR--RQIGV--VLQDV----------FLFSGTIREN-----------ITLGDPDATd 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 284 ----EAAQLAEIygkLEEIEADkaPAR-ASVILAGlGftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNML 358
Cdd:COG2274 579 eeiiEAARLAGL---HDFIEAL--PMGyDTVVGEG-G----------SNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
250 260 270
....*....|....*....|....*....|
gi 29789050 359 DV---RAILwleNYLQTW--PSTILVVSHD 383
Cdd:COG2274 643 DAeteAIIL---ENLRRLlkGRTVIIIAHR 669
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
179-404 |
5.68e-16 |
|
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: 77.63 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHveqevagDDTPALQsv 254
Cdd:cd03245 2 RIEFRNVSFSypnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLA--GLYKPTSGSVLL-------DGTDIRQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESDTVREDL--LRQEREL---SLR--IAAGRAEGSEAAQLAeiygkleeieadkaparaSVILAGLgfTPKMQQQPT-- 325
Cdd:cd03245 71 LDPADLRRNIgyVPQDVTLfygTLRdnITLGAPLADDERILR------------------AAELAGV--TDFVNKHPNgl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 --------REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHdRNFLNAIATDII 395
Cdd:cd03245 131 dlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRII 209
|
250
....*....|.
gi 29789050 396 HLHSQRL--DG 404
Cdd:cd03245 210 VMDSGRIvaDG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
490-667 |
7.34e-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: 81.25 E-value: 7.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYYDPKHSIFSRlsVSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLK 556
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPPVLDG--VSLDLPpgERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssLDQDEVRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQH-HVeqLDLNVSAVELLARkfPGLPEEEYRHQLGRYGISGELAMRP----------VASLSGGQKSRVAFAQMT 625
Cdd:TIGR02868 411 VSVCAQDaHL--FDTTVRENLRLAR--PDATDEELWAALERVGLADWLRALPdgldtvlgegGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 626 MPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDE 667
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAALSGrtVVLITHHL 530
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
520-686 |
7.90e-16 |
|
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: 77.54 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 520 RICVVGENGAGKSTMLKLLMG-----------DLSPVRGIRHAHRNLKIGYFSQHHVEQLD--LNVSAVELLARKFPGLP 586
Cdd:COG1124 33 SFGLVGESGSGKSTLLRALAGlerpwsgevtfDGRPVTRRRRKAFRRRVQMVFQDPYASLHprHTVDRILAEPLRIHGLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYR--HQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGQALNNFRG-GV 660
Cdd:COG1124 113 DREERiaELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVqaeILNLLKDLREERGlTY 192
|
170 180
....*....|....*....|....*.
gi 29789050 661 ILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:COG1124 193 LFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
178-402 |
1.87e-15 |
|
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: 75.99 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGD----RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLlhveqEVAGDDTPALqs 253
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGG--LDRPTSGEV-----RVDGTDISKL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 vleSDTVREDLLRQE-----------RELSLRiaagraegsEAAQLAEIYGKLEEIEAdkaPARASVILAGLGFTPKMQQ 322
Cdd:cd03255 72 ---SEKELAAFRRRHigfvfqsfnllPDLTAL---------ENVELPLLLAGVPKKER---RERAEELLERVGLGDRLNH 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 323 QPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILWLENYLQTwpsTILVVSHDRNfLNAIATDII 395
Cdd:cd03255 137 YPS-ELSGGQQQRVAIARALANDPKIILADEPTGNLDsetgkevMELLRELNKEAGT---TIVVVTHDPE-LAEYADRII 211
|
....*..
gi 29789050 396 HLHSQRL 402
Cdd:cd03255 212 ELRDGKI 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
179-402 |
2.49e-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: 75.94 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRvPAHISLLHVEQEVAGddTPALQ------ 252
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLI-SGFLR-PTSGSVLFDGEDITG--LPPHEiarlgi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 -------SVLESDTVREDLlrqerelslRIAAGRAEGSEAAQLAEIYGKLEeieadkAPARASVILAGLGFTPKMQQqPT 325
Cdd:cd03219 78 grtfqipRLFPELTVLENV---------MVAAQARTGSGLLLARARREERE------ARERAEELLERVGLADLADR-PA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03219 142 GELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
178-383 |
4.28e-15 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 75.90 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDT----- 248
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA--GLEKPTSGEVLVDGKPVTGPGPdrgvv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 ---PALqsvLESDTVREDLlrqerELSLRIA-AGRAEGSE-AAQLAEIYGkLEEiEADKAParasvilaglgftpkmqqq 323
Cdd:COG1116 86 fqePAL---LPWLTVLDNV-----ALGLELRgVPKAERRErARELLELVG-LAG-FEDAYP------------------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 324 ptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 383
Cdd:COG1116 137 --HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltRERLqdELLRLWQETGKTVLFVTHD 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
488-679 |
4.69e-15 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 78.48 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLK 556
Cdd:TIGR02857 318 PASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGsiavngvpladADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQHHVeQLDLNVSAVELLARkfPGLPEEEYRHQLGRYGISGELAMRPV----------ASLSGGQKSRVAFAQMTM 626
Cdd:TIGR02857 398 IAWVPQHPF-LFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQgldtpigeggAGLSGGQAQRLALARAFL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 627 PCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLvCKELWV 679
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALAQGrtVLLVTHRLALAAL-ADRIVV 528
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
193-402 |
5.70e-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: 75.06 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHV---EQEVAGDDtPALQsvlesdtvREDLLR--- 266
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILS----------GLLQPtsgEVRVAGLV-PWKR--------RKKFLRrig 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 267 ----QERELSLRIAAgrAEGseAAQLAEIYGkleeIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARAL 342
Cdd:cd03267 98 vvfgQKTQLWWDLPV--IDS--FYLLAAIYD----LPPARFKKRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 343 FARPDLLLLDEPTNMLDVRAILWLENYLQTW----PSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
524-674 |
7.60e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 78.01 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAV------ELLARK--------FPGLPEEE 589
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTvimghtELWEVKqerdriyaLPEMSEED 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 590 YRH------QLGRY----------------GISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIE 647
Cdd:PRK15064 113 GMKvadlevKFAEMdgytaearagelllgvGIPEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIR 192
|
170 180
....*....|....*....|....*..
gi 29789050 648 ALGQALNNFRGGVILVSHDERFIRLVC 674
Cdd:PRK15064 193 WLEDVLNERNSTMIIISHDRHFLNSVC 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
490-691 |
1.25e-14 |
|
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: 77.25 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYYdPKHSIFSRLSVSADLE--SRICVVGENGAGKSTMLKLLMGDLSP--------------VRGIRHAHR 553
Cdd:COG1123 3 PLLEVRDLSVRY-PGGDVPAVDGVSLTIApgETVALVGESGSGKSTLALALMGLLPHggrisgevlldgrdLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 554 NLKIGYFSQHHVEQLD-LNVSAVELLARKFPGLPEEEYRHQ----LGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPC 628
Cdd:COG1123 82 GRRIGMVFQDPMTQLNpVTVGDQIAEALENLGLSRAEARARvlelLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 629 PNFYILDEPTNHLDMET---IEALGQALNNFRG-GVILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:COG1123 161 PDLLIADEPTTALDVTTqaeILDLLRELQRERGtTVLLITHDLGVVAEIADRVVVMDDGRI--VEDG 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
489-668 |
1.33e-14 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 73.54 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 489 PPILQLDEVDFYYDPKHSIFSRLS-VSADLES--RICVVGENGAGKSTMLKLLMGDLSP------VRGI---------RH 550
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRgVSLSIEAgeFVAIVGPSGSGKSTLLNILGGLDRPtsgevlIDGQdisslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 551 AHRNLKIGY-FSQHH------VEQldlNVSAVELLARKFPGLPEEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQ 623
Cdd:COG1136 82 RLRRRHIGFvFQFFNllpeltALE---NVALPLLLAGVSRKERRERARELLERVGLGDRLDHRP-SQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 624 MTMPCPNFYILDEPTNHLDMET----IEALgQALNNFRG-GVILVSHDER 668
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgeevLELL-RELNRELGtTIVMVTHDPE 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
178-401 |
1.76e-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: 71.65 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLA---------------------TRSLRvpAHI 234
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIkpGEKVAIVGPSGSGKSTLLKLLLrlydptsgeilidgvdlrdldLESLR--KNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 235 SLlhVEQEvagddtpalqSVLESDTVREDLLrqerelslriaagraegseaaqlaeiygkleeieadkaparasvilagl 314
Cdd:cd03228 79 AY--VPQD----------PFLFSGTIRENIL------------------------------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 315 gftpkmqqqptrefSGGWRMRLALARALFARPDLLLLDEPTNMLDVR-AILWLENyLQTWP--STILVVSHDRNfLNAIA 391
Cdd:cd03228 98 --------------SGGQRQRIAIARALLRDPPILILDEATSALDPEtEALILEA-LRALAkgKTVIVIAHRLS-TIRDA 161
|
250
....*....|
gi 29789050 392 TDIIHLHSQR 401
Cdd:cd03228 162 DRIIVLDDGR 171
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
180-367 |
1.76e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKmlATRSLRVPAHISLLhveqeVAGDDTPALQSvlesdt 259
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLR--AINGTLTPTAGTVL-----VAGDDVEALSA------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 vredllrqeRELSLRIAAGRAEGSEA-----AQLAEI-----YGKLEEI-EADKAPARASVILAGlgfTPKMQQQPTREF 328
Cdd:PRK09536 73 ---------RAASRRVASVPQDTSLSfefdvRQVVEMgrtphRSRFDTWtETDRAAVERAMERTG---VAQFADRPVTSL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV-RAILWLE 367
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLE 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
496-685 |
2.40e-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: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 496 EVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL------KIGYFS 561
Cdd:cd03292 5 NVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqdVSDLRGRAipylrrKIGVVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 562 QHHVEQLDLNVSAVELLARKFPGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03292 85 QDFRLLPDRNVYENVAFALEVTGVPPREIRKRvpaaLELVGLSHKHRALP-AELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 638 TNHLDMETIEALGQALN--NFRGGVILVS-HDERFIRLVCKELWVCENGSV 685
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
150-397 |
2.43e-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: 76.17 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 150 VLEEASASQAGSRKESRLESSGknksydVRIENFDVSFGDR-VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSL 228
Cdd:TIGR02857 300 VLDAAPRPLAGKAPVTAAPASS------LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL--GF 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 229 RVPAHISLLHVEQEVAGDDTPALQS---------VLESDTVREDLLRQERElslriaAGRAEGSEAAQLAeiyGKLEEIE 299
Cdd:TIGR02857 372 VDPTEGSIAVNGVPLADADADSWRDqiawvpqhpFLFAGTIAENIRLARPD------ASDAEIREALERA---GLDEFVA 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 300 AdkaparasvilAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTw 373
Cdd:TIGR02857 443 A-----------LPQGLDTPIGEGGAG-LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDaeteaeVLEA--LRALAQG- 507
|
250 260
....*....|....*....|....
gi 29789050 374 pSTILVVSHDRNfLNAIATDIIHL 397
Cdd:TIGR02857 508 -RTVLLVTHRLA-LAALADRIVVL 529
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
178-383 |
2.43e-14 |
|
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: 72.50 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDR----VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDtPALQS 253
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAG--LERPTSGEVLVDGEPVTGPG-PDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLESD------TVREDLLrqereLSLRIA--AGRAEGSEAAQLAEIYGkLEEIEaDKAParasvilaglgftpkmqqqpt 325
Cdd:cd03293 78 VFQQDallpwlTVLDNVA-----LGLELQgvPKAEARERAEELLELVG-LSGFE-NAYP--------------------- 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--RAIL--WLENYLQTWPSTILVVSHD 383
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltREQLqeELLDIWRETGKTVLLVTHD 191
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
523-666 |
2.94e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 73.23 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGYFSQHHVEQLDLNVSAVELLAR----KFPGLPE 587
Cdd:COG4559 32 IIGPNGAGKSTLLKLLTGELTPSSGeVRLNGRPLaawspwelarRRAVLPQHSSLAFPFTVEEVVALGRaphgSSAAQDR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 588 EEYRHQLGRYGISGeLAMRPVASLSGGQKSRVAFA-------QMTMPCPNFYILDEPTNHLD-------METIEALGQAl 653
Cdd:COG4559 112 QIVREALALVGLAH-LAGRSYQTLSGGEQQRVQLArvlaqlwEPVDGGPRWLFLDEPTSALDlahqhavLRLARQLARR- 189
|
170
....*....|...
gi 29789050 654 nnfRGGVILVSHD 666
Cdd:COG4559 190 ---GGGVVAVLHD 199
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
178-399 |
4.45e-14 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 70.68 E-value: 4.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIA--------------------GLEEPDSGSILID 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQERELSLRIAAgraegseAAQLAEIYGKLEEIEAdkaparasvILAGLgftpkmqqqptrefSGGWRMRLA 337
Cdd:cd03229 61 GEDLTDLEDELPPLRRRIGM-------VFQDFALFPHLTVLEN---------IALGL--------------SGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 338 LARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHDRNFLNAIATDIIHLHS 399
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
491-691 |
4.62e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 73.34 E-value: 4.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL-----KI 557
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGrilfdgkpIDYSRKGLmklreSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHVEQL-------DLNVSAVELlarkfpGLPEEEYR----HQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTM 626
Cdd:PRK13636 85 GMVFQDPDNQLfsasvyqDVSFGAVNL------KLPEDEVRkrvdNALKRTGIE-HLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 627 PCPNFYILDEPTNHLD----METIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTrVEGG 691
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI-LQGN 225
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
507-668 |
5.68e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.24 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 507 IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVELL 578
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGeVRWNGTPLAEQRDEPHenilylgHLPGLKPELSALENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 579 A--RKFPGLPEEEYRHQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF 656
Cdd:TIGR01189 95 HfwAAIHGGAQRTIEDALAAVGLTG-FEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAH 173
|
170
....*....|....*
gi 29789050 657 --RGG-VILVSHDER 668
Cdd:TIGR01189 174 laRGGiVLLTTHQDL 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
180-691 |
5.73e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 75.13 E-value: 5.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSF----GDRVLLAGADVNLAWGRRYGLVGRNGLGKT-TLLKMLatRSLRVPAHISLlhveqevAGDDTPALQSV 254
Cdd:PRK15134 8 IENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSPPVVYP-------SGDIRFHGESL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESDtvrEDLLRQ-----------------------ERELSLRIAAGRAEGSEAAQlAEIYGKLEEIEADKAPARasvil 311
Cdd:PRK15134 79 LHAS---EQTLRGvrgnkiamifqepmvslnplhtlEKQLYEVLSLHRGMRREAAR-GEILNCLDRVGIRQAAKR----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 312 agLGFTPkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHDRNFL 387
Cdd:PRK15134 150 --LTDYP-------HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVqaqILQLLRELqQELNMGLLFITHNLSIV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 388 NAIATDIIHLHSQRLdgyrgdFETfikSKQERLLNQqreyeAQQQYRQhiqvfidrfrynanrasqvqsklKMLEKLPEL 467
Cdd:PRK15134 221 RKLADRVAVMQNGRC------VEQ---NRAATLFSA-----PTHPYTQ-----------------------KLLNSEPSG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 468 KPVDKESEvvlkfpdgfekfSPPILQLDEVDFYYDPKHSIFSRL--------SVSADL---ESrICVVGENGAGKST--- 533
Cdd:PRK15134 264 DPVPLPEP------------ASPLLDVEQLQVAFPIRKGILKRTvdhnvvvkNISFTLrpgET-LGLVGESGSGKSTtgl 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 534 -MLKLLMG------DLSPVRGIRhahRNLKIGYFSQHHVEQLD--------LNVSAV--ELLARKFPGLP----EEEYRH 592
Cdd:PRK15134 331 aLLRLINSqgeiwfDGQPLHNLN---RRQLLPVRHRIQVVFQDpnsslnprLNVLQIieEGLRVHQPTLSaaqrEQQVIA 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 593 QLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGQALNN-FRGGVILVSHDER 668
Cdd:PRK15134 408 VMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvQAQILALLKSLQQkHQLAYLFISHDLH 487
|
570 580
....*....|....*....|...
gi 29789050 669 FIRLVCKELWVCENGSVtrVEGG 691
Cdd:PRK15134 488 VVRALCHQVIVLRQGEV--VEQG 508
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
507-664 |
5.88e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 5.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 507 IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIG-YFSQ-H---HVEQLDLNVSAVELLA- 579
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGtIKLDGGDIDDPdVAEAcHylgHRNAMKPALTVAENLEf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 580 -RKFPGLPEEEYRHQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQA----LN 654
Cdd:PRK13539 97 wAAFLGGEELDIAAALEAVGLAP-LAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELirahLA 175
|
170
....*....|
gi 29789050 655 nfRGGVILVS 664
Cdd:PRK13539 176 --QGGIVIAA 183
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
179-355 |
7.06e-14 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 71.31 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLK----MLATRSLRVpahisllhveqEVAGDDTPALQS- 253
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtimgLLPPRSGSI-----------RFDGRDITGLPPh 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 ---------VLESD------TVREDLlrqerelslRIAA-GRAEGSEAAQLAEIYG---KLEEieadkaparasvilagl 314
Cdd:cd03224 71 eraragigyVPEGRrifpelTVEENL---------LLGAyARRRAKRKARLERVYElfpRLKE----------------- 124
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 315 gftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPT 355
Cdd:cd03224 125 -----RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
507-665 |
1.12e-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: 70.21 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 507 IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIGYFSQH-------HVEQLDLNVSAVELL 578
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGrVLLNGGPLDFQRDSIArgllylgHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 579 ARKFPGLPEEEYRHQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF-- 656
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHca 173
|
170
....*....|
gi 29789050 657 RGG-VILVSH 665
Cdd:cd03231 174 RGGmVVLTTH 183
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
492-666 |
1.15e-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: 70.58 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLS-VSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRnlKIGYF 560
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEdISLSVEEGefVALVGPSGCGKSTLLRIIAGLERPTSGevlvdgepVTGPGP--DRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHH-------VEQldlNVsaveLLARKFPGLP----EEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCP 629
Cdd:cd03293 79 FQQDallpwltVLD---NV----ALGLELQGVPkaeaRERAEELLELVGLSGFENAYP-HQLSGGMRQRVALARALAVDP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 630 NFYILDEPTNHLDMETIEALGQAL----NNFRGGVILVSHD 666
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
513-702 |
1.18e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMGDLSPVRGirHAHRNLKIGYFsqhhveqLDLNV------SAVE---LLARk 581
Cdd:COG1134 45 VSFEVERgeSVGIIGRNGAGKSTLLKLIAGILEPTSG--RVEVNGRVSAL-------LELGAgfhpelTGREniyLNGR- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 FPGLPEEEYRH---------QLGRYgisgelAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEptnhldmetieALG-- 650
Cdd:COG1134 115 LLGLSRKEIDEkfdeivefaELGDF------IDQPVKTYSSGMRARLAFAVATAVDPDILLVDE-----------VLAvg 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 651 ---------QALNNFR---GGVILVSHDERFIRLVCKE-LWVcENGSVT---RVEGGFDQYRALLQEQ 702
Cdd:COG1134 178 daafqkkclARIRELResgRTVIFVSHSMGAVRRLCDRaIWL-EKGRLVmdgDPEEVIAAYEALLAGR 244
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
172-382 |
1.22e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.05 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 172 KNKSYDVRIENfdVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA---------------------TRS 227
Cdd:COG1132 334 PPVRGEIEFEN--VSFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrfydptsgrilidgvdirdltLES 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 228 LRvpAHISLlhVEQEVagddtpalqsVLESDTVREDllrqerelslrIAAGRAEGSEAaqlaEIygkleeIEADKApARA 307
Cdd:COG1132 412 LR--RQIGV--VPQDT----------FLFSGTIREN-----------IRYGRPDATDE----EV------EEAAKA-AQA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 308 SVILAGL--GFtpkmqQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILW-LENYLQTwpSTI 377
Cdd:COG1132 456 HEFIEALpdGY-----DTVVGErgvnLSGGQRQRIAIARALLKDPPILILDEATSALDTeteALIQEaLERLMKG--RTT 528
|
....*
gi 29789050 378 LVVSH 382
Cdd:COG1132 529 IVIAH 533
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
129-382 |
1.75e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 129 RLKAKQEKRSEKETLKTSNPLVLEEASASQAGSRKESRLESSGKNKSYdvrienfdvsfGDRVLLAGADVNLAWGRRYGL 208
Cdd:PRK13536 4 RAVAEEAPRRLELSPIERKHQGISEAKASIPGSMSTVAIDLAGVSKSY-----------GDKAVVNGLSFTVASGECFGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 209 VGRNGLGKTTLLKML-----------ATRSLRVPAHISLLHVEQEVagddTPALQSVLESDTVREDLLrqerelslriAA 277
Cdd:PRK13536 73 LGPNGAGKSTIARMIlgmtspdagkiTVLGVPVPARARLARARIGV----VPQFDNLDLEFTVRENLL----------VF 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 278 GRAEGSEAAQLAEIYGKLEEIE--ADKAPARASvilaglgftpkmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPT 355
Cdd:PRK13536 139 GRYFGMSTREIEAVIPSLLEFArlESKADARVS------------------DLSGGMKRRLTLARALINDPQLLILDEPT 200
|
250 260 270
....*....|....*....|....*....|
gi 29789050 356 NMLD--VRAILWLE-NYLQTWPSTILVVSH 382
Cdd:PRK13536 201 TGLDphARHLIWERlRSLLARGKTILLTTH 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
178-382 |
1.88e-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: 70.88 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQ---SV 254
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLIT--------------------GDLPPTYGndvRL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESDTVREDL--LRQE-----RELSLRIAAG-RAE--------GSeaaqlAEIYGKLEEIEAdkapARASVILAGLGFTP 318
Cdd:COG1119 64 FGERRGGEDVweLRKRiglvsPALQLRFPRDeTVLdvvlsgffDS-----IGLYREPTDEQR----ERARELLELLGLAH 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 319 KMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTW----PSTILVVSH 382
Cdd:COG1119 135 LADR-PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegAPTLVLVTH 201
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
178-384 |
2.24e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 72.10 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVP--AHISLlhveqevAGDDTPALQSVL 255
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIA--GLETPdsGRIVL-------NGRDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 256 ESD--------------TVREDllrqerelslrIAAG--RAEGSEAAQLAEIYGKLEEIEadkaparasviLAGLGftpk 319
Cdd:COG1118 74 ERRvgfvfqhyalfphmTVAEN-----------IAFGlrVRPPSKAEIRARVEELLELVQ-----------LEGLA---- 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 320 mQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 384
Cdd:COG1118 128 -DRYPS-QLSGGQRQRVALARALAVEPEVLLLDEPFGALDakVRKELrrWLRRLHDELGGTTVFVTHDQ 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
492-665 |
2.50e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 73.28 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLK----------IGYF 560
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGrILIDGVDIRdltleslrrqIGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHV-------EQL---DLNVSAVELLA-----------RKFPglpeEEYRHQLGRYGisgelamrpvASLSGGQKSRV 619
Cdd:COG1132 420 PQDTFlfsgtirENIrygRPDATDEEVEEaakaaqahefiEALP----DGYDTVVGERG----------VNLSGGQRQRI 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 620 AFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSH 665
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGrtTIVIAH 533
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
519-666 |
3.06e-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: 69.90 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 519 SRICVVGENGAGKSTMLKLLMGDLSPVRG------------IRHAHRNL--KIGYFSQHHveQLDLNVSAVE-----LLA 579
Cdd:cd03256 28 EFVALIGPSGAGKSTLLRCLNGLVEPTSGsvlidgtdinklKGKALRQLrrQIGMIFQQF--NLIERLSVLEnvlsgRLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 580 RK------FPGLPEEEYR---HQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG 650
Cdd:cd03256 106 RRstwrslFGLFPKEEKQralAALERVGLL-DKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVM 184
|
170 180
....*....|....*....|
gi 29789050 651 QAL---NNFRGGVILVS-HD 666
Cdd:cd03256 185 DLLkriNREEGITVIVSlHQ 204
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
523-666 |
3.09e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNLKIGYFSQ--HHVEQLDLNVSAVELLArkfPGLPEEEYRHQLGRYGiS 600
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQklYLDTTLPLTVNRFLRLR---PGTKKEDILPALKRVQ-A 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 601 GELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG----GVILVSHD 666
Cdd:PRK09544 111 GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReldcAVLMVSHD 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
180-402 |
3.38e-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: 69.14 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAgaDVNLAWGR-RYGLVGRNGLGKTTLLKMLATrsLRVPahisllhVEQEVAGDDtpalQSVLES- 257
Cdd:cd03264 3 LENLTKRYGKKRALD--GVSLTLGPgMYGLLGPNGAGKTTLMRILAT--LTPP-------SSGTIRIDG----QDVLKQp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDL--LRQERELSLRIAAgraegseAAQLAEIyGKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMR 335
Cdd:cd03264 68 QKLRRRIgyLPQEFGVYPNFTV-------REFLDYI-AWLKGIPSKEVKARVDEVLELVNLGDR-AKKKIGSLSGGMRRR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 336 LALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03264 139 VGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEdrIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
513-697 |
3.99e-13 |
|
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: 69.39 E-value: 3.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRH--AHR-----------------------NLKI 557
Cdd:cd03219 19 VSFSVRpgEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlfdgedITGlpPHEiarlgigrtfqiprlfpeltvleNVMV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHVEQLDLNVSAVELLARkfpglpeEEYRHQLGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03219 99 AAQARTGSGLLLARARREEREAR-------ERAEELLERVGL-ADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 638 T---NHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTrVEGGFDQYRA 697
Cdd:cd03219 171 AaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVI-AEGTPDEVRN 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
523-666 |
4.27e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 69.80 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLK----------IGYFSQHHVEQLDLNVSAVELLAR-KFPGLPEEEY 590
Cdd:PRK13548 33 ILGPNGAGKSTLLRALSGELSPDSGeVRLNGRPLAdwspaelarrRAVLPQHSSLSFPFTVEEVVAMGRaPHGLSRAEDD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 591 R---HQLGRYGISGeLAMRPVASLSGGQKSRVAFA----QMTMPC--PNFYILDEPTNHLD----METIEALGQALNNFR 657
Cdd:PRK13548 113 AlvaAALAQVDLAH-LAGRDYPQLSGGEQQRVQLArvlaQLWEPDgpPRWLLLDEPTSALDlahqHHVLRLARQLAHERG 191
|
....*....
gi 29789050 658 GGVILVSHD 666
Cdd:PRK13548 192 LAVIVVLHD 200
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
492-702 |
5.33e-13 |
|
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: 69.18 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLL--MGDLS---------PVRGIRHAHRNLKIGYF 560
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfrFYDVSsgsilidgqDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQ----------HHVEQLDLNVSAVEL--------LARKFPGLPEEeYRHQLGRYGISgelamrpvasLSGGQKSRVAFA 622
Cdd:cd03253 81 PQdtvlfndtigYNIRYGRPDATDEEVieaakaaqIHDKIMRFPDG-YDTIVGERGLK----------LSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 623 QMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIrLVCKELWVCENGSVTRvEGGFDQ------ 694
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGrtTIVIAHRLSTI-VNADKIIVLKDGRIVE-RGTHEEllakgg 227
|
....*....
gi 29789050 695 -YRALLQEQ 702
Cdd:cd03253 228 lYAEMWKAQ 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
521-674 |
5.42e-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: 69.07 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG------------IRHAHRNL--KIGYFSQHHVEQLDLNVSA-VELLARKFPGL 585
Cdd:cd03261 29 LAIIGPSGSGKSTLLRLIVGLLRPDSGevlidgedisglSEAELYRLrrRMGMLFQSGALFDSLTVFEnVAFPLREHTRL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 586 PEEEYR----HQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEALGQALN 654
Cdd:cd03261 109 SEEEIReivlEKLEAVGLRGAEDLYP-AELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgviDDLIRSLKKELG 187
|
170 180
....*....|....*....|
gi 29789050 655 NfrgGVILVSHDERFIRLVC 674
Cdd:cd03261 188 L---TSIMVTHDLDTAFAIA 204
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
494-702 |
5.97e-13 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 69.11 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 494 LDEVDFYYD--PKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IR----HAHRNlKIGY 559
Cdd:cd03249 3 FKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGeilldgvdIRdlnlRWLRS-QIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHV-------EQL-----DLNVSAVELLARK------FPGLPEEeYRHQLGRYGisgelamrpvASLSGGQKSRVAF 621
Cdd:cd03249 82 VSQEPVlfdgtiaENIrygkpDATDEEVEEAAKKanihdfIMSLPDG-YDTLVGERG----------SQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 622 AQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHderfiRLV----CKELWVCENGSVtrVE-GGFDQ 694
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGrtTIVIAH-----RLStirnADLIAVLQNGQV--VEqGTHDE 223
|
250
....*....|....*
gi 29789050 695 -------YRALLQEQ 702
Cdd:cd03249 224 lmaqkgvYAKLVKAQ 238
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
524-686 |
6.05e-13 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 68.90 E-value: 6.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRG-------------IRHAHRnlkIGY-FSQHhvEQLDLNVSAVE---LLARKFpGLP 586
Cdd:cd03267 53 IGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrrKKFLRR---IGVvFGQK--TQLWWDLPVIDsfyLLAAIY-DLP 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYRHQLGRygIS-----GELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGQALNNFRG 658
Cdd:cd03267 127 PARFKKRLDE--LSelldlEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRNFLKEYNRERG 204
|
170 180
....*....|....*....|....*....
