|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-528 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 649.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHMTVFE 87
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 AVLSSDTPTLRIIKKYEEAVNryALDQSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIHDT--TKKIVELSGGQQ 165
Cdd:COG0488 81 TVLDGDAELRALEAELEELEA--KLAEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEdlDRPVSELSGGWR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYEDYI 245
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 246 VMRAENELVEQKQQEKQKALYKQELAWM-RAGAKARTTKQ-QARINRFNQLESDVKtQHTQDKGELNL-AYSRLGKQVYE 322
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAKEEEFIrRFRAKARKAKQaQSRIKALEKLEREEP-PRRDKTVEIRFpPPERLGKKVLE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDRDIRVI 402
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPDKTVL 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYLREESEmakekDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILE 482
Cdd:COG0488 398 DELRDGAP-----GGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1842088001 483 DYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFEDYE 528
Cdd:COG0488 473 EALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYL 518
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-532 |
1.99e-148 |
|
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: 440.53 E-value: 1.99e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 6 YKIEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHMT 84
Cdd:TIGR03719 5 YTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLSSDTPTLRIIKKYEEAVNRYALDQSDSN--FNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIHDTTKKIVELSG 162
Cdd:TIGR03719 85 VRENVEEGVAEIKDALDRFNEISAKYAEPDADFDklAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYE 242
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 243 DYIVMRAENELVEQKQQEK-QKALyKQELAWMRAGAKARTTKQQARINRFNQLESdvktQHTQDKGELNLAY----SRLG 317
Cdd:TIGR03719 245 SWLEQKQKRLEQEEKEESArQKTL-KRELEWVRQSPKGRQAKSKARLARYEELLS----QEFQKRNETAEIYippgPRLG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDR 397
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 DIRVIDYLREESEMAKeKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:TIGR03719 400 NKTVWEEISGGLDIIK-LGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 478 LTILEDYIDDFGGSVITVSHDRYFLNKVVQEYW-FIHDGKIEKIIGSFEDYESFKK 532
Cdd:TIGR03719 479 LRALEEALLNFAGCAVVISHDRWFLDRIATHILaFEGDSHVEWFEGNFSEYEEDKK 534
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-533 |
2.01e-146 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 435.70 E-value: 2.01e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 6 YKIEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHMT 84
Cdd:PRK11819 7 YTMNRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLSSDTPTLRIIKKYEEAVNRYALDQSDSN--FNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIHDTTKKIVELSG 162
Cdd:PRK11819 87 VRENVEEGVAEVKAALDRFNEIYAAYAEPDADFDalAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPWDAKVTKLSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYE 242
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 243 DYIVMRAENELVEQKQQEK-QKALyKQELAWMRAGAKARTTKQQARINRFNQLESdvktQHTQDKGELNLAY----SRLG 317
Cdd:PRK11819 247 SWLEQKAKRLAQEEKQEAArQKAL-KRELEWVRQSPKARQAKSKARLARYEELLS----EEYQKRNETNEIFippgPRLG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDR 397
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDP 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 DIRVIDYLREESEMAKEKdGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVG-NREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 478 LTILEDYIDDFGGSVITVSHDRYFLNKVVQeywfiH------DGKIEKIIGSFEDYESFKKE 533
Cdd:PRK11819 481 LRALEEALLEFPGCAVVISHDRWFLDRIAT-----HilafegDSQVEWFEGNFQEYEEDKKR 537
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-628 |
2.94e-140 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 422.44 E-value: 2.94e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG---LDE---DFTADIThpnqyrirYSSQKQDLNGHM--TV 85
Cdd:PRK11147 12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDgriIYEQDLI--------VARLQQDPPRNVegTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTPTLRIIKKYEEAVNRYALDQSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIhDTTKKIVELSGGQQ 165
Cdd:PRK11147 84 YDFVAEGIEEQAEYLKRYHDISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGL-DPDAALSSLSGGWL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYEDYI 245
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 246 VMRAENELVEQKQQEKQKALYKQELAWMRAGAKARTTKQQARINRFNQLESDvKTQHTQDKGELNLAY---SRLGKQVYE 322
Cdd:PRK11147 243 LEKEEALRVEELQNAEFDRKLAQEEVWIRQGIKARRTRNEGRVRALKALRRE-RSERREVMGTAKMQVeeaSRSGKIVFE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDRDIRVI 402
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAELDPEKTVM 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYLRE-ESEMakEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTIL 481
Cdd:PRK11147 402 DNLAEgKQEV--MVNGRPRHVLGYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 482 EDYIDDFGGSVITVSHDRYFLNKVVQE-YWFIHDGKIEKIIGSFEDYESFKKEH--ERQAMLSKQTEQQNKHKHQPKKKT 558
Cdd:PRK11147 480 EELLDSYQGTVLLVSHDRQFVDNTVTEcWIFEGNGKIGRYVGGYHDARQQQAQYlaLKQPAVKKKEEAAAPKAETVKRSS 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 559 G-LSYKEKLEYETIMTRIEMTETRLEDLeQEMINASDNYAR--------IKELNEEKEQLEATYEaditRWSELEEIKE 628
Cdd:PRK11147 560 KkLSYKLQRELEQLPQLLEDLEAEIEAL-QAQVADADFFSQpheqtqkvLADLADAEQELEVAFE----RWEELEALKN 633
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
18-527 |
1.31e-84 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 274.85 E-value: 1.31e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 18 KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHMTVFEAVLSSDTPtL 97
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFTVLDTVIMGHTE-L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 98 RIIKKYEEAVnrYAL-DQSDSNFNKM--MEAQ-EEMDqkdawDYNAEIKT--ILSKLGI----HDTTKKivELSGGQQKR 167
Cdd:PRK15064 93 WEVKQERDRI--YALpEMSEEDGMKVadLEVKfAEMD-----GYTAEARAgeLLLGVGIpeeqHYGLMS--EVAPGWKLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 168 VVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYEDYivM 247
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEY--M 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 248 RAENELVEQKQQEKQKAlyKQELAWM-----RAGAKARTTKQQAriNRFNQLE----SDVKT--------QHTQDKgeln 310
Cdd:PRK15064 242 TAATQARERLLADNAKK--KAQIAELqsfvsRFSANASKAKQAT--SRAKQIDkiklEEVKPssrqnpfiRFEQDK---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 311 laysRLGKQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQ 390
Cdd:PRK15064 314 ----KLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQ 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 -TEKTLDRDIRVIDYLreeSEMAKEKDGTSiSVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEP 469
Cdd:PRK15064 390 dHAYDFENDLTLFDWM---SQWRQEGDDEQ-AVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 470 TNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFEDY 527
Cdd:PRK15064 466 TNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-629 |
1.14e-69 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 237.76 E-value: 1.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 27 SISEHERIGLVGINGTGKSTLLKVIGGldeDFTAD---ITHPNQYRIRYSSQKQDLNGhMTVFEAVLSSDtptlRIIKKY 103
Cdd:PRK10636 23 TINPGQKVGLVGKNGCGKSTLLALLKN---EISADggsYTFPGNWQLAWVNQETPALP-QPALEYVIDGD----REYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 104 EEAVNRyALDQSDSNFNKMMEAQeeMDQKDAWDYNAEIKTILSKLGIHDT--TKKIVELSGGQQKRVVLAKTLIEQPDLL 181
Cdd:PRK10636 95 EAQLHD-ANERNDGHAIATIHGK--LDAIDAWTIRSRAASLLHGLGFSNEqlERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 182 LLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYEDYIVMRAeNELVEQK---Q 258
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRA-TRLAQQQamyE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 259 QEKQKALYKQELAwMRAGAKARTTKQ-QARINRFNQLESdVKTQHTQDKGELNL-AYSRLGKQVYELKNLSKSINNKVLF 336
Cdd:PRK10636 251 SQQERVAHLQSYI-DRFRAKATKAKQaQSRIKMLERMEL-IAPAHVDNPFHFSFrAPESLPNPLLKMEKVSAGYGDRIIL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEktldrdirvIDYLR-EESEMAKEK 415
Cdd:PRK10636 329 DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ---------LEFLRaDESPLQHLA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 416 DGTSISVTQLLERFLFPSATHGKKVY----KLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGS 491
Cdd:PRK10636 400 RLAPQELEQKLRDYLGGFGFQGDKVTeetrRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 492 VITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFEDYesfkkeherQAMLSKQTEQQNKHKHQPKKKTGLSYKEKLEYE-- 569
Cdd:PRK10636 480 LVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY---------QQWLSDVQKQENQTDEAPKENNANSAQARKDQKrr 550
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 570 --TIMTRIEMTETRLEDLEQEMINASDnyarikELNEEKEQLEATYEADITRWSELEEIKEQ 629
Cdd:PRK10636 551 eaELRTQTQPLRKEIARLEKEMEKLNA------QLAQAEEKLGDSELYDQSRKAELTACLQQ 606
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
7-528 |
1.51e-59 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 212.03 E-value: 1.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLK-----VIGGLDEDftADITHPNQyriryssqkQDLNG 81
Cdd:PLN03073 179 HMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGIPKN--CQILHVEQ---------EVVGD 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEAVLSSDTPTLRII---------KKYEEAVNRYALDQSDSNFN--------KMMEAQEEMDQKDAWDYNAEIKTI 144
Cdd:PLN03073 248 DTTALQCVLNTDIERTQLLeeeaqlvaqQRELEFETETGKGKGANKDGvdkdavsqRLEEIYKRLELIDAYTAEARAASI 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LSKLGIHD--TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEV 222
Cdd:PLN03073 328 LAGLSFTPemQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTV 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 223 STRIIELDRGKLKTYPGNYEDYIVMRAENELVEQK---QQEKQKALYKQELAWMRAGAKaRTTKQQARINRFNQLES-DV 298
Cdd:PLN03073 408 VTDILHLHGQKLVTYKGDYDTFERTREEQLKNQQKafeSNERSRSHMQAFIDKFRYNAK-RASLVQSRIKALDRLGHvDA 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 299 KTQHTQDKGELNLAYSRLGKQVYELKNLSKSI-NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGEL 377
Cdd:PLN03073 487 VVNDPDYKFEFPTPDDRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 378 KIGQTVKVAYFKQtektldrdirvidylreesemaKEKDGTSISVTQLLERF-LFPSATHGK-----------------K 439
Cdd:PLN03073 567 FRSAKVRMAVFSQ----------------------HHVDGLDLSSNPLLYMMrCFPGVPEQKlrahlgsfgvtgnlalqP 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 440 VYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEK 519
Cdd:PLN03073 625 MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTP 704
|
....*....
gi 1842088001 520 IIGSFEDYE 528
Cdd:PLN03073 705 FHGTFHDYK 713
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
323-552 |
2.45e-58 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 204.53 E-value: 2.45e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQtEKTLDRDIRVI 402
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQ-EPPLDDDLTVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYLRE--------ESEMAK--------EKDGTSIS-----------------VTQLLERFLFPSATHGKKVYKLSGGEQK 449
Cdd:COG0488 80 DTVLDgdaelralEAELEEleaklaepDEDLERLAelqeefealggweaearAEEILSGLGFPEEDLDRPVSELSGGWRR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFEDYEs 529
Cdd:COG0488 160 RVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSAYL- 238
|
250 260
....*....|....*....|...
gi 1842088001 530 FKKEHERQAMLSKQTEQQNKHKH 552
Cdd:COG0488 239 EQRAERLEQEAAAYAKQQKKIAK 261
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
322-516 |
2.42e-55 |
|
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: 184.57 E-value: 2.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQtektldrdirv 401
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 idylreesemakekdgtsisvtqllerflfpsathgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTIL 481
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170 180 190
....*....|....*....|....*....|....*
gi 1842088001 482 EDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:cd03221 110 EEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-233 |
1.48e-50 |
|
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: 171.48 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQkqdlnghmtvf 86
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eavlssdtptlriikkyeeavnryaldqsdsnfnkmmeaqeemdqkdawdynaeiktilsklgihdttkkiveLSGGQQK 166
Cdd:cd03221 71 -------------------------------------------------------------------------LSGGEKM 77
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:cd03221 78 RLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
322-517 |
1.05e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 144.57 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQ 390
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 tEKTLDRDiRVIDYLREESEMAKEKDGTSIsVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPT 470
Cdd:COG4619 82 -EPALWGG-TVRDNLPFPFQLRERKFDRER-ALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 471 NDLDTETLTILEDYIDDF----GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG4619 159 SALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-517 |
9.60e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 149.67 E-value: 9.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIF--NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadITHPNQYRIRYSSQKQDLNGHM-- 83
Cdd:COG1123 7 VRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGL-------LPHGGRISGEVLLDGRDLLELSea 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 -------TVFEAVLSSDTPtLRIIKKYEEAVNRYALDQsdsnfnkmmeaqEEMDQKdawdynaeIKTILSKLGIHDTTKK 156
Cdd:COG1123 80 lrgrrigMVFQDPMTQLNP-VTVGDQIAEALENLGLSR------------AEARAR--------VLELLEAVGLERRLDR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 -IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:COG1123 139 yPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 232 GKlktypgnyedyIVMRAENELVEQKQQekqkALYKQELAWMRAGAKARTTKQQARInrfnqLE-SDVKTQHTQDKGELN 310
Cdd:COG1123 219 GR-----------IVEDGPPEEILAAPQ----ALAAVPRLGAARGRAAPAAAAAEPL-----LEvRNLSKRYPVRGKGGV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 311 LAysrlgkqvyeLKNLSksinnkvlFEdvteiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvAYFK 389
Cdd:COG1123 279 RA----------VDDVS--------LT-----LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFdGKDLT-KLSR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QTEKTLDRDI---------------RVIDYLREESEMAKEKDGTSIS--VTQLLERF-LFPSATHgKKVYKLSGGEQKRL 451
Cdd:COG1123 335 RSLRELRRRVqmvfqdpysslnprmTVGDIIAEPLRLHGLLSRAERRerVAELLERVgLPPDLAD-RYPHELSGGQRQRV 413
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKI 517
Cdd:COG1123 414 AIARALALEPKLLILDEPTSALDvsvqAQILNLLRDLQRELGLTYLFISHDlavvRYIADRVA----VMYDGRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-233 |
6.12e-38 |
|
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: 139.52 E-value: 6.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQKQdLNGHM- 83
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKE-LRRKVg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVF---EAVLSSDTPtlriikkYEEAVnrYALDQsdsnfnkMMEAQEEMDQKdawdynaeIKTILSKLGIHDTTKK-IVE 159
Cdd:cd03225 79 LVFqnpDDQFFGPTV-------EEEVA--FGLEN-------LGLPEEEIEER--------VEEALELVGLEGLRDRsPFT 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:cd03225 135 LSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKaegKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-251 |
7.00e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.91 E-value: 7.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT------HPNQYRIRYSS 74
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGH--MTVFEAVLSSDTPTLRIIKKYeeavnryaldqsdsnfnkmmeaqeemDQKDawdyNAEIKTILSKLGIHD 152
Cdd:COG1121 82 QRAEVDWDfpITVRDVVLMGRYGRRGLFRRP--------------------------SRAD----REAVDEALERVGLED 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 -TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK---QYPHTVLFVTHDryfLNEVS---TR 225
Cdd:COG1121 132 lADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelrREGKTILVVTHD---LGAVReyfDR 208
|
250 260
....*....|....*....|....*.
gi 1842088001 226 IIELDRGKLktYPGNYEDyiVMRAEN 251
Cdd:COG1121 209 VLLLNRGLV--AHGPPEE--VLTPEN 230
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-244 |
1.45e-34 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 138.10 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftaDIThPNQYRIRYSsqkqdlnghmt 84
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG-------ELE-PDSGTVKWS----------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 vfeavlssdtptlriikkyEEA-VNRYALDQSDsNFNKMMEAQEEMDQ-KDAWDYNAEIKTILSKL--GIHDTTKKIVEL 160
Cdd:PRK15064 380 -------------------ENAnIGYYAQDHAY-DFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLlfSQDDIKKSVKVL 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 161 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGN 240
Cdd:PRK15064 440 SGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGT 519
|
....
gi 1842088001 241 YEDY 244
Cdd:PRK15064 520 YEEY 523
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
7-234 |
4.53e-34 |
|
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: 130.16 E-value: 4.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---HP-NQYRIR-------YSSQ 75
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLldgRDlASLSRRelarriaYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDLNGHMTVFEAVLSSDTPTLRIIKKYEEAvnryaldqsdsnfnkmmeaqeemdqkdawDYNAeIKTILSKLGIHD-TT 154
Cdd:COG1120 83 EPPAPFGLTVRELVALGRYPHLGLFGRPSAE-----------------------------DREA-VEEALERTGLEHlAD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDryfLN---EVSTRII 227
Cdd:COG1120 133 RPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD---LNlaaRYADRLV 209
|
....*..
gi 1842088001 228 ELDRGKL 234
Cdd:COG1120 210 LLKDGRI 216
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-234 |
1.08e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 128.64 E-value: 1.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQyRIRYSSQK 76
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlrptsgevrvlGEDVARDPAEVRR-RIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGHMTVFEavlssdtpTLRIIKKYeeavnrYALDQSdsnfnkmmEAQEEMDQkdawdynaeiktILSKLGIHDT-TK 155
Cdd:COG1131 82 PALYPDLTVRE--------NLRFFARL------YGLPRK--------EARERIDE------------LLELFGLTDAaDR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY---PHTVLFVTHDryfLNEV---STRIIEL 229
Cdd:COG1131 128 KVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHY---LEEAerlCDRVAII 204
|
....*
gi 1842088001 230 DRGKL 234
Cdd:COG1131 205 DKGRI 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-234 |
1.15e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 127.62 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYR--IRYSSQ 75
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYldgkplsamPPPEWRrqVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDLnGHMTVFEavlssdtptlriikkyeeavnryaldqsdsNFNK-MMEAQEEMDQKDAwdynaeiKTILSKLGIHDT- 153
Cdd:COG4619 82 EPAL-WGGTVRD------------------------------NLPFpFQLRERKFDRERA-------LELLERLGLPPDi 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 -TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIE 228
Cdd:COG4619 124 lDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAeegrAVLWVSHDPEQIERVADRVLT 203
|
....*.
gi 1842088001 229 LDRGKL 234
Cdd:COG4619 204 LEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-235 |
8.14e-33 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 126.51 E-value: 8.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL---DE-----DFTADITHPNQYR--IRYSSQK 76
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLlkpDSgsiliDGEDVRKEPREARrqIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGHMTVFEavlssdtptlrIIKKYeeavnryaldqsdSNFNKMMEAQeemdqkdawdYNAEIKTILSKLGIHDTT-K 155
Cdd:COG4555 83 RGLYDRLTVRE-----------NIRYF-------------AELYGLFDEE----------LKKRIEELIELLGLEEFLdR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY---PHTVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:COG4555 129 RVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
...
gi 1842088001 233 KLK 235
Cdd:COG4555 209 KVV 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-234 |
1.19e-32 |
|
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: 124.95 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT------HPNQYRIRYSSQKQDLN 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 GHM--TVFEAVLSSDTPTLRIIKKYeeavnryaldqSDSNFNKMMEAQEEMDQKDAWDynaeiktilsklgihdttKKIV 158
Cdd:cd03235 81 RDFpiSVRDVVLMGLYGHKGLFRRL-----------SKADKAKVDEALERVGLSELAD------------------RQIG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRW---LINYVKQYPHTVLFVTHDryfLNEVST---RIIELDRG 232
Cdd:cd03235 132 ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDiyeLLRELRREGMTILVVTHD---LGLVLEyfdRVLLLNRT 208
|
..
gi 1842088001 233 KL 234
Cdd:cd03235 209 VV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-234 |
2.86e-32 |
|
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: 122.51 E-value: 2.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSqkqdlnGHMTVF 86
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL---------------LKPDS------GEIKVL 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EavlssdtptLRIIKKYEEAVNR-YALDQSDSNFNKMmeaqeemdqkdawdynaeiktilsklgihdTTKKIVELSGGQQ 165
Cdd:cd03230 61 G---------KDIKKEPEEVKRRiGYLPEEPSLYENL------------------------------TVRENLKLSGGMK 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY---PHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:cd03230 102 QRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
320-507 |
7.35e-32 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 130.24 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSIN-NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQtEKTLDRD 398
Cdd:PRK11819 6 IYTMNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQ-EPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVidylREESEMA-KEkdgtsisVTQLLERF-----LF--PSATHGK-------------------------------- 438
Cdd:PRK11819 85 KTV----RENVEEGvAE-------VKAALDRFneiyaAYaePDADFDAlaaeqgelqeiidaadawdldsqleiamdalr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 439 ------KVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQ 507
Cdd:PRK11819 154 cppwdaKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAG 228
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-234 |
1.47e-30 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 119.16 E-value: 1.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFT-------ADITH--PNQYRIRYSSQKQ 77
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSgeilidgRDVTGvpPERRNIGMVFQDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVlssdtptlriikkyeeavnRYALDQsdsnfNKMMEAQEEmdqkdawdynAEIKTILSKLGI-HDTTKK 156
Cdd:cd03259 82 ALFPHLTVAENI-------------------AFGLKL-----RGVPKAEIR----------ARVRELLELVGLeGLLNRY 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelgiTTIYVTHDQEEALALADRIAVMNEG 207
|
..
gi 1842088001 233 KL 234
Cdd:cd03259 208 RI 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-233 |
3.10e-30 |
|
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: 116.19 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdLNGHmtvf 86
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIL---------------IDGK---- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eAVLSSDTPTLRiikkyeeavnryaldqsdsnfnkmmeaqeemdqkdawdynaeiktilSKLGIhdttkkIVELSGGQQK 166
Cdd:cd00267 62 -DIAKLPLEELR-----------------------------------------------RRIGY------VPQLSGGQRQ 87
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:cd00267 88 RVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAeegRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-234 |
6.66e-30 |
|
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: 117.21 E-value: 6.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD----KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLD---------EDFtaDITH-PNQYRIRY 72
Cdd:cd03255 2 ELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDrptsgevrvDGT--DISKlSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 73 SSQK-----QDLN--GHMTVFEAVLssdtptlriikkyeeavnrYALdqsdsnfnkmmeaqeEMDQKDAWDYNAEIKTIL 145
Cdd:cd03255 80 RRRHigfvfQSFNllPDLTALENVE-------------------LPL---------------LLAGVPKKERRERAEELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 146 SKLGI-HDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----IRWLINYVKQYPHTVLFVTHDRyFLN 220
Cdd:cd03255 126 ERVGLgDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELA 204
|
250
....*....|....
gi 1842088001 221 EVSTRIIELDRGKL 234
Cdd:cd03255 205 EYADRIIELRDGKI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-520 |
1.03e-29 |
|
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: 123.37 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadiTHPNQYRIRY-------------- 72
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQ------YEPTSGRIIYhvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 73 ---SSQKQDLNGHMTVFEAVL--SSDTPTLRIIKKYEEAVNR-YALDQSDSNFNKMMEAQEEM--DQKDAWDYNAEIKTI 144
Cdd:TIGR03269 76 skvGEPCPVCGGTLEPEEVDFwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIgyEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LsKLGiHDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRW----LINYVKQYPHTVLFVTHDRYFLN 220
Cdd:TIGR03269 156 V-QLS-HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 221 EVSTRIIELDRGKlktypgnyedyIVMRAENELVeqkqqekqkalykqelawmragakarttkqqarINRFNQLESDVKT 300
Cdd:TIGR03269 234 DLSDKAIWLENGE-----------IKEEGTPDEV---------------------------------VAVFMEGVSEVEK 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 301 QHTQDkgelnlaysrLGKQVYELKNLSK---SINNKVL--FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEG 375
Cdd:TIGR03269 270 ECEVE----------VGEPIIKVRNVSKryiSVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 376 ELKIgqTVKVAYFKQTEKTLD---RDIRVIDYLREESEMAKEKD-----GTSISVtQLLERFLFPSATHGKKV------- 440
Cdd:TIGR03269 340 EVNV--RVGDEWVDMTKPGPDgrgRAKRYIGILHQEYDLYPHRTvldnlTEAIGL-ELPDELARMKAVITLKMvgfdeek 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 441 ---------YKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHDRYFLNKVVQ 507
Cdd:TIGR03269 417 aeeildkypDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkarEEMEQTFIIVSHDMDFVLDVCD 496
|
570
....*....|...