gi 29789050 659 G-VILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:cd03267 205 TtVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
492-685 |
6.24e-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: 67.24 E-value: 6.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYY-DPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLK---IGY 559
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGrvrldgadISQWDPNELgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHhveqldlnvsaVELLarkfpglpeeeyrhqlgrygiSGELAMrpvASLSGGQKSRVAFAQMTMPCPNFYILDEPTN 639
Cdd:cd03246 81 LPQD-----------DELF---------------------SGSIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789050 640 HLDMETIEALGQALNNFRGG---VILVSHDERFIRLVCKELwVCENGSV 685
Cdd:cd03246 126 HLDVEGERALNQAIAALKAAgatRIVIAHRPETLASADRIL-VLEDGRV 173
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
178-383 |
8.42e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML------ATRSLRVPAHISLLHVEQEVAGDDTPAL 251
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVlglvapDEGVIKRNGKLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 qsvlesdTVredllrqERELSLRIAAGRAegseaaqlaeiygkleeieaDKAPARASVILAGLgftpkmQQQPTREFSGG 331
Cdd:PRK09544 85 -------TV-------NRFLRLRPGTKKE--------------------DILPALKRVQAGHL------IDAPMQKLSGG 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 332 WRMRLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYLQTWPSTILVVSHD 383
Cdd:PRK09544 125 ETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
522-685 |
9.27e-13 |
|
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: 67.63 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSPVRGI---------RHAHRNLKIGYFSQHHVeqLDLNVSAVE--LLARKFPGLPEEEY 590
Cdd:cd03268 30 GFLGPNGAGKTTTMKIILGLIKPDSGEitfdgksyqKNIEALRRIGALIEAPG--FYPNLTAREnlRLLARLLGIRKKRI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 591 RHQLGRYGISGElAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQ---ALNNFRGGVILVSHDE 667
Cdd:cd03268 108 DEVLDVVGLKDS-AKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRElilSLRDQGITVLISSHLL 186
|
170
....*....|....*...
gi 29789050 668 RFIRLVCKELWVCENGSV 685
Cdd:cd03268 187 SEIQKVADRIGIINKGKL 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
197-398 |
9.46e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.94 E-value: 9.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNL--AWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQ---EVAGDDTP--ALQSVLESD-TVREDLLRQE 268
Cdd:cd03220 40 DVSFevPRGERIGLIGRNGAGKSTLLRLLA----------GIYPPDSgtvTVRGRVSSllGLGGGFNPElTGRENIYLNG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 269 RELSLRIAagraegseaaqlaEIYGKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDL 348
Cdd:cd03220 110 RLLGLSRK-------------EIDEKIDEIIE----------FSELG---DFIDLPVKTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 349 LLLDEPTNMLDV----RAILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:cd03220 164 LLIDEVLAVGDAafqeKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
488-666 |
9.81e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 68.96 E-value: 9.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSRLS-VSADLESR--ICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLKIG 558
Cdd:COG1116 4 AAPALELRGVSKRFPTGGGGVTALDdVSLTVAAGefVALVGPSGCGKSTLLRLIAGLEKPtsgevlVDGKPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 559 Y-FSQHH------VEQldlNVsaveLLARKFPGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMP 627
Cdd:COG1116 84 VvFQEPAllpwltVLD---NV----ALGLELRGVPKAERRERarelLELVGLAGFEDAYP-HQLSGGMRQRVAIARALAN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29789050 628 CPNFYILDEPTNHLDMETIEALGQAL----NNFRGGVILVSHD 666
Cdd:COG1116 156 DPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
207-394 |
9.90e-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: 67.92 E-value: 9.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLAtrSLRVP----AHISllhvEQEVAGDDTPALQSV---------LESDTVREDLlrqerelsl 273
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLT--GELRPtsgtAYIN----GYSIRTDRKAARQSLgycpqfdalFDELTVREHL--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 274 riaagraegseaaqlaEIYGKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGWRMRLALARALFARPDLLLLDE 353
Cdd:cd03263 97 ----------------RFYARLKGLPKSEIKEEVELLLRVLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 354 PTNMLDVRA--ILWleNYLQTWP--STILVVSHDRNFLNAIATDI 394
Cdd:cd03263 160 PTSGLDPASrrAIW--DLILEVRkgRSIILTTHSMDEAEALCDRI 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
151-398 |
1.01e-12 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 71.38 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 151 LEEA-SASQAGSRKESRLESSGKNksyDVRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA---- 224
Cdd:COG4178 338 FEEAlEAADALPEAASRIETSEDG---ALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwp 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 225 --TRSLRVPAHISLLHVEQevagddtpalQSVLESDTVREDLLRqerelslriaAGRAEGSEAAQLAEIygkLEEieadk 302
Cdd:COG4178 415 ygSGRIARPAGARVLFLPQ----------RPYLPLGTLREALLY----------PATAEAFSDAELREA---LEA----- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 303 aparasvilAGLG-FTPKM-QQQP-TREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL-QTWPSTIL 378
Cdd:COG4178 467 ---------VGLGhLAERLdEEADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLrEELPGTTV 537
|
250 260
....*....|....*....|.
gi 29789050 379 V-VSHdRNFLNAIATDIIHLH 398
Cdd:COG4178 538 IsVGH-RSTLAAFHDRVLELT 557
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
195-360 |
1.02e-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: 71.25 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 195 GADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRvpahisLLHVEQEVAGDDTPAlqsvlesDTVREDLLRQERE---- 270
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLGLAL----LR------LIPSEGEIRFDGQDL-------DGLSRRALRPLRRrmqv 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 271 --------LSLRIAAGR--AEGseaaqLAeiygkLEEIEADKAPARASVI--LAGLGFTPKMQQQPTREFSGGWRMRLAL 338
Cdd:COG4172 367 vfqdpfgsLSPRMTVGQiiAEG-----LR-----VHGPGLSAAERRARVAeaLEEVGLDPAARHRYPHEFSGGQRQRIAI 436
|
170 180
....*....|....*....|..
gi 29789050 339 ARALFARPDLLLLDEPTNMLDV 360
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDV 458
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
179-397 |
1.12e-12 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 67.84 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSF-----GDRVL--LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHVEQEVagddtpa 250
Cdd:COG4778 6 EVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCI-YGNYLPDSgSILVRHDGGWV------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 lqsvlesdtvreDLLR-QERE-LSLRiaagRAEGSEAAQ----------LAEIYGKLEE--IEADKAPARASVILAGLGF 316
Cdd:COG4778 78 ------------DLAQaSPREiLALR----RRTIGYVSQflrviprvsaLDVVAEPLLErgVDREEARARARELLARLNL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 317 TPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWPSTILVVSHDRNFLNAI 390
Cdd:COG4778 142 PERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDaanravVVELI---EEAKARGTAIIGIFHDEEVREAV 218
|
....*..
gi 29789050 391 ATDIIHL 397
Cdd:COG4778 219 ADRVVDV 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
179-398 |
1.18e-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: 68.53 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHveQEVAGDDTPAL------ 251
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLI-TGFYRPTSgRILFDG--RDITGLPPHRIarlgia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 ---Q--SVLESDTVREdllrqerelSLRIAAGRAEGSEAAQLAEIYGKLEEIEADkAPARASVILAGLGFTPKMQQqPTR 326
Cdd:COG0411 83 rtfQnpRLFPELTVLE---------NVLVAAHARLGRGLLAALLRLPRARREERE-ARERAEELLERVGLADRADE-PAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPT---NMLDVRAIL-WLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHDMDLVMGLADRIVVLD 227
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
513-686 |
1.23e-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: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMGDLSPVRGirHAHRNLKIGYFsqhhveqLDLNVSavellarkF-PGLPEEE 589
Cdd:cd03220 41 VSFEVPRgeRIGLIGRNGAGKSTLLRLLAGIYPPDSG--TVTVRGRVSSL-------LGLGGG--------FnPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 590 YRHQLGR-YGIS-----------------GELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQ 651
Cdd:cd03220 104 NIYLNGRlLGLSrkeidekideiiefselGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQR 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 29789050 652 ALNNFR---GGVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:cd03220 184 RLRELLkqgKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
180-395 |
1.64e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 68.17 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqevAGDdTPALQsvlesdt 259
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA--GLETPSAGELL------AGT-APLAE------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 VRED--LLRQE-RELSLR-----IAAG-RAEGSEAAQLAeiygkleeieadkaparasviLAGLGFTPKMQQQPTrEFSG 330
Cdd:PRK11247 79 AREDtrLMFQDaRLLPWKkvidnVGLGlKGQWRDAALQA---------------------LAAVGLADRANEWPA-ALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 331 GWRMRLALARALFARPDLLLLDEPTNMLDvrAI-----------LWLENYLqtwpsTILVVSHDRNFLNAIATDII 395
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALD--ALtriemqdliesLWQQHGF-----TVLLVTHDVSEAVAMADRVL 205
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
521-706 |
1.64e-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: 67.82 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNlKIGYFSQHhvEQLDLNVSAVELLARKFPGLpeeeYRHQLGRYGIS 600
Cdd:cd03237 28 IGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQY--IKADYEGTVRDLLSSITKDF----YTHPYFKTEIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 601 GELAM-----RPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF----RGGVILVSHDERFIR 671
Cdd:cd03237 101 KPLQIeqildREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMID 180
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29789050 672 LVCKELWVCE-----NGSVTRVEG---GFDQYRALLQEQFRRE 706
Cdd:cd03237 181 YLADRLIVFEgepsvNGVANPPQSlrsGMNRFLKNLDITFRRD 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
178-404 |
1.71e-12 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 67.81 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQEVAGDDTPALQSVLeS 257
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRC-----------INKL--EEITSGDLIVDGLKVN-D 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQErelslriaAGRAegseaAQLAEIYGKLEEIE-----------ADKAPAR--ASVILAGLGFTPKMQQQP 324
Cdd:PRK09493 68 PKVDERLIRQE--------AGMV-----FQQFYLFPHLTALEnvmfgplrvrgASKEEAEkqARELLAKVGLAERAHHYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 325 TrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VR-AILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:PRK09493 135 S-ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDpeLRhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
....*
gi 29789050 402 L--DG 404
Cdd:PRK09493 214 IaeDG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
179-355 |
2.36e-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: 67.31 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLK----MLATRS----------LRVPAH------ISllH 238
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaisgLLPPRSgsirfdgediTGLPPHriarlgIG--Y 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 239 VEQEvagddtpalQSVLESDTVREDLlrqerELSLRIAAGRAEGseAAQLAEIYG---KLEEieadkaparasvilaglg 315
Cdd:COG0410 83 VPEG---------RRIFPSLTVEENL-----LLGAYARRDRAEV--RADLERVYElfpRLKE------------------ 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 316 ftpkMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPT 355
Cdd:COG0410 129 ----RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
491-689 |
2.45e-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: 67.15 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRL-SVSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------- 555
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALdDVSFSIKkgETLGLVGESGSGKSTLARAILGLLKPTSGsIIFDGKDLlklsrrlrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 556 --KIGYFSQHHVEQLD--LNVSA--VELLARKFPGLPEEEYRHQLGRYGISGELA-----MRPvASLSGGQKSRVAFAqM 624
Cdd:cd03257 81 rkEIQMVFQDPMSSLNprMTIGEqiAEPLRIHGKLSKKEARKEAVLLLLVGVGLPeevlnRYP-HELSGGQRQRVAIA-R 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 625 TMPC-PNFYILDEPTNHLDMET---IEALGQALNNFRG-GVILVSHDERFIRLVCKELWVCENGSVtrVE 689
Cdd:cd03257 159 ALALnPKLLIADEPTSALDVSVqaqILDLLKKLQEELGlTLLFITHDLGVVAKIADRVAVMYAGKI--VE 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
521-666 |
2.68e-12 |
|
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: 67.46 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSAV-------- 575
Cdd:TIGR04520 31 VAIIGHNGSGKSTLAKLLNGLLLPTSGkvtvdgldtldeenlweIRK-----KVGMVFQNPDNQF---VGATveddvafg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 576 -ELLarkfpGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLD------- 642
Cdd:TIGR04520 103 lENL-----GVPREEMRKRvdeaLKLVGME-DFRDREPHLLSGGQKQRVAIAGvLAMR-PDIIILDEATSMLDpkgrkev 175
|
170 180
....*....|....*....|....*
gi 29789050 643 METIealgQALNNFRG-GVILVSHD 666
Cdd:TIGR04520 176 LETI----RKLNKEEGiTVISITHD 196
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
492-683 |
2.76e-12 |
|
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: 65.67 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYdPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------------IRHAHRNlKI 557
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGsilidgedltdledELPPLRR-RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHveQLDLNVSAVELLArkfpglpeeeyrhqlgrYGisgelamrpvasLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03229 79 GMVFQDF--ALFPHLTVLENIA-----------------LG------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 638 TNHLDMET---IEALGQALN-NFRGGVILVSHDERFIRLVCKELWVCENG 683
Cdd:cd03229 128 TSALDPITrreVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-686 |
2.78e-12 |
|
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: 65.14 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLKigyfsqhhvEQLDLNVSAVellarkfpglpeeeyrHQLg 595
Cdd:cd03216 30 ALLGENGAGKSTLMKILSGLYKPdsgeilVDGKEVSFASPR---------DARRAGIAMV----------------YQL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 596 rygisgelamrpvaslSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSHDERFIRL 672
Cdd:cd03216 84 ----------------SVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISHRLDEVFE 147
|
170
....*....|....
gi 29789050 673 VCKELWVCENGSVT 686
Cdd:cd03216 148 IADRVTVLRDGRVV 161
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
173-402 |
2.79e-12 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 66.61 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 173 NKSYDVRIENFDVsfgdrvlLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPA--HISLLhvEQEVAGDDTPA 250
Cdd:COG1136 11 TKSYGTGEGEVTA-------LRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGG--LDRPTsgEVLID--GQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 L------------QS--VLESDTVREDLlrqerELSLRIAAgraegseaaqlaeiygkleeIEADKAPARASVILAGLGF 316
Cdd:COG1136 80 LarlrrrhigfvfQFfnLLPELTALENV-----ALPLLLAG--------------------VSRKERRERARELLERVGL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 317 TPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTWPSTILVVSHDRNFLnAI 390
Cdd:COG1136 135 GDRLDHRPS-QLSGGQQQRVAIARALVNRPKLILADEPTGNLDsktgeeVLEL--LRELNRELGTTIVMVTHDPELA-AR 210
|
250
....*....|..
gi 29789050 391 ATDIIHLHSQRL 402
Cdd:COG1136 211 ADRVIRLRDGRI 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
523-673 |
2.95e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.01 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMG--DLSPVRG-IRHAHRNLkigyfsqhhveqLDLNvsavellarkfpglPEEeyRHQLGRY-- 597
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpKYEVTEGeILFKGEDI------------TDLP--------------PEE--RARLGIFla 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 598 --------GISGELAMRPV-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSH 665
Cdd:cd03217 83 fqyppeipGVKNADFLRYVnEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITH 162
|
....*...
gi 29789050 666 DERFIRLV 673
Cdd:cd03217 163 YQRLLDYI 170
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
180-407 |
2.96e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 66.61 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSF---GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtRSLRVPA-HISLLhvEQEVA---GDDTPAL- 251
Cdd:COG2884 2 IRFENVSKrypGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-GEERPTSgQVLVN--GQDLSrlkRREIPYLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 QSV---------LESDTVREDLlrqerELSLRIAaGRAEgseaaqlaeiygklEEIEAdkapaRASVILAGLGFTPKMQQ 322
Cdd:COG2884 79 RRIgvvfqdfrlLPDRTVYENV-----ALPLRVT-GKSR--------------KEIRR-----RVREVLDLVGLSDKAKA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 323 QPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL--E-NYLQTwpsTILVVSHDRNFLNAIATDIIH 396
Cdd:COG2884 134 LP-HELSGGEQQRVAIARALVNRPELLLADEPTGNLDpetSWEIMELleEiNRRGT---TVLIATHDLELVDRMPKRVLE 209
|
250
....*....|...
gi 29789050 397 LHSQRL--DGYRG 407
Cdd:COG2884 210 LEDGRLvrDEARG 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
523-672 |
6.86e-12 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 65.32 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLK----LLMGDLSPvRGIRHAHRNLKIGyfSQHHVEQLDLNVSAVE----LLARKFPGLPEEEYRHQl 594
Cdd:cd03240 27 IVGQNGAGKTTIIEalkyALTGELPP-NSKGGAHDPKLIR--EGEVRAQVKLAFENANgkkyTITRSLAILENVIFCHQ- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 595 gryGISGELAMRPVASLSGGQKS------RVAFAQ-MTMPCPnFYILDEPTNHLDMETIE-ALGQALNNFRGG----VIL 662
Cdd:cd03240 103 ---GESNWPLLDMRGRCSGGEKVlasliiRLALAEtFGSNCG-ILALDEPTTNLDEENIEeSLAEIIEERKSQknfqLIV 178
|
170
....*....|
gi 29789050 663 VSHDERFIRL 672
Cdd:cd03240 179 ITHDEELVDA 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
188-363 |
7.03e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTP----------ALQSVLes 257
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA--GLLPPAAGTIKLDGGDIDDPDVAeachylghrnAMKPAL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dTVREDLlrqerelslriaagraegseaAQLAEIYGkleEIEADKAPARASVILAGLGFTPkmqqqpTREFSGGWRMRLA 337
Cdd:PRK13539 89 -TVAENL---------------------EFWAAFLG---GEELDIAAALEAVGLAPLAHLP------FGYLSAGQKRRVA 137
|
170 180
....*....|....*....|....*.
gi 29789050 338 LARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALDAAAV 163
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
203-398 |
7.20e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.87 E-value: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLA----------TRSLRVPAhisLLhveqEVAGddtpALQSVLesdTVREDLlrqerels 272
Cdd:COG1134 52 GESVGIIGRNGAGKSTLLKLIAgileptsgrvEVNGRVSA---LL----ELGA----GFHPEL---TGRENI-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 lrIAAGRAEGseaAQLAEIYGKLEEIEAdkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLD 352
Cdd:COG1134 110 --YLNGRLLG---LSRKEIDEKFDEIVE----------FAELG---DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 353 EptnMLDV-------RAILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:COG1134 172 E---VLAVgdaafqkKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLE 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
177-385 |
7.44e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 66.19 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTPALQSVLE 256
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFA--RLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 sdtvredLLRQE---------RELslrIAAGRAEgseaaqLAEIYGKLeeieADKAPARASVILAGLGfTPKMQQQPTRE 327
Cdd:PRK11231 80 -------LLPQHhltpegitvREL---VAYGRSP------WLSLWGRL----SAEDNARVNQAMEQTR-INHLADRRLTD 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK11231 139 LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINhqvELMRLMRELNTQGKTVVTVLHDLN 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
178-398 |
8.33e-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: 65.24 E-value: 8.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllHVEQEVAG----DDTPALQS 253
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCIN-------------LLEEPDSGtiiiDGLKLTDD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLESDTVREDL--LRQERELSLRIAAgraegSEAAQLAEIygKLEEIEADKAPARASVILAGLGFTPKMQQQPtREFSGG 331
Cdd:cd03262 68 KKNINELRQKVgmVFQQFNLFPHLTV-----LENITLAPI--KVKGMSKAEAEERALELLEKVGLADKADAYP-AQLSGG 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 332 WRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLH 398
Cdd:cd03262 140 QQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
179-402 |
8.67e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 65.95 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPA-HISLLHveQEVAGDDTPAL------ 251
Cdd:PRK13548 4 EARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL-SGELSPDSgEVRLNG--RPLADWSPAELarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 ---QSVLESD-TVREdllrqerelslRIAAGRAEGSEAAQlaeiygkleeiEADKAPARA--SVILAGLGftpkmqQQPT 325
Cdd:PRK13548 81 lpqHSSLSFPfTVEE-----------VVAMGRAPHGLSRA-----------EDDALVAAAlaQVDLAHLA------GRDY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 326 REFSGGWRMRLALARAL------FARPDLLLLDEPTNMLDVR---AILWL-ENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:PRK13548 133 PQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAhqhHVLRLaRQLAHERGLAVIVVLHDLNLAARYADRIV 212
|
....*..
gi 29789050 396 HLHSQRL 402
Cdd:PRK13548 213 LLHQGRL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
524-665 |
8.77e-12 |
|
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: 64.99 E-value: 8.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRGIRH--------AHRNlKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQ-- 593
Cdd:cd03269 32 LGPNGAGKTTTIRMILGIILPDSGEVLfdgkpldiAARN-RIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRid 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 594 --LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVSH 665
Cdd:cd03269 111 ewLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAgktVILSTH 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
523-666 |
9.67e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 65.22 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG---------------IRHAHRNLKIGYFSQHHVEQLDL----NVSAVELLARKFP 583
Cdd:PRK11629 40 IVGSSGSGKSTLLHLLGGLDTPTSGdvifngqpmsklssaAKAELRNQKLGFIYQFHHLLPDFtaleNVAMPLLIGKKKP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 584 GLPEEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALN--NFRGGV- 660
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGelNRLQGTa 198
|
....*..
gi 29789050 661 -ILVSHD 666
Cdd:PRK11629 199 fLVVTHD 205
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
492-687 |
1.08e-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: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIfsrLSVSADLESRICV-VGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL--KIGYF 560
Cdd:cd03264 1 LQLENLTKRYGKKRAL---DGVSLTLGPGMYGlLGPNGAGKTTLMRILATLTPPSSGtiridgqdVLKQPQKLrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHveQLDLNVSAVELLAR--KFPGLPEEEYRHQ----LGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:cd03264 78 PQEF--GVYPNFTVREFLDYiaWLKGIPSKEVKARvdevLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 635 DEPTNHLDMETIEAlgqalnnFRG---------GVILVSHDERFIRLVCKELWVCENGSVTR 687
Cdd:cd03264 155 DEPTAGLDPEERIR-------FRNllselgedrIVILSTHIVEDVESLCNQVAVLNKGKLVF 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
488-665 |
1.19e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 64.87 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLKIGY 559
Cdd:PRK13543 8 APPLLAAHALAFSRNEE-PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGqiqidgktATRGDRSRFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSqhHVEQLDLNVSAVELL----------ARKFPGlpeeeyrHQLGRYGISGElAMRPVASLSGGQKSRVAFAQMTM-PC 628
Cdd:PRK13543 87 LG--HLPGLKADLSTLENLhflcglhgrrAKQMPG-------SALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLsPA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 629 PnFYILDEPTNHLDMETIEALGQALN---NFRGGVILVSH 665
Cdd:PRK13543 157 P-LWLLDEPYANLDLEGITLVNRMISahlRGGGAALVTTH 195
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
492-686 |
1.46e-11 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 63.49 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgYFSQHHVEQLDL 570
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQG--------EI-TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 571 NVS-AVELLARKfPGLPEEEYRHQLGRygisgelamrpvaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---- 645
Cdd:cd03247 72 ALSsLISVLNQR-PYLFDTTLRNNLGR-------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITerql 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 646 IEALGQALNNfrGGVILVSHDERFIRLVcKELWVCENGSVT 686
Cdd:cd03247 138 LSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
492-686 |
1.51e-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: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSrLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IR-----------HAHRNLKIGY 559
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRG-VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGsIRldgeditklppHERARAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 -------FSQHHVEQlDLNVSAvELLARKFPGLPEEEYrhqlGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR03410 80 vpqgreiFPRLTVEE-NLLTGL-AALPRRSRKIPDEIY----ELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 633 ILDEPTNHLDMETIEALGQALNNFRG----GVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAeggmAILLVEQYLDFARELADRYYVMERGRVV 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
492-666 |
1.58e-11 |
|
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: 64.51 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSrlsVSADLESRIC--VVGENGAGKSTMLKLL--MGDLSPvrGIRHAHRnlkIGYFSQhhvEQ 567
Cdd:cd03260 1 IELRDLNVYYGDKHALKD---ISLDIPKGEItaLIGPSGCGKSTLLRLLnrLNDLIP--GAPDEGE---VLLDGK---DI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 LDLNVSAVELLAR---------KFPG-------------------LPEEEYRHQLGRYGISGELAMRPVA-SLSGGQKSR 618
Cdd:cd03260 70 YDLDVDVLELRRRvgmvfqkpnPFPGsiydnvayglrlhgiklkeELDERVEEALRKAALWDEVKDRLHAlGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 619 VAFAQMTMPCPNFYILDEPTNHLD---METIEALGQALNNfRGGVILVSHD 666
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDpisTAKIEELIAELKK-EYTIVIVTHN 199
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
492-666 |
1.64e-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: 64.08 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHsIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL--------KIGYFSQ 562
Cdd:cd03259 1 LELKGLSKTYGSVR-ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGeILIDGRDVtgvpperrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 HH-------VEQldlNVSavelLARKFPGLPEEEYRHQLGRY----GISGELAmRPVASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:cd03259 80 DYalfphltVAE---NIA----FGLKLRGVPKAEIRARVRELlelvGLEGLLN-RYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 29789050 632 YILDEPTNHLDMETIEALGQAL----NNFRGGVILVSHD 666
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELkelqRELGITTIYVTHD 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
178-416 |
1.88e-11 |
|
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: 64.52 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDR----VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhveqevagdDTPALQS 253
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRC-----------INGL---------ERPTSGS 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VL----ESDTVREDLLRQERE-----------LSLRIAAGRAegseAAQLaeiygKLEEIEADKAPARASVILAGLGFTP 318
Cdd:cd03258 62 VLvdgtDLTLLSGKELRKARRrigmifqhfnlLSSRTVFENV----ALPL-----EIAGVPKAEIEERVLELLELVGLED 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 319 KMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL-WLENYLQTWPSTILVVSHDRNFLNAIATDI 394
Cdd:cd03258 133 KADAYPA-QLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTQSILaLLRDINRELGLTIVLITHEMEVVKRICDRV 211
|
250 260
....*....|....*....|..
gi 29789050 395 IHLHSQRLDGYRGDFETFIKSK 416
Cdd:cd03258 212 AVMEKGEVVEEGTVEEVFANPQ 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
150-382 |
2.35e-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: 67.05 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 150 VLEEASASQAGSRKESRLESsgknksyDVRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKML---- 223
Cdd:TIGR02203 310 LLDSPPEKDTGTRAIERARG-------DVEFRNVTFRYPGRDRPALDSISLviEPGETVALVGRSGSGKSTLVNLIprfy 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 224 -----------------ATRSLRvpAHISLlhVEQEVagddtpalqsVLESDTVREDllrqerelslrIAAGRAEGSEAA 286
Cdd:TIGR02203 383 epdsgqilldghdladyTLASLR--RQVAL--VSQDV----------VLFNDTIANN-----------IAYGRTEQADRA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 287 qlaeiygkleEIEADKAPARASVILAGLgftPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV-- 360
Cdd:TIGR02203 438 ----------EIERALAAAYAQDFVDKL---PLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNes 504
|
250 260
....*....|....*....|....
gi 29789050 361 -RAI-LWLENYLQTwpSTILVVSH 382
Cdd:TIGR02203 505 eRLVqAALERLMQG--RTTLVIAH 526
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
207-383 |
2.39e-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: 63.85 E-value: 2.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLATrSLRVPA-HISLlhveqevagDDTPALQSVLESDTVRED----LLRQEREL--SLRIAAGR 279
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAG-LEKPDGgTIVL---------NGTVLFDSRKKINLPPQQrkigLVFQQYALfpHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 280 AEGSEAAQLAEIYGKLEEIeadkaparasVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03297 97 AFGLKRKRNREDRISVDEL----------LDLLGLD---HLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180
....*....|....*....|....*...
gi 29789050 360 VRAILWLENYLQTWPS----TILVVSHD 383
Cdd:cd03297 164 RALRLQLLPELKQIKKnlniPVIFVTHD 191
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
511-686 |
2.57e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 64.82 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 511 LSVSADLESRICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLK-----IGYFSQHHVEQL-------DLNV 572
Cdd:PRK13652 23 INFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPtsgsvlIRGEPITKENIRevrkfVGLVFQNPDDQIfsptveqDIAF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 SAVELlarkfpGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 648
Cdd:PRK13652 103 GPINL------GLDEETVAHRvssaLHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 649 LGQALNNF--RGG--VILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:PRK13652 176 LIDFLNDLpeTYGmtVIFSTHQLDLVPEMADYIYVMDKGRIV 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
490-666 |
2.65e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.04 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYY-DPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KI 557
Cdd:PRK13635 4 EIIRVEHISFRYpDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGtITVGGMVLseetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHVEQLdlnVSA-VE---LLARKFPGLPEEEY----RHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCP 629
Cdd:PRK13635 84 GMVFQNPDNQF---VGAtVQddvAFGLENIGVPREEMvervDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 630 NFYILDEPTNHLD-------METIEALGQALNnfrGGVILVSHD 666
Cdd:PRK13635 160 DIIILDEATSMLDprgrrevLETVRQLKEQKG---ITVLSITHD 200
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
178-383 |
3.54e-11 |
|
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: 63.86 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslRVPAHISllhveqevaGDDTPALQSVLE 256
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMIN----RLIEPTS---------GEIFIDGEDIRE 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 SDTVRedlLRqeRELSLRI-AAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPK--MQQQPtREFSGGWR 333
Cdd:cd03295 68 QDPVE---LR--RKIGYVIqQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYP-HELSGGQQ 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHD 383
Cdd:cd03295 142 QRVGVARALAADPPLLLMDEPFGALDpiTRDQLQEEfkRLQQELGKTIVFVTHD 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
497-665 |
3.61e-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: 63.40 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 497 VDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMG-----------DLSPVRGI-RHAHRNlKIGY----- 559
Cdd:cd03254 8 VNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRfydpqkgqiliDGIDIRDIsRKSLRS-MIGVvlqdt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 --FSQHHVEQLDLNVS----AVELLARKFPGLP------EEEYRHQLGRYGisgelamrpvASLSGGQKSRVAFAQMTMP 627
Cdd:cd03254 87 flFSGTIMENIRLGRPnatdEEVIEAAKEAGAHdfimklPNGYDTVLGENG----------GNLSQGERQLLAIARAMLR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 628 CPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSH 665
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGrtSIIIAH 196
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
504-670 |
4.67e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 63.05 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 504 KHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGdlspvrgirhAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFP 583
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG----------ALKGTPVAGCVDVPDNQFGREASLIDAIGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 584 GLPEEEYrhqLGRYGISGELAM-RPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGQALNNFRG 658
Cdd:COG2401 112 FKDAVEL---LNAVGLSDAVLWlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDrqtaKRVARNLQKLARRAGI 188
|
170
....*....|..
gi 29789050 659 GVILVSHDERFI 670
Cdd:COG2401 189 TLVVATHHYDVI 200
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
492-685 |
4.78e-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 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: 64.01 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKhSIFSRLS---VSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRG------------------- 547
Cdd:TIGR04521 1 IKLKNVSYIYQPG-TPFEKKAlddVSLTIEDGefVAIIGHTGSGKSTLIQHLNGLLKPTSGtvtidgrditakkkkklkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 548 IRHahrnlKIGY---FSQHhveQL--------------DLNVSAVELLAR-----KFPGLPEEeyrhqlgrygisgeLAM 605
Cdd:TIGR04521 80 LRK-----KVGLvfqFPEH---QLfeetvykdiafgpkNLGLSEEEAEERvkealELVGLDEE--------------YLE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 606 RPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEALGQALNNfrgGVILVSHDERFIRLVCKELW 678
Cdd:TIGR04521 138 RSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDpkgrkeiLDLFKRLHKEKGL---TVILVTHSMEDVAEYADRVI 214
|
....*..
gi 29789050 679 VCENGSV 685
Cdd:TIGR04521 215 VMHKGKI 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
328-402 |
4.92e-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: 4.92e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLnAIATDIIHLHSQRL 402
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegeRALNQAIAALKAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
302-420 |
6.22e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 63.45 E-value: 6.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 302 KAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTIL 378
Cdd:PRK10619 127 EARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMV 206
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 29789050 379 VVSHDRNFLNAIATDIIHLHSQRLDGYRGDFETFIKSKQERL 420
Cdd:PRK10619 207 VVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRL 248
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
523-691 |
6.43e-11 |
|
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: 62.98 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLL-----------------MGDLSPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 581
Cdd:cd03258 36 IIGRSGAGKSTLIRCInglerptsgsvlvdgtdLTLLSG-KELRKARR--RIGMIFQH-----------FNLLSSRtvfe 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 ---FP----GLP----EEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IE 647
Cdd:cd03258 102 nvaLPleiaGVPkaeiEERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 648 ALGQALNNFRG-GVILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:cd03258 181 ALLRDINRELGlTIVLITHEMEVVKRICDRVAVMEKGEV--VEEG 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
188-402 |
7.47e-11 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 62.43 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHIsllhveqEVAGDDTPALQSVlesdtvREDLLRQ 267
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTI-------RVNGQDVSDLRGR------AIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 268 E--------RELSLRIAAGRAegseAAQLAEIYGKLEEIeadkaPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALA 339
Cdd:cd03292 79 KigvvfqdfRLLPDRNVYENV----AFALEVTGVPPREI-----RKRVPAALELVGLSHKHRALPA-ELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 340 RALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDpdtTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
492-685 |
8.13e-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: 62.45 E-value: 8.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSrLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHA--HR--NLKIGY 559
Cdd:cd03224 1 LEVENLNAGYGKSQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGsirfdgrdITGLppHEraRAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 -------FSQHHVEQlDLNVSAVELLARKFPGLPEE---------EYRHQLGrygisgelamrpvASLSGGQKSRVAFAQ 623
Cdd:cd03224 80 vpegrriFPELTVEE-NLLLGAYARRRAKRKARLERvyelfprlkERRKQLA-------------GTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 624 MTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVSHDERFIRLVCKELWVCENGSV 685
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEgvtILLVEQNARFALEIADRAYVLERGRV 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
193-395 |
8.17e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.83 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahisllhVEQEVAGDDTPALQSVLESDTVREDLLRQEREL- 271
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTM-------------IETPTGGELYYQGQDLLKADPEAQKLLRQKIQIv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 272 ------SL--RIAAGraegseaAQLAE---IYGKLEEieADKApARASVILAGLGFTPKMQQQPTREFSGGWRMRLALAR 340
Cdd:PRK11308 98 fqnpygSLnpRKKVG-------QILEEpllINTSLSA--AERR-EKALAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 341 ALFARPDLLLLDEPTNMLDV--RA-ILWLENYLQTWPSTILV-VSHDRNFLNAIATDII 395
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVsvQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIADEVM 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
178-383 |
8.54e-11 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 62.64 E-value: 8.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLES 257
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIA--------------------GFETPTSGEILLD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQERELS-----------LRIAAGRAEGSEAAQLAEiygklEEIEADKAPARASVILAGLGftpkmqQQPTR 326
Cdd:cd03300 61 GKDITNLPPHKRPVNtvfqnyalfphLTVFENIAFGLRLKKLPK-----AEIKERVAEALDLVQLEGYA------NRKPS 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR----AILWLENYLQTWPSTILVVSHD 383
Cdd:cd03300 130 QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKlrkdMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
506-672 |
1.12e-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: 60.45 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 506 SIFSRLSVSADLESRICVVGENGAGKSTMLKllmgDLSPVRGIRHAHRNlkigyfsQHHVEQLDLNVSAVELLARKFpgl 585
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILD----AIGLALGGAQSATR-------RRSGVKAGCIVAAVSAELIFT--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 586 peeeyRHQlgrygisgelamrpvasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGQALNNFRGG- 659
Cdd:cd03227 75 -----RLQ-----------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKg 131
|
170
....*....|....*
gi 29789050 660 --VILVSHDERFIRL 672
Cdd:cd03227 132 aqVIVITHLPELAEL 146
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
192-402 |
1.18e-10 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 62.90 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 192 LLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrslrvpahislLHVEQEVAGDDTPALQSVLESDtvREDLLRQEREL 271
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLL-------------LGLEKPAQGTVSFRGQDLYQLD--RKQRRAFRRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 272 SL----RIAAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:TIGR02769 91 QLvfqdSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 348 LLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:TIGR02769 171 LIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
521-645 |
1.39e-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: 61.93 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG----------------IRHAHRnlKIGYFSQHH--VEQLDL--NV-------- 572
Cdd:TIGR02315 31 VAIIGPSGAGKSTLLRCINRLVEPSSGsillegtditklrgkkLRKLRR--RIGMIFQHYnlIERLTVleNVlhgrlgyk 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 573 SAVELLARKFPGLPEEEYRHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 645
Cdd:TIGR02315 109 PTWRSLLGRFSEEDKERALSALERVGLA-DKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKT 180
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-420 |
1.46e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpaHISLLHVEQEVAGDDTPALQSVLES 257
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--------RMNELESEVRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvREDLLRQERELSLRIAAGR----AEGSEAAQLAEIYGKLEEIEADKApARASVILAGLGFTPKMQ-QQPTREFSGGW 332
Cdd:PRK14258 80 ---RVNLNRLRRQVSMVHPKPNlfpmSVYDNVAYGVKIVGWRPKLEIDDI-VESALKDADLWDEIKHKiHKSALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWP----STILVVSHDRNFLNAIAtdiihlhsqrldgyrgD 408
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLS----------------D 219
|
250
....*....|..
gi 29789050 409 FETFIKSKQERL 420
Cdd:PRK14258 220 FTAFFKGNENRI 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
488-674 |
1.68e-10 |
|
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: 61.92 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHsIFSRlsVSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL--------- 555
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRV-VLDG--VSLDVPrgEILAIIGGSGSGKSVLLKLIIGLLRPDSGeILVDGQDItglsekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 556 ----KIGY-------FSqhhveqlDLNVSA-VELLARKFPGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRV 619
Cdd:COG1127 79 elrrRIGMlfqggalFD-------SLTVFEnVAFPLREHTDLSEAEIRELvlekLELVGLPGAADKMP-SELSGGMRKRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 620 AFAQMTMPCPNFYILDEPTNHLD---METIEALGQALNNFRGG-VILVSHDERFIRLVC 674
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpitSAVIDELIRELRDELGLtSVVVTHDLDSAFAIA 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
181-389 |
1.80e-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: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLH-VEQEVAGDDTPalqsvleSDT 259
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILA----------GLLRpDSGEVRWNGTP-------LAE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 VREDLLRQERELSLRiAAGRAEGSEAAQL---AEIYGkleeiEADKAP--ARASVILAGLgftpkmQQQPTREFSGGWRM 334
Cdd:TIGR01189 67 QRDEPHENILYLGHL-PGLKPELSALENLhfwAAIHG-----GAQRTIedALAAVGLTGF------EDLPAAQLSAGQQR 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLDVRAILWL----ENYLQTWPSTILVVSHDRNFLNA 389
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDKAGVALLagllRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
197-402 |
1.89e-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: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtPALQSVleSDTVREDLLRQERELSLRIA 276
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIA--GFETPQSGRVLINGVDVTAAP-PADRPV--SMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 277 AGRAEGSeaaqlaeiygKLEEIEADkapaRASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTN 356
Cdd:cd03298 93 LGLSPGL----------KLTAEDRQ----AIEVALARVGLAGLEKRLP-GELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 357 MLD--VRA---ILWLENYLQTwPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:cd03298 158 ALDpaLRAemlDLVLDLHAET-KMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
207-383 |
2.30e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLAtrslrvpahiSLLHV---EQEVAGDDtPALQsvlesdtvREDLLR-------QEREL----- 271
Cdd:COG4586 52 GFIGPNGAGKSTTIKMLT----------GILVPtsgEVRVLGYV-PFKR--------RKEFARrigvvfgQRSQLwwdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 272 ---SLRIaagraegseaaqLAEIYgkleEIEADKAPARASVILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDL 348
Cdd:COG4586 113 aidSFRL------------LKAIY----RIPDAEYKKRLDELVELLDLGELLDT-PVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 29789050 349 LLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 383
Cdd:COG4586 176 LFLDEPTIGLDVvskEAIReFLKEYNRERGTTILLTSHD 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
522-674 |
2.54e-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: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVV--GENGAGKSTMLKLLMGDLSPVRG---IRHAHRNL----------------KIGYFSQHhveqldLN----VSAVE 576
Cdd:COG4778 39 CVAltGPSGAGKSTLLKCIYGNYLPDSGsilVRHDGGWVdlaqaspreilalrrrTIGYVSQF------LRviprVSALD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 577 -----LLARkfpGLPEEEYRHQ----LGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-- 645
Cdd:COG4778 113 vvaepLLER---GVDREEARARarelLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANra 189
|
170 180 190
....*....|....*....|....*....|..
gi 29789050 646 --IEALGQALNnfRG-GVILVSHDERFIRLVC 674
Cdd:COG4778 190 vvVELIEEAKA--RGtAIIGIFHDEEVREAVA 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
503-687 |
2.54e-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: 63.52 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 503 PKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL---KIGYFSQ--------- 562
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGsvrldgadLKQWDRETfgkHIGYLPQdvelfpgtv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 -HHVEQLDLNVSAVELL-ARKFPGLPE------EEYRHQLGRYGisgelamrpvASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:TIGR01842 409 aENIARFGENADPEKIIeAAKLAGVHElilrlpDGYDTVIGPGG----------ATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 635 DEPTNHLDMETIEALGQALNNF--RGG-VILVSHDERFIRLVCKELwVCENGSVTR 687
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALkaRGItVVVITHRPSLLGCVDKIL-VLQDGRIAR 533
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
193-383 |
2.60e-10 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 60.94 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEV---AGDDTPALQ--SVLESDTVREDLlrq 267
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLIS--GLAQPTSGGVILEGKQItepGPDRMVVFQnySLLPWLTVRENI--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 268 erelSLRIAAGRAEGSEAAQLAEIYGKLEeieadkaparasviLAGLGftpKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:TIGR01184 76 ----ALAVDRVLPDLSKSERRAIVEEHIA--------------LVGLT---EAADKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 348 LLLLDEPTNMLD--VRAILWlENYLQTWPS---TILVVSHD 383
Cdd:TIGR01184 135 VLLLDEPFGALDalTRGNLQ-EELMQIWEEhrvTVLMVTHD 174
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
167-360 |
2.72e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 61.48 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 167 LESSGKNKSYDVRIENFDVSFgdrvllagadvNLAWGRRYGLVGRNGLGKTTLLKMLATRSlrVPAHISLLHVEQEVAGD 246
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSF-----------DLYPGEVLGIVGESGSGKTTLLNALSARL--APDAGEVHYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DTPALqsvleSDTVREDLLRQE--------RE-LSLRIAAGRAEGSE-AAQLAEIYGK--------LEEIEADkaPARas 308
Cdd:PRK11701 74 DLYAL-----SEAERRRLLRTEwgfvhqhpRDgLRMQVSAGGNIGERlMAVGARHYGDiratagdwLERVEID--AAR-- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 309 vilaglgftpkMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK11701 145 -----------IDDLP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV 184
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
492-685 |
3.33e-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: 60.58 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYdpkHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAH------------- 552
Cdd:cd03298 1 VRLDKIRFSY---GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPqsgrvlINGVDVTAappadrpvsmlfq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 553 -RNLkigyFSQHHVEQ-LDLNVSavellarkfPGLPEEEYRHQ-----LGRYGISGELAMRPvASLSGGQKSRVAFAQMT 625
Cdd:cd03298 78 eNNL----FAHLTVEQnVGLGLS---------PGLKLTAEDRQaievaLARVGLAGLEKRLP-GELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 626 MPCPNFYILDEPTNHLDMETIEALGQALNNFRG----GVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAetkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
487-693 |
3.75e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.56 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 487 FSPPILqLDEVDFYYDPKHSIFSRLSVSADLESR----ICVVGENGAGKSTMLKL------------LMGD------LSP 544
Cdd:PRK13645 3 FSKDII-LDNVSYTYAKKTPFEFKALNNTSLTFKknkvTCVIGTTGSGKSTMIQLtngliisetgqtIVGDyaipanLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 545 VRGIRHAHRNLKIGY-FSQHHVEQ----LDLNVSAVELLARKfpglpEEEYR---HQLGRYGISGELAMRPVASLSGGQK 616
Cdd:PRK13645 82 IKEVKRLRKEIGLVFqFPEYQLFQetieKDIAFGPVNLGENK-----QEAYKkvpELLKLVQLPEDYVKRSPFELSGGQK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 617 SRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGQALN-NFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGGF 692
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDpkgEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
.
gi 29789050 693 D 693
Cdd:PRK13645 237 E 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
491-665 |
3.77e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLE----SRICVVGENGAGKSTMLKLLMGDLSPVRG-----------------IR 549
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEvkkgSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgdivvsstskqkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 550 HAHRnlKIGYFSQHHVEQL--DLNVSAVELLARKFpGLPEEEYR----HQLGRYGISGELAMRPVASLSGGQKSRVAFAQ 623
Cdd:PRK13643 81 PVRK--KVGVVFQFPESQLfeETVLKDVAFGPQNF-GIPKEKAEkiaaEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 624 MTMPCPNFYILDEPTNHLD----------METIEALGQAlnnfrggVILVSH 665
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDpkariemmqlFESIHQSGQT-------VVLVTH 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
178-401 |
4.13e-10 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 59.99 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRVpahisLLHVEQEVAGDDTPalqsvlES 257
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI----LGI-----ILPDSGEVLFDGKP------LD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDL--LRQERELSLRiaagRAEGSEAAQLAEIYG-KLEEieadkAPARASVILAGLGFTPKmQQQPTREFSGGWRM 334
Cdd:cd03269 66 IAARNRIgyLPEERGLYPK----MKVIDQLVYLAQLKGlKKEE-----ARRRIDEWLERLELSEY-ANKRVEELSKGNQQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:cd03269 136 KVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
525-685 |
4.25e-10 |
|
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: 60.07 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSP------VRGIRhAHRN-----LKIGYFSQHhvEQLDLNVSAVELLA--RKFPGLPEEEYR 591
Cdd:cd03266 38 GPNGAGKTTTLRMLAGLLEPdagfatVDGFD-VVKEpaearRRLGFVSDS--TGLYDRLTARENLEyfAGLYGLKGDELT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 592 HQL----GRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVS 664
Cdd:cd03266 115 ARLeelaDRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkcILFST 193
|
170 180
....*....|....*....|.
gi 29789050 665 HDERFIRLVCKELWVCENGSV 685
Cdd:cd03266 194 HIMQEVERLCDRVVVLHRGRV 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
488-668 |
4.49e-10 |
|
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: 60.53 E-value: 4.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYY-DPKHS--IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGI---------------R 549
Cdd:COG4181 5 SAPIIELRGLTKTVgTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTvrlagqdlfaldedaR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 550 HAHRNLKIGYFSQHhvEQLDLNVSAVE--LLARKFPGLPE--EEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMT 625
Cdd:COG4181 85 ARLRARHVGFVFQS--FQLLPTLTALEnvMLPLELAGRRDarARARALLERVGLGHRLDHYP-AQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 626 MPCPNFYILDEPTNHLDMET---IEALGQALNNFRGG-VILVSHDER 668
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATgeqIIDLLFELNRERGTtLVLVTHDPA 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
178-361 |
4.88e-10 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 60.32 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAHI 234
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLdiPAGETVALVGPSGSGKSTLVNLIprfydvdsgrilidghdvrdyTLASLR--RQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 235 SLlhVEQEVagddtpalqsVLESDTVREDLLRQERElslriaAGRAEGSEAAQLAEIYGKLEEIEadkaparasvilagL 314
Cdd:cd03251 79 GL--VSQDV----------FLFNDTVAENIAYGRPG------ATREEVEEAARAANAHEFIMELP--------------E 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 315 GFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:cd03251 127 GYDTVIGERGVK-LSGGQRQRIAIARALLKDPPILILDEATSALDTE 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
508-688 |
5.50e-10 |
|
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: 60.04 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 508 FSRLSVSADLE-SRICVV-GENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNlkIGYFSQHHVEQLDLNVS- 573
Cdd:cd03299 13 FKLKNVSLEVErGDYFVIlGPTGSGKSVLLETIAGFIKPDSGkillngkditnLPPEKRD--ISYVPQNYALFPHMTVYk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 574 --AVELLARKFPGLPEEEYRHQLGRY-GISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET----I 646
Cdd:cd03299 91 niAYGLKKRKVDKKEIERKVLEIAEMlGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 647 EALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRV 688
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQV 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
523-673 |
6.03e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMG-------------------DLSPvrgirhAHR-NLKIGYFSQHHVE----------QLDLN- 571
Cdd:COG0396 31 IMGPNGSGKSTLAKVLMGhpkyevtsgsilldgedilELSP------DERaRAGIFLAFQYPVEipgvsvsnflRTALNa 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 VSAVELLARKFpglpEEEYRHQLGRYGISGELAMRPV-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALG 650
Cdd:COG0396 105 RRGEELSAREF----LKLLKEKMKELGLDEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVA 180
|
170 180
....*....|....*....|....*.
gi 29789050 651 QALNNFRG---GVILVSHDERFIRLV 673
Cdd:COG0396 181 EGVNKLRSpdrGILIITHYQRILDYI 206
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
491-686 |
6.53e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 60.41 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGY 559
Cdd:PRK11231 2 TLRTENLTVGYGTK-RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtVFLGDKPIsmlssrqlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHVEQLDLNVSavELLAR-KFPGLP-------EEEYRHQ--LGRYGISgELAMRPVASLSGGQKSRvAFAQMTMPC- 628
Cdd:PRK11231 81 LPQHHLTPEGITVR--ELVAYgRSPWLSlwgrlsaEDNARVNqaMEQTRIN-HLADRRLTDLSGGQRQR-AFLAMVLAQd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 629 PNFYILDEPTNHLDM----ETIEALGQaLNNFRGGVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:PRK11231 157 TPVVLLDEPTTYLDInhqvELMRLMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVM 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
179-361 |
6.65e-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: 6.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRvPA--HISLLhvEQEVAGDDTPALQSVLe 256
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLL-TGELT-PSsgEVRLN--GRPLAAWSPWELARRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 sdTVredlLRQERELSLR------IAAGRA-EGSEAAQLAEIygkleeieADKAPARASviLAGLGftpkmqQQPTREFS 329
Cdd:COG4559 78 --AV----LPQHSSLAFPftveevVALGRApHGSSAAQDRQI--------VREALALVG--LAHLA------GRSYQTLS 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 29789050 330 GGWRMRLALARAL-------FARPDLLLLDEPTNMLDVR 361
Cdd:COG4559 136 GGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALDLA 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
504-666 |
6.87e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.39 E-value: 6.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 504 KHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG---------IRHAHRNL--KIGYFSQHHVEQLDLNV 572
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGhvwldgehiQHYASKEVarRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 SavELLAR-KFPGLP---------EEEYRHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK10253 99 Q--ELVARgRYPHQPlftrwrkedEEAVTKAMQATGIT-HLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180
....*....|....*....|....*....
gi 29789050 643 ----METIEALGQaLNNFRGGVI-LVSHD 666
Cdd:PRK10253 176 ishqIDLLELLSE-LNREKGYTLaAVLHD 203
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
492-687 |
7.68e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 60.61 E-value: 7.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSI----FSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGI----------RHAHRNLK- 556
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTitiagyhitpETGNKNLKk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 ----IGYFSQHHVEQLDLN--VSAVELLARKFpGLPEEEYRHQ----LGRYGISGELAMRPVASLSGGQKSRVAFAQMTM 626
Cdd:PRK13641 83 lrkkVSLVFQFPEAQLFENtvLKDVEFGPKNF-GFSEDEAKEKalkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 627 PCPNFYILDEPTNHLDMETIEALGQALNNF-RGG--VILVSHDERFIRLVCKELWVCENGSVTR 687
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGhtVILVTHNMDDVAEYADDVLVLEHGKLIK 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
486-666 |
7.86e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 60.39 E-value: 7.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 486 KFSPPILQLDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrNLKI-GY-FSQ 562
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSG------EIKIdGItISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 HHVEQLDLNV-------------SAVE------LLARKFPglPEE------EYRHQLgryGISGELAMRPvASLSGGQKS 617
Cdd:PRK13632 76 ENLKEIRKKIgiifqnpdnqfigATVEddiafgLENKKVP--PKKmkdiidDLAKKV---GMEDYLDKEP-QNLSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 618 RVAFAQMTMPCPNFYILDEPTNHLD----METIEALGQALNNFRGGVILVSHD 666
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
506-698 |
8.20e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.40 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 506 SIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGYFSQHHVEQLDLNVSA 574
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGtVLVAGDDVealsaraasrRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 575 VELLAR-----KFPGLPEEEYR---HQLGRYGISgELAMRPVASLSGGQKSRV----AFAQMTmpcPNFyILDEPTNHLD 642
Cdd:PRK09536 97 VVEMGRtphrsRFDTWTETDRAaveRAMERTGVA-QFADRPVTSLSGGERQRVllarALAQAT---PVL-LLDEPTASLD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 643 M----ETIEaLGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVT------------RVEGGFDQYRAL 698
Cdd:PRK09536 172 InhqvRTLE-LVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRaagppadvltadTLRAAFDARTAV 242
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
301-419 |
8.93e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 8.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 301 DKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWP 374
Cdd:COG4161 116 EQAREKAMKLLARLRLTDKADRFPLH-LSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqVVEII---RELSQTG 191
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 29789050 375 STILVVSHDRNFLNAIATDIIHLHSQRLDGYrGDFETFIKSKQER 419
Cdd:COG4161 192 ITQVIVTHEVEFARKVASQVVYMEKGRIIEQ-GDASHFTQPQTEA 235
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
482-684 |
9.02e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 482 DGFEKFSPPILQLDEVDFYYDPkHSIFSRLsvsadlesricvvGENGAGKSTMLKLLMGDLSPVRGI---------RHAH 552
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYP-GEIHALL-------------GENGAGKSTLMKVLSGIHEPTKGTitinninynKLDH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 553 R---NLKIGYFSQHH--VEQLDL--NVSAVELLARKFPGLPEEEYRHQ-------LGRYGISGELAMRpVASLSGGQKSR 618
Cdd:PRK09700 75 KlaaQLGIGIIYQELsvIDELTVleNLYIGRHLTKKVCGVNIIDWREMrvraammLLRVGLKVDLDEK-VANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 619 VAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSHDERFIRLVCKELWVCENGS 684
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDRYTVMKDGS 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
179-409 |
9.43e-10 |
|
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: 59.50 E-value: 9.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGD-RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHISLLHVEQEVAGDDTPALQSVles 257
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNG--LVEPTSGSVLIDGTDINKLKGKALRQL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvRED--LLRQERELSLRIAA------GR-AEGSEAAQLAEIYGKLEEIEADKAPARasVILAGLGFtpkmqqQPTREF 328
Cdd:cd03256 77 ---RRQigMIFQQFNLIERLSVlenvlsGRlGRRSTWRSLFGLFPKEEKQRALAALER--VGLLDKAY------QRADQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWPSTILVVSHDRNFLNAIATDIIHLHSQRL-- 402
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQVDLAREYADRIVGLKDGRIvf 225
|
....*..
gi 29789050 403 DGYRGDF 409
Cdd:cd03256 226 DGPPAEL 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
184-382 |
9.96e-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: 59.41 E-value: 9.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 184 DVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVAGDDTPALQSVLEsd 258
Cdd:cd03248 16 NVTFAyptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALL--ENFYQPQGGQVLLDGKPISQYEHKYLHSKVS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 tvredLLRQERELSLRiaagraegSEAAQLAeiYGkLEEIEADKAPARASVILAGlGFTPKMQQQPTRE-------FSGG 331
Cdd:cd03248 92 -----LVGQEPVLFAR--------SLQDNIA--YG-LQSCSFECVKEAAQKAHAH-SFISELASGYDTEvgekgsqLSGG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 332 WRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPErrTVLVIAH 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
505-665 |
1.15e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 505 HSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHA----HRNLK-IGyfsqhHVEQLDLN 571
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGevlwqgepIRRQrdeyHQDLLyLG-----HQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 VSAVELL--ARKFPGLPEEEYRHQ-LGRYGISG-ELAmrPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIE 647
Cdd:PRK13538 89 LTALENLrfYQRLHGPGDDEALWEaLAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVA 166
|
170 180
....*....|....*....|.
gi 29789050 648 ALGQALNNF--RGG-VILVSH 665
Cdd:PRK13538 167 RLEALLAQHaeQGGmVILTTH 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
301-383 |
1.58e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 301 DKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPST- 376
Cdd:PRK11629 120 AEINSRALEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadSIFQLLGELNRLQGTa 198
|
....*..
gi 29789050 377 ILVVSHD 383
Cdd:PRK11629 199 FLVVTHD 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
492-691 |
1.68e-09 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 58.33 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYdpkHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG---------IRHAHRNLKIGYFSQ 562
Cdd:TIGR01277 1 LALDKVRYEY---EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGsikvndqshTGLAPYQRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 HHVEQLDLNVSAVELLARKfPGLP----EEEYRHQLGR-YGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLH-PGLKlnaeQQEKVVDAAQqVGIADYLDRLP-EQLSGGQRQRVALARCLVRPNPILLLDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 638 TNHLD----METIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTRVEGG 691
Cdd:TIGR01277 156 FSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
207-383 |
1.89e-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: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLA--------------------TRSLRVPAH---ISLlhVEQEvagddtPALQSVLesdTVRED 263
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAglerpdsgrirlggevlqdsARGIFLPPHrrrIGY--VFQE------ARLFPHL---SVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 264 LLrqereLSLRIAAGRAEGSEAAQLAEIygkleeieadkaparasvilagLGFTPKMQQQPTReFSGGWRMRLALARALF 343
Cdd:COG4148 98 LL-----YGRKRAPRAERRISFDEVVEL----------------------LGIGHLLDRRPAT-LSGGERQRVAIGRALL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 344 ARPDLLLLDEPTNMLDV---RAILwleNYLQTWPST----ILVVSHD 383
Cdd:COG4148 150 SSPRLLLMDEPLAALDLarkAEIL---PYLERLRDEldipILYVSHS 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
178-402 |
2.12e-09 |
|
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: 58.04 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPA----LQS 253
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIA--GLEEPTSGRIYIGGRDVT--DLPPkdrdIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLES------DTVREDL---LRQ----ERELSLRIaagraegSEAAQLAEIYGKLeeieaDKAParasvilaglgftpkm 320
Cdd:cd03301 77 VFQNyalyphMTVYDNIafgLKLrkvpKDEIDERV-------REVAELLQIEHLL-----DRKP---------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 321 qqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIH 396
Cdd:cd03301 129 -----KQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAV 203
|
....*.
gi 29789050 397 LHSQRL 402
Cdd:cd03301 204 MNDGQI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
176-383 |
2.15e-09 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 58.50 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 176 YDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDTPALQ--- 252
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIA--GLERPDSGTILFGGEDATDVPVQERNvgf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 -----SVLESDTVREDLlrqerELSLRIAAGRAEGSEAaqlaEIYGKLEEIeadkapaRASVILAGLGftpkmQQQPTrE 327
Cdd:cd03296 79 vfqhyALFRHMTVFDNV-----AFGLRVKPRSERPPEA----EIRAKVHEL-------LKLVQLDWLA-----DRYPA-Q 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHD 383
Cdd:cd03296 137 LSGGQRQRVALARALAVEPKVLLLDEPFGALDakVRKELrrWLRRLHDELHVTTVFVTHD 196
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
180-397 |
2.26e-09 |
|
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: 58.43 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR-SLRVPA-HISLlhveqevAGDDTPAL------ 251
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpSYEVTSgTILF-------KGQDLLELepdera 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 --------QSVLESDTVR-EDLLRqerelSLRIAAGRAEGSEAAQLAEIYGKLEEIeadkaparasviLAGLGFTPKMQQ 322
Cdd:TIGR01978 76 raglflafQYPEEIPGVSnLEFLR-----SALNARRSARGEEPLDLLDFEKLLKEK------------LALLDMDEEFLN 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 323 QPTRE-FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:TIGR01978 139 RSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIdalKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVHV 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
301-395 |
2.27e-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: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 301 DKAPARASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTI 377
Cdd:PRK11264 119 EEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDpelVGEVLNTIRQLAQEKRTM 197
|
90
....*....|....*...
gi 29789050 378 LVVSHDRNFLNAIATDII 395
Cdd:PRK11264 198 VIVTHEMSFARDVADRAI 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
494-687 |
2.35e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 59.26 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 494 LDEVDFYYDPKhSIFSRL-----SVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIGYfSQHHVEQ 567
Cdd:PRK13634 5 FQKVEHRYQYK-TPFERRalydvNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtVTIGERVITAGK-KNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 LDLNVSAVellaRKFP--------------------GLPEEE----YRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQ 623
Cdd:PRK13634 83 LRKKVGIV----FQFPehqlfeetvekdicfgpmnfGVSEEDakqkAREMIELVGLPEELLARSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 624 MTMPCPNFYILDEPTNHLD-------METIEALGQalnnfRGG--VILVSHDERFIRLVCKELWVCENGSVTR 687
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDpkgrkemMEMFYKLHK-----EKGltTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
492-671 |
2.39e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.86 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHS----IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirHAHRNLKIGYFSQ----- 562
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSG--SVSVPGSIAYVSQepwiq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 563 -------------HHVEQLDLNVSAVELLA--RKFPGLPEEEyrhqLGRYGIsgelamrpvaSLSGGQKSRVAFAQMTMP 627
Cdd:cd03250 79 ngtirenilfgkpFDEERYEKVIKACALEPdlEILPDGDLTE----IGEKGI----------NLSGGQKQRISLARAVYS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789050 628 CPNFYILDEPTNHLDMET---I--EALGQALNNFRgGVILVSHDERFIR 671
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVgrhIfeNCILGLLLNNK-TRILVTHQLQLLP 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
179-383 |
2.51e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 60.10 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSF-----------GDRVLLAGADVNLAWGRRYGLVGRNGLGKTT----LLKMLATR-----------SLRVPA 232
Cdd:PRK15134 277 DVEQLQVAFpirkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQgeiwfdgqplhNLNRRQ 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 233 HISLLHVEQEVAGDDTPALQSVLESDTVREDLLR-QERELSlriaagraegsEAAQLAEIYGKLEEIeadkaparasvil 311
Cdd:PRK15134 357 LLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRvHQPTLS-----------AAQREQQVIAVMEEV------------- 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 312 aglGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA-ILWLENYLQ-TWPSTILVVSHD 383
Cdd:PRK15134 413 ---GLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktVQAqILALLKSLQqKHQLAYLFISHD 485
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
521-673 |
2.61e-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: 57.92 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL-----KIGYFSQH-----HVEQLDlNVSaveLLARKF 582
Cdd:cd03262 29 VVIIGPSGSGKSTLLRCINLLEEPDSGtiiidglkLTDDKKNInelrqKVGMVFQQfnlfpHLTVLE-NIT---LAPIKV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 583 PGLPEEEY----RHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI-EALGQALNNFR 657
Cdd:cd03262 105 KGMSKAEAeeraLELLEKVGLADKADAYP-AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVgEVLDVMKDLAE 183
|
170
....*....|....*...