gi 1842088001 508 EYWFIHDGKIEKI 520
Cdd:TIGR03269 497 RAALMRDGKIVKI 509
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
322-502 |
1.15e-29 |
|
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: 116.42 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK---VAYFKQT-----E 392
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdarEDYRRRLaylghA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTLDRDIRVIDYLREESEMaKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTND 472
Cdd:COG4133 84 DGLKPELTVRENLRFWAAL-YGLRADREAIDEALEAVGLAGLAD-LPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 473 LDTETLTILEDYIDDF---GGSVITVSHDRYFL 502
Cdd:COG4133 162 LDAAGVALLAELIAAHlarGGAVLLTTHQPLEL 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
322-517 |
1.23e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 115.23 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDIRV 401
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLD---------------GKDLAS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IDYLreesEMAKEkdgtsIS-VTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD---- 474
Cdd:cd03214 66 LSPK----ELARK-----IAyVPQALELL---GLAHlaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDiahq 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1842088001 475 TETLTILEDYIDDFGGSVITVSHDryfLNKVVQ---EYWFIHDGKI 517
Cdd:cd03214 134 IELLELLRRLARERGKTVVMVLHD---LNLAARyadRVILLKDGRI 176
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
7-234 |
1.57e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 115.23 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdLNGhmtvf 86
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------LDG----- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eavlssdtptlRIIKKYEEAvnryaldqsdsnfnkmmeaqeEMDQKDAWdynaeIKTILSKLGIHDTTKKIV-ELSGGQQ 165
Cdd:cd03214 61 -----------KDLASLSPK---------------------ELARKIAY-----VPQALELLGLAHLADRPFnELSGGER 103
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDryfLN---EVSTRIIELDRGKL 234
Cdd:cd03214 104 QRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRI 176
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
322-516 |
1.78e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 114.26 E-value: 1.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektldrdirv 401
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 idylreesemakEKDGTSISVTQLLERFLFpsathgkkVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTIL 481
Cdd:cd00267 60 ------------GKDIAKLPLEELRRRIGY--------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*...
gi 1842088001 482 EDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:cd00267 120 LELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-234 |
2.85e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 119.10 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEaykIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADItHPNQYR 69
Cdd:COG1118 1 MSIE---VRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLetpdsgrivlnGRDLFTNL-PPRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 70 IRYSSQKQDLNGHMTVFEAV---LSSDTPTLRIIKkyeEAVNRYaLDqsdsnfnkMMEAQEEMDQKDAwdynaeiktils 146
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIafgLRVRPPSKAEIR---ARVEEL-LE--------LVQLEGLADRYPS------------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 147 klgihdttkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDR---Yfl 219
Cdd:COG1118 133 ------------QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDELGGTTVFVTHDQeeaL-- 198
|
250
....*....|....*
gi 1842088001 220 nEVSTRIIELDRGKL 234
Cdd:COG1118 199 -ELADRVVVMNQGRI 212
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
322-517 |
3.24e-29 |
|
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: 114.03 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTLDRdir 400
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIK----KEPEEVKRR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 vIDYLREESemakekdgtsisvtqllerFLFPSAThGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTI 480
Cdd:cd03230 75 -IGYLPEEP-------------------SLYENLT-VRENLKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 481 LEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03230 134 FWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-234 |
4.26e-29 |
|
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: 115.51 E-value: 4.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSqkqdlnGHMTV 85
Cdd:COG1122 2 ELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL---------------LKPTS------GEVLV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTPTlRIIKK-----------------YEE-AvnrYALdqsdSNFNKmmeAQEEMDQKdawdynaeIKTILSK 147
Cdd:COG1122 61 DGKDITKKNLR-ELRRKvglvfqnpddqlfaptvEEDvA---FGP----ENLGL---PREEIRER--------VEEALEL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 148 LGIHDTTKKIV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVS 223
Cdd:COG1122 122 VGLEHLADRPPhELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNkegKTVIIVTHDLDLVAELA 201
|
250
....*....|.
gi 1842088001 224 TRIIELDRGKL 234
Cdd:COG1122 202 DRVIVLDDGRI 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
322-517 |
7.28e-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: 115.34 E-value: 7.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---------KVAYFKQt 391
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLPD- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDIRVIDYLREESEMAKEKDGTSIS-VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPT 470
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKrIEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1842088001 471 NDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG4555 161 NGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-234 |
2.94e-28 |
|
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: 112.62 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE---------DFTADITHPNQYRIRYSS--- 74
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpdsgtiiidGLKLTDDKKNINELRQKVgmv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 -QKQDLNGHMTVFEAVlssdTPTLRIIKKyeeavnryaldqsdsnfnkmmeaqeeMDQKDAwdyNAEIKTILSKLGIHD- 152
Cdd:cd03262 82 fQQFNLFPHLTVLENI----TLAPIKVKG--------------------------MSKAEA---EERALELLEKVGLADk 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIEL 229
Cdd:cd03262 129 ADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEegmTMVVVTHEMGFAREVADRVIFM 208
|
....*
gi 1842088001 230 DRGKL 234
Cdd:cd03262 209 DDGRI 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-234 |
4.78e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 115.58 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITH--PNQYRI 70
Cdd:COG3842 1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGF-ETPDSgrilldgrDVTGlpPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQKQDLNGHMTVFEAVLSSdtptLRIIKKYEEAVNRyaldqsdsnfnKMMEAQEEMDqkdawdynaeiktiLSKLGi 150
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFG----LRMRGVPKAEIRA-----------RVAELLELVG--------------LEGLA- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 151 hdtTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLI-NYVKQYPHTVLFVTHDRyflNE---VS 223
Cdd:COG3842 130 ---DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAklrEEMREELrRLQRELGITFIYVTHDQ---EEalaLA 203
|
250
....*....|.
gi 1842088001 224 TRIIELDRGKL 234
Cdd:COG3842 204 DRIAVMNDGRI 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-188 |
8.50e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 109.27 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 21 FNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQYRIRYSSQKQDLNGHMTVFEAV 89
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilldGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 lssdtptlriikkyeeavnryaldqsdsnfnkmMEAQEEMDQKDAWDyNAEIKTILSKLGIHDTTKKIV-----ELSGGQ 164
Cdd:pfam00005 81 ---------------------------------RLGLLLKGLSKREK-DARAEEALEKLGLGDLADRPVgerpgTLSGGQ 126
|
170 180
....*....|....*....|....
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTN 188
Cdd:pfam00005 127 RQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-256 |
1.30e-27 |
|
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: 111.61 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTaDITHPNQYRIR---- 71
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLlrpdsgeilvdGQDIT-GLSEKELYELRrrig 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 --------YSSqkqdlnghMTVFEAVLssdtptlriikkyeeavnrYALDQsdsnFNKMMEAqeEMDQKdawdynAEIKt 143
Cdd:COG1127 86 mlfqggalFDS--------LTVFENVA-------------------FPLRE----HTDLSEA--EIREL------VLEK- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 144 iLSKLGIHDTTKK-IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRwliNYVKQYPHTVLFVTHD 215
Cdd:COG1127 126 -LELVGLPGAADKmPSELSGGMRKRVALARALALDPEILLYDEPTAGLDpitsaviDELIR---ELRDELGLTSVVVTHD 201
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1842088001 216 RYFLNEVSTRIIELDRGKLKTYpGNYEDyiVMRAENELVEQ 256
Cdd:COG1127 202 LDSAFAIADRVAVLADGKIIAE-GTPEE--LLASDDPWVRQ 239
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-233 |
1.36e-27 |
|
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: 109.58 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE-------------DFTADITHPNQYRIRYS 73
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpdsgsilidgedlTDLEDELPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 SQKQDLNGHMTVFEAVLssdtptlriikkyeeavnryaldqsdsnfnkmmeaqeemdqkdawdynaeiktilskLGihdt 153
Cdd:cd03229 82 FQDFALFPHLTVLENIA---------------------------------------------------------LG---- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 tkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK----QYPHTVLFVTHDRYFLNEVSTRIIEL 229
Cdd:cd03229 101 ------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaQLGITVVLVTHDLDEAARLADRVVVL 174
|
....
gi 1842088001 230 DRGK 233
Cdd:cd03229 175 RDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-521 |
1.97e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.95 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV-----KVAYFKQTEkTL 395
Cdd:COG1121 8 ELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQRA-EV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRD--IRVID-----------YLREESEMAKEKdgtsisVTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHK 460
Cdd:COG1121 87 DWDfpITVRDvvlmgrygrrgLFRRPSRADREA------VDEALERV---GLEDlaDRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 461 PNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHD-----RYF-----LNKVVqeywfIHDGKIEKII 521
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELrreGKTILVVTHDlgavrEYFdrvllLNRGL-----VAHGPPEEVL 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
322-517 |
6.18e-27 |
|
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: 108.73 E-value: 6.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS----INNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTLD 396
Cdd:cd03255 2 ELKNLSKTygggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIS----KLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIR-----------VIDYL--REESEMAKEKDGTSIS-----VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLV 458
Cdd:cd03255 78 AFRRrhigfvfqsfnLLPDLtaLENVELPLLLAGVPKKerrerAEELLERVGLGDRLN-HYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 459 HKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHDRYFLN---KVVqeywFIHDGKI 517
Cdd:cd03255 157 NDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDPELAEyadRII----ELRDGKI 218
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
322-517 |
7.98e-27 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 109.75 E-value: 7.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQ 390
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 tEKTLDRDIRVIDY-----------LREESEMAKEKdgtsisVTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLL 457
Cdd:COG1120 83 -EPPAPFGLTVRELvalgryphlglFGRPSAEDREA------VEEALERT---GLEHlaDRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 458 VHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD-----RYFlNKVvqeyWFIHDGKI 517
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDlahqLEVLELLRRLARERGRTVVMVLHDlnlaaRYA-DRL----VLLKDGRI 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
8-233 |
8.01e-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: 108.34 E-value: 8.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT--------HPNQYR--IRYSSQKQ 77
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLwngepirdAREDYRrrLAYLGHAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAvlssdtptLRIIKKYeeavnrYALDQSDsnfnkmmeaqeemdqkdawdynAEIKTILSKLGIHD-TTKK 156
Cdd:COG4133 85 GLKPELTVREN--------LRFWAAL------YGLRADR----------------------EAIDEALEAVGLAGlADLP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVstRIIELDRGK 233
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLArggAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-234 |
1.73e-26 |
|
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: 108.35 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSY----ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQK------ 76
Cdd:COG1124 3 EVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGR-PVTRRRRKafrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 ----QD----LNGHMTVFEAVlssDTPtLRIIKKYeeavnryaldqsdsnfnkmmeaqeemdqkdawDYNAEIKTILSKL 148
Cdd:COG1124 82 qmvfQDpyasLHPRHTVDRIL---AEP-LRIHGLP--------------------------------DREERIAELLEQV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDT--TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEV 222
Cdd:COG1124 126 GLPPSflDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDLAVVAHL 205
|
250
....*....|..
gi 1842088001 223 STRIIELDRGKL 234
Cdd:COG1124 206 CDRVAVMQNGRI 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
322-517 |
2.06e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 107.84 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---------KVAYFKQt 391
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIGYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDIRVIDYLREESEMAKEKDGTSIS-VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPT 470
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARErIDELLELFGLTDAAD-RKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 471 NDLD----TETLTILEDYIDDfGGSVITVSH---------DRyflnkVVqeywFIHDGKI 517
Cdd:COG1131 160 SGLDpearRELWELLRELAAE-GKTVLLSTHyleeaerlcDR-----VA----IIDKGRI 209
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
7-233 |
4.77e-26 |
|
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: 107.48 E-value: 4.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG------------LDEDF----TADITHpnqyRI 70
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdlpptygndvrlFGERRggedVWELRK----RI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQK--QDLNGHMTVFEAVLSSDTPTLRIIKKYEEavnryaldqsdsnfnkmmeaqEEMDQKDAWdynaeiktiLSKL 148
Cdd:COG1119 81 GLVSPAlqLRFPRDETVLDVVLSGFFDSIGLYREPTD---------------------EQRERAREL---------LELL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GI-HDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYV----KQYPHTVLFVTHdryFLNEVS 223
Cdd:COG1119 131 GLaHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLdklaAEGAPTLVLVTH---HVEEIP 207
|
250
....*....|...
gi 1842088001 224 ---TRIIELDRGK 233
Cdd:COG1119 208 pgiTHVLLLKDGR 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
7-234 |
5.94e-26 |
|
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: 106.44 E-value: 5.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADK----EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGH 82
Cdd:cd03257 3 EVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 M--TVFEAVLSSDTPTLRIIKKYEEAVNryaldqsdsnFNKMMEAQEEMDQKdawdynaeIKTILSKLGIHDT--TKKIV 158
Cdd:cd03257 83 EiqMVFQDPMSSLNPRMTIGEQIAEPLR----------IHGKLSKKEARKEA--------VLLLLVGVGLPEEvlNRYPH 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:cd03257 145 ELSGGQRQRVAIARALALNPKLLIADEPTSALDvsvqAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-227 |
8.86e-26 |
|
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: 105.63 E-value: 8.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADK----EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDedftaditHPNQYRIRYSSQK-QDLNG 81
Cdd:cd03293 2 EVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLE--------RPTSGEVLVDGEPvTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVfeaVLSSDT--PTLRIIKkyeeavN-RYALDQsdsNFNKMMEAQEEMDQkdawdynaeiktILSKLGIHDTTKK-I 157
Cdd:cd03293 74 DRGY---VFQQDAllPWLTVLD------NvALGLEL---QGVPKAEARERAEE------------LLELVGLSGFENAyP 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIR-WLINYVKQYPHTVLFVTHDryfLNE---VSTRII 227
Cdd:cd03293 130 HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltrEQLQeELLDIWRETGKTVLLVTHD---IDEavfLADRVV 203
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-234 |
1.54e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 105.13 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEA-YKIEHLNKSYADKE----IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDeDFTA--------DITH-PNQY 68
Cdd:COG1136 1 MSPlLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLD-RPTSgevlidgqDISSlSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 69 RIRYSSQK-----QDLN--GHMTVFEAVLssdTPtLRIIKKYEEAVNRYALDqsdsnfnkmmeaqeemdqkdawdynaei 141
Cdd:COG1136 80 LARLRRRHigfvfQFFNllPELTALENVA---LP-LLLAGVSRKERRERARE---------------------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 142 ktILSKLGIHD-TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----IRWLINYVKQYPHTVLFVTHDR 216
Cdd:COG1136 128 --LLERVGLGDrLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDP 205
|
250
....*....|....*...
gi 1842088001 217 yFLNEVSTRIIELDRGKL 234
Cdd:COG1136 206 -ELAARADRVIRLRDGRI 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
322-516 |
1.58e-25 |
|
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: 104.47 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN--KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTLDRD 398
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLT----KLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 I--------------RVIDYL--------REESEMAKEkdgtsisVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRL 456
Cdd:cd03225 77 VglvfqnpddqffgpTVEEEVafglenlgLPEEEIEER-------VEEALELVGLEGLRD-RSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 457 LVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLkaeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-234 |
1.65e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 105.13 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGlDEDFTA--------DITHPNQYRIRYSSQK- 76
Cdd:COG2884 3 RFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG-EERPTSgqvlvngqDLSRLKRREIPYLRRRi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 ----QD---LNgHMTVFEAV-LSsdtptLRIIKKYEEAVNRyaldqsdsnfnkmmeaqeemdqkdawdynaEIKTILSKL 148
Cdd:COG2884 82 gvvfQDfrlLP-DRTVYENVaLP-----LRVTGKSRKEIRR------------------------------RVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDTTKKIV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVST 224
Cdd:COG2884 126 GLSDKAKALPhELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrgtTVLIATHDLELVDRMPK 205
|
250
....*....|
gi 1842088001 225 RIIELDRGKL 234
Cdd:COG2884 206 RVLELEDGRL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-234 |
2.02e-25 |
|
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: 111.46 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSY--ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYR--IR 71
Cdd:COG2274 473 DIELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLRrqIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQkqdlnghmtvfEAVLSSDTptLR--IikkyeeavnryALDQSDSNFNKMMEAqeemdqkdawdynAEIktilskLG 149
Cdd:COG2274 553 VVLQ-----------DVFLFSGT--IRenI-----------TLGDPDATDEEIIEA-------------ARL------AG 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 150 IHDTTKK--------IVE----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHTVLFVTHD 215
Cdd:COG2274 590 LHDFIEAlpmgydtvVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLlkGRTVIIIAHR 669
|
250
....*....|....*....
gi 1842088001 216 RYFLNEVStRIIELDRGKL 234
Cdd:COG2274 670 LSTIRLAD-RIIVLDKGRI 687
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
320-519 |
2.35e-25 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 104.74 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSINN-----KVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayFKQTEK 393
Cdd:COG1136 4 LLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDI----SSLSER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRdIR------------VIDYL--REESEMAKEKDGTSIS-----VTQLLERF-LFPSATHgkKVYKLSGGEQKRLYL 453
Cdd:COG1136 79 ELAR-LRrrhigfvfqffnLLPELtaLENVALPLLLAGVSRKerrerARELLERVgLGDRLDH--RPSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 454 LRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHDR---YFLNKVVqeywFIHDGKIEK 519
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVMVTHDPelaARADRVI----RLRDGRIVS 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
322-505 |
2.71e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 104.15 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV-----KVAYFKQTEkTL 395
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfGKPLekerkRIGYVPQRR-SI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRD--IRVID-----------YLREESEMAKEKdgtsisVTQLLERfLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPN 462
Cdd:cd03235 80 DRDfpISVRDvvlmglyghkgLFRRLSKADKAK------VDEALER-VGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 463 VLLLDEPTNDLDTET----LTILEDYIDDfGGSVITVSHDryfLNKV 505
Cdd:cd03235 153 LLLLDEPFAGVDPKTqediYELLRELRRE-GMTILVVTHD---LGLV 195
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
322-516 |
3.05e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 102.65 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqTVKVAYFKQTEKTLDRDIRV 401
Cdd:cd03229 2 ELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IdylreesemakekdgtsisvtqlLERF-LFPSATHGKKV-YKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLT 479
Cdd:cd03229 81 V-----------------------FQDFaLFPHLTVLENIaLGLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1842088001 480 ILEDYI----DDFGGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:cd03229 138 EVRALLkslqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-234 |
3.89e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.09 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEaykIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYRIR 71
Cdd:PRK10851 1 MSIE---IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVLSSdtptLRIIKKYEEAvNRYALDQsdsnfnKMMEAQEeMDQKDawdynaeiktilsklgiH 151
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFG----LTVLPRRERP-NAAAIKA------KVTQLLE-MVQLA-----------------H 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK10851 129 LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAqvrkELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVV 208
|
....*..
gi 1842088001 228 ELDRGKL 234
Cdd:PRK10851 209 VMSQGNI 215
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
336-471 |
4.47e-25 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 101.57 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 336 FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQT-----EKTLDRDI 399
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLdGQDLtdderkslrkEIGYVFQDpqlfpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 400 RVIDYLREESEMAKEKDgtsisVTQLLERFLFPSATH---GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:pfam00005 81 RLGLLLKGLSKREKDAR-----AEEALEKLGLGDLADrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-235 |
7.76e-25 |
|
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: 102.34 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADK-EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSQKQDLNGhmtvf 86
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL---------------IKESSGSILLNG----- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eavlssdtptlRIIKKYEEAVNRYALDQsDSNFNKMME-AQEEMD--QKDAWDYNAEIKTILSKLGIHDTTKKI-VELSG 162
Cdd:cd03226 62 -----------KPIKAKERRKSIGYVMQ-DVDYQLFTDsVREELLlgLKELDAGNEQAETVLKDLDLYALKERHpLSLSG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLK 235
Cdd:cd03226 130 GQKQRLAIAAALLSGKDLLIFDEPTSGLDYknmERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-233 |
8.21e-25 |
|
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: 103.42 E-value: 8.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHP-NQYRIRYS 73
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLveptsgsvlidGTDINKLKGKAlRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 SQKQDLN--GHMTVFEAVLS---SDTPTLRII----KKYEEAVNRYALDQSDsnfnkmmeaqeemdqkdawdynaeiktI 144
Cdd:cd03256 82 MIFQQFNliERLSVLENVLSgrlGRRSTWRSLfglfPKEEKQRALAALERVG---------------------------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LSKLgihdtTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLN 220
Cdd:cd03256 135 LDKA-----YQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQVDLAR 209
|
250
....*....|...
gi 1842088001 221 EVSTRIIELDRGK 233
Cdd:cd03256 210 EYADRIVGLKDGR 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
322-497 |
2.07e-24 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 100.15 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN--KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDI 399
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILID---------------GVDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVID--YLREesemakekdgtSIS-VTQllERFLFpSAThgkkVYK--LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:cd03228 67 RDLDleSLRK-----------NIAyVPQ--DPFLF-SGT----IREniLSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180
....*....|....*....|....*
gi 1842088001 475 TETLTILEDYIDDFGG--SVITVSH 497
Cdd:cd03228 129 PETEALILEALRALAKgkTVIVIAH 153
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-234 |
2.35e-24 |
|
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: 102.13 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDEDftaDITHPNQYRI------ 70
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflrptsgsvlFDGE---DITGLPPHEIarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RySSQKQDLNGHMTVFEAVLssdtptlriikkyeeaVNRYALDQSDSNFNKMMEAQEEMDQKdawdynaeIKTILSKLGI 150
Cdd:cd03219 79 R-TFQIPRLFPELTVLENVM----------------VAAQARTGSGLLLARARREEREARER--------AEELLERVGL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 151 HDTTKKIV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPT---NHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRI 226
Cdd:cd03219 134 ADLADRPAgELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRV 213
|
....*...
gi 1842088001 227 IELDRGKL 234
Cdd:cd03219 214 TVLDQGRV 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-227 |
2.87e-24 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 102.48 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIE--HLNKSYA----DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFT-------ADITHPNQ 67
Cdd:COG1116 1 MSAAAPALElrGVSKRFPtgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSgevlvdgKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 68 yRIRYSSQKQDLNGHMTVFEAVlssdtptlriikkyeeavnRYALdqsdsnfnkmmeaqeEMDQKDAWDYNAEIKTILSK 147
Cdd:COG1116 81 -DRGVVFQEPALLPWLTVLDNV-------------------ALGL---------------ELRGVPKAERRERARELLEL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 148 LGIHDTTKKIV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIR-WLINYVKQYPHTVLFVTHDryfLNE- 221
Cdd:COG1116 126 VGLAGFEDAYPhQLSGGMRQRVAIARALANDPEVLLMDEPFGALDAltrERLQdELLRLWQETGKTVLFVTHD---VDEa 202
|
....*...