gi 29789050 658 GG--VILVSHDERFIRLV 673
Cdd:cd03262 184 EGmtMVVVTHEMGFAREV 201
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
492-685 |
2.76e-09 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 58.23 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSrLSVSADleSRICVVGENGAGKSTMLKLLMGDLSPVRG-IR-----HAHR------------ 553
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFD-LTIAAG--ERVAILGPSGAGKSTLLNLIAGFLPPDSGrILwngqdLTALppaerpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 554 --NLkigyFSQHHVEQldlNVSavelLARKfPGL-PEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTM 626
Cdd:COG3840 79 enNL----FPHLTVAQ---NIG----LGLR-PGLkLTAEQRAQveqaLERVGLAGLLDRLP-GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 627 ---PCpnfYILDEPTNHLD-------METIEALGQALNNfrgGVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:COG3840 146 rkrPI---LLLDEPFSALDpalrqemLDLVDELCRERGL---TVLMVTHDPEDAARIADRVLLVADGRI 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
327-700 |
2.77e-09 |
|
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: 60.08 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTwpST---ILVVSHDRNFLNAIATDIIHLHsq 400
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDLLKDLQR--ELgmaLLLITHDLGVVRRFADRVAVMR-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 401 rlDGY---RGDFETFIKSkqerllnqqreyeAQQQYRQHiqvfidrfrynanrasqvqsklkMLEKLPELKPVDKESEvv 477
Cdd:COG4172 232 --QGEiveQGPTAELFAA-------------PQHPYTRK-----------------------LLAAEPRGDPRPVPPD-- 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 478 lkfpdgfekfSPPILQLDEVDFYYDPKHSIFSRL--------SVSADL---ESrICVVGENGAGKST----MLKLL---- 538
Cdd:COG4172 272 ----------APPLLEARDLKVWFPIKRGLFRRTvghvkavdGVSLTLrrgET-LGLVGESGSGKSTlglaLLRLIpseg 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 539 ----MG-DLSPVRG--IRHAHRNLKI------GYFS-QHHVEQLdlnVSavELLARKFPGLPEEEYRHQ----LGRYGIS 600
Cdd:COG4172 341 eirfDGqDLDGLSRraLRPLRRRMQVvfqdpfGSLSpRMTVGQI---IA--EGLRVHGPGLSAAERRARvaeaLEEVGLD 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 601 GELAMRPVASLSGGQKSRVAFAQ-MTMPcPNFYILDEPTNHLDMeTIEAlgQALNNFRG-----GV--ILVSHDERFIRL 672
Cdd:COG4172 416 PAARHRYPHEFSGGQRQRIAIARaLILE-PKLLVLDEPTSALDV-SVQA--QILDLLRDlqrehGLayLFISHDLAVVRA 491
|
410 420 430
....*....|....*....|....*....|....*...
gi 29789050 673 VCKELWVCENGSVtrVEGG-----FDQ----Y-RALLQ 700
Cdd:COG4172 492 LAHRVMVMKDGKV--VEQGpteqvFDApqhpYtRALLA 527
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
492-704 |
3.22e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMG-----------DLSPVRGIRHA--------- 551
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegeirlDGRPLSSLSHSvlrqgvamv 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 552 -----------HRNLKIGY-FSQHHVEQLdlnVSAVEL--LARKFPGlpeeeyrhqlGRYGISGELAmrpvASLSGGQKS 617
Cdd:PRK10790 421 qqdpvvladtfLANVTLGRdISEEQVWQA---LETVQLaeLARSLPD----------GLYTPLGEQG----NNLSVGQKQ 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 618 RVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLV-CKELWVCENGSVtrVEGGfdQYR 696
Cdd:PRK10790 484 LLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVeADTILVLHRGQA--VEQG--THQ 559
|
....*...
gi 29789050 697 ALLQEQFR 704
Cdd:PRK10790 560 QLLAAQGR 567
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
491-685 |
3.28e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 58.55 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL-----KI 557
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgepIKYDKKSLlevrkTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHVEQL-------DLNVSAVELlarkfpGLPEEEY----RHQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTM 626
Cdd:PRK13639 81 GIVFQNPDDQLfaptveeDVAFGPLNL------GLSKEEVekrvKEALKAVGMEG-FENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 627 PCPNFYILDEPTNHLDMETIEALGQALN--NFRGGVILVS-HDERFIRLVCKELWVCENGSV 685
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYdlNKEGITIIIStHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
178-382 |
3.30e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 58.00 E-value: 3.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLkmlatrslRVPAHISLLHVEQEVAGDDTPALQSVLES 257
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLL--------RVFNRLIELYPEARVSGEVYLDGQDIFKM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVredLLRQEREL---------SLRIAAGRAEGSEAAQLAEIYGKLEEieadkaPARASVILAGLGFTPKMQ-QQPTRE 327
Cdd:PRK14247 76 DVI---ELRRRVQMvfqipnpipNLSIFENVALGLKLNRLVKSKKELQE------RVRWALEKAQLWDEVKDRlDAPAGK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:PRK14247 147 LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTH 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
191-359 |
3.84e-09 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 57.44 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 191 VLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPAlqsvleSDTVR---EDLLR- 266
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLA--------------------GLDRPT------SGTVRlagQDLFAl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 267 QERELslriAAGRAEG------SEaaQL-------------AEIYGkleeieADKAPARASVILAGLGFTPKMQQQPtRE 327
Cdd:COG4181 80 DEDAR----ARLRARHvgfvfqSF--QLlptltalenvmlpLELAG------RRDARARARALLERVGLGHRLDHYP-AQ 146
|
170 180 190
....*....|....*....|....*....|..
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
207-395 |
3.94e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLA----------TRSLRV---PAHISllhVEQEVagddtpalqsvlesdTVrEDLLRQerelsl 273
Cdd:PRK13409 369 GIVGPNGIGKTTFAKLLAgvlkpdegevDPELKIsykPQYIK---PDYDG---------------TV-EDLLRS------ 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 274 riAAGRAEGSeaaqlaeiYGKLEeieadkaparasvILAGLGFTPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDE 353
Cdd:PRK13409 424 --ITDDLGSS--------YYKSE-------------IIKPLQLERLLDK-NVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789050 354 PTNMLDV-------RAIlwlENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:PRK13409 480 PSAHLDVeqrlavaKAI---RRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
492-645 |
4.08e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 59.75 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGI------------RHAHRNLkIGY 559
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEillngfslkdidRHTLRQF-INY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQhhvEQLDLNVSAVE-LLARKFPGLPEEEYRHQLGRYGISGELAMRPV----------ASLSGGQKSRVAFAQMTMPC 628
Cdd:TIGR01193 553 LPQ---EPYIFSGSILEnLLLGAKENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegSSISGGQKQRIALARALLTD 629
|
170
....*....|....*..
gi 29789050 629 PNFYILDEPTNHLDMET 645
Cdd:TIGR01193 630 SKVLILDESTSNLDTIT 646
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
197-384 |
4.18e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 4.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAW--GRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPALQSVLesdtvreDLLRQEREL--S 272
Cdd:PRK11607 37 DVSLTIykGEIFALLGASGCGKSTLLRMLA--GFEQPTAGQIMLDGVDLS--HVPPYQRPI-------NMMFQSYALfpH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 LRIAAGRAEGSEAAQL--AEIYGKLEEIeadkaparasvilagLGFTpKMQQQPTR---EFSGGWRMRLALARALFARPD 347
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLpkAEIASRVNEM---------------LGLV-HMQEFAKRkphQLSGGQRQRVALARSLAKRPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 348 LLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 384
Cdd:PRK11607 170 LLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQ 210
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
182-383 |
4.55e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 58.97 E-value: 4.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 182 NFDVSFGDRVLlaGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhveqevagDDTpalqsVLESDTVR 261
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVL---------NGR-----TLFDSRKG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 262 EDLLRQERELSLRIAAGRAEGSEAAQLAEIYGkLEEIEADKAPARASVILAGLGFTPkMQQQPTREFSGGWRMRLALARA 341
Cdd:TIGR02142 68 IFLPPEKRRIGYVFQEARLFPHLSVRGNLRYG-MKRARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29789050 342 LFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSHD 383
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDprkYEILpYLERLHAEFGIPILYVSHS 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-665 |
4.61e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.27 E-value: 4.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSP------VRG----IRHAH--RNLKIGYFSQHH--VEQLdlnvSAVE--LLA---RKF 582
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGLYQPdsgeilIDGkpvrIRSPRdaIALGIGMVHQHFmlVPNL----TVAEniVLGlepTKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 583 PGLPEEEYRHQL----GRYGISGELAmRPVASLSGGQKSRV----AFAQmtmpCPNFYILDEPTNHLDMETIEALGQALN 654
Cdd:COG3845 111 GRLDRKAARARIrelsERYGLDVDPD-AKVEDLSVGEQQRVeilkALYR----GARILILDEPTAVLTPQEADELFEILR 185
|
170
....*....|....
gi 29789050 655 NFRG---GVILVSH 665
Cdd:COG3845 186 RLAAegkSIIFITH 199
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
513-685 |
5.24e-09 |
|
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: 57.74 E-value: 5.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG-IR---------HAHR-----------------------NLKI 557
Cdd:COG0411 23 VSLEVErgEIVGLIGPNGAGKTTLFNLITGFYRPTSGrILfdgrditglPPHRiarlgiartfqnprlfpeltvleNVLV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHveqldlnvSAVELLARKFPGLPEEEYR------HQLGRYGIsGELAMRPVASLSGGQKSRVAFAqMTMPC-PN 630
Cdd:COG0411 103 AAHARLG--------RGLLAALLRLPRARREEREareraeELLERVGL-ADRADEPAGNLSYGQQRRLEIA-RALATePK 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 631 FYILDEPT---NHLDMETIEALGQALNNFRG-GVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:COG0411 173 LLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
492-666 |
5.48e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 57.54 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVdfyydpkhSIFSRLS-VSADLES--RICVVGENGAGKSTMLKLLMG-------------DLSPVRGIRHAHRNl 555
Cdd:COG4138 1 LQLNDV--------AVAGRLGpISAQVNAgeLIHLIGPNGAGKSTLLARMAGllpgqgeillngrPLSDWSAAELARHR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 556 kiGYFSQHHVEQLDLNVsaVELLARKFPGLPEEEYRHQL-----GRYGISGELaMRPVASLSGGQKSRVAFAQMTM---- 626
Cdd:COG4138 72 --AYLSQQQSPPFAMPV--FQYLALHQPAGASSEAVEQLlaqlaEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwp 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29789050 627 ---PCPNFYILDEPTNHLDMETIEALGQALNNFR---GGVILVSHD 666
Cdd:COG4138 147 tinPEGQLLLLDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
492-665 |
5.86e-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: 55.62 E-value: 5.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLmGDLSPVRG---IRHAHRNLkigYFsqhhveql 568
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWGSgriGMPEGEDL---LF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 569 dlnvsavelLARKfPGLPEEEYRHQLgRYGISGELamrpvaslSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 648
Cdd:cd03223 69 ---------LPQR-PYLPLGTLREQL-IYPWDDVL--------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|....*..
gi 29789050 649 LGQALNNFRGGVILVSH 665
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
497-699 |
6.80e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.35 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 497 VDFYYD--PKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMG-----------DLSPVRGIRHAHRNLKIGYFSQH 563
Cdd:TIGR00958 484 VSFSYPnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNlyqptggqvllDGVPLVQYDHHYLHRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 564 HV-----------------EQLDLNVSAVELLARKFPGLPEEEYRHQLGRYGisgelamrpvASLSGGQKSRVAFAQMTM 626
Cdd:TIGR00958 564 PVlfsgsvreniaygltdtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG----------SQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 627 PCPNFYILDEPTNHLDMEtIEALGQALNNFRG-GVILVSHDERFIR-----LVCKELWVCENGSVTRVEGGFDQYRALL 699
Cdd:TIGR00958 634 RKPRVLILDEATSALDAE-CEQLLQESRSRASrTVLLIAHRLSTVEradqiLVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
178-360 |
7.35e-09 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 57.76 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF--GDRVLLA--GADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRvpahisLLHVEQEVAGDdtpalqs 253
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKAvdGVSFDVRRGETLGLVGESGSGKSTLARAI----LG------LLPPPGITSGE------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 vlesdtVR---EDLLR-QEREL-SLRiaagraeGSEAA------------------QLAEIYGKLEEIEADKAPARASVI 310
Cdd:COG0444 65 ------ILfdgEDLLKlSEKELrKIR-------GREIQmifqdpmtslnpvmtvgdQIAEPLRIHGGLSKAEARERAIEL 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 311 LAGLGFTPkmqqqPTR-------EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:COG0444 132 LERVGLPD-----PERrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
292-383 |
8.02e-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: 56.58 E-value: 8.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 292 YG-KLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL 370
Cdd:cd03299 94 YGlKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
90
....*....|....*..
gi 29789050 371 QTWPS----TILVVSHD 383
Cdd:cd03299 173 KKIRKefgvTVLHVTHD 189
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
492-665 |
8.05e-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: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLKIGY 559
Cdd:cd03252 1 ITFEHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGrvlvdghdlalADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQhhvEQLDLNVSAVELLARKFPGLPEEEY--------RHQ------LGRYGISGELAmrpvASLSGGQKSRVAFAQMT 625
Cdd:cd03252 81 VLQ---ENVLFNRSIRDNIALADPGMSMERVieaaklagAHDfiselpEGYDTIVGEQG----AGLSGGQRQRIAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 626 MPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSH 665
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGrtVIIIAH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
523-666 |
9.27e-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: 56.99 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNLKIGYFSQHHVEQLDLNVSA--VELLARKFPG----- 584
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGkfddppdwdeiLDEFRGSELQNYFTKLLEGDVKVIVKPqyVDLIPKAVKGkvgel 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 585 LPEEEYRHQLGRYGISGELAM---RPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME---TIEALGQALNNFRG 658
Cdd:cd03236 111 LKKKDERGKLDELVDQLELRHvldRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDDN 190
|
....*...
gi 29789050 659 GVILVSHD 666
Cdd:cd03236 191 YVLVVEHD 198
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
524-666 |
9.58e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.40 E-value: 9.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSP------VRGI---RHAHRNLK-IGY-FSQHhvEQLDLNVSAVE--LLARKFPGLPEEEY 590
Cdd:COG4586 54 IGPNGAGKSTTIKMLTGILVPtsgevrVLGYvpfKRRKEFARrIGVvFGQR--SQLWWDLPAIDsfRLLKAIYRIPDAEY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 591 RHQLGRY----GIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQAL---NNFRGG-VIL 662
Cdd:COG4586 132 KKRLDELvellDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLkeyNRERGTtILL 210
|
....
gi 29789050 663 VSHD 666
Cdd:COG4586 211 TSHD 214
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
488-683 |
1.17e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 57.12 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGI----------RHAHRNLKI 557
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSislcgepvpsRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQhhVEQLDLNVSAVELL---ARKFpGLPEEEYRHQ---LGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNF 631
Cdd:PRK13537 83 GVVPQ--FDNLDPDFTVRENLlvfGRYF-GLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 632 YILDEPTNHLDMETIEALGQALNNF--RGGVILVSHD--ERFIRLvCKELWVCENG 683
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLlaRGKTILLTTHfmEEAERL-CDRLCVIEEG 214
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
301-397 |
1.17e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 56.18 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 301 DKAPARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAIlwleNYLQTW 373
Cdd:PRK11124 116 DQALARAEKLLERLRLKPYADRFPL-HLSGGQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSII----RELAET 190
|
90 100
....*....|....*....|....
gi 29789050 374 PSTILVVSHDRNFLNAIATDIIHL 397
Cdd:PRK11124 191 GITQVIVTHEVEVARKTASRVVYM 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
491-666 |
1.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 56.67 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGY 559
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGrVKVMGREVnaenekwvrsKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHVEQL--------------DLNVSAVELLARKFPGLPE---EEYRHqlgrygisgelamRPVASLSGGQKSRVAFA 622
Cdd:PRK13647 84 VFQDPDDQVfsstvwddvafgpvNMGLDKDEVERRVEEALKAvrmWDFRD-------------KPPYHLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 623 QMTMPCPNFYILDEPTNHLD---METIEALGQALNNFRGGVILVSHD 666
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHD 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
178-382 |
1.27e-08 |
|
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: 54.74 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqsvles 257
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILS--------------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvredllrqerelslriaagraeGSEAAQLAEIY--GKLEEIeadKAPARAsvILAGLGFTPKMqqqptrefSGGWRMR 335
Cdd:cd03216 48 ------------------------GLYKPDSGEILvdGKEVSF---ASPRDA--RRAGIAMVYQL--------SVGERQM 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 336 LALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSH 382
Cdd:cd03216 91 VEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAqgvAVIFISH 140
|
|
| CP_lyasePhnL |
TIGR02324 |
phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ... |
193-392 |
1.42e-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: 55.86 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLHVEQEVagDDTPALQsvlesdtvREDLLRQERELS 272
Cdd:TIGR02324 24 LKNVSLTVNAGECVALSGPSGAGKSTLLKSLYANYLPDSGRILVRHEGAWV--DLAQASP--------REVLEVRRKTIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 -----LRIAAGRAEGSEAAQLAEIYGkleeIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:TIGR02324 94 yvsqfLRVIPRVSALEVVAEPLLERG----VPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 348 LLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSHDRNFLNAIAT 392
Cdd:TIGR02324 170 ILLLDEPTASLDAanrQVVVELIAEAKARGAALIGIFHDEEVRELVAD 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
491-684 |
1.49e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 58.49 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG------------IRHAHRNLki 557
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagksiltnISDVHQNM-- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHH-VEQLDLNVSAVELLARkFPGLPEEEYRhQLGRYGISG----ELAMRPVASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR01257 2015 GYCPQFDaIDDLLTGREHLYLYAR-LRGVPAEEIE-KVANWSIQSlglsLYADRLAGTYSGGNKRKLSTAIALIGCPPLV 2092
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 633 ILDEPTNHLDMETIEALGQALNN-FRGG--VILVSHDERFIRLVCKELWVCENGS 684
Cdd:TIGR01257 2093 LLDEPTTGMDPQARRMLWNTIVSiIREGraVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
178-384 |
1.52e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 57.02 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhveqevAGDDTPALQS---- 253
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRF-------HGTDVSRLHArdrk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 ---------VLESDTVRED-------LLRQERELSLRIAAGRAEGSEAAQLAEIygkleeieADKAPArasvilaglgft 317
Cdd:PRK10851 76 vgfvfqhyaLFRHMTVFDNiafgltvLPRRERPNAAAIKAKVTQLLEMVQLAHL--------ADRYPA------------ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 318 pkmqqqptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAIL--WLENYLQTWPSTILVVSHDR 384
Cdd:PRK10851 136 ---------QLSGGQKQRVALARALAVEPQILLLDEPFGALDaqVRKELrrWLRQLHEELKFTSVFVTHDQ 197
|
|
| 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 29789050 319 KMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYL-QTWPSTILVVSHD 383
Cdd:PRK09473 154 RMKMYP-HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVqaqIMTLLNELkREFNTAIIMITHD 221
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
197-642 |
1.95e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.33 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAWGRRYGLVGRNGLGKTTLLKMLA----------TRSLRVPAHISLlhvEQevagddtpaLQSVLESDTVRE--DL 264
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAgelpllsgerQSQFSHITRLSF---EQ---------LQKLVSDEWQRNntDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 265 LRQERELSLRIAAgraegseaaqlaEIYgkLEEIeadKAPARASVILAGLGFTPKMqqqpTREF---SGGWRMRLALARA 341
Cdd:PRK10938 91 LSPGEDDTGRTTA------------EII--QDEV---KDPARCEQLAQQFGITALL----DRRFkylSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 342 LFARPDLLLLDEPTNMLDVRAILWLENYLQTWPST----ILVVshdrNFLNAIAtdiihlhsqrldgyrgDFETFIKSKQ 417
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSgitlVLVL----NRFDEIP----------------DFVQFAGVLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 418 ERLLNQQREyeaqqqyRQHIQvfidrfrynanrASQVQSKLKMLEKLPELK-PVDKESEVVLKFPDGfekfSPPILQLDE 496
Cdd:PRK10938 210 DCTLAETGE-------REEIL------------QQALVAQLAHSEQLEGVQlPEPDEPSARHALPAN----EPRIVLNNG 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 497 VDFYYDPKhsIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGD-----------LSPVRG-------IRHahrnlKIG 558
Cdd:PRK10938 267 VVSYNDRP--ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltlFGRRRGsgetiwdIKK-----HIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 559 YFS-QHHveqLDLNVS-------------------AV----ELLARKFpglpeeeyrhqLGRYGISGELAMRPVASLSGG 614
Cdd:PRK10938 340 YVSsSLH---LDYRVStsvrnvilsgffdsigiyqAVsdrqQKLAQQW-----------LDILGIDKRTADAPFHSLSWG 405
|
490 500
....*....|....*....|....*...
gi 29789050 615 QKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK10938 406 QQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
489-638 |
1.96e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 55.37 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 489 PPILQLDEVDFYYDPKHSIFSrlsVSADLE--SRICVVGENGAGKSTMLKLLMGDLSPVRG-IR---------HAHR--- 553
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHG---VSLEVEegEIVALLGRNGAGKTTLLKAISGLLPPRSGsIRfdgeditglPPHRiar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 554 --------------------NLKIGYFSQHHVEQLDLNVSAV-ELlarkFPGLpeEEYRHQLGrygisgelamrpvASLS 612
Cdd:COG0410 78 lgigyvpegrrifpsltveeNLLLGAYARRDRAEVRADLERVyEL----FPRL--KERRRQRA-------------GTLS 138
|
170 180
....*....|....*....|....*.
gi 29789050 613 GGQKSRVAFAQMTMPCPNFYILDEPT 638
Cdd:COG0410 139 GGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
523-666 |
2.18e-08 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 56.69 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL---------KIGYFSQH-----H--VEQldlNVsAVELLARKfpgL 585
Cdd:COG1118 33 LLGPSGSGKTTLLRIIAGLETPDSGrIVLNGRDLftnlpprerRVGFVFQHyalfpHmtVAE---NI-AFGLRVRP---P 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 586 PEEEYR----HQLGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------METIeaLGQALNN 655
Cdd:COG1118 106 SKAEIRarveELLELVQLEG-LADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRRW--LRRLHDE 182
|
170
....*....|.
gi 29789050 656 FRGGVILVSHD 666
Cdd:COG1118 183 LGGTTVFVTHD 193
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
179-359 |
2.21e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 55.64 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSF--GDRVLLAGADVNLAWGRRYGLV--GRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtpALQSV 254
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVValGASGCGKTTLLNLIA--GFLAPSSGEITLDGVPVTGPG--ADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESD-------TVREDLlrqerELSLRIAagraeGSEAAQLAEIygkleeieADKAPARasVILAGLGftpkmqQQPTRE 327
Cdd:COG4525 81 VFQKdallpwlNVLDNV-----AFGLRLR-----GVPKAERRAR--------AEELLAL--VGLADFA------RRRIWQ 134
|
170 180 190
....*....|....*....|....*....|..
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4525 135 LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
521-666 |
2.48e-08 |
|
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: 55.16 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL------KIGYFSQHHV-------EQLDLNVSAVellarkFPGLP 586
Cdd:TIGR01184 14 ISLIGHSGCGKSTLLNLISGLAQPTSGgVILEGKQItepgpdRMVVFQNYSLlpwltvrENIALAVDRV------LPDLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYR----HQLGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQAL----NNFRG 658
Cdd:TIGR01184 88 KSERRaiveEHIALVGL-TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRV 166
|
....*...
gi 29789050 659 GVILVSHD 666
Cdd:TIGR01184 167 TVLMVTHD 174
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
178-359 |
2.53e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.79 E-value: 2.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKmlatrslrvpaHISLLhveqeVAGDDTPALQSVLES 257
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLR-----------HLSGL-----ITGDKSAGSHIELLG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVRedllrQERELSLRIAAGRAEGSEAAQLAEIYGKLEEIEadkaparaSVILAGLG-----------FTPKMQQ---- 322
Cdd:PRK09984 69 RTVQ-----REGRLARDIRKSRANTGYIFQQFNLVNRLSVLE--------NVLIGALGstpfwrtcfswFTREQKQralq 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789050 323 ------------QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK09984 136 altrvgmvhfahQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
513-685 |
2.67e-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: 55.58 E-value: 2.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLESRICV--VGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIGYFSQHHVEQLDLNV------SAV--ELLARK 581
Cdd:TIGR02769 30 VSLSIEEGETVglLGRSGCGKSTLARLLLGLEKPAQGtVSFRGQDLYQLDRKQRRAFRRDVQLvfqdspSAVnpRMTVRQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 FPGLPEEEY------------RHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM------ 643
Cdd:TIGR02769 110 IIGEPLRHLtsldeseqkariAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqavi 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29789050 644 -ETIEALGQAlnnFRGGVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:TIGR02769 190 lELLRKLQQA---FGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
188-370 |
2.92e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 188 GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAhisllhvEQEVAGDDTPALQsvlesdtVREDLLRQ 267
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILA--GLARPD-------AGEVLWQGEPIRR-------QRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 268 ----------ERELS----LRIAAGRAEGSEAAQLAEiygkleeieadkapARASVILAGlgftpkMQQQPTREFSGGWR 333
Cdd:PRK13538 76 llylghqpgiKTELTalenLRFYQRLHGPGDDEALWE--------------ALAQVGLAG------FEDVPVRQLSAGQQ 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL 370
Cdd:PRK13538 136 RRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
178-382 |
3.01e-08 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 55.43 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAgaDVNLAWGRR--YGLVGRNGLGKTTLLkmlatRSL-RVPAHISLLHVEQEVAGDDtpalQSV 254
Cdd:COG1117 12 IEVRNLNVYYGDKQALK--DINLDIPENkvTALIGPSGCGKSTLL-----RCLnRMNDLIPGARVEGEILLDG----EDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 LESDTVREDL-------------------------LRQERELSLRIAAGRAEGS--EAAQLAEIYGKLeeieadKAPARA 307
Cdd:COG1117 81 YDPDVDVVELrrrvgmvfqkpnpfpksiydnvaygLRLHGIKSKSELDEIVEESlrKAALWDEVKDRL------KKSALG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 308 sviLAGlGftpkmQQQptrefsggwrmRLALARALFARPDLLLLDEPTNMLDVRA-------ILWL-ENYlqtwpsTILV 379
Cdd:COG1117 155 ---LSG-G-----QQQ-----------RLCIARALAVEPEVLLMDEPTSALDPIStakieelILELkKDY------TIVI 208
|
...
gi 29789050 380 VSH 382
Cdd:COG1117 209 VTH 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
329-389 |
3.13e-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: 3.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD-------VRAILwlenYLQTWPSTILVVSHDRNFLNA 389
Cdd:COG4618 469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeaalAAAIR----ALKARGATVVVITHRPSLLAA 532
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
511-686 |
3.30e-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: 56.27 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 511 LSVSADLES--RICVVGENGAGKSTMLKLLMGDLSPVRGIRH----------------AHRNlKIGYFSQHhveqldlnv 572
Cdd:TIGR02142 14 LDADFTLPGqgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtlfdsrkgiflpPEKR-RIGYVFQE--------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 573 savellARKFPGLpeeEYRHQLgRYGIS--------------------GELAMRPVASLSGGQKSRVAFAQMTMPCPNFY 632
Cdd:TIGR02142 84 ------ARLFPHL---SVRGNL-RYGMKrarpserrisferviellgiGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 633 ILDEPTNHLDM----ETIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:TIGR02142 154 LMDEPLAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
491-642 |
3.59e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYY-DPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP---------VRGIRHAHRNL----- 555
Cdd:PRK13640 5 IVEFKHVSFTYpDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitVDGITLTAKTVwdire 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 556 KIGYFSQHHVEQ-LDLNVS---AVELLARkfpGLPEEEY----RHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMP 627
Cdd:PRK13640 85 KVGIVFQNPDNQfVGATVGddvAFGLENR---AVPRPEMikivRDVLADVGMLDYIDSEP-ANLSGGQKQRVAIAGILAV 160
|
170
....*....|....*
gi 29789050 628 CPNFYILDEPTNHLD 642
Cdd:PRK13640 161 EPKIIILDESTSMLD 175
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
177-359 |
3.67e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 55.85 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENFDVSFGDRVLLAgaDVNLAW--GRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAH---ISLl 237
Cdd:COG3839 3 SLELENVSKSYGGVEALK--DIDLDIedGEFLVLLGPSGCGKSTLLRMIAgledptsgeiliggRDVTDLPPKdrnIAM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 238 hVEQevagddTPALqsvLESDTVREDLlrqerELSLRIAaGRAEgseaaqlAEIYGKLEEIeadkapARAsvilagLGFT 317
Cdd:COG3839 80 -VFQ------SYAL---YPHMTVYENI-----AFPLKLR-KVPK-------AEIDRRVREA------AEL------LGLE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 318 PKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG3839 125 DLLDRKP-KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
491-666 |
4.02e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRG----------------IRHah 552
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGewLSIIGHNGSGKSTTVRLIDGLLEAESGqiiidgdllteenvwdIRH-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 553 rnlKIGYFSQHHVEQLdlnVSA-VEL-----LARKfpGLPEEEYR----HQLGRYGISgELAMRPVASLSGGQKSRVAFA 622
Cdd:PRK13650 82 ---KIGMVFQNPDNQF---VGAtVEDdvafgLENK--GIPHEEMKervnEALELVGMQ-DFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 623 QMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG----VILVSHD 666
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqmtVISITHD 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
600-706 |
4.03e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 600 SGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVILVSHDERFIRLVCKELWV 679
Cdd:PLN03073 334 TPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILH 413
|
90 100
....*....|....*....|....*..