gi 1842088001 222 --VSTRII 227
Cdd:COG1116 203 vfLADRVV 210
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
7-234 |
4.53e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 101.67 E-value: 4.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQyRIR--- 71
Cdd:COG3638 4 ELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLveptsgeilvdGQDVTALRGRALR-RLRrri 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 -YSSQKQDLNGHMTVFEAVLS---SDTPTLR-IIKKYEEAVNRYALDqsdsnfnkmmeaqeemdqkdawdynaeiktILS 146
Cdd:COG3638 83 gMIFQQFNLVPRLSVLTNVLAgrlGRTSTWRsLLGLFPPEDRERALE------------------------------ALE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 147 KLGIHDT-TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHD-----R 216
Cdd:COG3638 133 RVGLADKaYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedgiTVVVNLHQvdlarR 212
|
250
....*....|....*...
gi 1842088001 217 YFlnevsTRIIELDRGKL 234
Cdd:COG3638 213 YA-----DRIIGLRDGRV 225
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
7-233 |
4.56e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.22 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQYRiryssQ 75
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLeepdsgtitvdGEDLTDSKKDINKLR-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 K-----QDLN--GHMTVFEAVlssdTPTLRIIKKyeeavnryaldqsdsnfnkmmeaqeeMDQKDAwdyNAEIKTILSKL 148
Cdd:COG1126 78 KvgmvfQQFNlfPHLTVLENV----TLAPIKVKK--------------------------MSKAEA---EERAMELLERV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHD-TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVST 224
Cdd:COG1126 125 GLADkADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKegmTMVVVTHEMGFAREVAD 204
|
....*....
gi 1842088001 225 RIIELDRGK 233
Cdd:COG1126 205 RVVFMDGGR 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-234 |
7.53e-24 |
|
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: 100.49 E-value: 7.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEaykIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYRIR 71
Cdd:cd03296 1 MSIE---VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILfggedatdvPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVLSSdtptLRIiKKYEEAVNRYALDQSDSNFNKMMEaqeemdqkdawdynaeiktiLSKLGih 151
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFG----LRV-KPRSERPPEAEIRAKVHELLKLVQ--------------------LDWLA-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 dtTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:cd03296 131 --DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVV 208
|
....*..
gi 1842088001 228 ELDRGKL 234
Cdd:cd03296 209 VMNKGRI 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-234 |
1.84e-23 |
|
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: 99.23 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITH--PNQYRIRYSSQK 76
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF-ETPTSgeilldgkDITNlpPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGHMTVFEAVLSSdtptLRIIKKYEEAVNRyaldqsdsnfnKMMEAQEemdqkdawdynaeiktiLSKLGIHDTtKK 156
Cdd:cd03300 81 YALFPHLTVFENIAFG----LRLKKLPKAEIKE-----------RVAEALD-----------------LVQLEGYAN-RK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:cd03300 128 PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelgiTFVFVTHDQEEALTMSDRIAVMNKG 207
|
..
gi 1842088001 233 KL 234
Cdd:cd03300 208 KI 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-234 |
3.55e-23 |
|
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: 103.44 E-value: 3.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-----DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITHPNQYRIRYS 73
Cdd:COG1123 262 EVRNLSKRYPvrgkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL-LRPTSgsilfdgkDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 SQK-----QD----LNGHMTVFEAVlssdtptlriikkyEEAvnryaldqsdsnfnkmMEAQEEMDQKDAWDynaEIKTI 144
Cdd:COG1123 341 RRRvqmvfQDpyssLNPRMTVGDII--------------AEP----------------LRLHGLLSRAERRE---RVAEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LSKLGIHDT--TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESIRW-----LINYVKQYPHTVLFVTHDRY 217
Cdd:COG1123 388 LERVGLPPDlaDRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD-VSVQAqilnlLRDLQRELGLTYLFISHDLA 466
|
250
....*....|....*..
gi 1842088001 218 FLNEVSTRIIELDRGKL 234
Cdd:COG1123 467 VVRYIADRVAVMYDGRI 483
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-234 |
3.83e-23 |
|
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: 98.34 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDED-------FTADITHPNQ---YRIRYSS--- 74
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPdsgevliDGEDISGLSEaelYRLRRRMgml 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 -QKQDLNGHMTVFEAVlssdtptlriikkyeeAVNRYaldqsdsnfnkmmeaqeEMDQKDAWDYNAEIKTILSKLGIHDT 153
Cdd:cd03261 83 fQSGALFDSLTVFENV----------------AFPLR-----------------EHTRLSEEEIREIVLEKLEAVGLRGA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQ-YPHTVLFVTHDRYFLNEVSTRIIE 228
Cdd:cd03261 130 EDLYPaELSGGMKKRVALARALALDPELLLYDEPTAGLDpiaSGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAV 209
|
....*.
gi 1842088001 229 LDRGKL 234
Cdd:cd03261 210 LYDGKI 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-234 |
5.39e-23 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 97.33 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYRIRYSSQKQ 77
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggrdvtdLPPKDRDIAMVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSSdtptLRIIKKYEEAVNRyaldqsdsnfnKMMEAqeemdqkdawdynAEIktilskLGI-HDTTKK 156
Cdd:cd03301 82 ALYPHMTVYDNIAFG----LKLRKVPKDEIDE-----------RVREV-------------AEL------LQIeHLLDRK 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:cd03301 128 PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
..
gi 1842088001 233 KL 234
Cdd:cd03301 208 QI 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
322-520 |
7.03e-23 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 97.20 E-value: 7.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkQTEKTLDRDIR 400
Cdd:cd03259 2 ELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDV------TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VI--DY---------------LREESEMAKEKDgtsISVTQLLERFLFpSATHGKKVYKLSGGEQKRLYLLRLLVHKPNV 463
Cdd:cd03259 76 MVfqDYalfphltvaeniafgLKLRGVPKAEIR---ARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 464 LLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHDR---YFL-NKVVqeywFIHDGKIEKI 520
Cdd:cd03259 152 LLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQeeaLALaDRIA----VMNEGRIVQV 212
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
333-590 |
9.72e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 102.94 E-value: 9.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDRDI--RVIDYLRE--- 407
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPAleYVIDGDREyrq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 408 -ESEM--AKEK-DGTSIS-----------------VTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLL 466
Cdd:PRK10636 94 lEAQLhdANERnDGHAIAtihgkldaidawtirsrAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 467 DEPTNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGsfeDYESFkkEHERQAMLSkqtEQ 546
Cdd:PRK10636 174 DEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTG---NYSSF--EVQRATRLA---QQ 245
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1842088001 547 QNKHKHQPKKKTGL-SYKEKLEYETimTRIEMTETRLEDLEQ-EMI 590
Cdd:PRK10636 246 QAMYESQQERVAHLqSYIDRFRAKA--TKAKQAQSRIKMLERmELI 289
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
322-537 |
1.15e-22 |
|
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: 97.57 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSI-----NNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQtektL 395
Cdd:COG1124 3 EVRNLSVSYgqggrRVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdGRPVTRRRRKA----F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRDIRVI--DY-----------------LREESEMAKEKDgtsisVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRL 456
Cdd:COG1124 78 RRRVQMVfqDPyaslhprhtvdrilaepLRIHGLPDREER-----IAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 457 LVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKIEKIIGSFEDYE 528
Cdd:COG1124 153 LILEPELLLLDEPTSALDvsvqAEILNLLKDLREERGLTYLFVSHDlavvAHLCDRVA----VMQNGRIVEELTVADLLA 228
|
....*....
gi 1842088001 529 SFKKEHERQ 537
Cdd:COG1124 229 GPKHPYTRE 237
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
322-517 |
1.28e-22 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 96.63 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN-KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkqTEKTLdRDI 399
Cdd:COG1122 2 ELENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDI-------TKKNL-REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 R------------------VID-------YLREESEMAKEKdgtsisVTQLLERFlfpSATH--GKKVYKLSGGEQKRLY 452
Cdd:COG1122 74 RrkvglvfqnpddqlfaptVEEdvafgpeNLGLPREEIRER------VEEALELV---GLEHlaDRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnkeGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-234 |
3.33e-22 |
|
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: 95.71 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL----------------DEDFTADITHPNQYRIR 71
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipgapdegevlldGKDIYDLDVDVLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNG-HMTVFEAVlsSDTPTLRIIKKYEEavnryaldqsdsnfnkMMEAQEEMDQKDA-WDynaEIKTILSKLG 149
Cdd:cd03260 83 VGMVFQKPNPfPGSIYDNV--AYGLRLHGIKLKEE----------------LDERVEEALRKAAlWD---EVKDRLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 150 ihdttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQyPHTVLFVTHD-----Ryflne 221
Cdd:cd03260 142 ----------LSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEELIAELKK-EYTIVIVTHNmqqaaR----- 205
|
250
....*....|...
gi 1842088001 222 VSTRIIELDRGKL 234
Cdd:cd03260 206 VADRTAFLLNGRL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-215 |
5.17e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 97.84 E-value: 5.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITH--PNQYRIRY 72
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGL-EDPTSgeiliggrDVTDlpPKDRNIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 73 SSQKQDLNGHMTVFEAVLSSdtptLRIIKkyeeavnryaldqsdsnfnkmmEAQEEMDQKdawdynaeIKTILSKLGIHD 152
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFP----LKLRK----------------------VPKAEIDRR--------VREAAELLGLED 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 153 T-TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFEsIRW-----LINYVKQYPHTVLFVTHD 215
Cdd:COG3839 126 LlDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK-LRVemraeIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-234 |
7.53e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 93.82 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYRIRYSSQKQ 77
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITfdgksyqknIEALRRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSSDTptLRIIKKyeeavnryaldqsdsnfnkmmeaqeemdqkdawdynAEIKTILSKLGIHDTTKKI 157
Cdd:cd03268 82 GFYPNLTARENLRLLAR--LLGIRK------------------------------------KRIDEVLDVVGLKDSAKKK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRW---LINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:cd03268 124 VKgFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKElreLILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
.
gi 1842088001 234 L 234
Cdd:cd03268 204 L 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
322-526 |
7.58e-22 |
|
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: 94.88 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtVKVAYFKQTEKTLDR---- 397
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDG-EDISGLSEAELYRLRrrmg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 ----------DIRVID----YLREESEMAKEkdgtSIS--VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKP 461
Cdd:cd03261 81 mlfqsgalfdSLTVFEnvafPLREHTRLSEE----EIReiVLEKLEAVGLRGAED-LYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 462 NVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEkIIGSFED 526
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV-AEGTPEE 223
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-237 |
9.96e-22 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 97.03 E-value: 9.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 2 SMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNg 81
Cdd:TIGR03265 1 SSPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 hmTVFEA-VLssdTPTLRIIKKYEeavnrYALdqsdsnFNKMMEAqEEMDQKdawdynaeIKTILSKLGIHDTTKKI-VE 159
Cdd:TIGR03265 80 --IVFQSyAL---FPNLTVADNIA-----YGL------KNRGMGR-AEVAER--------VAELLDLVGLPGSERKYpGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYV-KQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLK 235
Cdd:TIGR03265 135 LSGGQQQRVALARALATSPGLLLLDEPLSALDArvrEHLRTEIRQLqRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
..
gi 1842088001 236 TY 237
Cdd:TIGR03265 215 QV 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-233 |
1.26e-21 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 92.06 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD--KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRyssqkqdLNGHMt 84
Cdd:cd03228 2 EFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD--------PTSGEIL-------IDGVD- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 vfeavlssdtptlriIKKYEEAVNRYA---LDQsdsnfnkmmeaqeemdqkDAWDYNAeikTILSKLgihdttkkiveLS 161
Cdd:cd03228 66 ---------------LRDLDLESLRKNiayVPQ------------------DPFLFSG---TIRENI-----------LS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHdRYFLNEVSTRIIELDRGK 233
Cdd:cd03228 99 GGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAkgKTVIVIAH-RLSTIRDADRIIVLDDGR 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
322-476 |
2.43e-21 |
|
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: 92.64 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRrIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK---------VAYFKQt 391
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGYLPQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDIRVIDYLREESEMAKEKDGTSIS-VTQLLERF-LFPSAThgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEP 469
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKArVDEVLELVnLGDRAK--KKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
....*..
gi 1842088001 470 TNDLDTE 476
Cdd:cd03264 158 TAGLDPE 164
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-235 |
2.50e-21 |
|
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: 92.64 E-value: 2.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHeRIGLVGINGTGKSTLLKVIGGLDEDFTADIT--------HPNQYR--IRYSSQK 76
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLRrrIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGHMTVFEAVlssdtptlriikkyeeavnRYaldqsdsnfnkmMEAQEEMDQKDAwdyNAEIKTILSKLGIHDT-TK 155
Cdd:cd03264 81 FGVYPNFTVREFL-------------------DY------------IAWLKGIPSKEV---KARVDEVLELVNLGDRaKK 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWLINYVKQyPHTVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:cd03264 127 KIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEeriRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKG 205
|
...
gi 1842088001 233 KLK 235
Cdd:cd03264 206 KLV 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
7-234 |
4.33e-21 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 92.75 E-value: 4.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQ--------------YRIR 71
Cdd:TIGR02315 3 EVENLSKVYpNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTditklrgkklrklrRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVLS---SDTPTLRIIkkyeeavnryaldqsdsnFNKMMEAQEEmdqkdawdynaEIKTILSKL 148
Cdd:TIGR02315 83 MIFQHYNLIERLTVLENVLHgrlGYKPTWRSL------------------LGRFSEEDKE-----------RALSALERV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHD-TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVS 223
Cdd:TIGR02315 134 GLADkAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKedgiTVIINLHQVDLAKKYA 213
|
250
....*....|.
gi 1842088001 224 TRIIELDRGKL 234
Cdd:TIGR02315 214 DRIVGLKAGEI 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-234 |
1.15e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 91.61 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEaykIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKV-------------IGGLDEDFTadiTHPNQ 67
Cdd:COG4161 1 MSIQ---LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVlnlletpdsgqlnIAGHQFDFS---QKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 68 YRIRYSSQK-----QDLN--GHMTVFEAVLSSDTPTLRIIKKyeeavnryaldqsdsnfnkmmEAQEEMDQkdawdynae 140
Cdd:COG4161 75 KAIRLLRQKvgmvfQQYNlwPHLTVMENLIEAPCKVLGLSKE---------------------QAREKAMK--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 141 iktILSKLGIHDTTKKI-VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDR 216
Cdd:COG4161 125 ---LLARLRLTDKADRFpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEV 201
|
250
....*....|....*...
gi 1842088001 217 YFLNEVSTRIIELDRGKL 234
Cdd:COG4161 202 EFARKVASQVVYMEKGRI 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-215 |
1.25e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHM--TVFEAVls 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDSLplTVRDLV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 92 sdtptlriikkyeeAVNRYA-------LDQSDsnfnkmmeaqeemdqkdawdyNAEIKTILSKLGIHDTTKK-IVELSGG 163
Cdd:NF040873 79 --------------AMGRWArrglwrrLTRDD---------------------RAAVDDALERVGLADLAGRqLGELSGG 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 164 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHD 215
Cdd:NF040873 124 QRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD 178
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-503 |
1.37e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 96.03 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 34 IGLVGINGTGKSTLLKVI--------GGLDEDFTAD--ITHpnqYRirySSQKQDLnghmtvFEAVLSSDtptLRIIKK- 102
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDevLKR---FR---GTELQNY------FKKLYNGE---IKVVHKp 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 103 -YEEAVNRYaldqsdsnFN-KMMEAQEEMDQKDAWDYnaeiktILSKLGI-HDTTKKIVELSGGQQKRVVLAKTLIEQPD 179
Cdd:PRK13409 167 qYVDLIPKV--------FKgKVRELLKKVDERGKLDE------VVERLGLeNILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 180 LLLLDEPTNHLDfesIRWLINYVK-----QYPHTVLFVTHDRYFLNEVSTrIIELDRGKlktyPGNY----EDYIVMRAE 250
Cdd:PRK13409 233 FYFFDEPTSYLD---IRQRLNVARlirelAEGKYVLVVEHDLAVLDYLAD-NVHIAYGE----PGAYgvvsKPKGVRVGI 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 251 NELVEQkqqekqkalYKQElawmragakarttkQQARInRFNQLESDVKTQHTQDKGELNLAYSrlgkqvyelkNLSKSI 330
Cdd:PRK13409 305 NEYLKG---------YLPE--------------ENMRI-RPEPIEFEERPPRDESERETLVEYP----------DLTKKL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 331 NNKVLFEDVTEIIQsGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkIGQTVKVAYFKQTEKTlDRDIRVIDYLReese 410
Cdd:PRK13409 351 GDFSLEVEGGEIYE-GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGE--VDPELKISYKPQYIKP-DYDGTVEDLLR---- 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 411 MAKEKDGTSISVTQLLERFLFPSaTHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE----TLTILEDYID 486
Cdd:PRK13409 423 SITDDLGSSYYKSEIIKPLQLER-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlaVAKAIRRIAE 501
|
490
....*....|....*..
gi 1842088001 487 DFGGSVITVSHDRYFLN 503
Cdd:PRK13409 502 EREATALVVDHDIYMID 518
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
7-344 |
2.27e-20 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 95.24 E-value: 2.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQdlnghmtvF 86
Cdd:PRK10636 314 KMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQ--------L 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPTLRIIKKyeeavnryaldqsdsnfnkmmeAQEEMDQKdawdynaeIKTILSKLGIH--DTTKKIVELSGGQ 164
Cdd:PRK10636 386 EFLRADESPLQHLARL----------------------APQELEQK--------LRDYLGGFGFQgdKVTEETRRFSGGE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTYPGNYEDY 244
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 245 ivmraENELVEQKQQEKQKALYKQElawmRAGAKARTTKQQARinrfnqLESDVKTQHTQDKGELNLAYSRLGKQVYELK 324
Cdd:PRK10636 516 -----QQWLSDVQKQENQTDEAPKE----NNANSAQARKDQKR------REAELRTQTQPLRKEIARLEKEMEKLNAQLA 580
|
330 340
....*....|....*....|....*
gi 1842088001 325 NLSKSINNKVLFE-----DVTEIIQ 344
Cdd:PRK10636 581 QAEEKLGDSELYDqsrkaELTACLQ 605
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-234 |
3.11e-20 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 89.57 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEI--FNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRY----SSQ--KQDLNGHM-- 83
Cdd:cd03245 11 SYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK--------PTSGSVLLdgtdIRQldPADLRRNIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 -----TVFEAVLSsDTPTLRiikkyeeavNRYALDQsdsnfnKMMEAqeemdqkdawdynAEIktilskLGIHDTTKK-- 156
Cdd:cd03245 83 vpqdvTLFYGTLR-DNITLG---------APLADDE------RILRA-------------AEL------AGVTDFVNKhp 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 ------IVE----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHTVLFVTHDRYFLNEVSt 224
Cdd:cd03245 128 ngldlqIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITHRPSLLDLVD- 206
|
250
....*....|
gi 1842088001 225 RIIELDRGKL 234
Cdd:cd03245 207 RIIVMDSGRI 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
7-234 |
3.92e-20 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 94.45 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSY--ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRYSSQ------KQD 78
Cdd:COG4987 335 ELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD--------PQSGSITLGGVdlrdldEDD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 79 LNGHMtvfeAVLSSDTP----TLRiikkyeeaVN-RYALDqsdsnfnkmmEAQEEmdqkdawdynaEIKTILSKLGIHDT 153
Cdd:COG4987 407 LRRRI----AVVPQRPHlfdtTLR--------ENlRLARP----------DATDE-----------ELWAALERVGLGDW 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIVE------------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHTVLFVTHDRYFL 219
Cdd:COG4987 454 LAALPDgldtwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGRTVLLITHRLAGL 533
|
250
....*....|....*
gi 1842088001 220 NEVsTRIIELDRGKL 234
Cdd:COG4987 534 ERM-DRILVLEDGRI 547
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-233 |
4.04e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 92.70 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNG------ 81
Cdd:PRK09452 17 LRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTvfqsya 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 ---HMTVFEAVL----SSDTPTLRIIKKYEEAVnryaldqsdsnfnKMMEAqEEMDQKdawdynaeiktilsklgihdtt 154
Cdd:PRK09452 97 lfpHMTVFENVAfglrMQKTPAAEITPRVMEAL-------------RMVQL-EEFAQR---------------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 kKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIELD 230
Cdd:PRK09452 141 -KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklgiTFVFVTHDQEEALTMSDRIVVMR 219
|
...
gi 1842088001 231 RGK 233
Cdd:PRK09452 220 DGR 222
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-234 |
5.95e-20 |
|
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: 93.67 E-value: 5.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYR--IRYSSQ 75
Cdd:COG4988 339 LEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvdlsdlDPASWRrqIAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 kqdlngHMTVFEAvlssdtpTLRiikkyeEAVNRYALDQSDSnfnKMMEAqeeMDQKDAWDYnaeIKTILSKLgihDTtk 155
Cdd:COG4988 419 ------NPYLFAG-------TIR------ENLRLGRPDASDE---ELEAA---LEAAGLDEF---VAALPDGL---DT-- 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVE----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHDRYFLNEVStRIIEL 229
Cdd:COG4988 466 PLGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAkgRTVILITHRLALLAQAD-RILVL 544
|
....*
gi 1842088001 230 DRGKL 234
Cdd:COG4988 545 DDGRI 549
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
322-526 |
8.41e-20 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 88.88 E-value: 8.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNIL--------------------SNEDQDYEGELKIG- 380
Cdd:COG1127 7 EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIigllrpdsgeilvdgqditgLSEKELYELRRRIGm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 381 --Q--------TVK--VAYFKQTEKTLDRD-IRvidylreesEMAKEKdgtsisvtqlLERF-------LFPSAthgkkv 440
Cdd:COG1127 87 lfQggalfdslTVFenVAFPLREHTDLSEAeIR---------ELVLEK----------LELVglpgaadKMPSE------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 441 ykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:COG1127 142 --LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
250
....*....|
gi 1842088001 517 IEkIIGSFED 526
Cdd:COG1127 220 II-AEGTPEE 228
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-254 |
8.70e-20 |
|
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: 88.93 E-value: 8.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDlNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDEdftADITH--PNQYRIRYSS 74
Cdd:cd03299 2 KVENLSKDWKEFKLKNV-SLEVERGDYFVILGPTGSGKSVLLETIAGfikpdsgkilLNG---KDITNlpPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGHMTVFEAVlssdtptlriikkyeeavnRYALdqsdsnfNKMMEAQEEMDQKdawdynaeIKTILSKLGI-HDT 153
Cdd:cd03299 78 QNYALFPHMTVYKNI-------------------AYGL-------KKRKVDKKEIERK--------VLEIAEMLGIdHLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYV-KQYPHTVLFVTHDRYFLNEVSTRIIEL 229
Cdd:cd03299 124 NRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
250 260
....*....|....*....|....*
gi 1842088001 230 DRGKLKTYpGNYEDyIVMRAENELV 254
Cdd:cd03299 204 LNGKLIQV-GKPEE-VFKKPKNEFV 226
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
323-594 |
1.20e-19 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 93.39 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDyeGELKIGQTVKVAYFKQTEKT------LD 396
Cdd:PLN03073 180 MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAID--GIPKNCQILHVEQEVVGDDTtalqcvLN 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDYLREESEMAK----------------------EKDGTSISVTQLLERF-------------------LFPSAT 435
Cdd:PLN03073 258 TDIERTQLLEEEAQLVAqqrelefetetgkgkgankdgvDKDAVSQRLEEIYKRLelidaytaearaasilaglSFTPEM 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 436 HGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDG 515
Cdd:PLN03073 338 QVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 516 KIEKIIGSFEDYESFKKEHERQAMLSKQTEQQNKHKHQpkkktglSYKEKLEYETimTRIEMTETRLEDLEQ-----EMI 590
Cdd:PLN03073 418 KLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQ-------AFIDKFRYNA--KRASLVQSRIKALDRlghvdAVV 488
|
....
gi 1842088001 591 NASD 594
Cdd:PLN03073 489 NDPD 492
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
320-503 |
1.28e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 88.68 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYfKQTE------- 392
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADW-SPAElarrrav 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 ----KTLDRDIRVidylREESEM-------AKEKDGTSIS-------VTQLLERFlFPSathgkkvykLSGGEQKRLYLL 454
Cdd:PRK13548 81 lpqhSSLSFPFTV----EEVVAMgraphglSRAEDDALVAaalaqvdLAHLAGRD-YPQ---------LSGGEQQRVQLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 455 RLLV------HKPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHDryfLN 503
Cdd:PRK13548 147 RVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHD---LN 202
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-237 |
1.68e-19 |
|
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: 87.56 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQyRIRYS 73
Cdd:cd03263 2 QIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrptsgtayinGYSIRTDRKAARQ-SLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 SQKQDLNGHMTVFEavlssdtpTLRIikkyeeavnrYALDQSDSNfnkmmeaqeemdqkdaWDYNAEIKTILSKLGIHD- 152
Cdd:cd03263 81 PQFDALFDELTVRE--------HLRF----------YARLKGLPK----------------SEIKEEVELLLRVLGLTDk 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIR--W-LINYVKQyPHTVLFVTHDryfLNEV---STRI 226
Cdd:cd03263 127 ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRaiWdLILEVRK-GRSIILTTHS---MDEAealCDRI 202
|
250
....*....|.
gi 1842088001 227 IELDRGKLKTY 237
Cdd:cd03263 203 AIMSDGKLRCI 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-256 |
1.77e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.53 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKqdLNGHMtvf 86
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRL--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eAVLSSDTPTLRIIKkYEEAVNrYALDQSDSNFNKMMEAQEEMDQKdawdynAEIKTILSKLGihdtTKKIVELSGGQQK 166
Cdd:PRK11231 79 -ALLPQHHLTPEGIT-VRELVA-YGRSPWLSLWGRLSAEDNARVNQ------AMEQTRINHLA----DRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRwLINYVKQYPHTVLFVTHDryfLNEVStriieldrgklktypgNYE 242
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDInhqvELMR-LMRELNTQGKTVVTVLHD---LNQAS----------------RYC 205
|
250
....*....|....
gi 1842088001 243 DYIVMRAENELVEQ 256
Cdd:PRK11231 206 DHLVVLANGHVMAQ 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
9-234 |
1.85e-19 |
|
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: 87.46 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 9 EHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTA-------DITHPNQYRIRYSSQK---- 76
Cdd:cd03292 4 INVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGtirvngqDVSDLRGRAIPYLRRKigvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 -QD--LNGHMTVFEAVLSSdtptLRIIKKYEEAVNRyaldqsdsnfnKMMEAQEEMDQKDAWDYNAEiktilsklgihdt 153
Cdd:cd03292 84 fQDfrLLPDRNVYENVAFA----LEVTGVPPREIRK-----------RVPAALELVGLSHKHRALPA------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 tkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIELD 230
Cdd:cd03292 136 -----ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKagtTVVVATHAKELVDTTRHRVIALE 210
|
....
gi 1842088001 231 RGKL 234
Cdd:cd03292 211 RGKL 214
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-503 |
2.58e-19 |
|
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: 91.77 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 34 IGLVGINGTGKSTLLKVIGG--------LDEDFTADithpnqyRI--RYS-SQKQDLnghmtvFEAVLSSDtptLRIIKK 102
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGelkpnlgdYDEEPSWD-------EVlkRFRgTELQDY------FKKLANGE---IKVAHK 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 103 --YEEAVNRYaldqsdsnFN-KMMEAQEEMDQKDAWDYnaeiktILSKLGI-HDTTKKIVELSGGQQKRVVLAKTLIEQP 178
Cdd:COG1245 166 pqYVDLIPKV--------FKgTVRELLEKVDERGKLDE------LAEKLGLeNILDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 179 DLLLLDEPTNHLD-FESIRW--LINYVKQYPHTVLFVTHDRYFLNEVStriieldrgklktypgnyeDYIVMraenelve 255
Cdd:COG1245 232 DFYFFDEPSSYLDiYQRLNVarLIRELAEEGKYVLVVEHDLAILDYLA-------------------DYVHI-------- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 256 qkqqekqkaLYKQElawmraGAKARTTK-QQAR--INRF--------------NQLESDVKTQHTQDKGELNLAYSrlgk 318
Cdd:COG1245 285 ---------LYGEP------GVYGVVSKpKSVRvgINQYldgylpeenvrirdEPIEFEVHAPRREKEEETLVEYP---- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 319 qvyelkNLSKSINNKVLfeDVTE-IIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkIGQTVKVAYFKQTEKTlDR 397
Cdd:COG1245 346 ------DLTKSYGGFSL--EVEGgEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE--VDEDLKISYKPQYISP-DY 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 DIRVIDYLReesEMAKEKDGTSISVTQLLERF----LFPsathgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:COG1245 415 DGTVEEFLR---SANTDDFGSSYYKTEIIKPLglekLLD-----KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
490 500 510
....*....|....*....|....*....|....
gi 1842088001 474 DTE----TLTILEDYIDDFGGSVITVSHDRYFLN 503
Cdd:COG1245 487 DVEqrlaVAKAIRRFAENRGKTAMVVDHDIYLID 520
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-235 |
2.71e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 88.10 E-value: 2.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYrIRYSsqkQDLN 80
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQT-INLV---RDKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 GHMTVFeavlssDTPTLRIIKKYEEAV-NRYALDQSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIHDTT--KKI 157
Cdd:PRK10619 77 GQLKVA------DKNQLRLLRTRLTMVfQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqgKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEegkTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
.
gi 1842088001 235 K 235
Cdd:PRK10619 231 E 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-234 |
4.44e-19 |
|
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: 87.40 E-value: 4.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIRYssQKQDLNG-------------------- 81
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITG--------FYRPTSGRILF--DGRDITGlpphriarlgiartfqnprl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 --HMTVFEAVLSSDTPTLRiikkyeeavnrYALDQSDSNFNKMMEAQEEMDQKdAWDynaeiktILSKLGIHDTTKKIV- 158
Cdd:COG0411 91 fpELTVLENVLVAAHARLG-----------RGLLAALLRLPRARREEREARER-AEE-------LLERVGLADRADEPAg 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPT---NHLDFESIRWLINYVKQ-YPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-234 |
7.33e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.34 E-value: 7.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE---------DFTADITHP---NQYRI 70
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQpeagtirvgDITIDTARSlsqQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQK-----QDLN--GHMTVFEAVLSSDTptlrIIKKyeeavnryaldqsdsnfnkmmEAQEEMDQKDawdynaeiKT 143
Cdd:PRK11264 81 RQLRQHvgfvfQNFNlfPHRTVLENIIEGPV----IVKG---------------------EPKEEATARA--------RE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 144 ILSKLGI---HDTTKKivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRY 217
Cdd:PRK11264 128 LLAKVGLagkETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQekrTMVIVTHEMS 205
|
250
....*....|....*..
gi 1842088001 218 FLNEVSTRIIELDRGKL 234
Cdd:PRK11264 206 FARDVADRAIFMDQGRI 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
322-517 |
7.57e-19 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 85.70 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILsNEDQDYEGELKIGQTVKVAyfkqtektlDRDIRV 401
Cdd:cd03260 2 ELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLL-NRLNDLIPGAPDEGEVLLD---------GKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IDY----LREESEMA------------------------KEKDGTSISVTQLLERF-LFPSATHGKKVYKLSGGEQKRLY 452
Cdd:cd03260 72 LDVdvleLRRRVGMVfqkpnpfpgsiydnvayglrlhgiKLKEELDERVEEALRKAaLWDEVKDRLHALGLSGGQQQRLC 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-304 |
9.19e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 9.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 6 YKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKV-IGGLDED-------FTADITHPNQYRiryssqkQ 77
Cdd:PRK11147 320 FEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADsgrihcgTKLEVAYFDQHR-------A 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSSdtptlriikKYEEAVN---RYALDQ-SDSNFNKMmeaqEEMDQKDAwdynaeiktilsklgihdt 153
Cdd:PRK11147 393 ELDPEKTVMDNLAEG---------KQEVMVNgrpRHVLGYlQDFLFHPK----RAMTPVKA------------------- 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 tkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHDRYFL-NEVSTRIIELDRG 232
Cdd:PRK11147 441 ------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVdNTVTECWIFEGNG 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 233 KLKTYPGNYEDYIVMRAENELVEQKQQEKQKALYKQELAWMRAGAKARTTKQQARIN----RFNQLESDVKTQHTQ 304
Cdd:PRK11147 515 KIGRYVGGYHDARQQQAQYLALKQPAVKKKEEAAAPKAETVKRSSKKLSYKLQRELEqlpqLLEDLEAEIEALQAQ 590
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-234 |
9.62e-19 |
|
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: 86.74 E-value: 9.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIF-----NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSqkqdlnG 81
Cdd:TIGR04521 2 KLKNVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGL---------------LKPTS------G 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEAVLSSDTPT-LRIIKK-------------YEEAVNRyaldqsD-----SNFNKmmeAQEEMDQKdawdynaeIK 142
Cdd:TIGR04521 61 TVTIDGRDITAKKKKkLKDLRKkvglvfqfpehqlFEETVYK------DiafgpKNLGL---SEEEAEER--------VK 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 143 TILSKLGIHDTTKKI--VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK----QYPHTVLFVTHDr 216
Cdd:TIGR04521 124 EALELVGLDEEYLERspFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKrlhkEKGLTVILVTHS- 202
|
250 260
....*....|....*....|.
gi 1842088001 217 yfLNEV---STRIIELDRGKL 234
Cdd:TIGR04521 203 --MEDVaeyADRVIVMHKGKI 221
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
322-498 |
1.14e-18 |
|
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: 85.86 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS-----INNKVLFEdvteiIQSGRRIGIVGPNGAGKTTLLNILSN-----------EDQDYEG-------ELK 378
Cdd:COG0411 6 EVRGLTKRfgglvAVDDVSLE-----VERGEIVGLIGPNGAGKTTLFNLITGfyrptsgrilfDGRDITGlpphriaRLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 379 IG---QTVKV-------------AYFKQTEKTLDRDIRVIDYLREESEMAKEkdgtsisVTQLLERF-LFPSAthGKKVY 441
Cdd:COG0411 81 IArtfQNPRLfpeltvlenvlvaAHARLGRGLLAALLRLPRARREEREARER-------AEELLERVgLADRA--DEPAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 442 KLSGGEQKRLYLLRLLVHKPNVLLLDEPT---NDLDTETLT-ILEDYIDDFGGSVITVSHD 498
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAeLIRRLRDERGITILLIEHD 212
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
284-498 |
1.69e-18 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 89.51 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 284 QQARI--NRFNQLesdVKTQHTQDKGELNLAYSRLGKQVyELKNLSKS--INNKVLFEDVTEIIQSGRRIGIVGPNGAGK 359
Cdd:COG2274 439 QDAKIalERLDDI---LDLPPEREEGRSKLSLPRLKGDI-ELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGK 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 360 TTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDIRVID--YLREesemakekdgtSIS-VTQllERFLF----- 431
Cdd:COG2274 515 STLLKLLLGLYEPTSGRILID---------------GIDLRQIDpaSLRR-----------QIGvVLQ--DVFLFsgtir 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 432 -------PSATHgKKVYK----------------------------LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:COG2274 567 enitlgdPDATD-EEIIEaarlaglhdfiealpmgydtvvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAE 645
|
250 260
....*....|....*....|....
gi 1842088001 477 TLTILEDYIDDFGG--SVITVSHD 498
Cdd:COG2274 646 TEAIILENLRRLLKgrTVIIIAHR 669
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
322-517 |
1.84e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 84.72 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS-INNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------KVAYFKqtek 393
Cdd:COG2884 3 RFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrrEIPYLR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 tldRDIRVI--DY---------------LR----EESEMAKEkdgtsisVTQLLERF-LfpSATHGKKVYKLSGGEQKRL 451
Cdd:COG2884 79 ---RRIGVVfqDFrllpdrtvyenvalpLRvtgkSRKEIRRR-------VREVLDLVgL--SDKAKALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDyIDDFGGSVITVSHDRYFLNK----VVQeywfIHDGKI 517
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETsweiMELLEE-INRRGTTVLIATHDLELVDRmpkrVLE----LEDGRL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
322-497 |
2.23e-18 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 83.87 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------KVAYFKQtEKT 394
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLdiaarnRIGYLPE-ERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 LDRDIRVID---YLREESEMAKEKdgTSISVTQLLERFLFpSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:cd03269 81 LYPKMKVIDqlvYLAQLKGLKKEE--ARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180
....*....|....*....|....*....
gi 1842088001 472 DLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:cd03269 158 GLDPVNVELLKDVIRELaraGKTVILSTH 186
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
345-520 |
2.69e-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: 83.88 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 345 SGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVkvaYFkQTEKTLD---RDiRVIDYLREESEM---------- 411
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LF-DSRKKINlppQQ-RKIGLVFQQYALfphlnvrenl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 -----AKEKDGTSISVTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDY 484
Cdd:cd03297 97 afglkRKRNREDRISVDELLDLL---GLDHllNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 485 ID----DFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKI 520
Cdd:cd03297 174 LKqikkNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
322-517 |
3.18e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 83.42 E-value: 3.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkigQTVKVAYFKQTEKTLDRdIRV 401
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGE----ITFDGKSYQKNIEALRR-IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 I-------DYLREESEM---AKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:cd03268 77 LieapgfyPNLTARENLrllARLLGIRKKRIDEVLDVVGLKDSAK-KKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1842088001 472 DLDTETLTILEDYI---DDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03268 156 GLDPDGIKELRELIlslRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-234 |
3.37e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 84.30 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEaykIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKV-------------IGGLDEDFTadiTHPNQ 67
Cdd:PRK11124 1 MSIQ---LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVlnllemprsgtlnIAGNHFDFS---KTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 68 YRIRYSSQK-----QDLN--GHMTVFEAVLSSDTPTLRIIKKyeeavnryaldqsdsnfnkmmEAQEEMDQkdawdynae 140
Cdd:PRK11124 75 KAIRELRRNvgmvfQQYNlwPHLTVQQNLIEAPCRVLGLSKD---------------------QALARAEK--------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 141 iktILSKLGIHDTTKKI-VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWLINYVKQYPHTVLFVTHDR 216
Cdd:PRK11124 125 ---LLERLRLKPYADRFpLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEitaQIVSIIRELAETGITQVIVTHEV 201
|
250
....*....|....*...
gi 1842088001 217 YFLNEVSTRIIELDRGKL 234
Cdd:PRK11124 202 EVARKTASRVVYMENGHI 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-498 |
4.62e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.84 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSY----ADKEIFNDLNLSISEHERIGLVGINGTGKS-TLLKVIGGLDedfTADITHPnQYRIRYSSQ 75
Cdd:PRK15134 1 MTQPLLAIENLSVAFrqqqTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLP---SPPVVYP-SGDIRFHGE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 kqdlnghmtvfeAVLSSDTPTLRIIKK-------YEEAVNRYALDQSDSNFNKMMEAQEEMDQKDAwdyNAEIKTILSKL 148
Cdd:PRK15134 77 ------------SLLHASEQTLRGVRGnkiamifQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAA---RGEILNCLDRV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDTTKKIV----ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWLINYVKQ-YPHTVLFVTHDryfLN 220
Cdd:PRK15134 142 GIRQAAKRLTdyphQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSvqaQILQLLRELQQeLNMGLLFITHN---LS 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 221 EVStriieldrgKLKtypgnyEDYIVMRaENELVEQKQQEK-----QKALYKQELAWMRAGAKARTTKQQARINRFNQLE 295
Cdd:PRK15134 219 IVR---------KLA------DRVAVMQ-NGRCVEQNRAATlfsapTHPYTQKLLNSEPSGDPVPLPEPASPLLDVEQLQ 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 296 SDVKTQhtqdKGELnlaySRLGKQVYELKNLSKSinnkvlfedvteiIQSGRRIGIVGPNGAGKTT----LLNILSNEDQ 371
Cdd:PRK15134 283 VAFPIR----KGIL----KRTVDHNVVVKNISFT-------------LRPGETLGLVGESGSGKSTtglaLLRLINSQGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 372 -DYEGE----------LKIGQTVKVAyFKQTEKTLDRDIRVIDYLREESEM------AKEKDGTSISVTQllERFLFPSA 434
Cdd:PRK15134 342 iWFDGQplhnlnrrqlLPVRHRIQVV-FQDPNSSLNPRLNVLQIIEEGLRVhqptlsAAQREQQVIAVME--EVGLDPET 418
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 435 THgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK15134 419 RH-RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
13-245 |
9.40e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 82.83 E-value: 9.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 13 KSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYRIRYSS----QKQDL 79
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLivdglkvndPKVDERLIRQEAgmvfQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 NGHMTVFEAVLSSdtpTLRIIKKYEEAVNRYALDqsdsnfnkmmeaqeemdqkdawdynaeiktILSKLGIHDTTKKI-V 158
Cdd:PRK09493 89 FPHLTALENVMFG---PLRVRGASKEEAEKQARE------------------------------LLAKVGLAERAHHYpS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIELDRGKLk 235
Cdd:PRK09493 136 ELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDKGRI- 214
|
250
....*....|
gi 1842088001 236 TYPGNYEDYI 245
Cdd:PRK09493 215 AEDGDPQVLI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-233 |
1.10e-17 |
|
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: 81.94 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---HPNQY----RIRYSSQKQDL 79
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLfdgKPLDIaarnRIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 NGHMTVFEAVLSsdTPTLRIIKKyeeavnRYALDQSDSnfnkmmeaqeemdqkdaWdynaeiktiLSKLGIHD-TTKKIV 158
Cdd:cd03269 82 YPKMKVIDQLVY--LAQLKGLKK------EEARRRIDE-----------------W---------LERLELSEyANKRVE 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:cd03269 128 ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-234 |
1.27e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 80.55 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQyriryssqkqdlnGHMTVF 86
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGL--------YKPDS-------------GEILVD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPtlriikkyeeavnryaldqsdsnfnkmmeaqeemdqKDAWDynaeiktilskLGIhdTTkkIVELSGGQQK 166
Cdd:cd03216 61 GKEVSFASP------------------------------------RDARR-----------AGI--AM--VYQLSVGERQ 89
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHdryFLNEV---STRIIELDRGKL 234
Cdd:cd03216 90 MVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRaqgVAVIFISH---RLDEVfeiADRVTVLRDGRV 160
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-234 |
1.28e-17 |
|
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: 81.77 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTA-------DITH--PNQYRIRYSSQKQDLNGHMTVFEAVLSSD 93
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGrvlingvDVTAapPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 94 TPTLRIikkyeeavnryaldqsdsnfnkmmeaqEEMDQKdawdynaEIKTILSKLGIHDTTKKIV-ELSGGQQKRVVLAK 172
Cdd:cd03298 96 SPGLKL---------------------------TAEDRQ-------AIEVALARVGLAGLEKRLPgELSGGERQRVALAR 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 173 TLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDpalrAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
343-499 |
1.81e-17 |
|
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: 85.80 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQT----EKTLDRDIRVI--DYL 405
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVnGVPLadadadswrdQIAWVPQHpflfAGTIAENIRLArpDAS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 406 REESEMAKEKDGTSISVTQLLERFLFPSATHGKKvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI 485
Cdd:TIGR02857 425 DAEIREALERAGLDEFVAALPQGLDTPIGEGGAG---LSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEAL 501
|
170
....*....|....*.
gi 1842088001 486 DDF--GGSVITVSHDR 499
Cdd:TIGR02857 502 RALaqGRTVLLVTHRL 517
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
322-497 |
3.78e-17 |
|
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: 80.10 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvkvayfkQTEKTLDRDIRV 401
Cdd:TIGR01189 2 AARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGT-------PLAEQRDEPHEN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IDYLREESEM-----AKEK--------DGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:TIGR01189 75 ILYLGHLPGLkpelsALENlhfwaaihGGAQRTIEDALAAVGLTGFED-LPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 1842088001 469 PTNDLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
322-498 |
4.78e-17 |
|
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: 80.94 E-value: 4.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN-----------EDQDYEG-------ELKIGQT- 382
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGflrptsgsvlfDGEDITGlppheiaRLGIGRTf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 383 --------------VKVAYFKQTEKTLDRDIRVidylREESEMAKEkdgtsisVTQLLERF-LFPSAthGKKVYKLSGGE 447
Cdd:cd03219 82 qiprlfpeltvlenVMVAAQARTGSGLLLARAR----REEREARER-------AEELLERVgLADLA--DRPAGELSYGQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 448 QKRLYLLRLLVHKPNVLLLDEPT---NDLDTETLTILEDYIDDFGGSVITVSHD 498
Cdd:cd03219 149 QRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-215 |
5.50e-17 |
|
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: 80.03 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSIS---EHERIGLVGINGTGKSTLLKVIGGLDedfTAD------------------ITHPNQYRIRYSSQKQDLNG 81
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLE---KPDggtivlngtvlfdsrkkiNLPPQQRKIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEAVLssdtptlriikkyeeavnrYALdqsdsnfnKMMEAQEEMDQKDAwdynaeiktILSKLGI-HDTTKKIVEL 160
Cdd:cd03297 89 HLNVRENLA-------------------FGL--------KRKRNREDRISVDE---------LLDLLGLdHLLNRYPAQL 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 161 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQ----YPHTVLFVTHD 215
Cdd:cd03297 133 SGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQikknLNIPVIFVTHD 191
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-234 |
6.57e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDedftaditHPNQyriryssqkqdlnGHMTVFE 87
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLE--------TPSA-------------GELLAGT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 AVLSSDTPTLRIIkkYEEAvnryaldqsdsnfnKMMEAQEEMDQ-----KDAWDYNAEikTILSKLGIHDTTKKI-VELS 161
Cdd:PRK11247 74 APLAEAREDTRLM--FQDA--------------RLLPWKKVIDNvglglKGQWRDAAL--QALAAVGLADRANEWpAALS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----------FESIrWLinyvkQYPHTVLFVTHDryfLNE---VSTRIIE 228
Cdd:PRK11247 136 GGQKQRVALARALIHRPGLLLLDEPLGALDaltriemqdlIESL-WQ-----QHGFTVLLVTHD---VSEavaMADRVLL 206
|
....*.
gi 1842088001 229 LDRGKL 234
Cdd:PRK11247 207 IEEGKI 212
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
322-497 |
7.07e-17 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 80.51 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNED-QDYegelkiGQTVKV--------------- 385
Cdd:COG1119 5 ELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTY------GNDVRLfgerrggedvwelrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 386 ----------AYFKQTEKTLD------RDirVIDYLREESEMAKEKdgtsisVTQLLERFlfpSATH--GKKVYKLSGGE 447
Cdd:COG1119 79 riglvspalqLRFPRDETVLDvvlsgfFD--SIGLYREPTDEQRER------ARELLELL---GLAHlaDRPFGTLSQGE 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 448 QKRLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSH 497
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-240 |
7.07e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 82.77 E-value: 7.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA-----------DIThPNQYRIR 71
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-EDITSgdlfigekrmnDVP-PAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVlsSDTPTLRIIKKyeeavnryaldqsdsnfnkmmeaqEEMDQKdaWDYNAEIKtilsKLGiH 151
Cdd:PRK11000 79 MVFQSYALYPHLSVAENM--SFGLKLAGAKK------------------------EEINQR--VNQVAEVL----QLA-H 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWLINYV-KQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK11000 126 LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAlrvQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKIV 205
|
250 260
....*....|....*....|..