gi 29789050 680 CENGSVTRVEGGFDQYRALLQEQFRRE 706
Cdd:PLN03073 414 LHGQKLVTYKGDYDTFERTREEQLKNQ 440
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
164-359 |
4.07e-08 |
|
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: 56.88 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 164 ESRLESSGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHI----SLLHV 239
Cdd:TIGR00957 625 ERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVhmkgSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 240 EQevagddtpalQSVLESDTVREDLLrqerelslriaagraegseaaqlaeiYGKLEEIEADKAPARASVILAGLGFTPK 319
Cdd:TIGR00957 705 PQ----------QAWIQNDSLRENIL--------------------------FGKALNEKYYQQVLEACALLPDLEILPS 748
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 320 MQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:TIGR00957 749 GDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
523-667 |
4.98e-08 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 54.02 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSP---VRG-IRHAHRNL--------KIGYFSQ------HhveqldLNVsaVELLArkFpG 584
Cdd:COG4136 32 LMGPSGSGKSTLLAAIAGTLSPafsASGeVLLNGRRLtalpaeqrRIGILFQddllfpH------LSV--GENLA--F-A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 585 LPEEEYRHQ--------LGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQ----A 652
Cdd:COG4136 101 LPPTIGRAQrrarveqaLEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREfvfeQ 179
|
170
....*....|....*
gi 29789050 653 LNNFRGGVILVSHDE 667
Cdd:COG4136 180 IRQRGIPALLVTHDE 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
172-400 |
5.66e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.95 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 172 KNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDDTPAL 251
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVA--SLISPTSGTLL-----FEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 ------QSV--------LESDTVREDL-----LRQERELSLRIAAGraegseaaqlaeiygkleeieadkaparasviLA 312
Cdd:PRK10247 75 kpeiyrQQVsycaqtptLFGDTVYDNLifpwqIRNQQPDPAIFLDD--------------------------------LE 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 313 GLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAIlwLENYLQTWPSTILVVSHDRNF 386
Cdd:PRK10247 123 RFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDesnkhnVNEI--IHRYVREQNIAVLWVTHDKDE 200
|
250
....*....|....
gi 29789050 387 LNAiATDIIHLHSQ 400
Cdd:PRK10247 201 INH-ADKVITLQPH 213
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
172-362 |
5.88e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 172 KNKSYDVRIENfdvsfGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRslrvpahisllhVEQEVAGDDT--- 248
Cdd:TIGR00956 763 RNLTYEVKIKK-----EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAER------------VTTGVITGGDrlv 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 --PALQSV--------------LESDTVREDL-----LRQERELSLriaagraegSEAAQLAEIYGKLEEIEAdkaPARA 307
Cdd:TIGR00956 826 ngRPLDSSfqrsigyvqqqdlhLPTSTVRESLrfsayLRQPKSVSK---------SEKMEYVEEVIKLLEMES---YADA 893
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 308 SVILAGLGFTpkMQQqptrefsggwRMRLALARALFARPDLLL-LDEPTNMLDVRA 362
Cdd:TIGR00956 894 VVGVPGEGLN--VEQ----------RKRLTIGVELVAKPKLLLfLDEPTSGLDSQT 937
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
523-645 |
6.94e-08 |
|
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: 53.53 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLK--IGYFSQHhvEQLDLNVSA---VELLARKFpGLPEEE 589
Cdd:cd03265 31 LLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRrrIGIVFQD--LSVDDELTGwenLYIHARLY-GVPGAE 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 590 YRH---QLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET 645
Cdd:cd03265 108 RREridELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
519-702 |
7.01e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 55.62 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 519 SRICVVGENGAGKSTMLKLLMGDLsPVRGirhahrNLKIGyfsqhHVE--QLDL-----------------------NVs 573
Cdd:PRK11174 377 QRIALVGPSGAGKTSLLNALLGFL-PYQG------SLKIN-----GIElrELDPeswrkhlswvgqnpqlphgtlrdNV- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 574 aveLLARkfPGLPEEEYRHQLGRYGISGELAMRPV----------ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 643
Cdd:PRK11174 444 ---LLGN--PDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 644 ETIEALGQALNNFRGG--VILVSHderfiRL----VCKELWVCENGSVtrVEGGfdQYRALLQEQ 702
Cdd:PRK11174 519 HSEQLVMQALNAASRRqtTLMVTH-----QLedlaQWDQIWVMQDGQI--VQQG--DYAELSQAG 574
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
523-666 |
8.48e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLS----------PVRGIRHAHRNLKIGYFSQH-------HVEQ-LDLNVSAvellarkfpG 584
Cdd:PRK03695 27 LVGPNGAGKSTLLARMAGLLPgsgsiqfagqPLEAWSAAELARHRAYLSQQqtppfamPVFQyLTLHQPD---------K 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 585 LPEEEYRHQL----GRYGISGELAmRPVASLSGGQKSRVAFAQMTM-------PCPNFYILDEPTNHLDMETIEALGQAL 653
Cdd:PRK03695 98 TRTEAVASALnevaEALGLDDKLG-RSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNSLDVAQQAALDRLL 176
|
170
....*....|....*.
gi 29789050 654 NNF--RGGVILVS-HD 666
Cdd:PRK03695 177 SELcqQGIAVVMSsHD 192
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
492-642 |
8.59e-08 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 53.43 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSifsRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG------IRHAH------------- 552
Cdd:PRK10771 2 LKLTDITWLYHHLPM---RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGsltlngQDHTTtppsrrpvsmlfq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 553 -RNLkigyFSQHHVEQ---LDLNvsavellarkfPGLP-EEEYRHQL----GRYGISGELAMRPvASLSGGQKSRVAFAQ 623
Cdd:PRK10771 79 eNNL----FSHLTVAQnigLGLN-----------PGLKlNAAQREKLhaiaRQMGIEDLLARLP-GQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 29789050 624 MTMPCPNFYILDEPTNHLD 642
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
177-384 |
9.03e-08 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 54.72 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------------TRSLRVPAH---ISLL-- 237
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAgfetpdsgrilldgRDVTGLPPEkrnVGMVfq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 238 ------H--VEQEVA-GddtpalqsvlesdtvredlLRQeRELSLRIAAGRAEgsEAAQLAEIYGKleeieADKAParas 308
Cdd:COG3842 85 dyalfpHltVAENVAfG-------------------LRM-RGVPKAEIRARVA--ELLELVGLEGL-----ADRYP---- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 309 vilaglgftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRAILWLE--NYLQTWPSTILVVSHDR 384
Cdd:COG3842 134 -----------------HQLSGGQQQRVALARALAPEPRVLLLDEPLSALDakLREEMREElrRLQRELGITFIYVTHDQ 196
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
170-418 |
9.46e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.90 E-value: 9.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 170 SGKNKSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVpaHISLLHVEQEVA--GDD 247
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL-NRLIEI--YDSKIKVDGKVLyfGKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 248 tpalqsVLESDTVRedlLRQERELSLRIAAGRAEGSEAAQLA---EIYGKLEEIEADKAPARAsviLAGLGFTPKMQQQ- 323
Cdd:PRK14246 80 ------IFQIDAIK---LRKEVGMVFQQPNPFPHLSIYDNIAyplKSHGIKEKREIKKIVEEC---LRKVGLWKEVYDRl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 324 --PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHDRNFLNAIATDIIHLHS 399
Cdd:PRK14246 148 nsPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYN 227
|
250
....*....|....*....
gi 29789050 400 QRLDGYRGDFETFIKSKQE 418
Cdd:PRK14246 228 GELVEWGSSNEIFTSPKNE 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
522-674 |
9.54e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.02 E-value: 9.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSP-------------VRGIRHAHRnLKIGYFSQHhveqLDL--NVSAVE-----LLARK 581
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGVYQPdsgeilldgepvrFRSPRDAQA-AGIAIIHQE----LNLvpNLSVAEniflgREPRR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 FPGLP----EEEYRHQLGRYGISGELAmRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR 657
Cdd:COG1129 109 GGLIDwramRRRARELLARLGLDIDPD-TPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLK 187
|
170 180
....*....|....*....|..
gi 29789050 658 G---GVILVSH--DErfIRLVC 674
Cdd:COG1129 188 AqgvAIIYISHrlDE--VFEIA 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
521-678 |
1.02e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMG--DLS---------PVRGI----RHAHRNLKIGYFSQHHVEQLDLN-VSAVELLARkFPG 584
Cdd:PRK10584 39 IALIGESGSGKSTLLAILAGldDGSsgevslvgqPLHQMdeeaRAKLRAKHVGFVFQSFMLIPTLNaLENVELPAL-LRG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 585 LPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGQALN-NF 656
Cdd:PRK10584 118 ESSRQSRNGakalLEQLGLGKRLDHLP-AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkIADLLFSLNrEH 196
|
170 180
....*....|....*....|....*....
gi 29789050 657 RGGVILVSHDE-------RFIRLVCKELW 678
Cdd:PRK10584 197 GTTLILVTHDLqlaarcdRRLRLVNGQLQ 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
167-461 |
1.09e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 167 LESSGKNKSYDVRIENFDVsfgdrvlLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrsLRVPAHisllhVEQEVAGD 246
Cdd:PRK10535 5 LELKDIRRSYPSGEEQVEV-------LKGISLDIYAGEMVAIVGASGSGKSTLMNILGC--LDKPTS-----GTYRVAGQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DTpalqSVLESDTVREdlLRQER------------ELSlriaagraegseAAQLAEIYGKLEEIEADKAPARASVILAGL 314
Cdd:PRK10535 71 DV----ATLDADALAQ--LRREHfgfifqryhllsHLT------------AAQNVEVPAVYAGLERKQRLLRAQELLQRL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 315 GFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILwleNYLQTWPSTILVVSHDRNfLN 388
Cdd:PRK10535 133 GLEDRVEYQPS-QLSGGQQQRVSIARALMNGGQVILADEPTGALDshsgeeVMAIL---HQLRDRGHTVIIVTHDPQ-VA 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 389 AIATDIIHLHsqrldgyrgDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFIDRFR------YNANRASQVQSKLKML 461
Cdd:PRK10535 208 AQAERVIEIR---------DGEIVRNPPAQEKVNVAGGTEPVVNTASGWRQFVSGFRealtmaWRAMAANKMRTLLTML 277
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
207-383 |
1.09e-07 |
|
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: 53.57 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLATRslrvpahISLLHVEQEVAGDDTPALQSVLESD---TVReDLLRQerelslrIAAGRAEGS 283
Cdd:cd03237 29 GILGPNGIGKTTFIKMLAGV-------LKPDEGDIEIELDTVSYKPQYIKADyegTVR-DLLSS-------ITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 284 eaaqlaeiYGKLEeieadkaparasvILAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV--- 360
Cdd:cd03237 94 --------YFKTE-------------IAKPLQIEQILDRE-VPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqr 151
|
170 180
....*....|....*....|....*..
gi 29789050 361 ----RAIlwlENYLQTWPSTILVVSHD 383
Cdd:cd03237 152 lmasKVI---RRFAENNEKTAFVVEHD 175
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
180-364 |
1.18e-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: 53.39 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatrsLRV--PAHISLLHVEQEVAGDDTPALQ-- 252
Cdd:cd03253 1 IEFENVTFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL----FRFydVSSGSILIDGQDIREVTLDSLRra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 -------SVLESDTVREDllrqerelslrIAAGRAEGS-----EAAQLAEIYGKLEEIEAdkaparasvilaglGFTPKM 320
Cdd:cd03253 77 igvvpqdTVLFNDTIGYN-----------IRYGRPDATdeeviEAAKAAQIHDKIMRFPD--------------GYDTIV 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 321 QQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 364
Cdd:cd03253 132 GERGLK-LSGGEKQRVAIARAILKNPPILLLDEATSALDThteREIQ 177
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
178-397 |
1.29e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.45 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLL----HVEQEVAGDDTPALQS 253
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLS--RLMTPAHGHVWldgeHIQHYASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLESDTVREDLLRQERelslrIAAGRAegseAAQLAEIYGKLEEIEADKAPARASvilaglGFTpKMQQQPTREFSGGWR 333
Cdd:PRK10253 86 LAQNATTPGDITVQEL-----VARGRY----PHQPLFTRWRKEDEEAVTKAMQAT------GIT-HLADQSVDTLSGGQR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLDVRAILWLENYL----QTWPSTILVVSHDRNFLNAIATDIIHL 397
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLselnREKGYTLAAVLHDLNQACRYASHLIAL 217
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
327-360 |
1.31e-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: 1.31e-07
10 20 30
....*....|....*....|....*....|....
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:COG4608 157 EFSGGQRQRIGIARALALNPKLIVCDEPVSALDV 190
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
179-385 |
1.41e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRslRVPAHISLLHVEQEVAGDDTPALQsvlesd 258
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRH--QPPSEGEILLDAQPLESWSSKAFA------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 tvredllRQERELSLRIAAgrAEGSEAAQLAEI-----YGKLEEI-EADKAPARASVILAGLgfTPkMQQQPTREFSGGW 332
Cdd:PRK10575 85 -------RKVAYLPQQLPA--AEGMTVRELVAIgrypwHGALGRFgAADREKVEEAISLVGL--KP-LAHRLVDSLSGGE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHDIN 209
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
178-354 |
1.51e-07 |
|
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: 52.93 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVP--------------------AHISLL 237
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIV--GLVKPdsgkilldgqditklpmhkrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 238 HVEQEvagddtpalQSVLESDTVREDLLrqerelslriaagraegseaaQLAEIYGKLEEIEADKAPArasvILAGLGFT 317
Cdd:cd03218 79 YLPQE---------ASIFRKLTVEENIL---------------------AVLEIRGLSKKEREEKLEE----LLEEFHIT 124
|
170 180 190
....*....|....*....|....*....|....*..
gi 29789050 318 pKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 354
Cdd:cd03218 125 -HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
181-360 |
1.53e-07 |
|
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: 52.50 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhvEQEVAGDDTPALQSVLesdtv 260
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL---NGGPLDFQRDSIARGL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 261 redllrqerelslrIAAGRAEGSEAAQLAEiyGKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALAR 340
Cdd:cd03231 76 --------------LYLGHAPGIKTTLSVL--ENLRFWHADHSDEQVEEALARVGLN-GFEDRPVAQLSAGQQRRVALAR 138
|
170 180
....*....|....*....|
gi 29789050 341 ALFARPDLLLLDEPTNMLDV 360
Cdd:cd03231 139 LLLSGRPLWILDEPTTALDK 158
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
328-397 |
1.59e-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: 1.59e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRNFLNAIATDIIHL 397
Cdd:cd03217 105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKPDRVHV 177
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
161-382 |
1.73e-07 |
|
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: 54.75 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 161 SRKESRLESSGKNKSYDVRIENFDVSFGDRVLlagADVNLA--WGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLLH 238
Cdd:TIGR01193 459 INKKKRTELNNLNGDIVINDVSYSYGYGSNIL---SDISLTikMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 239 VEqeVAGDDTPAL---------QSVLESDTVREDLLRQERElslriAAGRAEGSEAAQLAEIYGKLEEIEadkaparasv 309
Cdd:TIGR01193 536 FS--LKDIDRHTLrqfinylpqEPYIFSGSILENLLLGAKE-----NVSQDEIWAACEIAEIKDDIENMP---------- 598
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 310 ilagLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIlwLENYLQTWPSTILVVSH 382
Cdd:TIGR01193 599 ----LGYQTELSEEGS-SISGGQKQRIALARALLTDSKVLILDESTSNLDTiteKKI--VNNLLNLQDKTIIFVAH 667
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
520-666 |
1.79e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 53.25 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 520 RIC-VVGENGAGKSTMLKLLMGDLSPVRGirhahrnlkigyfsqhhveQLDLNVSAVE-----LLARKFPGLPEE----- 588
Cdd:PRK10575 38 KVTgLIGHNGSGKSTLLKMLGRHQPPSEG-------------------EILLDAQPLEswsskAFARKVAYLPQQlpaae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 589 -------------EYRHQLGRYGISGE--------------LAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL 641
Cdd:PRK10575 99 gmtvrelvaigryPWHGALGRFGAADRekveeaislvglkpLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180
....*....|....*....|....*....
gi 29789050 642 DME---TIEALGQALNNFRG-GVILVSHD 666
Cdd:PRK10575 179 DIAhqvDVLALVHRLSQERGlTVIAVLHD 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
179-382 |
1.90e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.34 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLL------------HVEQ 241
Cdd:TIGR00958 478 LIEFQDVSFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALL--QNLYQPTGGQVLldgvplvqydhhYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 242 EVAgddTPALQSVLESDTVREDllrqerelslrIAAG-----RAEGSEAAQLAEIYGKLEEIEADkaparasvILAGLGf 316
Cdd:TIGR00958 556 QVA---LVGQEPVLFSGSVREN-----------IAYGltdtpDEEIMAAAKAANAHDFIMEFPNG--------YDTEVG- 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 317 tPKMQQqptreFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAilwlENYLQTWPS----TILVVSH 382
Cdd:TIGR00958 613 -EKGSQ-----LSGGQKQRIAIARALVRKPRVLILDEATSALDAEC----EQLLQESRSrasrTVLLIAH 672
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
197-359 |
2.03e-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: 52.49 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNL--AWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVAGDDTPALQS----VLESDTVredllrqere 270
Cdd:cd03252 20 NISLriKPGEVVGIVGRSGSGKSTLTKLI--QRFYVPENGRVLVDGHDLALADPAWLRRqvgvVLQENVL---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 271 LSLRIAAGRAEGSEAAQLAEIygkleeIEADK-APARASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLL 349
Cdd:cd03252 88 FNRSIRDNIALADPGMSMERV------IEAAKlAGAHDFISELPEGYDTIVGEQGA-GLSGGQRQRIAIARALIHNPRIL 160
|
170
....*....|
gi 29789050 350 LLDEPTNMLD 359
Cdd:cd03252 161 IFDEATSALD 170
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
606-671 |
2.04e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 2.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 606 RPVASLSGGQKSRVAFAQM--TMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSHDERFIR 671
Cdd:cd03238 83 QKLSTLSGGELQRVKLASElfSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDlgnTVILIEHNLDVLS 153
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
521-666 |
2.16e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGirhahrNLKIGYFSQHHV-EQLDLNVSAVELLARK---------FPGLPEEEY 590
Cdd:PRK11247 41 VAVVGRSGCGKSTLLRLLAGLETPSAG------ELLAGTAPLAEArEDTRLMFQDARLLPWKkvidnvglgLKGQWRDAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 591 RHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET-------IEALGQAlNNFRggVILV 663
Cdd:PRK11247 115 LQALAAVGLADRANEWP-AALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemqdlIESLWQQ-HGFT--VLLV 190
|
...
gi 29789050 664 SHD 666
Cdd:PRK11247 191 THD 193
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
497-686 |
2.56e-07 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 52.40 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 497 VDFYYDPKHsiFSRLSVSADLESRIC------VVGENGAGKSTMLK------------LLMGDLS------PVRGIRhah 552
Cdd:PRK09493 2 IEFKNVSKH--FGPTQVLHNIDLNIDqgevvvIIGPSGSGKSTLLRcinkleeitsgdLIVDGLKvndpkvDERLIR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 553 rnLKIGY-FSQHHveqLDLNVSAVELLA---RKFPGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQM 624
Cdd:PRK09493 77 --QEAGMvFQQFY---LFPHLTALENVMfgpLRVRGASKEEAEKQarelLAKVGLAERAHHYP-SELSGGQQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 625 TMPCPNFYILDEPTNHLDMETI-EALG--QALNNFRGGVILVSHDERFIRLVCKELWVCENGSVT 686
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIA 215
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
493-703 |
2.70e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.81 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 493 QLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP----------------VRGIRHAhrnlk 556
Cdd:PRK13657 336 EFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPqsgrilidgtdirtvtRASLRRN----- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQhhvEQLDLNVSAVELLARKFPGLPEEEYRHQLGRYGISGELAMRPVA----------SLSGGQKSRVAFAQMTM 626
Cdd:PRK13657 411 IAVVFQ---DAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGydtvvgergrQLSGGERQRLAIARALL 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 627 PCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSHDERFIRLVcKELWVCENGSVtrVE-GGFDQ-------YR 696
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGrtTFIIAHRLSTVRNA-DRILVFDNGRV--VEsGSFDElvarggrFA 564
|
....*..
gi 29789050 697 ALLQEQF 703
Cdd:PRK13657 565 ALLRAQG 571
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
168-437 |
2.76e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 53.68 E-value: 2.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 168 ESSGKNKSYDVRIENFDVSFGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMLaTRSlRVPAHISLLHVEQEVAG 245
Cdd:PRK11160 329 TSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLqiKAGEKVALLGRTGCGKSTLLQLL-TRA-WDPQQGEILLNGQPIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 246 DDTPAL--------QSV-LESDTVREDLLrqerelslrIAAGRAEGseaAQLAEIygkLEEIEADK---APARASVILAG 313
Cdd:PRK11160 407 YSEAALrqaisvvsQRVhLFSATLRDNLL---------LAAPNASD---EALIEV---LQQVGLEKlleDDKGLNAWLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 314 LGftpkmqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWL-----ENylqtwpSTILVVSHdRn 385
Cdd:PRK11160 472 GG----------RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeteRQILELlaehaQN------KTVLMITH-R- 533
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 386 fLNAIAT-DIIHLhsqrLDGYR----GDFETfikskqerLLNQQREYeaqQQYRQHI 437
Cdd:PRK11160 534 -LTGLEQfDRICV----MDNGQiieqGTHQE--------LLAQQGRY---YQLKQRL 574
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
326-397 |
2.90e-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: 2.90e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPSTILVVSHdRNFLNAIATDIIHL 397
Cdd:cd03223 90 DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDL 160
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
190-383 |
2.96e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 52.38 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 190 RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHisllhveQEVAGDDTPalqsVLESDTVREDLLRQER 269
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLV--GLESPSQ-------GNVSWRGEP----LAKLNRAQRKAFRRDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 270 ELSLR--IAAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPD 347
Cdd:PRK10419 92 QMVFQdsISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 348 LLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK10419 172 LLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHD 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
490-649 |
3.33e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.45 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYYDPKHSI-FSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgYFSQHHVEQL 568
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EI-FYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 569 DLNvsavELlaRKFPGL----PEEEYRHQLGRYGISGELAMRPVA--------------------------SLSGGQKSR 618
Cdd:PRK13648 77 NFE----KL--RKHIGIvfqnPDNQFVGSIVKYDVAFGLENHAVPydemhrrvsealkqvdmleradyepnALSGGQKQR 150
|
170 180 190
....*....|....*....|....*....|.
gi 29789050 619 VAFAQMTMPCPNFYILDEPTNHLDMETIEAL 649
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNL 181
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
513-664 |
3.57e-07 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 51.50 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMG---DLSPVRG-IRHAHRNLKIGYFSQH--HVEQLDLNVS----------- 573
Cdd:cd03234 26 VSLHVESgqVMAILGSSGSGKTTLLDAISGrveGGGTTSGqILFNGQPRKPDQFQKCvaYVRQDDILLPgltvretltyt 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 574 AVELLARKFPglpeEEYRHQLGRYGISGELAMRPVA-----SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEA 648
Cdd:cd03234 106 AILRLPRKSS----DAIRKKRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170
....*....|....*...
gi 29789050 649 LGQALNNF--RGGVILVS 664
Cdd:cd03234 182 LVSTLSQLarRNRIVILT 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
179-359 |
3.58e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 51.33 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpAHISLLHVEQEVAGDDT-----PALQ- 252
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG------TLSPAFSASGEVLLNGRrltalPAEQr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 253 --SVLESD-------TVREDLLrqereLSLRIAAGRAEGSEAAQLAeiygkLEEIEadkaparasviLAGLGF-TPKmqq 322
Cdd:COG4136 77 riGILFQDdllfphlSVGENLA-----FALPPTIGRAQRRARVEQA-----LEEAG-----------LAGFADrDPA--- 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 29789050 323 qptrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG4136 133 ----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
491-666 |
4.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 4.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSI--FSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGI------RHAHRNL-----KI 557
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKvkidgeLLTAENVwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHVEQ-LDLNVSAVELLARKFPGLPEEEYRHQLGRYGISG---ELAMRPVASLSGGQKSRVAFAQMTMPCPNFYI 633
Cdd:PRK13642 84 GMVFQNPDNQfVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVnmlDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 29789050 634 LDEPTNHLD----METIEALGQALNNFRGGVILVSHD 666
Cdd:PRK13642 164 LDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
180-383 |
5.14e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.69 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSF--GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpAHISLLHVEQEVAGDDTPALQsvles 257
Cdd:PRK11831 8 VDMRGVSFtrGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIG-------GQIAPDHGEILFDGENIPAMS----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 dtvREDLLRQERELSLRIAAGrAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGL---GFTPKMQQQPTrEFSGGWRM 334
Cdd:PRK11831 76 ---RSRLYTVRKRMSMLFQSG-ALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLeavGLRGAAKLMPS-ELSGGMAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 335 RLALARALFARPDLLLLDEP-------TNMLDVRAILWLENYLQTwpsTILVVSHD 383
Cdd:PRK11831 151 RAALARAIALEPDLIMFDEPfvgqdpiTMGVLVKLISELNSALGV---TCVVVSHD 203
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
178-364 |
5.53e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 52.90 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENfdVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAH 233
Cdd:COG5265 358 VRFEN--VSFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfrfydvtsgrilidgqdirdvTQASLR--AA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 234 ISLlhVEQevagdDTpalqsVLESDTVREDllrqerelslrIAAGRAEGSEaaqlaeiygklEEIEAdkaPARASVILAG 313
Cdd:COG5265 434 IGI--VPQ-----DT-----VLFNDTIAYN-----------IAYGRPDASE-----------EEVEA---AARAAQIHDF 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 314 LGFTPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL 364
Cdd:COG5265 477 IESLPDGYDTRVGErglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSrteRAIQ 534
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
193-383 |
5.98e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 5.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHV-EQEVAGDDTPALQSVLESDTV---REDLLRQE 268
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHL--NALLLPDTGTIEWIfKDEKNKKKTKEKEKVLEKLVIqktRFKKIKKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 269 RELSLRIAAgraegseAAQLAEiYGKLEE-IEAD-------------KAPARASVILAGLGFTPKMQQQPTREFSGGWRM 334
Cdd:PRK13651 101 KEIRRRVGV-------VFQFAE-YQLFEQtIEKDiifgpvsmgvskeEAKKRAAKYIELVGLDESYLQRSPFELSGGQKR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 335 RLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
505-666 |
6.38e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 6.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 505 HSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLS-------------------PVRGIRHAHRNLKIGYFSQHHV 565
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgarvtgdvtlngePLAAIDAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 566 EQLDLNVSAVELLARkFP-----GLPEEEYR----HQLGRYGISGeLAMRPVASLSGGQKSRVAFAQM---------TMP 627
Cdd:PRK13547 94 PAFAFSAREIVLLGR-YPharraGALTHRDGeiawQALALAGATA-LVGRDVTTLSGGELARVQFARVlaqlwpphdAAQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 29789050 628 CPNFYILDEPTNHLD-------METIEALGQalnNFRGGVILVSHD 666
Cdd:PRK13547 172 PPRYLLLDEPTAALDlahqhrlLDTVRRLAR---DWNLGVLAIVHD 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
513-667 |
8.15e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 51.62 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMG--------------DLSPVrgirHAhRNLKIGYFSQH-----HVEQLDlN 571
Cdd:PRK10851 21 ISLDIPSgqMVALLGPSGSGKTTLLRIIAGlehqtsghirfhgtDVSRL----HA-RDRKVGFVFQHyalfrHMTVFD-N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 VS-AVELLARkfpglpeeeyRHQLGRYGIS------------GELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPT 638
Cdd:PRK10851 95 IAfGLTVLPR----------RERPNAAAIKakvtqllemvqlAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190
....*....|....*....|....*....|...
gi 29789050 639 NHLD----METIEALGQALNNFRGGVILVSHDE 667
Cdd:PRK10851 165 GALDaqvrKELRRWLRQLHEELKFTSVFVTHDQ 197
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
178-383 |
8.36e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.85 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSfGDRVLLAGADVNLAWGRRYGLVGRNGLGKTtlLKMLATRSLrVPAHISLLHveQEVAGDDTPALQSVLES 257
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGI-LPAGVRQTA--GRVLLDGKPVAPCALRG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVrEDLLRQERELSLRIAAGRAEGSEAAQLAeiyGKLeeieADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLA 337
Cdd:PRK10418 79 RKI-ATIMQNPRSAFNPLHTMHTHARETCLAL---GKP----ADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 338 LARALFARPDLLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHD 383
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVvaqaRILDLLESIVQKRALGMLLVTHD 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
178-385 |
8.38e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 8.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA--------TRSLRVPAHISLlhVEQEVAGDDTP 249
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggaPRGARVTGDVTL--NGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 250 AL---QSVLeSDTVREDLLRQERELSL--RIAAGRAEGSEAAQLAEIygkleeieADKAPARA-SVILAGLGFTpkmqqq 323
Cdd:PRK13547 80 RLarlRAVL-PQAAQPAFAFSAREIVLlgRYPHARRAGALTHRDGEI--------AWQALALAgATALVGRDVT------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 324 ptrEFSGGWRMRLALARAL---------FARPDLLLLDEPTNMLDV----RAILWLENYLQTWPSTILVVSHDRN 385
Cdd:PRK13547 145 ---TLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLahqhRLLDTVRRLARDWNLGVLAIVHDPN 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
524-669 |
8.75e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 51.26 E-value: 8.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSP------VRG--IRHAHRNlKIGY-------FSQHHV-EQLdlnvsaVELLARKfpGLPE 587
Cdd:COG4152 33 LGPNGAGKTTTIRIILGILAPdsgevlWDGepLDPEDRR-RIGYlpeerglYPKMKVgEQL------VYLARLK--GLSK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 588 EEYRHQ----LGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR--G-GV 660
Cdd:COG4152 104 AEAKRRadewLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAakGtTV 182
|
170
....*....|...