gi 1842088001 228 ELDRGK---------LKTYPGN 240
Cdd:PRK11000 206 VLDAGRvaqvgkpleLYHYPAN 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
322-526 |
7.43e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 84.04 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLS-KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQT-----------VKVAYFK 389
Cdd:COG4988 338 ELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVdlsdldpaswrRQIAWVP 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QTEKTLDRDIRviDYLReeseMAKEkDGTSISVTQLLER-----FL--FPS--ATH-GKKVYKLSGGEQKRLYLLRLLVH 459
Cdd:COG4988 418 QNPYLFAGTIR--ENLR----LGRP-DASDEELEAALEAagldeFVaaLPDglDTPlGEGGRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 460 KPNVLLLDEPTNDLDTETLTILEDYIDDFGGS--VITVSHDRYFLnKVVQEYWFIHDGKIEKiIGSFED 526
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGrtVILITHRLALL-AQADRILVLDDGRIVE-QGTHEE 557
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-256 |
7.79e-17 |
|
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: 80.42 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYR--IRYSS 74
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireQDPVELRrkIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGHMTVFEAVlsSDTPTLriiKKYEEavnryaldqsdsnfnkmmeaqEEMDQKdawdynaeIKTILSKLGIHDTT 154
Cdd:cd03295 82 QQIGLFPHMTVEENI--ALVPKL---LKWPK---------------------EKIRER--------ADELLALVGLDPAE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 ---KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPH-TVLFVTHDryfLNE---VST 224
Cdd:cd03295 128 fadRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDpitRDQLQEEFKRLQQELGkTIVFVTHD---IDEafrLAD 204
|
250 260 270
....*....|....*....|....*....|..
gi 1842088001 225 RIIELDRGKLKTYpGNYEDyIVMRAENELVEQ 256
Cdd:cd03295 205 RIAIMKNGEIVQV-GTPDE-ILRSPANDFVAE 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
7-215 |
8.28e-17 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG-LDEDFTA---------DITH--PNQYRIRYSS 74
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAFSAsgevllngrRLTAlpAEQRRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGHMTVFEAvLSSDTPtlriikkyeEAVNRYALDQsdsnfnKMMEAQEEMDqkdawdynaeiktiLSKLGIHDtt 154
Cdd:COG4136 83 QDDLLFPHLSVGEN-LAFALP---------PTIGRAQRRA------RVEQALEEAG--------------LAGFADRD-- 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 155 kkIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIR-WLINYVKQYPHTVLFVTHD 215
Cdd:COG4136 131 --PATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAalrAQFReFVFEQIRQRGIPALLVTHD 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-215 |
1.08e-16 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 79.80 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADkEIFNdLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTAdiTHPNQYRIRYSSQ 75
Cdd:COG3840 3 RLDDLTYRYGD-FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFlppdsgrilwnGQDLTA--LPPAERPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDLNGHMTVFEAV---LSsdtPTLRiikkyeeavnryaLDQsdsnfnkmmeaqeemDQKdawdynAEIKTILSKLGIHD 152
Cdd:COG3840 79 ENNLFPHLTVAQNIglgLR---PGLK-------------LTA---------------EQR------AQVEQALERVGLAG 121
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 153 -TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHD 215
Cdd:COG3840 122 lLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHD 189
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
322-517 |
1.11e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.16 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIG--------------------Q 381
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrplaawspwelarrravlpQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 382 TVKVAY-FK------------QTEKTLDRDIrVIDYLREesemakekdgtsISVTQLLERFlFPSathgkkvykLSGGEQ 448
Cdd:COG4559 83 HSSLAFpFTveevvalgraphGSSAAQDRQI-VREALAL------------VGLAHLAGRS-YQT---------LSGGEQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 449 KRLYLLRLLV-------HKPNVLLLDEPTNDLDT----ETLTILEDYIDDfGGSVITVSHDryfLN-------KVVqeyw 510
Cdd:COG4559 140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLahqhAVLRLARQLARR-GGGVVAVLHD---LNlaaqyadRIL---- 211
|
....*..
gi 1842088001 511 FIHDGKI 517
Cdd:COG4559 212 LLHQGRL 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-215 |
1.68e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIggldedftADITHPNQYRIRyssqkqdLNGHmtvf 86
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRII--------LGILAPDSGEVL-------WDGE---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eavlssdTPTLRIIKK--Y--EEavnR--YaldqsdsnfnKMMEAQEE---------MDQKDAwdyNAEIKTILSKLGIH 151
Cdd:COG4152 64 -------PLDPEDRRRigYlpEE---RglY----------PKMKVGEQlvylarlkgLSKAEA---KRRADEWLERLGLG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 152 D-TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHD 215
Cdd:COG4152 121 DrANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkgtTVIFSSHQ 188
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-233 |
1.69e-16 |
|
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: 79.02 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFT-------ADITH-PNQYRIR----YSS 74
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSgsirfdgRDITGlPPHERARagigYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGHMTVFEavlssdtpTLRiikkyeeaVNRYALDQSDsnfnkmmeAQEEMDQkdAWDYNAEIKTILSKLGIHdtt 154
Cdd:cd03224 82 EGRRIFPELTVEE--------NLL--------LGAYARRRAK--------RKARLER--VYELFPRLKERRKQLAGT--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 kkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLinyvKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:cd03224 133 -----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLApkiveeiFEAIREL----RDEGVTILLVEQNARFALEIADRAY 203
|
....*.
gi 1842088001 228 ELDRGK 233
Cdd:cd03224 204 VLERGR 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-233 |
1.92e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 79.46 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 4 EAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDedftaditHPNQYRIRY----------- 72
Cdd:COG4598 7 PALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLE--------TPDSGEIRVggeeirlkpdr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 73 ------SSQKQ---------------DLNGHMTVFEAVLSSDTPTLRIIKKyeeavnryaldqsdsnfnkmmEAQEEmdq 131
Cdd:COG4598 79 dgelvpADRRQlqrirtrlgmvfqsfNLWSHMTVLENVIEAPVHVLGRPKA---------------------EAIER--- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 132 kdawdynAEikTILSKLGIHDTTKKI-VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFEsirwLINYV-------K 203
Cdd:COG4598 135 -------AE--ALLAKVGLADKRDAYpAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPE----LVGEVlkvmrdlA 201
|
250 260 270
....*....|....*....|....*....|
gi 1842088001 204 QYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:COG4598 202 EEGRTMLVVTHEMGFARDVSSHVVFLHQGR 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-234 |
1.95e-16 |
|
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: 78.91 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 12 NKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIR------YSSQKQDLNGHMTV 85
Cdd:cd03267 28 KRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSG--------LLQPTSGEVRvaglvpWKRRKKFLRRIGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 F--EAVLSSDTP---TLRIIK-----KYEEAVNRyaLDQsdsnFNKMMEAQEEMDQKdawdynaeiktilsklgihdttk 155
Cdd:cd03267 100 FgqKTQLWWDLPvidSFYLLAaiydlPPARFKKR--LDE----LSELLDLEELLDTP----------------------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 kIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIR-WLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:cd03267 151 -VRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVvaqENIRnFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
...
gi 1842088001 232 GKL 234
Cdd:cd03267 230 GRL 232
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
22-234 |
2.03e-16 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 82.99 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRYS--SQKQ----DLNGHMtvfeAVLSSDTP 95
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL--------YQPTEGSVLLDgvDIRQidpaDLRRNI----GYVPQDPR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 ----TLRiikkyeeavnryaldqsDsnfNKMMEAQEEMDQkdawdynaEIKTILSKLGIHDTTKK--------IVE---- 159
Cdd:TIGR03375 550 lfygTLR-----------------D---NIALGAPYADDE--------EILRAAELAGVTEFVRRhpdgldmqIGErgrs 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH--TVLFVTHDRYFLNEVsTRIIELDRGKL 234
Cdd:TIGR03375 602 LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAgkTLVLVTHRTSLLDLV-DRIIVMDNGRI 677
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
322-520 |
2.15e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 80.96 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAyfkqtEKTLDRDI- 399
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLFTN-----LPPRERRVg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 ----------------------RVIDYLREEsemAKEKdgtsisVTQLLERFlfpSATHGKKVY--KLSGGEQKRLYLLR 455
Cdd:COG1118 79 fvfqhyalfphmtvaeniafglRVRPPSKAE---IRAR------VEELLELV---QLEGLADRYpsQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 456 LLVHKPNVLLLDEPTNDLDTETLTILE----DYIDDFGGSVITVSHDR---YFL-NKVVqeywFIHDGKIEKI 520
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRrwlrRLHDELGGTTVFVTHDQeeaLELaDRVV----VMNQGRIEQV 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
322-497 |
2.38e-16 |
|
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: 76.81 E-value: 2.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLS-KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEktldrdir 400
Cdd:cd03223 2 ELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 vidYLreesemakeKDGTsisvtqLLERFLFPSAThgkkvyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTI 480
Cdd:cd03223 74 ---YL---------PLGT------LREQLIYPWDD------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170
....*....|....*..
gi 1842088001 481 LEDYIDDFGGSVITVSH 497
Cdd:cd03223 130 LYQLLKELGITVISVGH 146
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
339-517 |
2.58e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.11 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 339 VTEIIQSGRRIGIVGPNGAGKTTLLNILSNEdQDYEGELKIGQT-----------VKVAYFKQTEKTLdRDIRVIDYL-- 405
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRplsdwsaaelaRHRAYLSQQQSPP-FAMPVFQYLal 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 406 -REESEMAKEKDGTsisVTQLLERF-----LfpsathGKKVYKLSGGEQKRLYLLR--LLVHkPNV------LLLDEPTN 471
Cdd:COG4138 93 hQPAGASSEAVEQL---LAQLAEALgledkL------SRPLTQLSGGEWQRVRLAAvlLQVW-PTInpegqlLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 472 DLDTETLTILEDYIDDF---GGSVITVSHDryfLNKVVQ---EYWFIHDGKI 517
Cdd:COG4138 163 SLDVAQQAALDRLLRELcqqGITVVMSSHD---LNHTLRhadRVWLLKQGKL 211
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
8-216 |
3.27e-16 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 81.95 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADK-EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFT-------ADITHPN----QYRIRYSSQ 75
Cdd:TIGR02857 324 FSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEgsiavngVPLADADadswRDQIAWVPQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 kqdlngHMTVFEAVLSsdtptlriikkyeEAVNRYALDQSDSnfnkmmEAQEEMDQKDAWDYNAEIKTIL-SKLGIHDTt 154
Cdd:TIGR02857 404 ------HPFLFAGTIA-------------ENIRLARPDASDA------EIREALERAGLDEFVAALPQGLdTPIGEGGA- 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 155 kkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHDR 216
Cdd:TIGR02857 458 ----GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAqgRTVLLVTHRL 517
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-234 |
3.51e-16 |
|
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: 79.85 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 36 LVGINGTGKSTLLKVIGGLDE-DFTA------DITH--PNQYRIRYSSQKQDLNGHMTVFEAVlssdtptlriikkyeea 106
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQpDSGSimldgeDVTNvpPHLRHINMVFQSYALFPHMTVEENV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 107 vnRYALdqsdsnfnkmmeaqeEMDQKDAWDYNAEIKTILSKLGIHD-TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDE 185
Cdd:TIGR01187 64 --AFGL---------------KMRKVPRAEIKPRVLEALRLVQLEEfADRKPHQLSGGQQQRVALARALVFKPKILLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 186 PTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:TIGR01187 127 PLSALDKKLRDQMQLELKTIQEqlgiTFVFVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
322-517 |
4.31e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 4.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfkqTEKTLDRDIR 400
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVdGLKVN------DPKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 -----VID--YL---------------------REESE-MAKE---KDGtsisvtqLLERF-LFPSathgkkvyKLSGGE 447
Cdd:PRK09493 77 qeagmVFQqfYLfphltalenvmfgplrvrgasKEEAEkQAREllaKVG-------LAERAhHYPS--------ELSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 448 QKRLYLLRLLVHKPNVLLLDEPTNDLDT----ETLTILEDYIDDfGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPelrhEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
343-517 |
4.90e-16 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 81.35 E-value: 4.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDIRVIDylreESEMAKekdgtSIS- 421
Cdd:COG4987 358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLG---------------GVDLRDLD----EDDLRR-----RIAv 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 422 VTQ--------LLERFLF--PSATHG------KKVY---------------------KLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:COG4987 414 VPQrphlfdttLRENLRLarPDATDEelwaalERVGlgdwlaalpdgldtwlgeggrRLSGGERRRLALARALLRDAPIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 465 LLDEPTNDLDTET-LTILEDYIDDFGG-SVITVSHDRYFLNKVVQEYwFIHDGKI 517
Cdd:COG4987 494 LLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLERMDRIL-VLEDGRI 547
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
322-517 |
5.24e-16 |
|
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: 76.91 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSIN-NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtVKVAYFKQTEKT------ 394
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN--GKPIKAKERRKSigyvmq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 -LDRDIRVIDYLREESEMAKEKDGTSISVTQLLERfLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:cd03226 79 dVDYQLFTDSVREELLLGLKELDAGNEQAETVLKD-LDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 474 DTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03226 158 DYKNMERVGELIRELaaqGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
318-497 |
7.49e-16 |
|
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: 76.44 E-value: 7.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLSKSINNKV------LFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN--EDQDYEGELKI-GQTVKVAYF 388
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPsksgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLInGRPLDKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 389 KqtektldrdiRVIDYLREEsemakekdgTSISVTQLLERFLFPSAthgkKVYKLSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:cd03213 81 R----------KIIGYVPQD---------DILHPTLTVRETLMFAA----KLRGLSGGERKRVSIALELVSNPSLLFLDE 137
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 469 PTNDLDTET----LTILEDYIDDfGGSVITVSH 497
Cdd:cd03213 138 PTSGLDSSSalqvMSLLRRLADT-GRTIICSIH 169
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-227 |
7.60e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.01 E-value: 7.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 28 ISEHERIGLVGINGTGKSTLLKVIGGL---DE---DFTADIThpnqYRIRYSSQKQDlnghMTVfEAVLSSDTPTLriik 101
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVlkpDEgevDPELKIS----YKPQYIKPDYD----GTV-EDLLRSITDDL---- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 102 kyeeavnryaldqsDSNFnkmmeaqeemdqkdawdYNAEIktiLSKLGIHDT-TKKIVELSGGQQKRVVLAKTLIEQPDL 180
Cdd:PRK13409 429 --------------GSSY-----------------YKSEI---IKPLQLERLlDKNVKDLSGGELQRVAIAACLSRDADL 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 181 LLLDEPTNHLDFE-------SIRwliNYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK13409 475 YLLDEPSAHLDVEqrlavakAIR---RIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-233 |
8.04e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 79.49 E-value: 8.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDedftaditHPNQYRIryssqkqdlnghmtVF 86
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFE--------QPTAGQI--------------ML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPtlriikKYEEAVNryALDQSDSNFNKMMEAQE-----EMDQKDAWDYNAEIKTILSKLGIHDTTK-KIVEL 160
Cdd:PRK11607 79 DGVDLSHVP------PYQRPIN--MMFQSYALFPHMTVEQNiafglKQDKLPKAEIASRVNEMLGLVHMQEFAKrKPHQL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 161 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESIR-----WLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALD-KKLRdrmqlEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
317-533 |
8.41e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 317 GKQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtvKVAYFkqtektlD 396
Cdd:PRK14246 7 AEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYF-------G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDY--LREESEMAKEKDGTSISVTqLLERFLFPSATHG---------------------KKVY--------KLSG 445
Cdd:PRK14246 78 KDIFQIDAikLRKEVGMVFQQPNPFPHLS-IYDNIAYPLKSHGikekreikkiveeclrkvglwKEVYdrlnspasQLSG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGS 523
Cdd:PRK14246 157 GQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
250
....*....|
gi 1842088001 524 FEDYESFKKE 533
Cdd:PRK14246 237 NEIFTSPKNE 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
322-520 |
1.26e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 78.59 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV--------KVAYFKQtE 392
Cdd:PRK10851 4 EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQ-H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTLDRDIRVIDYL---------REESEMA--KEKdgtsisVTQLLE---------RflFPSathgkkvyKLSGGEQKRLY 452
Cdd:PRK10851 83 YALFRHMTVFDNIafgltvlprRERPNAAaiKAK------VTQLLEmvqlahladR--YPA--------QLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKI 520
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQA 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
8-234 |
1.29e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITHPN-QYR-IRYSSQKQ 77
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEgqifidgeDVTHRSiQQRdICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVlssdtptlriikkyeeavnRYALdqsdsnfnKMME-AQEEMDQKdawdynaeIKTILSKLGIHDTTKK 156
Cdd:PRK11432 88 ALFPHMSLGENV-------------------GYGL--------KMLGvPKEERKQR--------VKEALELVDLAGFEDR 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IV-ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF-------ESIRWLinyVKQYPHTVLFVTHDRYFLNEVSTRIIE 228
Cdd:PRK11432 133 YVdQISGGQQQRVALARALILKPKVLLFDEPLSNLDAnlrrsmrEKIREL---QQQFNITSLYVTHDQSEAFAVSDTVIV 209
|
....*.
gi 1842088001 229 LDRGKL 234
Cdd:PRK11432 210 MNKGKI 215
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-227 |
1.30e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 80.21 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 27 SISEHERIGLVGINGTGKSTLLKVIGGLDE------DFTADIThpnqYRIRYSSQKQDlnghMTVfEAVLSSDTPtlrii 100
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKpdegevDEDLKIS----YKPQYISPDYD----GTV-EEFLRSANT----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 101 kkyeeavnryalDQSDSNFnkmmeaqeemdqkdawdYNAEIktiLSKLGIHDT-TKKIVELSGGQQKRVVLAKTLIEQPD 179
Cdd:COG1245 428 ------------DDFGSSY-----------------YKTEI---IKPLGLEKLlDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 180 LLLLDEPTNHLDFES-------IRwliNYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:COG1245 476 LYLLDEPSAHLDVEQrlavakaIR---RFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
8-234 |
1.36e-15 |
|
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: 76.25 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKE----IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSQKQDLNGhm 83
Cdd:cd03266 4 ADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGL---------------LEPDAGFATVDG-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 tvfeavlssdtptLRIIKKYEEAVNRYALDQSDSNFNKMMEAQEEMD--------QKDAwdYNAEIKTILSKLGIHDTTK 155
Cdd:cd03266 67 -------------FDVVKEPAEARRRLGFVSDSTGLYDRLTARENLEyfaglyglKGDE--LTARLEELADRLGMEELLD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:cd03266 132 RRVGgFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRalgKCILFSTHIMQEVERLCDRVVVLHR 211
|
...
gi 1842088001 232 GKL 234
Cdd:cd03266 212 GRV 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
320-517 |
1.40e-15 |
|
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: 76.39 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSI-----NNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKT 394
Cdd:cd03257 1 LLEVKNLSVSFptgggSVKAL-DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 LDRDI---------------RVIDYLRE---ESEMAKEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRL 456
Cdd:cd03257 80 RRKEIqmvfqdpmsslnprmTIGEQIAEplrIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 457 LVHKPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKI 517
Cdd:cd03257 160 LALNPKLLIADEPTSALDVsvqaQILDLLKKLQEELGLTLLFITHDlgvvAKIADRVA----VMYAGKI 224
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
333-517 |
1.45e-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: 76.60 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKvayFKQTEKTLDR-------------DI 399
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVP---WKRRKKFLRRigvvfgqktqlwwDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYLR--------EESEMAKEKDGtsisVTQLL--ERFLFpsathgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEP 469
Cdd:cd03267 111 PVIDSFYllaaiydlPPARFKKRLDE----LSELLdlEELLD------TPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 470 TNDLDTET-LTI---LEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03267 181 TIGLDVVAqENIrnfLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-498 |
1.64e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQT---EKTLDRDI 399
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKlylDTTLPLTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYLREEsemAKEKDgtsisVTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:PRK09544 87 NRFLRLRPG---TKKED-----ILPALKRV---QAGHliDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*
gi 1842088001 478 LTILEDYID----DFGGSVITVSHD 498
Cdd:PRK09544 156 QVALYDLIDqlrrELDCAVLMVSHD 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
322-517 |
1.64e-15 |
|
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: 75.91 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVL-FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------KVAYFKQTEK 393
Cdd:cd03292 2 EFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRDIRVIDYLREESEMA-----KEKDGTSIS--VTQLLERFlfpSATHGKKVY--KLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAfalevTGVPPREIRkrVPAALELV---GLSHKHRALpaELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 465 LLDEPTNDLDTET----LTILEDyIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03292 159 IADEPTGNLDPDTtweiMNLLKK-INKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
227-295 |
2.50e-15 |
|
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: 71.45 E-value: 2.50e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 227 IELDRGKLKTYPGNYEDYIVMRAENELVEQKQQEKQKALYKQELAWM-RAGAKARTTKQ-QARINRFNQLE 295
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIdRFRAKASKAKQaQSRIKALEKME 71
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-517 |
2.67e-15 |
|
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: 75.48 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---------KVAYFKQt 391
Cdd:cd03265 2 EVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDI----------RVIDYLREEsemAKEKdgtsisVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKP 461
Cdd:cd03265 81 DLSVDDELtgwenlyihaRLYGVPGAE---RRER------IDELLDFVGLLEAAD-RLVKTYSGGMRRRLEIARSLVHRP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 462 NVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03265 151 EVLFLDEPTIGLDPQTRAHVWEYIeklkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
25-474 |
2.89e-15 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 78.90 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 25 NLSISEHERIGLVGINGTGKSTLLKVIGG----LDEDFTADITHP-----NQYRIRYSSQKQDLNGHMtvfeavLSSDtp 95
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGelplLSGERQSQFSHItrlsfEQLQKLVSDEWQRNNTDM------LSPG-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 tlriikkyEEAVNRYAldqsdsnfnkmmeaqEEMDQKDAWDyNAEIKTILSKLGI-HDTTKKIVELSGGQQKRVVLAKTL 174
Cdd:PRK10938 95 --------EDDTGRTT---------------AEIIQDEVKD-PARCEQLAQQFGItALLDRRFKYLSTGETRKTLLCQAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 175 IEQPDLLLLDEPTNHLDFESirwlinyVKQYPHTVLFVTHDRYFLNEVSTRIIELdrgklktyPgNYEDYIVMRAENELV 254
Cdd:PRK10938 151 MSEPDLLILDEPFDGLDVAS-------RQQLAELLASLHQSGITLVLVLNRFDEI--------P-DFVQFAGVLADCTLA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 255 EQ--KQQEKQKALYKQeLAWMRAGAKARTTkqqarinrfnqlESDVKTQHTQDKGELNLaysrlgkqvYELKNLSKSINN 332
Cdd:PRK10938 215 ETgeREEILQQALVAQ-LAHSEQLEGVQLP------------EPDEPSARHALPANEPR---------IVLNNGVVSYND 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNED-QDYEGELKI-------GQTV-----KVAYfkqTEKTLDRDI 399
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDLTLfgrrrgsGETIwdikkHIGY---VSSSLHLDY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RV---------------IDYLREESEMAKEKdgtsisVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:PRK10938 350 RVstsvrnvilsgffdsIGIYQAVSDRQQKL------AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLL 423
|
490
....*....|
gi 1842088001 465 LLDEPTNDLD 474
Cdd:PRK10938 424 ILDEPLQGLD 433
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-214 |
2.99e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 77.56 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT-----HPNQYR-----I 70
Cdd:PRK13536 37 MSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITvlgvpVPARARlararI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQKQDLNGHMTVFEAVLssdtptlrIIKKYEEAVNRyaldQSDSNFNKMMEAQEEMDQKDAwdynaeiktilsklgi 150
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLL--------VFGRYFGMSTR----EIEAVIPSLLEFARLESKADA---------------- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 151 hdttkKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTN-------HLDFESIRWLINYVKqyphTVLFVTH 214
Cdd:PRK13536 169 -----RVSDLSGGMKRRLTLARALINDPQLLILDEPTTgldpharHLIWERLRSLLARGK----TILLTTH 230
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
322-498 |
3.07e-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: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS----INNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkqteKTLD 396
Cdd:COG1116 9 ELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdGKPV---------TGPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVI--DY---------------LREESEMAKEKDGTsisVTQLLERF-LfpSATHGKKVYKLSGGEQKRLYLLRLLV 458
Cdd:COG1116 80 PDRGVVfqEPallpwltvldnvalgLELRGVPKAERRER---ARELLELVgL--AGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 459 HKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHD 498
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELlrlwQETGKTVLFVTHD 198
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
334-498 |
3.13e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.19 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 334 VLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQtEKTLDRD--IRVID-------- 403
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-RSEVPDSlpLTVRDlvamgrwa 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 404 ------YLREESEMAkekdgtsisVTQLLERfLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:NF040873 85 rrglwrRLTRDDRAA---------VDDALER-VGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....
gi 1842088001 478 LTILEDYIDDF---GGSVITVSHD 498
Cdd:NF040873 155 RERIIALLAEEharGATVVVVTHD 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
322-517 |
3.85e-15 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 75.30 E-value: 3.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN-KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTEKTLDRDI- 399
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 ------------RVID-------------------YLREESEMAKEkdgtsisvtqLLERF-LFPSAThgKKVYKLSGGE 447
Cdd:cd03256 82 mifqqfnlierlSVLEnvlsgrlgrrstwrslfglFPKEEKQRALA----------ALERVgLLDKAY--QRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 448 QKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHD----RYFLNKVVQeywfIHDGKI 517
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinREEGITVIVSLHQvdlaREYADRIVG----LKDGRI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-470 |
4.04e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.14 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedFTAD------------ITHPNQyrirysSQK-------QDLN-- 80
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGV---YQPDsgeilldgepvrFRSPRD------AQAagiaiihQELNlv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 GHMTVFEAVLSSDTPTlriikkyeeavNRYALDQsdsnfNKMmeaqeemdqkdawdyNAEIKTILSKLGIH-DTTKKIVE 159
Cdd:COG1129 92 PNLSVAENIFLGREPR-----------RGGLIDW-----RAM---------------RRRARELLARLGLDiDPDTPVGD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPT--------NHLdFESIRWLinyvKQYPHTVLFVTHdryFLNEvstrIIEL-D 230
Cdd:COG1129 141 LSVAQQQLVEIARALSRDARVLILDEPTaslterevERL-FRIIRRL----KAQGVAIIYISH---RLDE----VFEIaD 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 231 RgklktypgnyedYIVMRaENELVEQkqqekqkalykqelawmraGAKARTTKQQ---ARINRfnQLESDVKTQHTQDkg 307
Cdd:COG1129 209 R------------VTVLR-DGRLVGT-------------------GPVAELTEDElvrLMVGR--ELEDLFPKRAAAP-- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 308 elnlaysrlGKQVYELKNLSKsinnKVLFEDVT------EIiqsgrrIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-G 380
Cdd:COG1129 253 ---------GEVVLEVEGLSV----GGVVRDVSfsvragEI------LGIAGLVGAGRTELARALFGADPADSGEIRLdG 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 381 QTVK-----------VAYFkqTE--KT----LDRDIR---------------VIDyLREESEMAKEkdgtsisvtqLLER 428
Cdd:COG1129 314 KPVRirsprdairagIAYV--PEdrKGeglvLDLSIRenitlasldrlsrggLLD-RRRERALAEE----------YIKR 380
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1842088001 429 FLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPT 470
Cdd:COG1129 381 LRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
322-533 |
4.87e-15 |
|
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: 74.10 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILsnedqdyegelkigqtVKVAYFKQTEKtldrDIRV 401
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI----------------MGHPKYEVTEG----EILF 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 idylreesemaKEKDGTSISVTqllER--------FLFPSATHGKKV--------YKLSGGEQKRLYLLRLLVHKPNVLL 465
Cdd:cd03217 62 -----------KGEDITDLPPE---ERarlgiflaFQYPPEIPGVKNadflryvnEGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 466 LDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFI-HDGKIEKiIGSFEDYESFKKE 533
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVHVlYDGRIVK-SGDKELALEIEKK 198
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-234 |
5.06e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 74.53 E-value: 5.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIRYSsqkqdlnGHMtv 85
Cdd:PRK10908 3 RFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICG--------IERPSAGKIWFS-------GHD-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTPTLR-----IIKKYEEAVNRYALDqsdsnfNKMME-----AQEEmdqkdawDYNAEIKTILSKLGIHDTTK 155
Cdd:PRK10908 66 ITRLKNREVPFLRrqigmIFQDHHLLMDRTVYD------NVAIPliiagASGD-------DIRRRVSAALDKVGLLDKAK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KI-VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:PRK10908 133 NFpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSD 212
|
...
gi 1842088001 232 GKL 234
Cdd:PRK10908 213 GHL 215
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
7-234 |
5.18e-15 |
|
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: 75.24 E-value: 5.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE------DFTADITHPNQYRIR-----YSSQ 75
Cdd:TIGR03873 3 RLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpdagtvDLAGVDLHGLSRRARarrvaLVEQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDLNGHMTVFEAVLSSDTPTLriikkyeeavNRYALDQSDSNfnkmmEAQEEMdqkdawdynaeiktiLSKLGI-HDTT 154
Cdd:TIGR03873 83 DSDTAVPLTVRDVVALGRIPHR----------SLWAGDSPHDA-----AVVDRA---------------LARTELsHLAD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:TIGR03873 133 RDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDG 212
|
...
gi 1842088001 232 GKL 234
Cdd:TIGR03873 213 GRV 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
322-498 |
5.32e-15 |
|
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: 74.43 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS----INNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkigqtvkVAYFKQTEKTLDR 397
Cdd:cd03293 2 EVRNVSKTygggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGE--------VLVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 DIRVI---DYL--------------------REEsemAKEKdgtsisVTQLLERF-------LFPSAthgkkvykLSGGE 447
Cdd:cd03293 74 DRGYVfqqDALlpwltvldnvalglelqgvpKAE---ARER------AEELLELVglsgfenAYPHQ--------LSGGM 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 448 QKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHD 498
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-230 |
5.43e-15 |
|
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: 75.14 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 27 SISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQKQDLNGHMTVfEAVLSSDTPtlriikkyeea 106
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQYIKADYEGTV-RDLLSSITK----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 107 vnryalDQSDSNFnkmmeaqeemdqkdawdYNAEIKTILSKLGIHDttKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEP 186
Cdd:cd03237 88 ------DFYTHPY-----------------FKTEIAKPLQIEQILD--REVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 187 TNHLDFES-------IRWLINYVKQyphTVLFVTHDRYFLNEVSTRIIELD 230
Cdd:cd03237 143 SAYLDVEQrlmaskvIRRFAENNEK---TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
331-477 |
5.75e-15 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 74.61 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 331 NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYE---GELKI-GQTVKVAYFKQTEKTLDRDIRVIDYL- 405
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKPDQFQKCVAYVRQDDILLPGLt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 406 --------------REESEMAKEKdgtsiSVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:cd03234 98 vretltytailrlpRKSSDAIRKK-----RVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
....*.
gi 1842088001 472 DLDTET 477
Cdd:cd03234 173 GLDSFT 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
322-517 |
6.07e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.41 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTeiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV--------KVAYFKQtE 392
Cdd:COG3840 3 RLDDLTYRYGDFPLRFDLT--IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLtalppaerPVSMLFQ-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTL--------------DRDIRVIDYLREESEMAKEKDGtsisVTQLLERFlfPSAthgkkvykLSGGEQKRLYLLRLLV 458
Cdd:COG3840 80 NNLfphltvaqniglglRPGLKLTAEQRAQVEQALERVG----LAGLLDRL--PGQ--------LSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 459 HKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKI 517
Cdd:COG3840 146 RKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTHDpedaARIADRVL----LVADGRI 208
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-234 |
6.22e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.23 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 6 YKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQ--YRIRYSSQKQDLNGHM 83
Cdd:TIGR02769 12 YRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQdlYQLDRKQRRAFRRDVQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVLSSDTPTLRIikkyeeavnRYALDQSDSNFNKMMEAQEEmdqkdawdynAEIKTILSKLGI--HDTTKKIVELS 161
Cdd:TIGR02769 92 LVFQDSPSAVNPRMTV---------RQIIGEPLRHLTSLDESEQK----------ARIAELLDMVGLrsEDADKLPRQLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-245 |
8.14e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 8.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVI---GGLDEDFT---------ADITHPN-- 66
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmNDLNPEVTitgsivyngHNIYSPRtd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 67 --QYRIRYSSQKQDLNGH-MTVFEAVLSSdtptLRIIKKYEEAVnryaLDQSdsnfnkmmeAQEEMDQKDAWDynaEIKT 143
Cdd:PRK14239 81 tvDLRKEIGMVFQQPNPFpMSIYENVVYG----LRLKGIKDKQV----LDEA---------VEKSLKGASIWD---EVKD 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 144 ILsklgiHDTTkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIR----WLINYVKQYphTVLFVTH----- 214
Cdd:PRK14239 141 RL-----HDSA---LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGkieeTLLGLKDDY--TMLLVTRsmqqa 210
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1842088001 215 ----DR--YFLN----EV-STRIIELDRGKLKTypgnyEDYI 245
Cdd:PRK14239 211 srisDRtgFFLDgdliEYnDTKQMFMNPKHKET-----EDYI 247
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
322-499 |
1.13e-14 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 73.44 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVL-FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------KVAYFKQTEK 393
Cdd:TIGR02673 3 EFHNVSKAYPGGVAaLHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIaGEDVnrlrgrQLPLLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRDIRVIDYLREESEMA-------KEKDGTSISVTQLLERFLFPsatHGKKVY--KLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:TIGR02673 83 VVFQDFRLLPDRTVYENVAlplevrgKKEREIQRRVGAALRQVGLE---HKADAFpeQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1842088001 465 LLDEPTNDLDTET----LTILEDyIDDFGGSVITVSHDR 499
Cdd:TIGR02673 160 LADEPTGNLDPDLseriLDLLKR-LNKRGTTVIVATHDL 197
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
322-497 |
1.32e-14 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 71.69 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayFKQTEKTLDRDIR 400
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVS---FASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VidylreesemakekdgtsisvtqllerflfpsathgkkVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTI 480
Cdd:cd03216 79 M--------------------------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVER 120
|
170 180
....*....|....*....|
gi 1842088001 481 LEDYIDDF---GGSVITVSH 497
Cdd:cd03216 121 LFKVIRRLraqGVAVIFISH 140
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
322-498 |
1.44e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQ 390
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVaGDDVealsaraasrRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 -TEKTLDRDIRVI------------DYLREESEMAKEKDGTSISVTQLLERflfpsathgkKVYKLSGGEQKRLYLLRLL 457
Cdd:PRK09536 85 dTSLSFEFDVRQVvemgrtphrsrfDTWTETDRAAVERAMERTGVAQFADR----------PVTSLSGGERQRVLLARAL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1842088001 458 VHKPNVLLLDEPTNDLD----TETLTILEDYIDDfGGSVITVSHD 498
Cdd:PRK09536 155 AQATPVLLLDEPTASLDinhqVRTLELVRRLVDD-GKTAVAAIHD 198
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
323-498 |
1.44e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvKVAYFKQTEKTLDRDIR-- 400
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-PLAEAREDTRLMFQDARll 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 ----VIDYL--------REESEMAKEKDGTSISVTQllerflFPSAthgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:PRK11247 94 pwkkVIDNVglglkgqwRDAALQALAAVGLADRANE------WPAA--------LSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....
gi 1842088001 469 PTNDLDTETLTILEDYIDDF----GGSVITVSHD 498
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwqqhGFTVLLVTHD 193
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
322-526 |
1.72e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 73.53 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIG---------QTVKVAYFKQtE 392
Cdd:cd03296 4 EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedatdvpvQERNVGFVFQ-H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTLDRDIRVIDYL--------REESEMAKEKDGTSISVTQL--LERFL--FPSathgkkvyKLSGGEQKRLYLLRLLVHK 460
Cdd:cd03296 83 YALFRHMTVFDNVafglrvkpRSERPPEAEIRAKVHELLKLvqLDWLAdrYPA--------QLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 461 PNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKiIGSFED 526
Cdd:cd03296 155 PKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ-VGTPDE 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-554 |
1.84e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKST-------LLKVIGGLDEDFTADITHPNQYRIRYS----SQKQDLNGH--MTVFEAV 89
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSeqsaAQMRHVRGAdmAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 LSSDTPTLRIIKKYEEAVNryaLDQSDSNFNKMMEAQEEMDQKDAwdynAEIKTILSKLGiHdttkkivELSGGQQKRVV 169
Cdd:PRK10261 114 MTSLNPVFTVGEQIAESIR---LHQGASREEAMVEAKRMLDQVRI----PEAQTILSRYP-H-------QLSGGMRQRVM 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 170 LAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQ-YPHTVLFVTHDRYFLNEVSTRIIELDRGKlktypgnyedyi 245
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGE------------ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 246 vmRAENELVEQKQQEKQKALYKQELAWM-RAGAkartTKQQARINRFnQLESDVKTQHTQDKGELNLAYSrlGKQVYELK 324
Cdd:PRK10261 247 --AVETGSVEQIFHAPQHPYTRALLAAVpQLGA----MKGLDYPRRF-PLISLEHPAKQEPPIEQDTVVD--GEPILQVR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 325 NL------SKSINNKV-----LFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTE 392
Cdd:PRK10261 318 NLvtrfplRSGLLNRVtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFnGQRIDTLSPGKLQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 kTLDRDIRVIDYLREESEMAKEKDGTSI-----------------SVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLR 455
Cdd:PRK10261 398 -ALRRDIQFIFQDPYASLDPRQTVGDSImeplrvhgllpgkaaaaRVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIAR 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 456 LLVHKPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFEDYESFK 531
Cdd:PRK10261 477 ALALNPKVIIADEAVSALDVsirgQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
570 580
....*....|....*....|...
gi 1842088001 532 KEHERQAMLSKQTEQQNKHKHQP 554
Cdd:PRK10261 557 HPYTRKLMAAVPVADPSRQRPQR 579
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-234 |
1.95e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.90 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSY--ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSqkqdlnGHMTV 85
Cdd:PRK13635 8 VEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGL---------------LLPEA------GTITV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTpTLRIIKK----YEEAVNRY--ALDQSDSNF---NKMMEaQEEMDQKdawdynaeIKTILSKLGIHD-TTK 155
Cdd:PRK13635 67 GGMVLSEET-VWDVRRQvgmvFQNPDNQFvgATVQDDVAFgleNIGVP-REEMVER--------VDQALRQVGMEDfLNR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLinyVKQYPHTVLFVTHDryfLNEV--STRI 226
Cdd:PRK13635 137 EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDprgrrevLETVRQL---KEQKGITVLSITHD---LDEAaqADRV 210
|
....*...
gi 1842088001 227 IELDRGKL 234
Cdd:PRK13635 211 IVMNKGEI 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
8-215 |
2.24e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNghmtvfe 87
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLD------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 avlssdtPTLRIikkyeeAVNRYALDQSDSNFNKMMEAQEEMdqkdawdyNAEiktilsklgiHDTTKKIVELSGGQQKR 167
Cdd:PRK09544 80 -------TTLPL------TVNRFLRLRPGTKKEDILPALKRV--------QAG----------HLIDAPMQKLSGGETQR 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 168 VVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHT----VLFVTHD 215
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREldcaVLMVSHD 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-227 |
2.35e-14 |
|
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: 74.32 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIF----NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQY---RIRYssQKQDL 79
Cdd:COG0444 3 EVRNLKVYFPTRRGVvkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLP--------PPGItsgEILF--DGEDL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 NgHMT--------------VFEAVLSSDTPTLRIIKKYEEAvnryaldqsdsnfnkmMEAQEEMDQKDAWdynAEIKTIL 145
Cdd:COG0444 73 L-KLSekelrkirgreiqmIFQDPMTSLNPVMTVGDQIAEP----------------LRIHGGLSKAEAR---ERAIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 146 SKLGIHDTTKKI----VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESIRW-----LINYVKQYPHTVLFVTHDR 216
Cdd:COG0444 133 ERVGLPDPERRLdrypHELSGGMRQRVMIARALALEPKLLIADEPTTALD-VTIQAqilnlLKDLQRELGLAILFITHDL 211
|
250
....*....|.
gi 1842088001 217 YFLNEVSTRII 227
Cdd:COG0444 212 GVVAEIADRVA 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
8-234 |
2.43e-14 |
|
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: 72.40 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKST-------LLKVIGGLDEDFTADIT-HPNQYR--IRYSSQKQ 77
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTtikmlttLLKPTSGRATVAGHDVVrEPREVRrrIGIVFQDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSSDtptlRIikkyeeavnrYALdqsdsnfnKMMEAQEEMDQkdawdynaeiktILSKLGIHDTTKKI 157
Cdd:cd03265 83 SVDDELTGWENLYIHA----RL----------YGV--------PGAERRERIDE------------LLDFVGLLEAADRL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQ----YPHTVLFVTHDRYFLNEVSTRIIELDRG 232
Cdd:cd03265 129 VKtYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKlkeeFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
..
gi 1842088001 233 KL 234
Cdd:cd03265 209 RI 210
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
12-235 |
2.57e-14 |
|
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: 72.20 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 12 NKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYRIRYSSQKQDLNGH 82
Cdd:TIGR01277 5 KVRYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIkvndqshtgLAPYQRPVSMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 MTVFEAVLSSDTPTLRIikkyeeavnryaldqsdsnfnkMMEAQEEMDQkdawdynaeiktILSKLGIHDTTKKIV-ELS 161
Cdd:TIGR01277 85 LTVRQNIGLGLHPGLKL----------------------NAEQQEKVVD------------AAQQVGIADYLDRLPeQLS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLK 235
Cdd:TIGR01277 131 GGQRQRVALARCLVRPNPILLLDEPFSALDpllrEEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-232 |
2.70e-14 |
|
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: 72.50 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRYSSQKQDLNG--HMTVFEAVlsSDTPTLRII 100
Cdd:TIGR01184 3 GVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQ--------PTSGGVILEGKQITEPGpdRMVVFQNY--SLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 101 KKYEEAVNRYALDQSDSNFNKMMEAQEEMdqkdawdynaeiktilskLGI-HDTTKKIVELSGGQQKRVVLAKTLIEQPD 179
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIVEEHIAL------------------VGLtEAADKRPGQLSGGMKQRVAIARALSIRPK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 180 LLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDryfLNE---VSTRIIELDRG 232
Cdd:TIGR01184 135 VLLLDEPFGALDAltrgNLQEELMQIWEEHRVTVLMVTHD---VDEallLSDRVVMLTNG 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-517 |
2.70e-14 |
|
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: 75.88 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYAD----KEIFNDLNLSISEHERIGLVGINGTGKS-TLLKVIGGLDEDftadITHPnQYRIRYssQ 75
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDP----AAHP-SGSILF--D 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDLNGH--------------MtVFEAVLSSDTPTLRIIKKYEEAvnryaldqsdsnfnkmMEAQEEMDQKDAWdynAEI 141
Cdd:COG4172 75 GQDLLGLserelrrirgnriaM-IFQEPMTSLNPLHTIGKQIAEV----------------LRLHRGLSGAAAR---ARA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 142 KTILSKLGIHDTTKKIV----ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVT 213
Cdd:COG4172 135 LELLERVGIPDPERRLDayphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqaQILDLLKDLQRELGMALLLIT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 214 HDryfLNEVStriieldrgklktypgNYEDYI-VMRAeNELVEQKQQEK-----QKALYKQELAWMRAGAKARTTKQQAR 287
Cdd:COG4172 215 HD---LGVVR----------------RFADRVaVMRQ-GEIVEQGPTAElfaapQHPYTRKLLAAEPRGDPRPVPPDAPP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 288 InrfnqLE-SDVKTQHTQDKGelnlaysRLGKQVYELKNLsksinnkvlfEDVTEIIQSGRRIGIVGPNGAGKTTL---- 362
Cdd:COG4172 275 L-----LEaRDLKVWFPIKRG-------LFRRTVGHVKAV----------DGVSLTLRRGETLGLVGESGSGKSTLglal 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 363 ----------------LNILSNED------------QDYEGEL----KIGQTV----KVAYFKQTEKtlDRDIRVIDYLR 406
Cdd:COG4172 333 lrlipsegeirfdgqdLDGLSRRAlrplrrrmqvvfQDPFGSLsprmTVGQIIaeglRVHGPGLSAA--ERRARVAEALE 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 407 E---ESEMakekdgtsisvtqlLERflFPsatHgkkvyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLT 479
Cdd:COG4172 411 EvglDPAA--------------RHR--YP---H-----EFSGGQRQRIAIARALILEPKLLVLDEPTSALDvsvqAQILD 466
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1842088001 480 ILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKI 517
Cdd:COG4172 467 LLRDLQREHGLAYLFISHDlavvRALAHRVM----VMKDGKV 504
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
287-497 |
2.85e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 287 RINRFNQLESDVK--TQHTQDKGELNLaysrlgkqvyELKNLSKSI---NNKVLfEDVTEIIQSGRRIGIVGPNGAGKTT 361
Cdd:PRK11160 313 RINEITEQKPEVTfpTTSTAAADQVSL----------TLNNVSFTYpdqPQPVL-KGLSLQIKAGEKVALLGRTGCGKST 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 362 LLNILSNEDQDYEGELKIGQTVKVAYfkqTEKTLDRDIRVI--------DYLREESEMAKEK--DGTSISVTQ------L 425
Cdd:PRK11160 382 LLQLLTRAWDPQQGEILLNGQPIADY---SEAALRQAISVVsqrvhlfsATLRDNLLLAAPNasDEALIEVLQqvglekL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 426 LERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDfgGSVITVSH 497
Cdd:PRK11160 459 LEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQN--KTVLMITH 532
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
295-474 |
2.95e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 295 ESDVKTQHTQDkGELNLAYSRLGKQvyelknLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDqdyE 374
Cdd:TIGR00955 7 NSDVFGRVAQD-GSWKQLVSRLRGC------FCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRS---P 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 375 GELKIGQTVKV--------------AYFKQTEK-----TLDRDIRVIDYLREESEMAkeKDGTSISVTQLLERFLFPSAT 435
Cdd:TIGR00955 77 KGVKGSGSVLLngmpidakemraisAYVQQDDLfiptlTVREHLMFQAHLRMPRRVT--KKEKRERVDEVLQALGLRKCA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 436 H-----GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:TIGR00955 155 NtrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
322-497 |
3.24e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.83 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSnedqdyeGELKI-GQTVKvayFKQTEKTLDRDIR 400
Cdd:PRK13539 4 EGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIA-------GLLPPaAGTIK---LDGGDIDDPDVAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VIDYLREESEM-------------AKEKDGTSISVTQLLERFLFPSATHGKKVYkLSGGEQKRLYLLRLLVHKPNVLLLD 467
Cdd:PRK13539 74 ACHYLGHRNAMkpaltvaenlefwAAFLGGEELDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 468 EPTNDLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHlaqGGIVIAATH 185
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
322-517 |
3.52e-14 |
|
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: 71.79 E-value: 3.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLL---NILSNEDqdyEGELKIGqtvkvayfkqtEKTLDRD 398
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLrciNLLEEPD---SGTIIID-----------GLKLTDD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVIDYLREESEM--------------------------AKEKDGTSISvTQLLERF-LFPSATHgkkvY--KLSGGEQK 449
Cdd:cd03262 68 KKNINELRQKVGMvfqqfnlfphltvlenitlapikvkgMSKAEAEERA-LELLEKVgLADKADA----YpaQLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03262 143 RVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLaeeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-221 |
3.85e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT--------HPNQYRIRY 72
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 73 S--SQKQDLNGHMTVFEavlssdtpTLRIIKKYeeavnrYALD--QSDSNFNKMMEAQEEMDQKDAwdynaeiktilskl 148
Cdd:PRK13537 83 GvvPQFDNLDPDFTVRE--------NLLVFGRY------FGLSaaAARALVPPLLEFAKLENKADA-------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 gihdttkKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTN-------HLDFESIRWLINYVKqyphTVLFVTHdryFLNE 221
Cdd:PRK13537 135 -------KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTgldpqarHLMWERLRSLLARGK----TILLTTH---FMEE 200
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
324-469 |
3.91e-14 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 72.31 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 324 KNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-----------VAYFKQt 391
Cdd:TIGR04406 5 ENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGYLPQ- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDIRVIDYLREESEMAKEKDGTSIS--VTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLD 467
Cdd:TIGR04406 84 EASIFRKLTVEENIMAVLEIRKDLDRAEREerLEALLEEF---QISHlrDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
..