gi 29789050 661 ILVSHD----ERF 669
Cdd:COG4152 183 IFSSHQmelvEEL 195
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
523-702 |
8.98e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 51.37 E-value: 8.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG------------IRHAHRnlKIGYFSQhhVEQLDLNVSAVE--LLARKFPGLPE- 587
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGkitvlgvpvparARLARA--RIGVVPQ--FDNLDLEFTVREnlLVFGRYFGMSTr 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 588 --EEYRHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF--RGGVILV 663
Cdd:PRK13536 148 eiEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlaRGKTILL 227
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 664 SHD--ERFIRLvCKELWVCENGsVTRVEGGFDqyrALLQEQ 702
Cdd:PRK13536 228 TTHfmEEAERL-CDRLCVLEAG-RKIAEGRPH---ALIDEH 263
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
523-691 |
9.29e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.34 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMG--------------DLS--PVRGIRHAHRnlKIGYFSQHhveqldLNvsaveLLARK----- 581
Cdd:PRK11153 36 VIGASGAGKSTLIRCINLlerptsgrvlvdgqDLTalSEKELRKARR--QIGMIFQH------FN-----LLSSRtvfdn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 --FP----GLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQ 651
Cdd:PRK11153 103 vaLPlelaGTPKAEIKARvtelLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 652 ALN--NFRGG--VILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:PRK11153 182 LLKdiNRELGltIVLITHEMDVVKRICDRVAVIDAGRL--VEQG 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
488-664 |
9.40e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 9.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNLKIGY 559
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGkisilgqpTRQALQKNLVAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHhvEQLDLNvsavellarkFPGLPEEEYrhQLGRYGISG-----------------------ELAMRPVASLSGGQK 616
Cdd:PRK15056 83 VPQS--EEVDWS----------FPVLVEDVV--MMGRYGHMGwlrrakkrdrqivtaalarvdmvEFRHRQIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 617 SRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR--GGVILVS 664
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdeGKTMLVS 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
178-404 |
9.42e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 50.26 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF-GDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHISLlhveqevAGDDTPALQSVlE 256
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-------SGHDITRLKNR-E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 SDTVRED--LLRQERELSLriaaGRAEGSEAAQLAEIYG-KLEEIEAdkapaRASVILAGLGFTPKMQQQPTrEFSGGWR 333
Cdd:PRK10908 74 VPFLRRQigMIFQDHHLLM----DRTVYDNVAIPLIIAGaSGDDIRR-----RVSAALDKVGLLDKAKNFPI-QLSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDG 404
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
492-665 |
9.99e-07 |
|
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: 50.31 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHS-IFSRLSVSADLESRICVVGENGAGKSTMLKLLMG-----------DLSPVRGIRHAHRNLKIGY 559
Cdd:cd03251 1 VEFKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRfydvdsgriliDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQhhvEQLDLNVSAVELLARKFPGLPEEEYR--------HQL------GRYGISGElamRPVaSLSGGQKSRVAFAQMT 625
Cdd:cd03251 81 VSQ---DVFLFNDTVAENIAYGRPGATREEVEeaaraanaHEFimelpeGYDTVIGE---RGV-KLSGGQRQRIAIARAL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 626 MPCPNFYILDEPTNHLDMETIEALGQALNNFRGG--VILVSH 665
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNrtTFVIAH 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
491-665 |
1.02e-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: 50.16 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYD--PKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMG-----------DLSPVRGIRHAHRNLKI 557
Cdd:cd03248 11 IVKFQNVTFAYPtrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENfyqpqggqvllDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 558 GYFSQHHV---EQLDLNVS--------------AVELLARKFPGLPEEEYRHQLGRYGisgelamrpvASLSGGQKSRVA 620
Cdd:cd03248 91 SLVGQEPVlfaRSLQDNIAyglqscsfecvkeaAQKAHAHSFISELASGYDTEVGEKG----------SQLSGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 621 FAQMTMPCPNFYILDEPTNHLDMETIEALGQAL--NNFRGGVILVSH 665
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALydWPERRTVLVIAH 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
521-665 |
1.04e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLK-------IGYFSQHHVEQL-------DLNVSAVELlar 580
Cdd:PRK13637 36 VGLIGHTGSGKSTLIQHLNGLLKPtsgkiiIDGVDITDKKVKlsdirkkVGLVFQYPEYQLfeetiekDIAFGPINL--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 581 kfpGLPEEEYRHQLGR----YGISGE-LAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 648
Cdd:PRK13637 113 ---GLSEEEIENRVKRamniVGLDYEdYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKE 189
|
170
....*....|....*..
gi 29789050 649 LGQALNNfrgGVILVSH 665
Cdd:PRK13637 190 LHKEYNM---TIILVSH 203
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
184-382 |
1.09e-06 |
|
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: 49.23 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 184 DVSFG----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevaGDDTPALQSVLESDT 259
Cdd:cd03247 5 NVSFSypeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLT--------------------GDLKPQQGEITLDGV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 vreDLLRQERELSLRIAAgraegseAAQLAEIYgkleeieadkaparASVILAGLGftpkmqqqptREFSGGWRMRLALA 339
Cdd:cd03247 65 ---PVSDLEKALSSLISV-------LNQRPYLF--------------DTTLRNNLG----------RRFSGGERQRLALA 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 340 RALFARPDLLLLDEPTNMLDVRAILWLENYL--QTWPSTILVVSH 382
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIfeVLKDKTLIWITH 155
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
197-395 |
1.17e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 50.93 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAW--GRRYGLVGRNGLGKTTLLKMLatRSLRVPAHISLLHVEQEVagddtpalqsvleSDTVREDLLRQERElslR 274
Cdd:PRK13646 25 DVNTEFeqGKYYAIVGQTGSGKSTLIQNI--NALLKPTTGTVTVDDITI-------------THKTKDKYIRPVRK---R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 275 IaaGRAEGSEAAQLAE-------IYG-KLEEIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARP 346
Cdd:PRK13646 87 I--GMVFQFPESQLFEdtvereiIFGpKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 347 DLLLLDEPTNMLDVRA---ILWLENYLQTWPS-TILVVSHDRNFLNAIATDII 395
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSkrqVMRLLKSLQTDENkTIILVSHDMNEVARYADEVI 217
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
180-397 |
1.32e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAGDDtpALQSVLESDt 259
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIA--GFVPYQHGSITLDGKPVEGPG--AERGVVFQN- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 260 vreDLLRQERELSLRIAAGraegseaAQLAEIyGKLEEIEAdkapARASVILAGL-GFtpkmQQQPTREFSGGWRMRLAL 338
Cdd:PRK11248 79 ---EGLLPWRNVQDNVAFG-------LQLAGV-EKMQRLEI----AHQMLKKVGLeGA----EKRYIWQLSGGQRQRVGI 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 339 ARALFARPDLLLLDEPTNMLDV--RAILWlENYLQTWPST---ILVVSHDRNFLNAIATDIIHL 397
Cdd:PRK11248 140 ARALAANPQLLLLDEPFGALDAftREQMQ-TLLLKLWQETgkqVLLITHDIEEAVFMATELVLL 202
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
524-642 |
1.32e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 50.51 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRN-------LKIGYFSQHHVEQL--DLNVSAVELLARKFpGLP 586
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGsvrvddtlITSTSKNkdikqirKKVGLVFQFPESQLfeETVLKDVAFGPQNF-GVS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEY----RHQLGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK13649 118 QEEAealaREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
508-685 |
1.36e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.39 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 508 FSRLSVSAdlesricVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL-----KIGYFSQHHVEQL---DLN 571
Cdd:PRK13638 24 FSLSPVTG-------LVGANGCGKSTLFMNLSGLLRPQKGavlwqgkpLDYSKRGLlalrqQVATVFQDPEQQIfytDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 572 vSAVELLARKFpGLPEEE----------------YRHQlgrygisgelamrPVASLSGGQKSRVAFAQMTMPCPNFYILD 635
Cdd:PRK13638 97 -SDIAFSLRNL-GVPEAEitrrvdealtlvdaqhFRHQ-------------PIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 636 EPTNHLD-------METIEALGQALNNfrggVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:PRK13638 162 EPTAGLDpagrtqmIAIIRRIVAQGNH----VIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
327-666 |
1.36e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.78 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPST-ILVVSHDRNFLNAIATDIIHLHsQRL 402
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTiqaQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMY-QGE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 403 DGYRGDFETFIKSkqerllnqqreyeAQQQYRQHIQVFIDRFryNANRASQVQSKLKMLEkLPELKPVDKESEVVLKFPd 482
Cdd:PRK10261 247 AVETGSVEQIFHA-------------PQHPYTRALLAAVPQL--GAMKGLDYPRRFPLIS-LEHPAKQEPPIEQDTVVD- 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 483 gfekfSPPILQLDEVDFYYDPKHSIFSRLS--------VSADL--ESRICVVGENGAGKST----MLKLLMG-------- 540
Cdd:PRK10261 310 -----GEPILQVRNLVTRFPLRSGLLNRVTrevhavekVSFDLwpGETLSLVGESGSGKSTtgraLLRLVESqggeiifn 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 541 ----DLSPVRGIRHAHRNlkIGYFSQHHVEQLD----LNVSAVELLaRKFPGLPEEEYRHQ----LGRYGISGELAMRPV 608
Cdd:PRK10261 385 gqriDTLSPGKLQALRRD--IQFIFQDPYASLDprqtVGDSIMEPL-RVHGLLPGKAAAARvawlLERVGLLPEHAWRYP 461
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 609 ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGQALNNFRGGVILVSHD 666
Cdd:PRK10261 462 HEFSGGQRQRICIARALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHD 523
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-666 |
1.49e-06 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 50.82 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMLKLLMGDLSP---VRG-IRHAHRNL-------------------------------KIGyfsqhhvE 566
Cdd:COG0444 35 GLVGESGSGKSTLARAILGLLPPpgiTSGeILFDGEDLlklsekelrkirgreiqmifqdpmtslnpvmTVG-------D 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 567 QLD------LNVS-------AVELLARKfpGLPEEEYRhqLGRYgisgelamrPVAsLSGGQKSRVAFAQMTMPCPNFYI 633
Cdd:COG0444 108 QIAeplrihGGLSkaearerAIELLERV--GLPDPERR--LDRY---------PHE-LSGGMRQRVMIARALALEPKLLI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 634 LDEPTNHLDMeTIEAlgQALN-------NFRGGVILVSHD 666
Cdd:COG0444 174 ADEPTTALDV-TIQA--QILNllkdlqrELGLAILFITHD 210
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
525-667 |
1.54e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSPVRGirhahrnlKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQL--------GR 596
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKG--------EILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENClydihfspGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 597 YGIS--------GELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR---GGVILVSH 665
Cdd:PRK13540 106 VGITelcrlfslEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSH 185
|
..
gi 29789050 666 DE 667
Cdd:PRK13540 186 QD 187
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
488-666 |
1.54e-06 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 50.87 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIfsrLSVSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL--------K 556
Cdd:COG3842 2 AMPALELENVSKRYGDVTAL---DDVSLSIEPGefVALLGPSGCGKTTLLRMIAGFETPDSGrILLDGRDVtglppekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 IGYFSQH-----H--VEQldlNVsAVELlarKFPGLPEEEYRHQ----LGRYGISGeLAMRPVASLSGGQKSRVAFAQMT 625
Cdd:COG3842 79 VGMVFQDyalfpHltVAE---NV-AFGL---RMRGVPKAEIRARvaelLELVGLEG-LADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 626 MPCPNFYILDEPTNHLD----METIEALGQALNNFRGGVILVSHD 666
Cdd:COG3842 151 APEPRVLLLDEPLSALDaklrEEMREELRRLQRELGITFIYVTHD 195
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
513-666 |
1.60e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 50.08 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRGirhahrnlKIgyfsqhHVEQLDLNVSAVELLARK--------- 581
Cdd:COG4604 20 VSLTIPKGgiTALIGPNGAGKSTLLSMISRLLPPDSG--------EV------LVDGLDVATTPSRELAKRlailrqenh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 ---------------FP---GLPEEEYRHQLGRYgIS----GELAMRPVASLSGGQKSR--VA--FAQMTMpcpnfYI-L 634
Cdd:COG4604 86 insrltvrelvafgrFPyskGRLTAEDREIIDEA-IAyldlEDLADRYLDELSGGQRQRafIAmvLAQDTD-----YVlL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 29789050 635 DEPTNHLDM----ETIEALGQALNNFRGGVILVSHD 666
Cdd:COG4604 160 DEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHD 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
484-670 |
1.72e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.49 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 484 FEKFSPPIL----QLDEVDFYYDPKHSIFsrlsvsadlesricVVGENGAGKSTMLKLLMG--------------DLSPV 545
Cdd:PRK10908 4 FEHVSKAYLggrqALQGVTFHMRPGEMAF--------------LTGHSGAGKSTLLKLICGierpsagkiwfsghDITRL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 546 RGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQ----LGRYGISGELAMRPVaSLSGGQKSRVAF 621
Cdd:PRK10908 70 KNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRvsaaLDKVGLLDKAKNFPI-QLSGGEQQRVGI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 622 AQMTMPCPNFYILDEPTNHLD---METIEALGQALNNFRGGVILVSHDERFI 670
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
488-694 |
1.89e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSrlsVSADLESR--ICVVGENGAGKSTMLKLLMGDLSPVRGI----------------- 548
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRD---VSFDLYPGevLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdgqlrdlyals 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 549 ----RHAHRNlKIGYFSQHHVEQLDLNVSA----VELL----ARKFpGLPEEEYRHQLGRYGISGELAMRPVASLSGGQK 616
Cdd:PRK11701 80 eaerRRLLRT-EWGFVHQHPRDGLRMQVSAggniGERLmavgARHY-GDIRATAGDWLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 617 SRVAFAQMTMPCPNFYILDEPTNHLDMETiealgQA--LNNFRG-------GVILVSHDERFIRLVCKELWVCENGSVtr 687
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSV-----QArlLDLLRGlvrelglAVVIVTHDLAVARLLAHRLLVMKQGRV-- 230
|
....*...
gi 29789050 688 VEGGF-DQ 694
Cdd:PRK11701 231 VESGLtDQ 238
|
|
| 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 29789050 317 TPKMQQqPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATD 393
Cdd:PRK10762 386 TPSMEQ-AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAkkeIYQLINQFKAEGLSIILVSSEMPEVLGMSDR 464
|
90 100
....*....|....*....|....*...
gi 29789050 394 IIHLHSQRLdgyRGDFETfIKSKQERLL 421
Cdd:PRK10762 465 ILVMHEGRI---SGEFTR-EQATQEKLM 488
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
521-673 |
2.95e-06 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 49.36 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLL------------MGDLS-----PVRGIRHAHRNLK--IGYFSQH-----HVEQLDlNVSAVE 576
Cdd:PRK11264 32 VAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarSLSQQKGLIRQLRqhVGFVFQNfnlfpHRTVLE-NIIEGP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 577 LLARKFP-GLPEEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIealGQALNN 655
Cdd:PRK11264 111 VIVKGEPkEEATARARELLAKVGLAGKETSYP-RRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELV---GEVLNT 186
|
170 180
....*....|....*....|....
gi 29789050 656 FRG------GVILVSHDERFIRLV 673
Cdd:PRK11264 187 IRQlaqekrTMVIVTHEMSFARDV 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
180-359 |
3.21e-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: 49.08 E-value: 3.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFG-----DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML---------------------ATRSLRvpAH 233
Cdd:cd03249 1 IEFKNVSFRypsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptsgeilldgvdirdlNLRWLR--SQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 234 ISLlhVEQEvagddtPalqsVLESDTVREDllrqerelslrIAAGRAEGSEAaqlaeiygklEEIEADKApARASVILAG 313
Cdd:cd03249 79 IGL--VSQE------P----VLFDGTIAEN-----------IRYGKPDATDE----------EVEEAAKK-ANIHDFIMS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 29789050 314 L--GFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03249 125 LpdGYDTLVGERGS-QLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
611-706 |
3.29e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 49.70 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME-TIEALG--QALNNFRGGVILVSHDERFIRLVCKELWVCENGSVTR 687
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIK 245
|
90
....*....|....*....
gi 29789050 688 vEGgfDQYRALLQEQFRRE 706
Cdd:PRK13651 246 -DG--DTYDILSDNKFLIE 261
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
306-383 |
3.34e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 48.62 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 306 RASVILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD------VRAILWLENylQTWPSTILV 379
Cdd:PRK10584 126 GAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDrqtgdkIADLLFSLN--REHGTTLIL 202
|
....
gi 29789050 380 VSHD 383
Cdd:PRK10584 203 VTHD 206
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
183-360 |
3.54e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 50.34 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 183 FDVSFgdrVLLAGADVnlawgrryGLVGRNGLGKTTLLKMLAtrslRV--PA--HISllhveqeVAGDD--TPALQSVLE 256
Cdd:PRK13657 352 EDVSF---EAKPGQTV--------AIVGPTGAGKSTLINLLQ----RVfdPQsgRIL-------IDGTDirTVTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 S-DTVREDLLRQERELSLRIAAGRAEGSEAaqlaEIYgkleeiEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMR 335
Cdd:PRK13657 410 NiAVVFQDAGLFNRSIEDNIRVGRPDATDE----EMR------AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
170 180
....*....|....*....|....*
gi 29789050 336 LALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDV 504
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
290-385 |
3.68e-06 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 49.18 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 290 EIYGKLEEIEADKApaRASVILAGLGftpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD--VRA----- 362
Cdd:cd03294 128 EVQGVPRAEREERA--AEALELVGLE---GWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplIRRemqde 202
|
90 100
....*....|....*....|...
gi 29789050 363 ILWLENYLQtwpSTILVVSHDRN 385
Cdd:cd03294 203 LLRLQAELQ---KTIVFITHDLD 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
178-364 |
3.92e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 49.69 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSF--GDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQ------EVAGDD 247
Cdd:COG1135 2 IELENLSKTFptKGGPVTALDDVSLtiEKGEIFGIIGYSGAGKSTLIRC-----------INLL--ERptsgsvLVDGVD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 248 TPALqsvlesdtvREDLLRQER----------------------ELSLRIAAgraegseaaqlaeiYGKlEEIEAdkapa 305
Cdd:COG1135 69 LTAL---------SERELRAARrkigmifqhfnllssrtvaenvALPLEIAG--------------VPK-AEIRK----- 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 306 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAIL 364
Cdd:COG1135 120 RVAELLELVGLSDKADAYP-SQLSGGQKQRVGIARALANNPKVLLCDEATSALDpetTRSIL 180
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
504-673 |
4.08e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 504 KHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKI-----GYFSQHHVEQLDLNVSAVEL 577
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsIVVNGQTINLvrdkdGQLKVADKNQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 578 LARKFP-------------------GLPEEEYRHQLGRY----GISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYIL 634
Cdd:PRK10619 97 VFQHFNlwshmtvlenvmeapiqvlGLSKQEARERAVKYlakvGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 635 DEPTNHLDMETI-EALG--QALNNFRGGVILVSHDERFIRLV 673
Cdd:PRK10619 177 DEPTSALDPELVgEVLRimQQLAEEGKTMVVVTHEMGFARHV 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
311-361 |
4.23e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 48.86 E-value: 4.23e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 311 LAGLGFTPKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK13635 125 LRQVGMEDFLNREPHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPR 174
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
173-395 |
4.40e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 48.42 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 173 NKSYDVRI--ENFDVSFGD--RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPahisllhveqevagddt 248
Cdd:COG2401 22 DLSERVAIvlEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTP----------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 palqsvlESDTVREDLLRQERELSLriaagraegseaaqlaeiygkLEEIEADKAPARASVIL--AGLGFTPKMQQQPtR 326
Cdd:COG2401 85 -------VAGCVDVPDNQFGREASL---------------------IDAIGRKGDFKDAVELLnaVGLSDAVLWLRRF-K 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR---------AILWLENYLqtwpsTILVVSHDRNFLNAIATDII 395
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtakrvarnlQKLARRAGI-----TLVVATHHYDVIDDLQPDLL 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
492-691 |
4.52e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.47 E-value: 4.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSrlsVSADLESRICVV--GENGAGKSTMLKLL-------MGDLS------------PVRGIRH 550
Cdd:PRK11124 3 IQLNGINCFYGAHQALFD---ITLDCPQGETLVllGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsktpSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 551 AHRNLKIgYFSQHHveqLDLNVSAVELLAR---KFPGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQ 623
Cdd:PRK11124 80 LRRNVGM-VFQQYN---LWPHLTVQQNLIEapcRVLGLSKDQALARaeklLERLRLK-PYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 624 MTMPCPNFYILDEPTNHLDME-------TIEALGQAlnnfrgGV--ILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEitaqivsIIRELAET------GItqVIVTHEVEVARKTASRVVYMENGHI--VEQG 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
492-666 |
4.76e-06 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 48.45 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL----------KIGYF 560
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGeIFIDGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQH-----H--VEQldlNVSAV----------------ELLarKFPGLPEEEYRHqlgRYgisgelamrPvASLSGGQKS 617
Cdd:cd03295 81 IQQiglfpHmtVEE---NIALVpkllkwpkekireradELL--ALVGLDPAEFAD---RY---------P-HELSGGQQQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 618 RVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF----RGGVILVSHD 666
Cdd:cd03295 143 RVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLqqelGKTIVFVTHD 195
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
521-689 |
5.22e-06 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 48.45 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG--------IRHAHRNL-----KIGYFSQH-----H--VEQldlNVsaveLLA- 579
Cdd:COG1126 30 VVIIGPSGSGKSTLLRCINLLEEPDSGtitvdgedLTDSKKDInklrrKVGMVFQQfnlfpHltVLE---NV----TLAp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 580 RKFPGLP----EEEYRHQLGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 648
Cdd:COG1126 103 IKVKKMSkaeaEERAMELLERVGLADKADAYP-AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDpelvgevLDVMRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 649 LGQalnnfRG-GVILVSHDERFIRLVCKELWVCENGSVtrVE 689
Cdd:COG1126 182 LAK-----EGmTMVVVTHEMGFAREVADRVVFMDGGRI--VE 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
488-642 |
5.28e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 48.62 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFSrlsVSADLESR--ICVVGENGAGKSTMLKLL--MGDLSP---VRG-IRHAHRNLkigY 559
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNS---VSLDFYPNeiTALIGPSGSGKSTLLRSInrMNDLNPevtITGsIVYNGHNI---Y 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 560 FSQHHVEQLDLNVSAVELLARKFP---------GLP----------EEEYRHQLGRYGISGELAMRPVAS---LSGGQKS 617
Cdd:PRK14239 76 SPRTDTVDLRKEIGMVFQQPNPFPmsiyenvvyGLRlkgikdkqvlDEAVEKSLKGASIWDEVKDRLHDSalgLSGGQQQ 155
|
170 180
....*....|....*....|....*
gi 29789050 618 RVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALD 180
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
492-667 |
6.03e-06 |
|
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: 47.63 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDPKHSIfSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-----------IRHAHRNlkIGYF 560
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggrdvtdLPPKDRD--IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 561 SQHHVEQLDLNVS---AVELLARKFPGLPEEEYRHQLGR-YGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDE 636
Cdd:cd03301 78 FQNYALYPHMTVYdniAFGLKLRKVPKDEIDERVREVAElLQIEHLLDRKP-KQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 29789050 637 PTNHLDMETIEALGQALNNF--RGGV--ILVSHDE 667
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLqqRLGTttIYVTHDQ 191
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
169-361 |
6.63e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.96 E-value: 6.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 169 SSGKNKSYDVRieNFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLgkttllkmlATRSLRVPAHisllhveqeVAGDDT 248
Cdd:NF000106 7 SNGARNAVEVR--GLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA---------A**RGALPAH---------V*GPDA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 PALQSVLESDTVREDLLRQERELSLRIAAGRAEGSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTReF 328
Cdd:NF000106 67 GRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAK-Y 145
|
170 180 190
....*....|....*....|....*....|...
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPR 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
521-642 |
7.55e-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: 49.56 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGirHAHRNLKIGYFSQHHVEQldlNVSAVELLARKFPgLPEEEYRHQLGRYGIS 600
Cdd:TIGR00957 667 VAVVGQVGCGKSSLLSALLAEMDKVEG--HVHMKGSVAYVPQQAWIQ---NDSLRENILFGKA-LNEKYYQQVLEACALL 740
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 601 GELAMRPVA----------SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:TIGR00957 741 PDLEILPSGdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
266-363 |
8.76e-06 |
|
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: 46.66 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 266 RQERELSLRIAAGR------AEGSEAAQLAE-IYGKLE----EIEADKAPARASV----ILAGLGFTPK-------MQQQ 323
Cdd:cd03215 14 GAVRDVSFEVRAGEivgiagLVGNGQTELAEaLFGLRPpasgEITLDGKPVTRRSprdaIRAGIAYVPEdrkreglVLDL 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 29789050 324 PTRE-------FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:cd03215 94 SVAEnialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
521-665 |
1.02e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 47.77 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG-----------------IRHahrnlKIGYFSQHHVEQLdlnVSA-VELLARKF 582
Cdd:PRK13633 39 LVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwdIRN-----KAGMVFQNPDNQI---VATiVEEDVAFG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 583 P---GLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEA 648
Cdd:PRK13633 111 PenlGIPPEEIRERvdesLKKVGMY-EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrrevVNTIKE 189
|
170
....*....|....*..
gi 29789050 649 LGQalnNFRGGVILVSH 665
Cdd:PRK13633 190 LNK---KYGITIILITH 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
329-382 |
1.06e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 48.33 E-value: 1.06e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAIL-WLENYLQTWPSTILVVSH 382
Cdd:PRK11144 130 SGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkRELLpYLERLAREINIPILYVSH 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
525-669 |
1.06e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLK--------IGYFSQHHVEQLDLnvsAVELLARKFP------- 583
Cdd:PRK11288 37 GENGAGKSTLLKILSGNYQPdagsilIDGQEMRFASTTaalaagvaIIYQELHLVPEMTV---AENLYLGQLPhkggivn 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 584 -GLPEEEYRHQLGRYGISGELAMrPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR--GGV 660
Cdd:PRK11288 114 rRLLNYEAREQLEHLGVDIDPDT-PLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRaeGRV 192
|
170
....*....|..
gi 29789050 661 IL-VSH--DERF 669
Cdd:PRK11288 193 ILyVSHrmEEIF 204
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
513-688 |
1.08e-05 |
|
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: 47.33 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 513 VSADLES--RICVVGENGAGKSTMLKLLMGDLSPVRG---------IRHAHRNLKIGYFSQH-----HVEQLDlNVSAVE 576
Cdd:cd03296 21 VSLDIPSgeLVALLGPSGSGKTTLLRLIAGLERPDSGtilfggedaTDVPVQERNVGFVFQHyalfrHMTVFD-NVAFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 577 LLARKFPGLPEEEYRHQ----LGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQA 652
Cdd:cd03296 100 RVKPRSERPPEAEIRAKvhelLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRW 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 29789050 653 LNNFRGGV----ILVSHDERFIRLVCKELWVCENGSVTRV 688
Cdd:cd03296 179 LRRLHDELhvttVFVTHDQEEALEVADRVVVMNKGRIEQV 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
521-683 |
1.10e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 47.76 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKIGYFSQHHVEQLDLN------VSAV-------ELLA---RKFP 583
Cdd:PRK10419 41 VALLGRSGCGKSTLARLLVGLESPSQGnVSWRGEPLAKLNRAQRKAFRRDIQmvfqdsISAVnprktvrEIIReplRHLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 584 GLPEEEYRHQ----LGRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM----ETIEALGQALNN 655
Cdd:PRK10419 121 SLDKAERLARasemLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQ 200
|
170 180
....*....|....*....|....*...
gi 29789050 656 FRGGVILVSHDERFIRLVCKELWVCENG 683
Cdd:PRK10419 201 FGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
178-359 |
1.14e-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: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllHVEQ------EVAGddtpal 251
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCIN-------------LLEEpdsgtiTVDG------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 QSVLESDTvreDLLRQERE---------------------LSLRIAAGRAEgSEAAQLAEIYgkLEEIE-ADKA---PAR 306
Cdd:COG1126 63 EDLTDSKK---DINKLRRKvgmvfqqfnlfphltvlenvtLAPIKVKKMSK-AEAEERAMEL--LERVGlADKAdayPAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 307 asviLAGlGftpkmQQQptrefsggwrmRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG1126 137 ----LSG-G-----QQQ-----------RVAIARALAMEPKVMLFDEPTSALD 168
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
329-390 |
1.20e-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: 1.20e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 329 SGGWRM------RLALARALFARPDLLLLDEPTNMLD---VRAIL--WLENYLQTWPSTILVVSHDRNFLNAI 390
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenIEESLaeIIEERKSQKNFQLIVITHDEELVDAA 189
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
523-691 |
1.27e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 47.77 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLL-----------------MGDLSPvRGIRHAHRnlKIGYFSQHhveqldlnvsaVELLARK---- 581
Cdd:COG1135 36 IIGYSGAGKSTLIRCInllerptsgsvlvdgvdLTALSE-RELRAARR--KIGMIFQH-----------FNLLSSRtvae 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 ---FP----GLPEEEyRHQ-----LGRYGISGELAMRPvASLSGGQKSRVAFAQ--MTMPcpnfYIL--DEPTNHLDMET 645
Cdd:COG1135 102 nvaLPleiaGVPKAE-IRKrvaelLELVGLSDKADAYP-SQLSGGQKQRVGIARalANNP----KVLlcDEATSALDPET 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 646 ---IEALGQALNNfRGG--VILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:COG1135 176 trsILDLLKDINR-ELGltIVLITHEMDVVRRICDRVAVLENGRI--VEQG 223
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
488-691 |
1.27e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 48.04 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPILQLDEVDFYYDPKHSIFS--RL-----SVSADLES--RICVVGENGAGKSTMLKLLM-------GDLS-------- 543
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKpeRLvkaldGVSFTLERgkTLAVVGESGCGKSTLARLLTmietptgGELYyqgqdllk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 544 PVRGIRHAHRNL----------------KIGyfsQHHVEQLDLN--VSAVEllaRKfpglpeEEYRHQLGRYGISGELAM 605
Cdd:PRK11308 82 ADPEAQKLLRQKiqivfqnpygslnprkKVG---QILEEPLLINtsLSAAE---RR------EKALAMMAKVGLRPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 606 RPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMeTIEAlgQALN-------NFRGGVILVSHDERFIRLVCKELW 678
Cdd:PRK11308 150 RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQA--QVLNlmmdlqqELGLSYVFISHDLSVVEHIADEVM 226
|
250
....*....|...