gi 1842088001 468 EP 469
Cdd:TIGR04406 161 EP 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-526 |
4.24e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.21 E-value: 4.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT----------HPNQYRIRYSSQK 76
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITinninynkldHKLAAQLGIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLN--GHMTVFEAVLSSDTPTLRIIkkyeeAVNRYaldqsdsNFNKMMEAQEEMdqkdawdynaeiktiLSKLGIH-DT 153
Cdd:PRK09700 87 QELSviDELTVLENLYIGRHLTKKVC-----GVNII-------DWREMRVRAAMM---------------LLRVGLKvDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLNEVSTRIIELD 230
Cdd:PRK09700 140 DEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 231 RGklkTYPGNYEdyiVMRAENelveqkqqekqkalykQELAWMRAGAKARttkqqariNRFNQLESDVKTQHtqdkgeln 310
Cdd:PRK09700 220 DG---SSVCSGM---VSDVSN----------------DDIVRLMVGRELQ--------NRFNAMKENVSNLA-------- 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 311 laysrlGKQVYELKNLSKSINNKVlfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK----- 384
Cdd:PRK09700 262 ------HETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISprspl 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 385 ------VAYFKQTEK--------TLDRDIRVIDYLREES-----EMAKEKDGTSISVTQlLERFLFPSATHGKKVYKLSG 445
Cdd:PRK09700 334 davkkgMAYITESRRdngffpnfSIAQNMAISRSLKDGGykgamGLFHEVDEQRTAENQ-RELLALKCHSVNQNITELSG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDfGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKII 521
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDvgakAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
|
....*
gi 1842088001 522 GSFED 526
Cdd:PRK09700 492 TNRDD 496
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
336-498 |
5.34e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 74.70 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 336 FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIG----QTVK-------VAYFKQTEKTLDRDIRviDY 404
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDgvpvSSLDqdevrrrVSVCAQDAHLFDTTVR--EN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 405 LR--------EESEMAKEKDGTSISVTQLLERFLFPSATHGKKvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:TIGR02868 429 LRlarpdatdEELWAALERVGLADWLRALPDGLDTVLGEGGAR---LSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
170 180
....*....|....*....|....
gi 1842088001 477 T-LTILEDYID-DFGGSVITVSHD 498
Cdd:TIGR02868 506 TaDELLEDLLAaLSGRTVVLITHH 529
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
8-234 |
7.24e-14 |
|
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: 74.78 E-value: 7.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYA-DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdLNGHmtvf 86
Cdd:TIGR01193 476 INDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIL---------------LNGF---- 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 eAVLSSDTPTLRIIKKYeeavnryaLDQSDSNF------NKMMEAQEEMDQKDAWDYN--AEIKTILSKLGIHDTTKKIV 158
Cdd:TIGR01193 537 -SLKDIDRHTLRQFINY--------LPQEPYIFsgsileNLLLGAKENVSQDEIWAACeiAEIKDDIENMPLGYQTELSE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 E---LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLI-NYVKQYPHTVLFVTHdRYFLNEVSTRIIELDRGKL 234
Cdd:TIGR01193 608 EgssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVnNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-474 |
7.42e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.20 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL--DEDFTADIT---HPNQYR-IRYSS 74
Cdd:PRK13549 1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIfegEELQASnIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QK------QDLN--GHMTVFEAV-LSSD-TPTLRIikkyeeavnryaldqsdsNFNKMmeaqeemdqkdawdyNAEIKTI 144
Cdd:PRK13549 81 RAgiaiihQELAlvKELSVLENIfLGNEiTPGGIM------------------DYDAM---------------YLRAQKL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LSKLGIH-DTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDryfLN 220
Cdd:PRK13549 128 LAQLKLDiNPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAhgiACIYISHK---LN 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 221 EV---STRIIELDRGK-LKTYPG---NYEDYIVMRAENELveqkqqekqKALYKQElawmragakarttkqqarinrfnq 293
Cdd:PRK13549 205 EVkaiSDTICVIRDGRhIGTRPAagmTEDDIITMMVGREL---------TALYPRE------------------------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 294 lesdvktQHTqdkgelnlaysrLGKQVYELKNLS---KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNED 370
Cdd:PRK13549 252 -------PHT------------IGEVILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 371 QD-YEGELKI-GQTVKV-----------AYFKQTEK-----------------TLDR--DIRVIDYLREESemakekdgt 418
Cdd:PRK13549 313 PGrWEGEIFIdGKPVKIrnpqqaiaqgiAMVPEDRKrdgivpvmgvgknitlaALDRftGGSRIDDAAELK--------- 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 419 siSVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK13549 384 --TILESIQRLKVKTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-498 |
7.70e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 72.45 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTL----LNILSnedqDYEGELKI-GQTVKvayfkqtektlD 396
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILA----PDSGEVLWdGEPLD-----------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDYLREE----SEM-------------------AKEKdgtsisVTQLLERF-LFPSAthGKKVYKLSGGEQKRLY 452
Cdd:COG4152 68 EDRRRIGYLPEErglyPKMkvgeqlvylarlkglskaeAKRR------ADEWLERLgLGDRA--NKKVEELSKGNQQKVQ 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHD 498
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELaakGTTVIFSSHQ 188
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
322-517 |
7.75e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 71.58 E-value: 7.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSI-NNKVLFeDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtvkvAYFKQTEKTLDRDIR 400
Cdd:COG4161 4 QLKNINCFYgSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAG----HQFDFSQKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 --------------------VIDYLREES----EMAKEKdgTSISVTQLLERF-------LFPSAthgkkvykLSGGEQK 449
Cdd:COG4161 79 llrqkvgmvfqqynlwphltVMENLIEAPckvlGLSKEQ--AREKAMKLLARLrltdkadRFPLH--------LSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVIT---VSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG4161 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITqviVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-234 |
8.30e-14 |
|
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: 71.15 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 12 NKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDED---FTADIT--------HPNQYRIRYSSQKQDLN 80
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILfngqprkpDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 GHMTVFEAVLSsdTPTLRIIKKYEEAVNryaldqsdsnfnKMMEAQEEMDQkdawdynaeiktilsklgIHDTT---KKI 157
Cdd:cd03234 94 PGLTVRETLTY--TAILRLPRKSSDAIR------------KKRVEDVLLRD------------------LALTRiggNLV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHD-RYFLNEVSTRIIELDRGK 233
Cdd:cd03234 142 KGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARrnrIVILTIHQpRSDLFRLFDRILLLSSGE 221
|
.
gi 1842088001 234 L 234
Cdd:cd03234 222 I 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
5-245 |
8.45e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 71.61 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadiTHPNQY---RIRY-----SSQK 76
Cdd:COG1117 11 KIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMND------LIPGARvegEILLdgediYDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGH---------------MTVFEAVLSSdtptLRII-----KKYEEAVnRYALdqsdsnfnkmmeaqeemdqKDA-- 134
Cdd:COG1117 85 VDVVELrrrvgmvfqkpnpfpKSIYDNVAYG----LRLHgikskSELDEIV-EESL-------------------RKAal 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 135 WDynaEIKTILSKLGihdttkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYpHTVLF 211
Cdd:COG1117 141 WD---EVKDRLKKSA--------LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakIEELILELKKD-YTIVI 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1842088001 212 VTH---------DR--YFLNevsTRIIELDR-GKLKTYPGNY--EDYI 245
Cdd:COG1117 209 VTHnmqqaarvsDYtaFFYL---GELVEFGPtEQIFTNPKDKrtEDYI 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
322-499 |
8.55e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.90 E-value: 8.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQ 390
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVSYCAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 T-----EKTLDRDIRVIDYLREESEMAKEKDGtsisvtqlLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLL 465
Cdd:PRK10247 89 TptlfgDTVYDNLIFPWQIRNQQPDPAIFLDD--------LERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1842088001 466 LDEPTNDLDTETLTILED----YIDDFGGSVITVSHDR 499
Cdd:PRK10247 161 LDEITSALDESNKHNVNEiihrYVREQNIAVLWVTHDK 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-186 |
9.05e-14 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 71.03 E-value: 9.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL----------DEdftADITHPNQYR-----IR 71
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLvkpdsgkillDG---QDITKLPMHKrarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVLSsdtpTLRIIKK-YEEAVNRyaLDQSDSNFNkmmeaqeemdqkdawdynaeIKTILSKLGI 150
Cdd:cd03218 79 YLPQEASIFRKLTVEENILA----VLEIRGLsKKEREEK--LEELLEEFH--------------------ITHLRKSKAS 132
|
170 180 190
....*....|....*....|....*....|....*.
gi 1842088001 151 HdttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEP 186
Cdd:cd03218 133 S--------LSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
322-498 |
9.36e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 71.27 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN-EDQDyEGELKI-GQTV----------KVAYFK 389
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRlLPPD-SGEVLVdGLDVattpsrelakRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 Q--------TEKTL----------------DRDI--RVIDYLreesemakekdgtsiSVTQLLERFLfpsathgkkvYKL 443
Cdd:COG4604 82 QenhinsrlTVRELvafgrfpyskgrltaeDREIidEAIAYL---------------DLEDLADRYL----------DEL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 444 SGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
7-234 |
9.74e-14 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 70.93 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE----IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDedftaditHPNQYRIRYSSQkqDLNG- 81
Cdd:COG4181 10 ELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLD--------RPTSGTVRLAGQ--DLFAl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 -----------HMT-VFEA--VLssdtPTLRiikkyeeavnryALDqsdsnfNKMMEAqEEMDQKDAWDYNAEIktiLSK 147
Cdd:COG4181 80 dedararlrarHVGfVFQSfqLL----PTLT------------ALE------NVMLPL-ELAGRRDARARARAL---LER 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 148 LGI-HDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----IRWLINYVKQYPHTVLFVTHDRYfLNEV 222
Cdd:COG4181 134 VGLgHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHDPA-LAAR 212
|
250
....*....|..
gi 1842088001 223 STRIIELDRGKL 234
Cdd:COG4181 213 CDRVLRLRAGRL 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-235 |
1.05e-13 |
|
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: 69.65 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVI-GGLDedftadithPNQYRIRyssqkqdLNGHMt 84
Cdd:cd03247 3 INNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDLK---------PQQGEIT-------LDGVP- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 vfeavlssdtptlriIKKYEEAVNRY--ALDQSDSNFNKmmeaqeemdqkdawdynaeikTILSKLGIhdttkkivELSG 162
Cdd:cd03247 66 ---------------VSDLEKALSSLisVLNQRPYLFDT---------------------TLRNNLGR--------RFSG 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHTVLFVTHdRYFLNEVSTRIIELDRGKLK 235
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVlkDKTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-215 |
1.09e-13 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.93 E-value: 1.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL----DEDFTADITHPNQY-------RIRYSS 74
Cdd:TIGR02868 336 ELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLldplQGEVTLDGVPVSSLdqdevrrRVSVCA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QkqdlNGHmtVFEAvlssdtpTLRiikkyeeavnryaldqsdsnfNKMMEAQEEMDQKDAWDynaeiktILSKLGIHD-- 152
Cdd:TIGR02868 416 Q----DAH--LFDT-------TVR---------------------ENLRLARPDATDEELWA-------ALERVGLADwl 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 153 ------TTKKIVE----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHD 215
Cdd:TIGR02868 455 ralpdgLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALsgRTVVLITHH 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-191 |
1.13e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 71.02 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 24 LNLSISEHERIGLVGINGTGKSTLLKVIGG---------LDEDFTADITHPNQYRIR-YSSQKQDLNGHMTVFEavlssd 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGllpgqgeilLNGRPLSDWSAAELARHRaYLSQQQSPPFAMPVFQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 94 tptlriikkyeeavnrY-ALDQSDSnfnkmmeAQEEMDQkdawdynAEIKTILSKLGIHDT-TKKIVELSGGQQKRVVLA 171
Cdd:COG4138 89 ----------------YlALHQPAG-------ASSEAVE-------QLLAQLAEALGLEDKlSRPLTQLSGGEWQRVRLA 138
|
170 180
....*....|....*....|....*..
gi 1842088001 172 KTLIE-------QPDLLLLDEPTNHLD 191
Cdd:COG4138 139 AVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
11-236 |
1.28e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.61 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 11 LNKSYAD----KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQ-KQDLNGH--- 82
Cdd:PRK11629 11 LCKRYQEgsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAaKAELRNQklg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 --------MTVFEAVLSSDTPTLrIIKKYEEAVNRYALDqsdsnfnkMMEAqeemdqkdawdynaeikTILSKLGIHDTT 154
Cdd:PRK11629 91 fiyqfhhlLPDFTALENVAMPLL-IGKKKPAEINSRALE--------MLAA-----------------VGLEHRANHRPS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 kkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPHTV-LFVTHDRYFLNEVStRIIELD 230
Cdd:PRK11629 145 ----ELSGGERQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGTAfLVVTHDLQLAKRMS-RQLEMR 219
|
....*.
gi 1842088001 231 RGKLKT 236
Cdd:PRK11629 220 DGRLTA 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
7-232 |
1.39e-13 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 70.54 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-----DKEI--FNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadiTH-PNQYRIRYSSQKQD 78
Cdd:COG4778 6 EVENLSKTFTlhlqgGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYG---------NYlPDSGSILVRHDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 79 LNghmtvfeavLSSDTPTlRIIkkyeeAVNRY----------------ALDQsdsnfnkMMEAQEEM--DQKDAwdyNAE 140
Cdd:COG4778 77 VD---------LAQASPR-EIL-----ALRRRtigyvsqflrviprvsALDV-------VAEPLLERgvDREEA---RAR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 141 IKTILSKLGIHD-------TTkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYPHTVL 210
Cdd:COG4778 132 ARELLARLNLPErlwdlppAT-----FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKARGTAII 206
|
250 260
....*....|....*....|..
gi 1842088001 211 FVTHDRYFLNEVSTRIIELDRG 232
Cdd:COG4778 207 GIFHDEEVREAVADRVVDVTPF 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
322-517 |
1.58e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.43 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSI-NNKVLFeDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtvkvAYFKQTEKTLDRDIR 400
Cdd:PRK11124 4 QLNGINCFYgAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAG----NHFDFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 --------------------VIDYLRE--------ESEMAKEKdgtsisVTQLLERF-------LFPsathgkkvYKLSG 445
Cdd:PRK11124 79 elrrnvgmvfqqynlwphltVQQNLIEapcrvlglSKDQALAR------AEKLLERLrlkpyadRFP--------LHLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGGSVIT---VSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITqviVTHEVEVARKTASRVVYMENGHI 219
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-234 |
1.74e-13 |
|
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: 70.19 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVI-------GG---LDEdftaditHP-NQYRIRYSSQKQDLNGHmtv 85
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLenfyqpqGGqvlLDG-------KPiSQYEHKYLHSKVSLVGQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 fEAVLSSDTPTLRIikkyeeavnRYALdqSDSNFNKMMEAQEEmdqkdawdYNAEIKTILSKLGIH-DTTKKIVELSGGQ 164
Cdd:cd03248 96 -EPVLFARSLQDNI---------AYGL--QSCSFECVKEAAQK--------AHAHSFISELASGYDtEVGEKGSQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHdRYFLNEVSTRIIELDRGKL 234
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPerRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
322-474 |
1.76e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 71.76 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---------KVAYFKQT 391
Cdd:PRK13537 9 DFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVPQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EkTLDRDIRVIDYLREESEMAKEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:PRK13537 89 D-NLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
...
gi 1842088001 472 DLD 474
Cdd:PRK13537 168 GLD 170
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
322-528 |
1.81e-13 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 70.34 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV-KVAYFKQTEKTLDRDI 399
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdGKDItNLPPHKRPVNTVFQNY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYLREESEMA-----KEKDGTSIS--VTQLLeRFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTND 472
Cdd:cd03300 82 ALFPHLTVFENIAfglrlKKLPKAEIKerVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 473 LD----TETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKiIGSFED-YE 528
Cdd:cd03300 161 LDlklrKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQ-IGTPEEiYE 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-232 |
1.86e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 73.30 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKqdlnghmtvfeavlssdtP- 95
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQR------------------Py 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 ----TLRiikkyeEAVnryALDQSDSNFNkmmeaqeemdqkdawdyNAEIKTILSKLGIHDTTKKI-------VELSGGQ 164
Cdd:COG4178 437 lplgTLR------EAL---LYPATAEAFS-----------------DAELREALEAVGLGHLAERLdeeadwdQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQ-YPH-TVLFVTHdRYFLNEVSTRIIELDRG 232
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGtTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
321-497 |
2.02e-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: 68.78 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 321 YELKNLSKSI--NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfkqtekTLDR 397
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADIS---------QWDP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 398 DI--RVIDYLREESEMAkekDGTsisvtqLLERFLfpsathgkkvyklSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDT 475
Cdd:cd03246 72 NElgDHVGYLPQDDELF---SGS------IAENIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180
....*....|....*....|....*
gi 1842088001 476 ETLTILEDYIDD---FGGSVITVSH 497
Cdd:cd03246 130 EGERALNQAIAAlkaAGATRIVIAH 154
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-215 |
2.15e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.81 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE----IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSS-QKQDLNG 81
Cdd:PRK10584 8 EVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEeARAKLRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMT--VFEAVLSsdTPTLRIIkkyeEAVNRYALDQSDSNFNKMMEAQEemdqkdawdynaeiktILSKLGIHDTTKKI-V 158
Cdd:PRK10584 88 KHVgfVFQSFML--IPTLNAL----ENVELPALLRGESSRQSRNGAKA----------------LLEQLGLGKRLDHLpA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES----IRWLINYVKQYPHTVLFVTHD 215
Cdd:PRK10584 146 QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-215 |
2.20e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 70.66 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSY----ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedFTAdithPNQYRIRyssqkqd 78
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAG----FLA----PSSGEIT------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 79 LNGHMT---------VF--EAVLssdtPTLRIIKKYEeavnrYALdqsdsnfnKM--MEAQEEMDQKDAWdynaeiktiL 145
Cdd:COG4525 66 LDGVPVtgpgadrgvVFqkDALL----PWLNVLDNVA-----FGL--------RLrgVPKAERRARAEEL---------L 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 146 SKLGIHDT-TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPH-TVLFVTHD 215
Cdd:COG4525 120 ALVGLADFaRRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQMQELLLDVWQRTGkGVFLITHS 194
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-233 |
2.30e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.03 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAY--KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIRYSSQKQDL 79
Cdd:PRK13636 1 MEDYilKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNG--------ILKPSSGRILFDGKPIDY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 N--GHMTVFEA---VLSSDTPTLRIIKKYEeavnryaldqsDSNFNKM-MEAQEEMDQKdawdynaEIKTILSKLGI-HD 152
Cdd:PRK13636 73 SrkGLMKLRESvgmVFQDPDNQLFSASVYQ-----------DVSFGAVnLKLPEDEVRK-------RVDNALKRTGIeHL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 TTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIE 228
Cdd:PRK13636 135 KDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFV 214
|
....*
gi 1842088001 229 LDRGK 233
Cdd:PRK13636 215 MKEGR 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
23-235 |
2.40e-13 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 71.68 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------------THPNQYRIRYSSQKQDLNGHMTVFE 87
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfdsrkgifLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 AVlssdtptlriikkyeeavnRYALDQSDSNFNKMMEAQeemdqkdawdynaeiktILSKLGI-HDTTKKIVELSGGQQK 166
Cdd:TIGR02142 95 NL-------------------RYGMKRARPSERRISFER-----------------VIELLGIgHLLGRLPGRLSGGEKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK------QYPhtVLFVTHDryfLNEV---STRIIELDRGKLK 235
Cdd:TIGR02142 139 RVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLErlhaefGIP--ILYVSHS---LQEVlrlADRVVVLEDGRVA 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
322-469 |
2.46e-13 |
|
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: 69.88 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQT------------VKVAYFK 389
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QtEKTLDRDIRVIDYLREESEMAKE-KDGTSISVTQLLERFlfpSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVLLL 466
Cdd:cd03218 82 Q-EASIFRKLTVEENILAVLEIRGLsKKEREEKLEELLEEF---HITHlrKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
...
gi 1842088001 467 DEP 469
Cdd:cd03218 158 DEP 160
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
322-497 |
2.92e-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: 69.06 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVkvayfkqtektldrDIRV 401
Cdd:cd03231 2 EADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGP--------------LDFQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IDYLREESEMAKEKDG--TSISVtqlLERFLFPSATHGKK------------------VYKLSGGEQKRLYLLRLLVHKP 461
Cdd:cd03231 68 RDSIARGLLYLGHAPGikTTLSV---LENLRFWHADHSDEqveealarvglngfedrpVAQLSAGQQRRVALARLLLSGR 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 1842088001 462 NVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:cd03231 145 PLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
19-254 |
3.06e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 19 EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTAdithpnQYRIryssQKQDLnghmtvfeAVLSSDT-PTL 97
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG------TYRV----AGQDV--------ATLDADAlAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 98 R------IIKKY--------EEAVNRYALDQSDSNFNKMMEAQEemdqkdawdynaeiktILSKLGIHDTTK-KIVELSG 162
Cdd:PRK10535 84 RrehfgfIFQRYhllshltaAQNVEVPAVYAGLERKQRLLRAQE----------------LLQRLGLEDRVEyQPSQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEvSTRIIELDRGKLKTYPG 239
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdrgHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPP 226
|
250
....*....|....*
gi 1842088001 240 NYEDYIVMRAENELV 254
Cdd:PRK10535 227 AQEKVNVAGGTEPVV 241
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
322-535 |
3.37e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.71 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNeDQDYE---GELKI-GQT--------------- 382
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG-HPKYEvtsGSILLdGEDilelspderaragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 383 -----------VKVAYFKQTEKTLDRD--IRVIDYLREESEMAKE----KDgtsisvtqLLERFLFpsathgkkvYKLSG 445
Cdd:COG0396 81 lafqypveipgVSVSNFLRTALNARRGeeLSAREFLKLLKEKMKElgldED--------FLDRYVN---------EGFSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEywFIH---DGKIEK 519
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrspDRGILIITHYQRILDYIKPD--FVHvlvDGRIVK 221
|
250 260
....*....|....*....|....