gi 29789050 679 VCENGSVtrVEGG 691
Cdd:PRK11308 227 VMYLGRC--VEKG 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
92-359 |
1.35e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 92 QLSKIMENYDCDTKLPglLKREQSSTVNAKKLEKAEARLKAKQEKrsekETLKTSNPLVL---EEASASQAGSRKESRLE 168
Cdd:PTZ00243 569 QLAAVLENVDVTAFVP--VKLPRAPKVKTSLLSRALRMLCCEQCR----PTKRHPSPSVVvedTDYGSPSSASRHIVEGG 642
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 169 SSGKNKSYDVRIENFDVSFGD---------RVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR----SLRVPAHIS 235
Cdd:PTZ00243 643 TGGGHEATPTSERSAKTPKMKtddffelepKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQfeisEGRVWAERS 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 236 LLHVEQevagddtpalQSVLESDTVREDLLRQERELSLRIA-AGRAEGSEAaQLAEIYGKLE-EIeadkapARASVILag 313
Cdd:PTZ00243 723 IAYVPQ----------QAWIMNATVRGNILFFDEEDAARLAdAVRVSQLEA-DLAQLGGGLEtEI------GEKGVNL-- 783
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29789050 314 lgftpkmqqqptrefSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PTZ00243 784 ---------------SGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
208-385 |
1.40e-05 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 47.23 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 208 LVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQEVAGDDTPALQ-SVLESDTVREDLLRQERE---------LSLRIAA 277
Cdd:PRK03695 27 LVGPNGAGKSTLLARMA----------GLLPGSGSIQFAGQPLEAwSAAELARHRAYLSQQQTPpfampvfqyLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 278 GRAEGSEAAQLAEIygkleeieadkapARAsvilagLGFTPKMQQqPTREFSGG-W-RMRLALA-----RALFARPDLLL 350
Cdd:PRK03695 97 KTRTEAVASALNEV-------------AEA------LGLDDKLGR-SVNQLSGGeWqRVRLAAVvlqvwPDINPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 29789050 351 LDEPTNMLDVRAILWLENYLQTWPS---TILVVSHDRN 385
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHDLN 194
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
172-362 |
1.43e-05 |
|
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: 46.47 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 172 KNKSYDVrienfDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSlrvpahisllhveqevagddtpal 251
Cdd:cd03232 7 KNLNYTV-----PVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 252 qsvlESDTVREDLL--RQERELSLRIAAGRAEgseaaQLAEIYGKLEEIEAdkapARASVILAGLGftpkmQQQptrefs 329
Cdd:cd03232 58 ----TAGVITGEILinGRPLDKNFQRSTGYVE-----QQDVHSPNLTVREA----LRFSALLRGLS-----VEQ------ 113
|
170 180 190
....*....|....*....|....*....|...
gi 29789050 330 ggwRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:cd03232 114 ---RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
178-359 |
1.44e-05 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 47.79 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDDtpalqsVLES 257
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVA--GLEKPTEGQIF-----IDGED------VTHR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVRED--LLRQERELSLRIAAGRAEGseaaqlaeiYG-KL-----EEIEADKAPARASVILAGlgftpkMQQQPTREFS 329
Cdd:PRK11432 74 SIQQRDicMVFQSYALFPHMSLGENVG---------YGlKMlgvpkEERKQRVKEALELVDLAG------FEDRYVDQIS 138
|
170 180 190
....*....|....*....|....*....|
gi 29789050 330 GGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
327-404 |
1.71e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 47.35 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHDRNFLNAIATDIIHLHSQR- 401
Cdd:PRK13637 144 ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKc 223
|
....
gi 29789050 402 -LDG 404
Cdd:PRK13637 224 eLQG 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
182-383 |
1.86e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 182 NFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHisllhveqEVAGDDTPALQSVLESDTVR 261
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGY--------RYSGDVLLGGRSIFNYRDVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 262 E------DLLRQERELSLRIAAGRAEGSEAAqlaeiygKLEEIEADKAPARASVILAGL--GFTPKMQQQPTReFSGGWR 333
Cdd:PRK14271 98 EfrrrvgMLFQRPNPFPMSIMDNVLAGVRAH-------KLVPRKEFRGVAQARLTEVGLwdAVKDRLSDSPFR-LSGGQQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 29789050 334 MRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 383
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHN 221
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
173-366 |
1.92e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 47.49 E-value: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 173 NKSYDVrienfdvsfGDRVLLAGADVNL--AWGRRYGLVGRNGLGKTTLLKMlatrslrvpahISLLhvEQ------EVA 244
Cdd:PRK11153 8 SKVFPQ---------GGRTIHALNNVSLhiPAGEIFGVIGASGAGKSTLIRC-----------INLL--ERptsgrvLVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 245 GDDTPALqsvlesdtvREDLLRQERE-----------LSLRIAAGRAegseAAQLaEIYGK-LEEIEAdkapaRASVILA 312
Cdd:PRK11153 66 GQDLTAL---------SEKELRKARRqigmifqhfnlLSSRTVFDNV----ALPL-ELAGTpKAEIKA-----RVTELLE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 313 GLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWL 366
Cdd:PRK11153 127 LVGLSDKADRYPA-QLSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSILEL 182
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
521-707 |
1.96e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGIRHAHRnLKIGYFSQHhveqldlnvsavellarkfpglpeeeyrhqlgrygis 600
Cdd:cd03222 28 IGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQY------------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 601 gelamrpvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF----RGGVILVSHDERFIRLVCKE 676
Cdd:cd03222 70 --------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseegKKTALVVEHDLAVLDYLSDR 141
|
170 180 190
....*....|....*....|....*....|.
gi 29789050 677 LWVcengsvtrVEGGFDQYRALLQEQFRREG 707
Cdd:cd03222 142 IHV--------FEGEPGVYGIASQPKGTREG 164
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
196-383 |
1.97e-05 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 46.67 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 196 ADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgDDTPALQSVlesdtvreDLLRQER----EL 271
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIA--GFLPPDSGRILWNGQDLT-ALPPAERPV--------SMLFQENnlfpHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 272 SLR--IAAGRAEGseaaqlaeiyGKLEEieADKApaRASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLL 349
Cdd:COG3840 87 TVAqnIGLGLRPG----------LKLTA--EQRA--QVEQALERVGLAGLLDRLP-GQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 350 LLDEP---------TNMLD-VRAIlwlenyLQTWPSTILVVSHD 383
Cdd:COG3840 152 LLDEPfsaldpalrQEMLDlVDEL------CRERGLTVLMVTHD 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
521-642 |
2.02e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 46.62 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNlkIGYFSQH-------HVEQldlNVSA-------VE---LLA--- 579
Cdd:COG1101 35 VTVIGSNGAGKSTLLNAIAGSLPPDSGsILIDGKD--VTKLPEYkrakyigRVFQ---DPMMgtapsmtIEenlALAyrr 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 580 ---RKF-PGLP---EEEYRHQLGRYGISGELAMR-PVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:COG1101 110 gkrRGLrRGLTkkrRELFRELLATLGLGLENRLDtKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
605-665 |
2.25e-05 |
|
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: 45.92 E-value: 2.25e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 605 MRPVASLSGGQKSRVA----FA-QMTMPCPnFYILDEPTNHLDMETIEALGQALNNFRGGV--ILVSH 665
Cdd:cd03278 108 VQRLSLLSGGEKALTAlallFAiFRVRPSP-FCVLDEVDAALDDANVERFARLLKEFSKETqfIVITH 174
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
523-669 |
2.27e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNlKIGYFS----QHHVEQ------LDL----------NVSAVELLARKF 582
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQFS-HITRLSfeqlQKLVSDewqrnnTDMlspgeddtgrTTAEIIQDEVKD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 583 PGLPEEeYRHQLGrygISGELAmRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF-RGGVI 661
Cdd:PRK10938 113 PARCEQ-LAQQFG---ITALLD-RRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLhQSGIT 187
|
....*...
gi 29789050 662 LVSHDERF 669
Cdd:PRK10938 188 LVLVLNRF 195
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
187-382 |
2.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 46.65 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 187 FGDRVLLaGADVNLAWGRRYGLVGRNGLGKTTLLkmlatrslrvpahisllhveQEVAGDDTPALQSVLESDTVREDLLR 266
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLL--------------------QHLNGLLQPTEGKVTVGDIVVSSTSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 267 QERELSLRIAAGRAEGSEAAQLAE-------IYGKLE-EIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLAL 338
Cdd:PRK13643 76 QKEIKPVRKKVGVVFQFPESQLFEetvlkdvAFGPQNfGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 339 ARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSH 382
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
523-668 |
2.45e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMG-------------------DLSPVRgirHAHRNLKIGYfsQHHVEQLdlNVSAVELL----- 578
Cdd:CHL00131 38 IMGPNGSGKSTLSKVIAGhpaykilegdilfkgesilDLEPEE---RAHLGIFLAF--QYPIEIP--GVSNADFLrlayn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 579 -ARKFPGLPE-------EEYRHQLGRYGISGELAMRPV-ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEAL 649
Cdd:CHL00131 111 sKRKFQGLPEldpleflEIINEKLKLVGMDPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKII 190
|
170 180
....*....|....*....|..
gi 29789050 650 GQALNNFRG---GVILVSHDER 668
Cdd:CHL00131 191 AEGINKLMTsenSIILITHYQR 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
174-382 |
2.49e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 46.37 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 174 KSYDVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRvpahislLHVEQEVAGDDTPALQS 253
Cdd:PRK14267 1 MKFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTF-NRLLE-------LNEEARVEGEVRLFGRN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLESDTvreDLLRQERELS-----------LRIAAGRAEGSEAAQLAEIYGKLEEI---EADKAPARASVilaglgfTPK 319
Cdd:PRK14267 73 IYSPDV---DPIEVRREVGmvfqypnpfphLTIYDNVAIGVKLNGLVKSKKELDERvewALKKAALWDEV-------KDR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 320 MQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSH 382
Cdd:PRK14267 143 LNDYPS-NLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKeyTIVLVTH 206
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
203-395 |
2.51e-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: 44.67 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLAtrslrvpahisllhveqevagddtpalqsvlesdtvredllrqerelslriaagraeg 282
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALA---------------------------------------------------------- 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 283 seaAQLAEIYGKLEEIEADKAPARASVILAGLGFTPKMqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:smart00382 24 ---RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK-----ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 29789050 363 ---------ILWLENYLQTWPSTILVVSHDRNFLNAIATDII 395
Cdd:smart00382 96 eallllleeLRLLLLLKSEKNLTVILTTNDEKDLGPALLRRR 137
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
523-642 |
2.80e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRGIRHAHRNL----------------KIGYFSQHHVEQLD--LNVSAVELLARKFPG 584
Cdd:PTZ00243 691 VLGATGSGKSTLLQSLLSQFEISEGRVWAERSIayvpqqawimnatvrgNILFFDEEDAARLAdaVRVSQLEADLAQLGG 770
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 585 LPEEEyrhqLGRYGISgelamrpvasLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PTZ00243 771 GLETE----IGEKGVN----------LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
179-354 |
2.94e-05 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 46.18 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----------------TRslrVPAH------IS 235
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVglvkpdsgrifldgediTH---LPMHkrarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 236 LLhvEQEvagddtpalQSVLESDTVREDLL--RQERELSlriAAGRAEgseaaqlaeiygKLEEIeadkaparasviLAG 313
Cdd:COG1137 82 YL--PQE---------ASIFRKLTVEDNILavLELRKLS---KKEREE------------RLEEL------------LEE 123
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 314 LGFTpKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEP 354
Cdd:COG1137 124 FGIT-HLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
512-665 |
3.00e-05 |
|
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: 47.44 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 512 SVSADLES--RICVVGENGAGKSTMLKLLmGDLSPVR-GIRHAHRNLKIGYFSQHHV-------EQLDLNVSAVELLARK 581
Cdd:TIGR00954 470 SLSFEVPSgnNLLICGPNGCGKSSLFRIL-GELWPVYgGRLTKPAKGKLFYVPQRPYmtlgtlrDQIIYPDSSEDMKRRG 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 FPGLPEEEY------RHQLGRYGisGELAMRPVAS-LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALN 654
Cdd:TIGR00954 549 LSDKDLEQIldnvqlTHILEREG--GWSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR 626
|
170
....*....|.
gi 29789050 655 NFRGGVILVSH 665
Cdd:TIGR00954 627 EFGITLFSVSH 637
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
523-651 |
3.03e-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: 45.23 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVR--------GIRHAHRNLK--IGYFSQHhvEQLDLNVSAVELLArkfpglpeeeyrh 592
Cdd:cd03213 40 IMGPSGAGKSTLLNALAGRRTGLGvsgevlinGRPLDKRSFRkiIGYVPQD--DILHPTLTVRETLM------------- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 593 qlgrygISGELamrpvASLSGGQKSRVAFA-QMTMPcPNFYILDEPTNHLD-------METIEALGQ 651
Cdd:cd03213 105 ------FAAKL-----RGLSGGERKRVSIAlELVSN-PSLLFLDEPTSGLDsssalqvMSLLRRLAD 159
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
492-691 |
3.16e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 46.16 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 492 LQLDEVDFYYDpKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRGIRH---------------AHRNL- 555
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdfsqkpsekAIRLLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 556 -KIGY-FSQHH------VEQlDLNVSAVELLarkfpGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFAQ 623
Cdd:COG4161 82 qKVGMvFQQYNlwphltVME-NLIEAPCKVL-----GLSKEQAREKamklLARLRLT-DKADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 624 MTMPCPNFYILDEPTNHLD-------METIEALGQAlnnfrgGV--ILVSHDERFIRLVCKELWVCENGSVtrVEGG 691
Cdd:COG4161 155 ALMMEPQVLLFDEPTAALDpeitaqvVEIIRELSQT------GItqVIVTHEVEFARKVASQVVYMEKGRI--IEQG 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
490-694 |
3.32e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 47.66 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 490 PILQLDEVDFYYDPKHS--IFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP-------VRG----------IRH 550
Cdd:PLN03232 613 PAISIKNGYFSWDSKTSkpTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetssvvIRGsvayvpqvswIFN 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 551 AHRNLKIGYFSQHHVEQL--DLNVSAVELLARKFPGlpeeEYRHQLGRYGIsgelamrpvaSLSGGQKSRVAFAQMTMPC 628
Cdd:PLN03232 693 ATVRENILFGSDFESERYwrAIDVTALQHDLDLLPG----RDLTEIGERGV----------NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 629 PNFYILDEPTNHLDMETIEALGQAL--NNFRGGV-ILVSHDERFIRLVCKELWVCEngSVTRVEGGFDQ 694
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCmkDELKGKTrVLVTNQLHFLPLMDRIILVSE--GMIKEEGTFAE 825
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
522-643 |
3.48e-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: 44.99 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 522 CVVGENGAGKSTMlkllMGDLSPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELLARKfpglpeeeyRHQLGRYGISG 601
Cdd:cd03239 26 AIVGPNGSGKSNI----VDAICFVLGGKAAKLRRGSLLFLAGGGVKAGINSASVEITFDK---------SYFLVLQGKVE 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 29789050 602 ELamrpvasLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDM 643
Cdd:cd03239 93 QI-------LSGGEKSLSALAlifalQEIKPSP-FYVLDEIDAALDP 131
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
304-362 |
3.73e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 3.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 304 PARASVIL----AGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:PRK15439 376 PARENAVLeryrRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
485-644 |
3.80e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 46.38 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 485 EKFSPPILQLDEVDFYYDpKHSIFsrlsvsadlesriCVVGENGAGKSTMLKLLMGDLSPVRG----------------- 547
Cdd:PRK13631 33 EKQENELVALNNISYTFE-KNKIY-------------FIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 548 --IRHAHRNLK--------IGYFSQHHVEQL-------DLNVSAVELlarkfpGLPEEEYRHQ----LGRYGISGELAMR 606
Cdd:PRK13631 99 liTNPYSKKIKnfkelrrrVSMVFQFPEYQLfkdtiekDIMFGPVAL------GVKKSEAKKLakfyLNKMGLDDSYLER 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 29789050 607 PVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDME 644
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| 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 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS--TILVVSHD 383
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
187-355 |
4.10e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 47.04 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 187 FGDRVllAGADVNLAWGRR--YGLVGRNGLGKTTLLKMLaTRSLrvPA---HISLLHveQEVAGDDTPALQSV------- 254
Cdd:NF033858 276 FGDFT--AVDHVSFRIRRGeiFGFLGSNGCGKSTTMKML-TGLL--PAsegEAWLFG--QPVDAGDIATRRRVgymsqaf 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 255 -LESD-TVREDLlrqerelslriaagraegseaaqlaEIYGKLEEIEADKAPARASVILAGLGFTPKMQQQPTReFSGGW 332
Cdd:NF033858 349 sLYGElTVRQNL-------------------------ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDS-LPLGI 402
|
170 180
....*....|....*....|...
gi 29789050 333 RMRLALARALFARPDLLLLDEPT 355
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPT 425
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
189-359 |
4.26e-05 |
|
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: 45.34 E-value: 4.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 189 DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLR-------------------VPAHISllHVEQevagDDTp 249
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilfngqprkpdqFQKCVA--YVRQ----DDI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 250 alqsVLESDTVREDL-----LRQERELSLRIAAGRAEGSEAAQLAeiygkLEEIeadkaparASVILAGLgftpkmqqqp 324
Cdd:cd03234 92 ----LLPGLTVRETLtytaiLRLPRKSSDAIRKKRVEDVLLRDLA-----LTRI--------GGNLVKGI---------- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 29789050 325 trefSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:cd03234 145 ----SGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
177-383 |
4.34e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 46.18 E-value: 4.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVaGDDTPALQSVle 256
Cdd:PRK11000 3 SVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIA--GLEDITSGDLFIGEKRM-NDVPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 257 sdtvreDLLRQEREL--SLRIAAGRAEGSEAAqlaeiygKLEEIEADKAPARASVIL--AGLgftpkMQQQPtREFSGGW 332
Cdd:PRK11000 78 ------GMVFQSYALypHLSVAENMSFGLKLA-------GAKKEEINQRVNQVAEVLqlAHL-----LDRKP-KALSGGQ 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNMLD------VRA-ILWLENYLQtwpSTILVVSHD 383
Cdd:PRK11000 139 RQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLHKRLG---RTMIYVTHD 193
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
195-360 |
4.37e-05 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 46.24 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 195 GADVNLAWGRRYGLVGRNGLGKTTLLKmlatrslrvpAHISLLHV-EQEVA--GDDTPALQSVlESDTVREDL--LRQER 269
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFAR----------AIIGLVKAtDGEVAwlGKDLLGMKDD-EWRAVRSDIqmIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 270 ELSL--RIAAGR--AEgseaaQLAEIYGKLEEIEADKapaRASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFAR 345
Cdd:PRK15079 108 LASLnpRMTIGEiiAE-----PLRTYHPKLSRQEVKD---RVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILE 179
|
170
....*....|....*
gi 29789050 346 PDLLLLDEPTNMLDV 360
Cdd:PRK15079 180 PKLIICDEPVSALDV 194
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
609-671 |
4.88e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 4.88e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 609 ASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG----VILVSHDERFIR 671
Cdd:PTZ00265 578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAHRLSTIR 644
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
525-637 |
4.90e-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: 45.23 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSPVRG--------IRHAH----RNLKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRH 592
Cdd:cd03218 33 GPNGAGKTTTFYMIVGLVKPDSGkilldgqdITKLPmhkrARLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREE 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 29789050 593 Q----LGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEP 637
Cdd:cd03218 113 KleelLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
207-359 |
5.05e-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: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 207 GLVGRNGLGKTTLLKMLATRslRVPAHIS---LL---------------HVEQevagDDtpalqSVLESDTVREdllrqe 268
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAGR--RTGLGVSgevLIngrpldkrsfrkiigYVPQ----DD-----ILHPTLTVRE------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 269 relSLRIAAGraegseaaqlaeiygkleeieadkaparasviLAGLgftpkmqqqptrefSGGWRMRLALARALFARPDL 348
Cdd:cd03213 102 ---TLMFAAK--------------------------------LRGL--------------SGGERKRVSIALELVSNPSL 132
|
170
....*....|.
gi 29789050 349 LLLDEPTNMLD 359
Cdd:cd03213 133 LFLDEPTSGLD 143
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
322-362 |
5.89e-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: 5.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 29789050 322 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:COG1129 389 EQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGA 429
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
178-359 |
6.06e-05 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 46.09 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLHVEQEVAgdDTPALQ----S 253
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA--GFETPDSGRIMLDGQDIT--HVPAENrhvnT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 254 VLESD------TVREDllrqerelslrIAAG-RAEGSEAAqlaeiygkleEIEADKAPARASVILAGLGftpkmQQQPTR 326
Cdd:PRK09452 91 VFQSYalfphmTVFEN-----------VAFGlRMQKTPAA----------EITPRVMEALRMVQLEEFA-----QRKPHQ 144
|
170 180 190
....*....|....*....|....*....|...
gi 29789050 327 eFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK09452 145 -LSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
193-383 |
6.27e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 45.61 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATrslrvpahiSLLHVEQEVAGDDTPAlqsvlesDTVREDLLRqerels 272
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNG---------ILKPSSGRILFDGKPI-------DYSRKGLMK------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 LRIAAGRAEGSEAAQL--AEIYGKLE------EIEADKAPARASVILAGLGFTPkMQQQPTREFSGGWRMRLALARALFA 344
Cdd:PRK13636 80 LRESVGMVFQDPDNQLfsASVYQDVSfgavnlKLPEDEVRKRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 29789050 345 RPDLLLLDEPTNMLDVRAIL----WLENYLQTWPSTILVVSHD 383
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSeimkLLVEMQKELGLTIIIATHD 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
177-382 |
6.87e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.17 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENFDVSFGDRVLLAGADVNLAW--GRRYGLVGRNGLGKTTLLKMLaTR----------------------SLRvpA 232
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIpaGKTVALVGRSGSGKSTIANLL-TRfydidegeilldghdlrdytlaSLR--N 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 233 HISLlhVEQEVAgddtpalqsvLESDTVREDllrqerelslrIAAGRAEgseaaqlaeIYGKlEEIEADKAPARAsvila 312
Cdd:PRK11176 418 QVAL--VSQNVH----------LFNDTIANN-----------IAYARTE---------QYSR-EQIEEAARMAYA----- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 313 gLGFTPKMQQ-------QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV---RAILWLENYLQTwPSTILVVSH 382
Cdd:PRK11176 460 -MDFINKMDNgldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTeseRAIQAALDELQK-NRTSLVIAH 537
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
320-383 |
7.08e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 45.11 E-value: 7.08e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 320 MQQQPTRE---FSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQT----WPSTILVVSHD 383
Cdd:PRK13650 130 MQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
521-642 |
7.14e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 46.19 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMG------DLSPVRGIRHAHRNLKI-----GYFSQHHV------EQLDLNVSAVELLARKfp 583
Cdd:TIGR00955 54 LAVMGSSGAGKTTLMNALAFrspkgvKGSGSVLLNGMPIDAKEmraisAYVQQDDLfiptltVREHLMFQAHLRMPRR-- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 584 gLPEEEYRH-------QLG-------RYGISGElamrpVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:TIGR00955 132 -VTKKEKRErvdevlqALGlrkcantRIGVPGR-----VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
173-361 |
7.39e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.99 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 173 NKSYDVRIENFDV-SFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA-----TRSLRVPAhISLlhveqevagd 246
Cdd:PRK11174 345 NDPVTIEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLgflpyQGSLKING-IEL---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 dtpalqSVLESDTVREDL--LRQEREL---SLR--IAAGRAEGSEaaqlaeiygklEEIEADKAPARASVILAGL--GFT 317
Cdd:PRK11174 414 ------RELDPESWRKHLswVGQNPQLphgTLRdnVLLGNPDASD-----------EQLQQALENAWVSEFLPLLpqGLD 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 29789050 318 PKMQQQPTReFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK11174 477 TPIGDQAAG-LSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
523-666 |
7.76e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.16 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG-----------------IRHAHRnlKIGYFSQHHVEQL-DLNVSAVELLARKFPG 584
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGtvtvdditithktkdkyIRPVRK--RIGMVFQFPESQLfEDTVEREIIFGPKNFK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 585 LPEEE---YRHQL-GRYGISGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD-------METIEALGQAL 653
Cdd:PRK13646 116 MNLDEvknYAHRLlMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDpqskrqvMRLLKSLQTDE 195
|
170
....*....|...
gi 29789050 654 NNfrgGVILVSHD 666
Cdd:PRK13646 196 NK---TIILVSHD 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
521-666 |
8.42e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.87 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLKLLMGDLSPVRGI-RHAHRNLK--------------IGY-FSQHHveqLDLNVSA---VELLArK 581
Cdd:PRK10535 37 VAIVGASGSGKSTLMNILGCLDKPTSGTyRVAGQDVAtldadalaqlrrehFGFiFQRYH---LLSHLTAaqnVEVPA-V 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 582 FPGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM---ETIEALGQALN 654
Cdd:PRK10535 113 YAGLERKQRLLRaqelLQRLGLEDRVEYQP-SQLSGGQQQRVSIARALMNGGQVILADEPTGALDShsgEEVMAILHQLR 191
|
170
....*....|..
gi 29789050 655 NFRGGVILVSHD 666
Cdd:PRK10535 192 DRGHTVIIVTHD 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
179-666 |
8.81e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 8.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTRSLRVPAHiSLLHVEQEVAGDDTPALQSVLESd 258
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVL-TGIYTRDAG-SILYLGKEVTFNGPKSSQEAGIG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 259 tvredLLRQEREL--SLRIAA----GRaegseaaqlaEIYGKLEEIEADKAPARASVILAGLGFTPKmQQQPTREFSGGW 332
Cdd:PRK10762 83 -----IIHQELNLipQLTIAEniflGR----------EFVNRFGRIDWKKMYAEADKLLARLNLRFS-SDKLVGELSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 333 RMRLALARALFARPDLLLLDEPTNML---DVRAILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHsqrlDGyrgdf 409
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFR----DG----- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 410 eTFIKSKQERLLNQQReyeaqqqyrqHIQVFIDRfrynanrasqvqsklkmleKLPELKP-VDKE-SEVVLKFpdgfEKF 487
Cdd:PRK10762 218 -QFIAEREVADLTEDS----------LIEMMVGR-------------------KLEDQYPrLDKApGEVRLKV----DNL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 488 SPPilQLDEVDFYYDpKHSIfsrLSVSadlesricvvGENGAGKSTMLKLLMGDLSPVRG----------IRHAHRNLK- 556
Cdd:PRK10762 264 SGP--GVNDVSFTLR-KGEI---LGVS----------GLMGAGRTELMKVLYGALPRTSGyvtldghevvTRSPQDGLAn 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 557 -IGYFSQHHVEQ---LDLNV------SAVELLARKFPGLPEEEYRHQLGRY----GISGELAMRPVASLSGGQKSRVAFA 622
Cdd:PRK10762 328 gIVYISEDRKRDglvLGMSVkenmslTALRYFSRAGGSLKHADEQQAVSDFirlfNIKTPSMEQAIGLLSGGNQQKVAIA 407
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 29789050 623 QMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG---GVILVSHD 666
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglSIILVSSE 454
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
611-703 |
1.23e-04 |
|
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: 45.18 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 611 LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETI----EALGQALNNFRGGVILVSHDERFI-RLVCKELWVcENGSV 685
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIeDLSDKAIWL-ENGEI 247
|
90
....*....|....*...
gi 29789050 686 TRvEGGFDQYRALLQEQF 703
Cdd:TIGR03269 248 KE-EGTPDEVVAVFMEGV 264
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
178-361 |
1.25e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 178 VRIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLA---------------TRSLRVPAH-----ISLL 237
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSgvyqpdsgeilldgePVRFRSPRDaqaagIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 238 HveQEVagddtpalqSVLESDTVREDL-LRQERELSLRIAAGRAEgSEAAQLaeiygkLEEIEADKAPARasvILAGLGF 316
Cdd:COG1129 85 H--QEL---------NLVPNLSVAENIfLGREPRRGGLIDWRAMR-RRAREL------LARLGLDIDPDT---PVGDLSV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 317 TpkmQQQptrefsggwrMrLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:COG1129 144 A---QQQ----------L-VEIARALSRDARVLILDEPTASLTER 174
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
203-396 |
1.26e-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: 44.28 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 203 GRRYGLVGRNGLGKTTLLKMLATRslRVPahiSLLHVEQEVAGDDT------PALQSVLESdtVREDLLR-----QEREL 271
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGK--LKP---NLGKFDDPPDWDEIldefrgSELQNYFTK--LLEGDVKvivkpQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 272 SLRIAAGRAEgsEAAQLAEIYGKLEEIeadkaparasviLAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLL 351
Cdd:cd03236 99 IPKAVKGKVG--ELLKKKDERGKLDEL------------VDQLELRHVLDRN-IDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 29789050 352 DEPTNMLDVR-----AILWLEnyLQTWPSTILVVSHDRNFLNAIAtDIIH 396
Cdd:cd03236 164 DEPSSYLDIKqrlnaARLIRE--LAEDDNYVLVVEHDLAVLDYLS-DYIH 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
491-666 |
1.31e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 44.31 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSP------VRGIRHAHRNLKIGYFSQHH 564
Cdd:PRK11248 1 MLQISHLYADYGGK-PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYqhgsitLDGKPVEGPGAERGVVFQNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 565 VEQLDLNVSAVELLARKFPGLPEEEYRHQ----LGRYGISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNH 640
Cdd:PRK11248 80 GLLPWRNVQDNVAFGLQLAGVEKMQRLEIahqmLKKVGLEG-AEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|
gi 29789050 641 LDMETIEALGQAL----NNFRGGVILVSHD 666
Cdd:PRK11248 159 LDAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
175-420 |
1.50e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.23 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 175 SYDVRIENFDVSFGDRV-----LLAGADVNLAWGRRYGLVGRNGLGKTTLLKMlaTRSLRVPahisllHVEQEVAGD-DT 248
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL--TNGLIIS------ETGQTIVGDyAI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 249 PA-LQSVLESDTVRED--LLRQERELSL-------RIAAGRAEGSEAAQlaEIYGKLEEIeadkaparasviLAGLGFTP 318
Cdd:PRK13645 76 PAnLKKIKEVKRLRKEigLVFQFPEYQLfqetiekDIAFGPVNLGENKQ--EAYKKVPEL------------LKLVQLPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 319 KMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVSHDRNFLNAIATDI 394
Cdd:PRK13645 142 DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGeedfINLFERLNKEYKKRIIMVTHNMDQVLRIADEV 221
|
250 260
....*....|....*....|....*.
gi 29789050 395 IHLHSQRLDGYRGDFETFikSKQERL 420
Cdd:PRK13645 222 IVMHEGKVISIGSPFEIF--SNQELL 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
329-354 |
1.59e-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: 1.59e-04
10 20
....*....|....*....|....*.
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEP 354
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDP 154
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
385-666 |
1.59e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.30 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 385 NFLNAIAtdiiHLHSQRLDGYRGDFETFIKSKQERLLNQQREYEAQQQYRQHIQVFID---RFRYNANRASQVQSKLKML 461
Cdd:pfam13304 14 NLLEALR----FLADFDALVIGLTDERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEdgvRYRYGLDLEREDVEEKLSS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 462 EKLPELKPVDKESEVVLKFPDGFEKFSPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENgagkSTMLKLLMGD 541
Cdd:pfam13304 90 KPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLL----LLDEGLLLED 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 542 LSPVRGIRHAHRNLKIGYFSQHHVEQLDLNVSAVELL--ARKFPGLPEEEYRHQLGRYGISGELAMRPVASLSGGQKSRV 619
Cdd:pfam13304 166 WAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLgeGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 29789050 620 AFA---QMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVSHD 666
Cdd:pfam13304 246 ALLaalLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNgaqLILTTHS 298
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
301-361 |
1.69e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 44.24 E-value: 1.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 301 DKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PRK13634 119 EDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
486-654 |
1.69e-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: 44.81 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 486 KFSPPILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMGDLSPVRG-IRHAHRNLKigyfsqhH 564
Cdd:COG5265 352 VVGGGEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGrILIDGQDIR-------D 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 565 VEQLDL--------------NVSAVELLARKFPGLPEEEYRH-----QLGRYGIS---------GELAMRpvasLSGGQK 616
Cdd:COG5265 425 VTQASLraaigivpqdtvlfNDTIAYNIAYGRPDASEEEVEAaaraaQIHDFIESlpdgydtrvGERGLK----LSGGEK 500
|
170 180 190
....*....|....*....|....*....|....*...
gi 29789050 617 SRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALN 654
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALR 538
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
329-359 |
1.78e-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: 1.78e-04
10 20 30
....*....|....*....|....*....|.
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:TIGR04520 138 SGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
197-382 |
1.79e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 43.42 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 197 DVNLAWGRRYGLVGRNGLGKTTLLKMLAtrSLRVPAHISLLhveqeVAGDD----TPALQSVlesdtvreDLLRQER--- 269
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIA--GFLTPASGSLT-----LNGQDhtttPPSRRPV--------SMLFQENnlf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 270 -ELSLR--IAAG-----RAEGSEAAQLAEIYGKLeeieadkaparasvilaglGFTPKMQQQPTrEFSGGWRMRLALARA 341
Cdd:PRK10771 84 sHLTVAqnIGLGlnpglKLNAAQREKLHAIARQM-------------------GIEDLLARLPG-QLSGGQRQRVALARC 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 342 LFARPDLLLLDEPTNMLD--VRA-ILWL-ENYLQTWPSTILVVSH 382
Cdd:PRK10771 144 LVREQPILLLDEPFSALDpaLRQeMLTLvSQVCQERQLTLLMVSH 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
298-360 |
1.83e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 298 IEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:PRK10261 434 LPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
440-664 |
2.39e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.41 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 440 FID------RFRYNANRASQVQSKLKMLEKLPELKPVDKESEvvlkfpdgfekfsPPILQLDEVDFYYDPKHSIFSRLSV 513
Cdd:COG4178 318 FVDnyqslaEWRATVDRLAGFEEALEAADALPEAASRIETSE-------------DGALALEDLTLRTPDGRPLLEDLSL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 514 SADLESRICVVGENGAGKSTMLKLLMGdLSP-VRGIRHAHRNLKIGYFSQH-HVEQLDLnvsaVELLArkFPGLPE---- 587
Cdd:COG4178 385 SLKPGERLLITGPSGSGKSTLLRAIAG-LWPyGSGRIARPAGARVLFLPQRpYLPLGTL----REALL--YPATAEafsd 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 588 EEYRHQLGRYGIsGELAMRP--VAS----LSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGVI 661
Cdd:COG4178 458 AELREALEAVGL-GHLAERLdeEADwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTT 536
|
...
gi 29789050 662 LVS 664
Cdd:COG4178 537 VIS 539
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
518-665 |
2.42e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 44.62 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 518 ESRICV-VGENGAGKSTMLKLLMGDLSPVRGI-----RHAHRNL-----KIGYFSQHHVEQLDLNVSAVELLARKFPGLP 586
Cdd:TIGR01257 955 ENQITAfLGHNGAGKTTTLSILTGLLPPTSGTvlvggKDIETNLdavrqSLGMCPQHNILFHHLTVAEHILFYAQLKGRS 1034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYRHQL-------GRYGISGELAMrpvaSLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG 659
Cdd:TIGR01257 1035 WEEAQLEMeamledtGLHHKRNEEAQ----DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
....*...
gi 29789050 660 --VILVSH 665
Cdd:TIGR01257 1111 rtIIMSTH 1118
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
574-666 |
2.59e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 44.29 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 574 AVELLARKfpGLPEEEYR-----HQLgrygisgelamrpvaslSGGQKSRVAFAqMTMPC-PNFYILDEPTNHLDMeTIE 647
Cdd:COG4172 134 ALELLERV--GIPDPERRldaypHQL-----------------SGGQRQRVMIA-MALANePDLLIADEPTTALDV-TVQ 192
|
90 100
....*....|....*....|....
gi 29789050 648 A----LGQALNNFRG-GVILVSHD 666
Cdd:COG4172 193 AqildLLKDLQRELGmALLLITHD 216
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
510-687 |
2.63e-04 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 43.94 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 510 RLSVSADLESR-ICVV-GENGAGKSTMLKLLMGDLSPVRG-IR---------HAHRNLK-----IGYFSQH-----Hveq 567
Cdd:COG4148 15 TLDVDFTLPGRgVTALfGPSGSGKTTLLRAIAGLERPDSGrIRlggevlqdsARGIFLPphrrrIGYVFQEarlfpH--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 568 ldLNVSAVELLARKFpgLPEEEYRHQLGR----YGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDM 643
Cdd:COG4148 92 --LSVRGNLLYGRKR--APRAERRISFDEvvelLGIGHLLDRRP-ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 644 ET-------IEALGQALNnfrGGVILVSHDERFIRLVCKELWVCENGSVTR 687
Cdd:COG4148 167 ARkaeilpyLERLRDELD---IPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
523-668 |
3.35e-04 |
|
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: 43.25 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG----------IRHAHRNlKIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEE--- 589
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGsimldgedvtNVPPHLR-HINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEikp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 590 -YRHQLGRYGIsGELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNF--RGGV--ILVS 664
Cdd:TIGR01187 80 rVLEALRLVQL-EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIqeQLGItfVFVT 158
|
....
gi 29789050 665 HDER 668
Cdd:TIGR01187 159 HDQE 162
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
525-667 |
3.45e-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: 42.61 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSPVRG-IRHAHRNL--------KIGYFSQHHVEQLDLNVSAVELLARKFPGLPEEEYRHQLG 595
Cdd:cd03300 33 GPSGCGKTTLLRLIAGFETPTSGeILLDGKDItnlpphkrPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 596 RY----GISGeLAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGGV----ILVSHDE 667
Cdd:cd03300 113 EAldlvQLEG-YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHDQ 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
208-402 |
3.61e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.28 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 208 LVGRNGLGKTTLlkMLATRSLRVPAHISLlhveqEVAGDDtpalqsvLESDTVREDLLRQERELSLRIAAGRAEGSEAAQ 287
Cdd:PRK13641 38 LVGHTGSGKSTL--MQHFNALLKPSSGTI-----TIAGYH-------ITPETGNKNLKKLRKKVSLVFQFPEAQLFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 288 LAEI-YGKLE-EIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILW 365
Cdd:PRK13641 104 LKDVeFGPKNfGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 29789050 366 L----ENYlQTWPSTILVVSHDRNFLNAIATDIIHLHSQRL 402
Cdd:PRK13641 184 MmqlfKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
193-401 |
3.69e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.80 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKML-----ATR-SLRVPAHISLLHVEQEVAG---------DDTpalqsvLES 257
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLngiylPQRgRVKVMGREVNAENEKWVRSkvglvfqdpDDQ------VFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 258 DTVREDLLRQERELSLRiaagraegseaaqlaeiygkLEEIEAdkapaRASVILAGLGFTpKMQQQPTREFSGGWRMRLA 337
Cdd:PRK13647 95 STVWDDVAFGPVNMGLD--------------------KDEVER-----RVEEALKAVRMW-DFRDKPPYHLSYGQKKRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 338 LARALFARPDLLLLDEPTNMLD------VRAILWLenyLQTWPSTILVVSHDRNFLNAIATDIIHLHSQR 401
Cdd:PRK13647 149 IAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDR---LHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
181-383 |
3.79e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 42.57 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 181 ENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATRSLRVPAHIsllhveqeVAGDDTPALQSVLESDTV 260
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI--------IIDDEDISLLPLHARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 261 REDLLRQERELSLRIaagraegSEAAQLAEIYGKLEEIEADKAPARASVILAGLGFTpKMQQQPTREFSGGWRMRLALAR 340
Cdd:PRK10895 79 GIGYLPQEASIFRRL-------SVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789050 341 ALFARPDLLLLDE------PTNMLDVRAILwleNYLQTWPSTILVVSHD 383
Cdd:PRK10895 151 ALAANPKFILLDEpfagvdPISVIDIKRII---EHLRDSGLGVLITDHN 196
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
605-642 |
4.60e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 4.60e-04
10 20 30
....*....|....*....|....*....|....*...
gi 29789050 605 MRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD 642
Cdd:PRK13549 400 ELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
606-672 |
4.61e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789050 606 RPVASLSGGQKSRVAFAQ--------MTmpcpnfYILDEPTNHLDMETIEALGQALNNFR---GGVILVSHDERFIRL 672
Cdd:PRK00635 472 RALATLSGGEQERTALAKhlgaeligIT------YILDEPSIGLHPQDTHKLINVIKKLRdqgNTVLLVEHDEQMISL 543
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
521-651 |
4.99e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 42.69 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 521 ICVVGENGAGKSTMLK----LLMGDLSP-----------------VRGIRHAHRNlkIGYFSQHH--VEQLDL--NVSAV 575
Cdd:PRK09984 33 VALLGPSGSGKSTLLRhlsgLITGDKSAgshiellgrtvqregrlARDIRKSRAN--TGYIFQQFnlVNRLSVleNVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 576 EL--------LARKFPGLPEEEYRHQLGRYGISgELAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----- 642
Cdd:PRK09984 111 ALgstpfwrtCFSWFTREQKQRALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDpesar 189
|
170
....*....|.
gi 29789050 643 --METIEALGQ 651
Cdd:PRK09984 190 ivMDTLRDINQ 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
177-361 |
5.07e-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: 42.21 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 177 DVRIENfdVSFG---DRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLaTR----------------------SLRvp 231
Cdd:cd03254 2 EIEFEN--VNFSydeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLL-MRfydpqkgqilidgidirdisrkSLR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 232 AHISLlhVEQEvagddtpalqSVLESDTVREDllrqerelslrIAAGRAEGSEAaqlaeiygklEEIEADKApARASVIL 311
Cdd:cd03254 77 SMIGV--VLQD----------TFLFSGTIMEN-----------IRLGRPNATDE----------EVIEAAKE-AGAHDFI 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789050 312 AGLgftPKMQQQPTRE----FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:cd03254 123 MKL---PNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
485-667 |
5.22e-04 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 42.90 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 485 EKFSPPILQLDEVDFYYDPKHSIfSRLSVSADLESRICVVGENGAGKSTMLKLLMG--------------DLSPV----R 546
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfeqptagqimldgvDLSHVppyqR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 547 GIRHAHRNLKIgyFSQHHVEQldlNVSavelLARKFPGLPEEEYRHQ----LGRYGISgELAMRPVASLSGGQKSRVAFA 622
Cdd:PRK11607 92 PINMMFQSYAL--FPHMTVEQ---NIA----FGLKQDKLPKAEIASRvnemLGLVHMQ-EFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 623 QMTMPCPNFYILDEPTNHLD--------METIEALGqalnnfRGGV--ILVSHDE 667
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDkklrdrmqLEVVDILE------RVGVtcVMVTHDQ 210
|
|
| 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 29789050 326 REFSGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
323-362 |
6.03e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 6.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 29789050 323 QPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA 362
Cdd:NF040905 400 QKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGA 439
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
296-394 |
6.14e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 296 EEIEADKAPARASVILAGLgftpkmQQQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLD---VRAILWLENYLQT 372
Cdd:PRK13639 112 EEVEKRVKEALKAVGMEGF------ENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNK 185
|
90 100
....*....|....*....|..
gi 29789050 373 WPSTILVVSHDRNFLNAIATDI 394
Cdd:PRK13639 186 EGITIIISTHDVDLVPVYADKV 207
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
491-649 |
6.28e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 42.28 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 491 ILQLDEVDFYYDPKHSIFSRLSVSADLESRICVVGENGAGKSTML------------KLLM-----GDLSPVRGIRH--- 550
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLAlhlngllrpqkgKVLVsgidtGDFSKLQGIRKlvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 551 -AHRNLKIGYFSQHHVEQL-----DLNVSAVELLARKFPGLPE---EEYRHqlgrygisgelamRPVASLSGGQKSRVAF 621
Cdd:PRK13644 81 iVFQNPETQFVGRTVEEDLafgpeNLCLPPIEIRKRVDRALAEiglEKYRH-------------RSPKTLSGGQGQCVAL 147
|
170 180
....*....|....*....|....*...
gi 29789050 622 AQMTMPCPNFYILDEPTNHLDMETIEAL 649
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
193-382 |
6.38e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 42.42 E-value: 6.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 193 LAGADVNLAWGRRYGLVGRNGLGKTTLLKMLatRSLRVPAhisllhvEQEVAGDDTpalqsVLESDTVREDLLRQERELS 272
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLL--NGLHVPT-------QGSVRVDDT-----LITSTSKNKDIKQIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 273 LRIAAGRAEGSEAAQLAEI------YGkleeIEADKAPARASVILAGLGFTPKMQQQPTREFSGGWRMRLALARALFARP 346
Cdd:PRK13649 89 LVFQFPESQLFEETVLKDVafgpqnFG----VSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 29789050 347 DLLLLDEPTNMLDV---RAILWLENYLQTWPSTILVVSH 382
Cdd:PRK13649 165 KILVLDEPTAGLDPkgrKELMTLFKKLHQSGMTIVLVTH 203
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
180-424 |
7.31e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR--------SLRVPAHISLLHVEQEVAGDDT-PA 250
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedyevtggTVEFKGKDLLELSPEDRAGEGIfMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 251 LQSVLESDTVREDLLRQERELSLRiaagRAEGSEAAQLAEIYGKLEE-IEADKAPARASVILAGLGFtpkmqqqptrefS 329
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQTALNAVR----SYRGQEPLDRFDFQDLMEEkIALLKMPEDLLTRSVNVGF------------S 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 330 GGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLE---NYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQRLDGYR 406
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKS 227
|
250 260
....*....|....*....|..
gi 29789050 407 GDFeTFIKSKQER----LLNQQ 424
Cdd:PRK09580 228 GDF-TLVKQLEEQgygwLTEQQ 248
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
208-359 |
7.43e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 42.73 E-value: 7.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 208 LVGRNGLGKTTLLKMLATRSLR------------VPAHISLLH-----VEQevagDD--TPALqsvlesdTVREDLLRQE 268
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKgvkgsgsvllngMPIDAKEMRaisayVQQ----DDlfIPTL-------TVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 269 RelsLRIAagraegseaaqlaeiygklEEIEADKAPARASVILAGLGFTPKMQ---QQPTRE--FSGGWRMRLALARALF 343
Cdd:TIGR00955 125 H---LRMP-------------------RRVTKKEKRERVDEVLQALGLRKCANtriGVPGRVkgLSGGERKRLAFASELL 182
|
170
....*....|....*.
gi 29789050 344 ARPDLLLLDEPTNMLD 359
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLD 198
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
523-688 |
8.12e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 42.33 E-value: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG----------------IRHAHRNlKIGYFSQHHVEQLDLNVSAVELLARKFPGLP 586
Cdd:PRK10070 59 IMGLSGSGKSTMVRLLNRLIEPTRGqvlidgvdiakisdaeLREVRRK-KIAMVFQSFALMPHMTVLDNTAFGMELAGIN 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD----METIEALGQALNNFRG 658
Cdd:PRK10070 138 AEERREKaldaLRQVGLENYAHSYP-DELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQR 216
|
170 180 190
....*....|....*....|....*....|
gi 29789050 659 GVILVSHDERFIRLVCKELWVCENGSVTRV 688
Cdd:PRK10070 217 TIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
528-666 |
8.80e-04 |
|
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: 40.88 E-value: 8.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 528 GAGKSTMLKLLMGDLSPVRG-IR-----------HAHRNLKIGYfsqhhveqldlnvsavellarkfpgLPEEeyRHQLG 595
Cdd:cd03215 36 GNGQTELAEALFGLRPPASGeITldgkpvtrrspRDAIRAGIAY-------------------------VPED--RKREG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789050 596 ---RYGISGELAMRpvASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFR---GGVILVSHD 666
Cdd:cd03215 89 lvlDLSVAENIALS--SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAdagKAVLLISSE 163
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
180-223 |
1.00e-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: 1.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 29789050 180 IENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKML 223
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII 47
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
327-419 |
1.01e-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: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAIL----WLENYLQTWPSTILVVSHDRNFLNAIAtDIIHLhsqrL 402
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLnaarAIRRLSEEGKKTALVVEHDLAVLDYLS-DRIHV----F 145
|
90
....*....|....*..
gi 29789050 403 DGYRGDFETFIKSKQER 419
Cdd:cd03222 146 EGEPGVYGIASQPKGTR 162
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
310-402 |
1.08e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.71 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 310 ILAGLGFTPKMQQQPTrEFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPS-TILVVSHDRN 385
Cdd:PRK13640 127 VLADVGMLDYIDSEPA-NLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGkeqILKLIRKLKKKNNlTVISITHDID 205
|
90
....*....|....*..
gi 29789050 386 FLNaIATDIIHLHSQRL 402
Cdd:PRK13640 206 EAN-MADQVLVLDDGKL 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
524-692 |
1.64e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.53 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLLMGDLS-----------PVR------------GIRHAHRNLkIGyfsqhhveqlDLNVSAVELLAR 580
Cdd:PRK10762 36 VGENGAGKSTMMKVLTGIYTrdagsilylgkEVTfngpkssqeagiGIIHQELNL-IP----------QLTIAENIFLGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 581 KFPG-----LPEEEYRHQ---LGRYGISGElAMRPVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHL-DMETiEALGQ 651
Cdd:PRK10762 105 EFVNrfgriDWKKMYAEAdklLARLNLRFS-SDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET-ESLFR 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 29789050 652 ALNNFRG---GVILVSHderfiRLvcKELW-VCENGSVTRvEGGF 692
Cdd:PRK10762 183 VIRELKSqgrGIVYISH-----RL--KEIFeICDDVTVFR-DGQF 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
329-359 |
1.72e-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: 1.72e-03
10 20 30
....*....|....*....|....*....|.
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
179-366 |
1.81e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 41.40 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 179 RIENFDVSFGDRVLLAGADVNLAWGRRYGLVGRNGLGKTTLLKMLATR------------SLRVPAHiSLLHVEQEVAGD 246
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqgnnftgtilaNNRKPTK-QILKRTGFVTQD 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 247 DT--PALqsvlesdTVRE-----DLLRQERELSlriaagRAEGSEAAqlaeiygklEEIEADKAPARASVILAGLGFTpk 319
Cdd:PLN03211 149 DIlyPHL-------TVREtlvfcSLLRLPKSLT------KQEKILVA---------ESVISELGLTKCENTIIGNSFI-- 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 29789050 320 mqqqptREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWL 366
Cdd:PLN03211 205 ------RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
|
| 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 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
606-653 |
1.88e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.88e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 29789050 606 RPVASLSGGQKSRVAFA-QMTMPC--PNFYILDEPTNHLDMETIEALGQAL 653
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAyELLAPSkkPTLYVLDEPTTGLHTHDIKALIYVL 855
|
|
| 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 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR--------AILwleNYLQTWPSTILVVSHDRNFL 387
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlmqeGIL---KFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
486-685 |
2.14e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 40.42 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 486 KFSPPILQLDEVDFYYDPKhSIFSRLSVSADLESRICVVGENGAGKSTMLKLLMgdlspvRGIRHAHRNLKIG----YFS 561
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDK-AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLN------RLIEIYDSKIKVDgkvlYFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 562 QHHVE----QLDLNVSAVELLARKFPGLP-EEEYRHQLGRYGISGELAMR----------------------PVASLSGG 614
Cdd:PRK14246 78 KDIFQidaiKLRKEVGMVFQQPNPFPHLSiYDNIAYPLKSHGIKEKREIKkiveeclrkvglwkevydrlnsPASQLSGG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 29789050 615 QKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRG--GVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| 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 29789050 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 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
607-666 |
3.00e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 3.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 607 PVASLSGGQKSRVAFAQMTMpcpnfYILDepTNHLDMETIEALGQALNNFRggviLVSHD 666
Cdd:COG0419 155 PIETLSGGERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA----IITHV 203
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
329-359 |
3.08e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 40.07 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|.
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLD 359
Cdd:PRK13633 146 SGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
610-685 |
3.10e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 39.88 E-value: 3.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 610 SLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD---METIEALGQALNNFRGGVILVSHDERFIRLVCKELWVCENGSV 685
Cdd:PRK10895 137 SLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
524-667 |
3.12e-03 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 40.40 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 524 VGENGAGKSTMLKLL-----------------MGDLSPvrgirhAHRNlkIGYFSQHHVEQLDLNVSAVELLARKFPGLP 586
Cdd:PRK11000 35 VGPSGCGKSTLLRMIagleditsgdlfigekrMNDVPP------AERG--VGMVFQSYALYPHLSVAENMSFGLKLAGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 587 EEEYRH---------QLGRYgisgeLAMRPVAsLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLD------MET-IEALG 650
Cdd:PRK11000 107 KEEINQrvnqvaevlQLAHL-----LDRKPKA-LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrvqMRIeISRLH 180
|
170
....*....|....*..
gi 29789050 651 QALNNfrgGVILVSHDE 667
Cdd:PRK11000 181 KRLGR---TMIYVTHDQ 194
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
329-383 |
3.20e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 40.12 E-value: 3.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQ-TWPSTILVVSHD 383
Cdd:PRK13648 144 SGGQKQRVAIAGVLALNPSVIILDEATSMLDPDArqnLLDLVRKVKsEHNITIISITHD 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
324-404 |
3.41e-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: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 324 PTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA---ILWLENYLQTWPSTILVVSHDRNFLNAIATDIIHLHSQ 400
Cdd:TIGR02633 400 PIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
....
gi 29789050 401 RLDG 404
Cdd:TIGR02633 480 KLKG 483
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
609-654 |
3.42e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 40.77 E-value: 3.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 29789050 609 ASLSGGQKSRVAFAQMTM-PCPnFYILDEPTNHLDMETIEALGQALN 654
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLrDSP-ILILDEATSALDTESERAIQAALD 524
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
612-666 |
3.60e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.09 E-value: 3.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 612 SGGQKSRVAFAqMTMPC-PNFYILDEPTNHLDMeTIEA-----LGQALNNFRGGVILVSHD 666
Cdd:PRK09473 163 SGGMRQRVMIA-MALLCrPKLLIADEPTTALDV-TVQAqimtlLNELKREFNTAIIMITHD 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
308-387 |
3.84e-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: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 308 SVILAGLGFTPKMQQQPTreFSGGWRMRLALARALFARPD--LLLLDEPTNMLDVRAILWLENYLQTW---PSTILVVSH 382
Cdd:cd03238 70 FLIDVGLGYLTLGQKLST--LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLidlGNTVILIEH 147
|
....*
gi 29789050 383 DRNFL 387
Cdd:cd03238 148 NLDVL 152
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
208-383 |
4.07e-03 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 39.87 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 208 LVGRNGLGKTTLLKMLAtrslrvpAHISLLHVEQEVAGDDTpalQSVLESDTVREDLLRQERELSLRIAAgraegsEAAQ 287
Cdd:PRK15056 38 LVGVNGSGKSTLFKALM-------GFVRLASGKISILGQPT---RQALQKNLVAYVPQSEEVDWSFPVLV------EDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 288 LAEIYGKLEEIEADKAPARASV--ILAGLGFTPKMQQQpTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA--- 362
Cdd:PRK15056 102 MMGRYGHMGWLRRAKKRDRQIVtaALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTear 180
|
170 180
....*....|....*....|.
gi 29789050 363 ILWLENYLQTWPSTILVVSHD 383
Cdd:PRK15056 181 IISLLRELRDEGKTMLVSTHN 201
|
|
| 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 29789050 328 FSGGWRMRLALARALFARPDLLLLDEPTNMLDVR 361
Cdd:PLN03130 1375 FSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
327-383 |
4.45e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 4.45e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 327 EFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAILWLENYLQTWPS----TILVVSHD 383
Cdd:PRK10070 164 ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAkhqrTIVFISHD 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
329-360 |
4.58e-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: 39.45 E-value: 4.58e-03
10 20 30
....*....|....*....|....*....|..
gi 29789050 329 SGGWRMRLALARALFARPDLLLLDEPTNMLDV 360
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
606-672 |
5.04e-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: 39.16 E-value: 5.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789050 606 RPVASLSGGQKSRVAFA-QMTMPCPN-FYILDEPT-------NHLDMETIEALGQALNNfrggVILVSHDERFIRL 672
Cdd:cd03270 133 RSAPTLSGGEAQRIRLAtQIGSGLTGvLYVLDEPSiglhprdNDRLIETLKRLRDLGNT----VLVVEHDEDTIRA 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
612-670 |
5.36e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 5.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 612 SGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMETIEALGQALNNFRGG---VILVSHDERFI 670
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkrsFIIVTHYQRIL 208
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
607-665 |
5.40e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 39.13 E-value: 5.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 607 PVASLSGGQKSRVAFAQMTMPCPNFYILDEPTNHLDMET---IEALGQALNNfRGGVILVSH 665
Cdd:PRK14247 143 PAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
611-667 |
5.97e-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: 39.20 E-value: 5.97e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789050 611 LSGGQKSRVAFAQ-MTM----PCPnFYILDEPTNHLDMETIEALGQAL-NNFRGG-VILVSHDE 667
Cdd:cd03273 167 LSGGQRSLVALSLiLALllfkPAP-MYILDEVDAALDLSHTQNIGRMIkTHFKGSqFIVVSLKE 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
306-425 |
6.15e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 39.02 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 306 RASVILAGLGFTPKMQQQPtREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRA----ILWLENYLQTWPSTILVVS 381
Cdd:PRK13652 117 RVSSALHMLGLEELRDRVP-HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFST 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 29789050 382 HDRNFLNAIATDIIHLHSQRLDGYRGDFETFIkskQERLLNQQR 425
Cdd:PRK13652 196 HQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL---QPDLLARVH 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
525-638 |
6.50e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 39.72 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 525 GENGAGKSTMLKLLMGDLSPVRG---------------IRHahrnlKIGYFSQHH-------VEQ-LDLNvsavellARK 581
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGeawlfgqpvdagdiaTRR-----RVGYMSQAFslygeltVRQnLELH-------ARL 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 582 FpGLPEEEYRHQ----LGRYGISGELAMRPvASLSGGQKSRVAFAQMTMPCPNFYILDEPT 638
Cdd:NF033858 367 F-HLPAAEIAARvaemLERFDLADVADALP-DSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
523-547 |
6.93e-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: 39.78 E-value: 6.93e-03
10 20
....*....|....*....|....*
gi 29789050 523 VVGENGAGKSTMLKLLMGDLSPVRG 547
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESG 387
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
605-670 |
8.65e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 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: 213239 [Multi-domain] Cd Length: 243 Bit Score: 38.40 E-value: 8.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789050 605 MRPVASLSGGQKSRVAFA-----QMTMPCPnFYILDEPTNHLDMETIEALGQALNNfrggvilVSHDERFI 670
Cdd:cd03272 153 QQEMQQLSGGQKSLVALAlifaiQKCDPAP-FYLFDEIDAALDAQYRTAVANMIKE-------LSDGAQFI 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-363 |
9.28e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 39.24 E-value: 9.28e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 29789050 322 QQPTREFSGGWRMRLALARALFARPDLLLLDEPTNMLDVRAI 363
Cdd:COG3845 397 DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAI 438
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
329-383 |
9.53e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789050 329 SGGWRM------RLALARALFARPDLLLLDEPTNMLD----VRAILWLENYLQTWPSTIlVVSHD 383
Cdd:PRK03918 790 SGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQVI-IVSHD 853
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
184-385 |
9.60e-03 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 38.28 E-value: 9.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 184 DVSFGDRVLLAGADVNLawGRRYGLVGRNGLGKTTLLKMLAtrslrvpahiSLLHVEQEVAGDDTPALQSVLESDTVRED 263
Cdd:COG4138 5 DVAVAGRLGPISAQVNA--GELIHLIGPNGAGKSTLLARMA----------GLLPGQGEILLNGRPLSDWSAAELARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789050 264 LLRQERE----------LSLRIAAGRAEGSEAAQLAEIYGKLeeieadkaparasvilaglGFTPKMQQqPTREFSGG-W 332
Cdd:COG4138 73 YLSQQQSppfampvfqyLALHQPAGASSEAVEQLLAQLAEAL-------------------GLEDKLSR-PLTQLSGGeW 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789050 333 -RMRLALA-----RALFARPDLLLLDEPTNMLDVR---AILWLENYLQTWPSTILVVSHDRN 385
Cdd:COG4138 133 qRVRLAAVllqvwPTINPEGQLLLLDEPMNSLDVAqqaALDRLLRELCQQGITVVMSSHDLN 194
|
|
| |