gi 1842088001 520 iIGSFE--------DYESFKKEHE 535
Cdd:COG0396 222 -SGGKElaleleeeGYDWLKEEAA 244
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
322-517 |
3.84e-13 |
|
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: 68.93 E-value: 3.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNK----VLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN----------------EDQDYEGELKIG- 380
Cdd:cd03266 3 TADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfatvdgfdvVKEPAEARRRLGf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 381 ----------QTVK--VAYF------KQTEKTlDRdirvIDYLREESEMAkekdgtsisvtQLLERflfpsathgkKVYK 442
Cdd:cd03266 83 vsdstglydrLTARenLEYFaglyglKGDELT-AR----LEELADRLGME-----------ELLDR----------RVGG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 443 LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYID---DFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03266 137 FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRqlrALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
322-535 |
3.92e-13 |
|
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: 72.14 E-value: 3.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQ--DYEGEL-----------------KIGQT 382
Cdd:TIGR03269 2 EVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpsKVGEP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 383 VKV---------AYFKQTEKTLDRDIR----------------------VIDYLRE---ESEMAKEKDGTSISVTQLLER 428
Cdd:TIGR03269 82 CPVcggtlepeeVDFWNLSDKLRRRIRkriaimlqrtfalygddtvldnVLEALEEigyEGKEAVGRAVDLIEMVQLSHR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 429 FlfpsaTHGKKvyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTI----LEDYIDDFGGSVITVSHDRYFLNK 504
Cdd:TIGR03269 162 I-----THIAR--DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 1842088001 505 VVQEYWFIHDGKI------EKIIGSF-EDYESFKKEHE 535
Cdd:TIGR03269 235 LSDKAIWLENGEIkeegtpDEVVAVFmEGVSEVEKECE 272
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-237 |
4.23e-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: 69.10 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 12 NKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIRYSSQKQDLNGHMTVFEAVLS 91
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAG--------IYPPDSGTVTVRGRVSSLLGLGGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 92 SdtptlriikkyEEAVNRYALdqsdsnfnkMMeaqeEMDQKDAWDYNAEIKTiLSKLG--IHdttKKIVELSGGQQKRVV 169
Cdd:cd03220 101 G-----------RENIYLNGR---------LL----GLSRKEIDEKIDEIIE-FSELGdfID---LPVKTYSSGMKARLA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 170 LAKTLIEQPDLLLLDEPTNHLD--F--ESIRWLINYVKQYPhTVLFVTHDRYFLNEVSTRIIELDRGKLKTY 237
Cdd:cd03220 153 FAIATALEPDILLIDEVLAVGDaaFqeKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
322-498 |
4.44e-13 |
|
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: 69.00 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNK----VLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfkqtekTLD 396
Cdd:COG4181 10 ELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLF---------ALD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIdyLREES------------------------EMAKEKDGTSISvTQLLERF-LFPSATHgkkvY--KLSGGEQK 449
Cdd:COG4181 81 EDARAR--LRARHvgfvfqsfqllptltalenvmlplELAGRRDARARA-RALLERVgLGHRLDH----YpaQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHD 498
Cdd:COG4181 154 RVALARAFATEPAILFADEPTGNLDAATgeqiIDLLFELNRERGTTLVLVTHD 206
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
322-517 |
5.02e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.06 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN-----KVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfkqtekTL 395
Cdd:PRK10535 6 ELKDIRRSYPSgeeqvEVL-KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVaGQDVA---------TL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRDirVIDYLREE------------SEMAKEKD--------GTSISVTQLLERFLFPSATHGKKVY----KLSGGEQKRL 451
Cdd:PRK10535 76 DAD--ALAQLRREhfgfifqryhllSHLTAAQNvevpavyaGLERKQRLLRAQELLQRLGLEDRVEyqpsQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLDT----ETLTILEDyIDDFGGSVITVSHDRYFLN---KVVQeywfIHDGKI 517
Cdd:PRK10535 154 SIARALMNGGQVILADEPTGALDShsgeEVMAILHQ-LRDRGHTVIIVTHDPQVAAqaeRVIE----IRDGEI 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
331-497 |
5.85e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 71.73 E-value: 5.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 331 NNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDIRVIDY--LREe 408
Cdd:COG1132 352 DRPVL-KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILID---------------GVDIRDLTLesLRR- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 409 semakekdgtSIS-VTQllERFLF------------PSATH---------------------------GKKVYKLSGGEQ 448
Cdd:COG1132 415 ----------QIGvVPQ--DTFLFsgtirenirygrPDATDeeveeaakaaqahefiealpdgydtvvGERGVNLSGGQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF--GGSVITVSH 497
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAH 533
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-234 |
6.25e-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: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 16 ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRyssqkqdLNGhmtvfeavlssdtp 95
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR--------PTSGRVR-------LDG-------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 tlriikkyeEAVNRYALDQsdsnfnkmmeaqeemdqkdawdYNAEIKTILSKLGIHDTTkkIVE--LSGGQQKRVVLAKT 173
Cdd:cd03246 64 ---------ADISQWDPNE----------------------LGDHVGYLPQDDELFSGS--IAEniLSGGQRQRLGLARA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 174 LIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVStRIIELDRGKL 234
Cdd:cd03246 111 LYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-234 |
7.10e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.68 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-----DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPN----QYRIRYSSQKQ 77
Cdd:TIGR00958 478 LIEFQDVSFSypnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHmtvfEAVLSSDTPTLRIIkkyeeavnrYALDQSDSNfnKMMEAQEEMD-----QKDAWDYNAEIKtilsklgihd 152
Cdd:TIGR00958 558 ALVGQ----EPVLFSGSVRENIA---------YGLTDTPDE--EIMAAAKAANahdfiMEFPNGYDTEVG---------- 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 ttKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTHdRYFLNEVSTRIIELDRG 232
Cdd:TIGR00958 613 --EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKG 689
|
..
gi 1842088001 233 KL 234
Cdd:TIGR00958 690 SV 691
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
322-498 |
7.89e-13 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 68.05 E-value: 7.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVkVAYFKQTektlDRDIRV 401
Cdd:cd03301 2 ELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-VTDLPPK----DRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 I--DY-----------------LREESEMAKEKDGTSIS----VTQLLERflfpsathgkKVYKLSGGEQKRLYLLRLLV 458
Cdd:cd03301 77 VfqNYalyphmtvydniafglkLRKVPKDEIDERVREVAellqIEHLLDR----------KPKQLSGGQRQRVALGRAIV 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 459 HKPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHD 498
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrvQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
322-518 |
8.25e-13 |
|
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: 66.95 E-value: 8.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSI--NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYfkqtEKTLDRDI 399
Cdd:cd03247 2 SINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYlreesemakekdgtsisvtqllERFLFpSATHGKKV-YKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET- 477
Cdd:cd03247 78 SVLNQ----------------------RPYLF-DTTLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITe 134
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1842088001 478 LTILEDYIDDF-GGSVITVSHDRYFLNKvVQEYWFIHDGKIE 518
Cdd:cd03247 135 RQLLSLIFEVLkDKTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| ABC_tran_CTD |
pfam16326 |
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. ... |
560-625 |
8.28e-13 |
|
ABC transporter C-terminal domain; This domain is found at the C-terminus of ABC transporters. It has a coiled coil structure with an atypical 3(10)-helix in the alpha-hairpin region. It is involved in DNA_binding.
Pssm-ID: 465095 [Multi-domain] Cd Length: 69 Bit Score: 63.64 E-value: 8.28e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 560 LSYKEKLEYETIMTRIEMTETRLEDLEQEMINAS--DNYARIKELNEEKEQLEATYEADITRWSELEE 625
Cdd:pfam16326 2 LSYKEQRELEELEAEIEKLEEEIAELEAQLADPElySDYEKLQELSAELEELEAELEELYERWEELEE 69
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
8-215 |
9.51e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQYRIRYSSQK 76
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTltptagtvlvaGDDVEALSARAASRRVASVPQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNGHMTVFEAVLSSDTPTLRIIKKYEEAvNRYALDQSdsnfnkmmeaqeeMDQKDAWDYNAeiktilsklgihdttKK 156
Cdd:PRK09536 86 TSLSFEFDVRQVVEMGRTPHRSRFDTWTET-DRAAVERA-------------MERTGVAQFAD---------------RP 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLINYVKqyphTVLFVTHD 215
Cdd:PRK09536 137 VTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhqvrtLELVRRLVDDGK----TAVAAIHD 198
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-256 |
9.73e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftaditHPNqYRIrySSQKQDLNG----H 82
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG----------HPK-YEV--TSGSILLDGedilE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 MTVFE-A----VLSSDTPTlRIikkyeEAVnryaldqSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIhdtTKKI 157
Cdd:COG0396 69 LSPDErAragiFLAFQYPV-EI-----PGV-------SVSNFLRTALNARRGEELSAREFLKLLKEKMKELGL---DEDF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VE------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHT-VLFVTHDRYFLNEVS-TRII 227
Cdd:COG0396 133 LDryvnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLrsPDRgILIITHYQRILDYIKpDFVH 212
|
250 260
....*....|....*....|....*....
gi 1842088001 228 ELDRGKlktypgnyedyIVMRAENELVEQ 256
Cdd:COG0396 213 VLVDGR-----------IVKSGGKELALE 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-234 |
9.91e-13 |
|
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: 67.99 E-value: 9.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADK----EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLD-------EDFTADITHPN-------QY 68
Cdd:cd03258 3 ELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLErptsgsvLVDGTDLTLLSgkelrkaRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 69 RIRYSSQKQDLNGHMTVFEAVlssdTPTLRIIKkyeeavnryaldqsdsnfnkmmEAQEEMDQKdawdynaeIKTILSKL 148
Cdd:cd03258 83 RIGMIFQHFNLLSSRTVFENV----ALPLEIAG----------------------VPKAEIEER--------VLELLELV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDTTKK-IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVS 223
Cdd:cd03258 129 GLEDKADAyPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRIC 208
|
250
....*....|.
gi 1842088001 224 TRIIELDRGKL 234
Cdd:cd03258 209 DRVAVMEKGEV 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-232 |
1.11e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.50 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedFTADIThpnqyrirySSQKQDLNGHMTVF 86
Cdd:PRK09984 6 RVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKS---------AGSHIELLGRTVQR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPTLR-----IIKKYEeAVNRYALDQS-------DSNFNKMMEAQEEMDQKDawdynaEIKTILSKLGI-HDT 153
Cdd:PRK09984 74 EGRLARDIRKSRantgyIFQQFN-LVNRLSVLENvligalgSTPFWRTCFSWFTREQKQ------RALQALTRVGMvHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHDRYFLNEVSTRIIEL 229
Cdd:PRK09984 147 HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVTLHQVDYALRYCERIVAL 226
|
...
gi 1842088001 230 DRG 232
Cdd:PRK09984 227 RQG 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
322-498 |
1.17e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 69.72 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN-EDQDyEGELKIGQTVkVAyfkqTEKTLDRDI- 399
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGlEDPT-SGEILIGGRD-VT----DLPPKDRNIa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 ----------------------RVIDYLREE-----SEMAKekdgtSISVTQLLERflFPSAthgkkvykLSGGEQKRLY 452
Cdd:COG3839 79 mvfqsyalyphmtvyeniafplKLRKVPKAEidrrvREAAE-----LLGLEDLLDR--KPKQ--------LSGGQRQRVA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:COG3839 144 LGRALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
322-505 |
1.31e-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: 67.46 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS-----INNKVL--FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILsnedqdY------EGELKI---GQTVKV 385
Cdd:COG4778 6 EVENLSKTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCI------YgnylpdSGSILVrhdGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 386 A----------------YFKQTEKTLDR----DIrVIDYLRE---ESEMAKEKdgtsisVTQLLERF--------LFPsA 434
Cdd:COG4778 80 AqaspreilalrrrtigYVSQFLRVIPRvsalDV-VAEPLLErgvDREEARAR------ARELLARLnlperlwdLPP-A 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 435 ThgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKV 505
Cdd:COG4778 152 T-------FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkarGTAIIGIFHDEEVREAV 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-532 |
1.42e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 68.14 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILsNEDQDYEGELKIGQtvKVAYFKQTekTLDRDIRv 401
Cdd:PRK14258 9 KVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEG--RVEFFNQN--IYERRVN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 IDYLREESEMAKEK---------DGTSISV----------------TQLLERFLFPSATHG--KKVYKLSGGEQKRLYLL 454
Cdd:PRK14258 83 LNRLRRQVSMVHPKpnlfpmsvyDNVAYGVkivgwrpkleiddiveSALKDADLWDEIKHKihKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 455 RLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFG----GSVITVSHDRYFLNKVVQEYWFIHDGkiEKIIGSFEDYESF 530
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrseLTMVIVSHNLHQVSRLSDFTAFFKGN--ENRIGQLVEFGLT 240
|
..
gi 1842088001 531 KK 532
Cdd:PRK14258 241 KK 242
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
338-498 |
1.48e-12 |
|
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: 69.37 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTV---------------KVAYFKQtEKTLDRDIRVI 402
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQ-EARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYLR--EESEMAKEKDGTSISVTQLL--ERFLfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD---- 474
Cdd:TIGR02142 94 GNLRygMKRARPSERRISFERVIELLgiGHLL------GRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprk 167
|
170 180
....*....|....*....|....
gi 1842088001 475 TETLTILEDYIDDFGGSVITVSHD 498
Cdd:TIGR02142 168 YEILPYLERLHAEFGIPILYVSHS 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
322-498 |
1.65e-12 |
|
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: 67.14 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSK--SINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtvkvaYFKQTEK------ 393
Cdd:cd03263 2 QIRNLTKtyKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-----YSIRTDRkaarqs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 --------TLDRDIRVIDYLR--------EESEMAKEkdgtsisVTQLLERF-LFPSAThgKKVYKLSGGEQKRLYLLRL 456
Cdd:cd03263 77 lgycpqfdALFDELTVREHLRfyarlkglPKSEIKEE-------VELLLRVLgLTDKAN--KRARTLSGGMKRKLSLAIA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 457 LVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHD 498
Cdd:cd03263 148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHS 191
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-233 |
1.70e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYA-----DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDEDftaDITHPNQY-RI 70
Cdd:COG1101 3 ELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslppdsgsilIDGK---DVTKLPEYkRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQK-QD-LNG---HMTVFE----AVLSSDTPTLRIikkyeeAVNRyaldqsdsnfnkmmeaqeemdqkdawDYNAEI 141
Cdd:COG1101 80 KYIGRVfQDpMMGtapSMTIEEnlalAYRRGKRRGLRR------GLTK--------------------------KRRELF 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 142 KTILSKLGI---HDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLIN----YVKQYPHTVLFVTH 214
Cdd:COG1101 128 RELLATLGLgleNRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLEltekIVEENNLTTLMVTH 207
|
250 260
....*....|....*....|
gi 1842088001 215 D-RYFLnEVSTRIIELDRGK 233
Cdd:COG1101 208 NmEQAL-DYGNRLIMMHEGR 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
7-232 |
1.86e-12 |
|
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: 67.17 E-value: 1.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTadiTHPNQYRIR---- 71
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLlpvksgsirldGEDIT---KLPPHERARagia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFEAVLSSDTPTLRIIKKYEEAVnrYALdqsdsnfnkmMEAQEEMDQKDAWDynaeiktilsklgih 151
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEI--YEL----------FPVLKEMLGRRGGD--------------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 dttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTnhldfESI---------RWLINYVKQYPHTVLFVTHDRYFLNEV 222
Cdd:TIGR03410 132 --------LSGGQQQQLAIARALVTRPKLLLLDEPT-----EGIqpsiikdigRVIRRLRAEGGMAILLVEQYLDFAREL 198
|
250
....*....|
gi 1842088001 223 STRIIELDRG 232
Cdd:TIGR03410 199 ADRYYVMERG 208
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
322-517 |
1.88e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQ-TVKVAYFKQTEKTLDRDIR 400
Cdd:PRK11264 5 EVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDiTIDTARSLSQQKGLIRQLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 -----------------VIDYLREESEMAKEKDGTSisVTQLLERFLFPSATHGKK-VY--KLSGGEQKRLYLLRLLVHK 460
Cdd:PRK11264 85 qhvgfvfqnfnlfphrtVLENIIEGPVIVKGEPKEE--ATARARELLAKVGLAGKEtSYprRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 461 PNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVItVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK11264 163 PEVILFDEPTSALDPelvgEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
9-234 |
1.91e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 70.19 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 9 EHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRYSSQ------KQDLNG 81
Cdd:COG1132 343 ENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD--------PTSGRILIDGVdirdltLESLRR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HM-TVF-EAVLSSDTptLR--IikkyeeavnRYA-LDQSDSnfnKMMEAqeeMDQKDAWD--------YNaeikTILSKL 148
Cdd:COG1132 415 QIgVVPqDTFLFSGT--IRenI---------RYGrPDATDE---EVEEA---AKAAQAHEfiealpdgYD----TVVGER 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GihdttkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH--TVLFVTHdRyflneVST-- 224
Cdd:COG1132 474 G--------VNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKgrTTIVIAH-R-----LSTir 539
|
250
....*....|...
gi 1842088001 225 ---RIIELDRGKL 234
Cdd:COG1132 540 nadRILVLDDGRI 552
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
322-499 |
2.10e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 69.09 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-VAYFKQTEKTLDRDI 399
Cdd:PRK11607 21 EIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLShVPPYQRPINMMFQSY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYLREESEMA---KEKDGTSISVTQLLERFLfpSATH-----GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:PRK11607 101 ALFPHMTVEQNIAfglKQDKLPKAEIASRVNEML--GLVHmqefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1842088001 472 DLDT--------ETLTILEdyidDFGGSVITVSHDR 499
Cdd:PRK11607 179 ALDKklrdrmqlEVVDILE----RVGVTCVMVTHDQ 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
322-498 |
2.25e-12 |
|
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: 66.98 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLN-------------ILSNED---------------QDY 373
Cdd:cd03299 2 KVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLEtiagfikpdsgkiLLNGKDitnlppekrdisyvpQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 374 EgeLKIGQTVK--VAY--FKQTEKTLDRDIRVIdylreesEMAKekdgtSISVTQLLERflfpsathgkKVYKLSGGEQK 449
Cdd:cd03299 81 A--LFPHMTVYknIAYglKKRKVDKKEIERKVL-------EIAE-----MLGIDHLLNR----------KPETLSGGEQQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHD 498
Cdd:cd03299 137 RVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-234 |
2.28e-12 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 66.04 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL--DEDFTADI------THPNQYR--IRYSSQKQDLNGHM 83
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVlingrpLDKRSFRkiIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVlssdtptlriikkyeeavnryaldqsdsnfnkmmeaqeemdqkdawDYNAEIKTIlsklgihdttkkivelSGG 163
Cdd:cd03213 98 TVRETL----------------------------------------------MFAAKLRGL----------------SGG 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 164 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHD-RYFLNEVSTRIIELDRGKL 234
Cdd:cd03213 116 ERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAdtgRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
7-498 |
2.42e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNQYRIRYSSQKQDLNGHMTVF 86
Cdd:PRK10762 6 QLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG--------IYTRDAGSILYLGKEVTFNGPKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLS------SDTPTLRI---IKKYEEAVNRYALdqsdSNFNKMmeaqeemdqkdawdyNAEIKTILSKLGI-HDTTKK 156
Cdd:PRK10762 78 EAGIGiihqelNLIPQLTIaenIFLGREFVNRFGR----IDWKKM---------------YAEADKLLARLNLrFSSDKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHL---DFESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:PRK10762 139 VGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 234 lktypgnyedYIVMRAENELVEQKQQEkqkalykqelawMRAGAKARttKQQARINrfnqlesdvktqhtQDKGELNLay 313
Cdd:PRK10762 219 ----------FIAEREVADLTEDSLIE------------MMVGRKLE--DQYPRLD--------------KAPGEVRL-- 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 314 srlgkqvyELKNLSKSINNKVLFEdvteiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-------- 384
Cdd:PRK10762 259 --------KVDNLSGPGVNDVSFT-----LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVtrspqdgl 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 385 ---VAYFKQTEKtldRD-------------IRVIDYLREESEMAKEKDgTSISVTQLLERFLFPSATHGKKVYKLSGGEQ 448
Cdd:PRK10762 326 angIVYISEDRK---RDglvlgmsvkenmsLTALRYFSRAGGSLKHAD-EQQAVSDFIRLFNIKTPSMEQAIGLLSGGNQ 401
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHD 498
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFkaeGLSIILVSSE 454
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
322-519 |
2.55e-12 |
|
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: 66.90 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNeDQDYE---GELKI-GQT--------------- 382
Cdd:TIGR01978 2 KIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-HPSYEvtsGTILFkGQDllelepderaraglf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 383 -----------VKVAYFKQTEKTLDRDIR---VIDyLREESEMAKEKDGTSISVTQLLERFLfpsathgkkVYKLSGGEQ 448
Cdd:TIGR01978 81 lafqypeeipgVSNLEFLRSALNARRSARgeePLD-LLDFEKLLKEKLALLDMDEEFLNRSV---------NEGFSGGEK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFI-HDGKIEK 519
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLrepDRSFLIITHYQRLLNYIKPDYVHVlLDGRIVK 225
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-256 |
2.85e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 15 YADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRYSSQKQDLNGhmtvfEAVLSSDT 94
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGL--------LRPQKGAVLWQGKPLDYSK-----RGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 95 PTLRIIKKYEEAVNRYALDqSDSNFN--KMMEAQEEMDQKdawdyNAEIKTILSKLGIHDttKKIVELSGGQQKRVVLAK 172
Cdd:PRK13638 78 QVATVFQDPEQQIFYTDID-SDIAFSlrNLGVPEAEITRR-----VDEALTLVDAQHFRH--QPIQCLSHGQKKRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 173 TLIEQPDLLLLDEPTNHLDFESIRWLINYVK---QYPHTVLFVTHDRYFLNEVSTRIIELDRGKLKTY--PGNyedyivM 247
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDPAGRTQMIAIIRrivAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHgaPGE------V 223
|
....*....
gi 1842088001 248 RAENELVEQ 256
Cdd:PRK13638 224 FACTEAMEQ 232
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
8-234 |
3.08e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 67.10 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftaDIThPNQYRIRYssQKQDLnGHMTVFE 87
Cdd:PRK13548 5 ARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSG-------ELS-PDSGEVRL--NGRPL-ADWSPAE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 -----AVLSSDTpTLRIIKKYEEAV--NRYALDQSDSNFNKMMEAQeeMDQKDAWDYnaeiktilsklgihdTTKKIVEL 160
Cdd:PRK13548 74 larrrAVLPQHS-SLSFPFTVEEVVamGRAPHGLSRAEDDALVAAA--LAQVDLAHL---------------AGRDYPQL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 161 SGGQQKRVVLAKTLI------EQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHD-----RYflnevSTR 225
Cdd:PRK13548 136 SGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLahqhHVLRLARQLAHERGLAVIVVLHDlnlaaRY-----ADR 210
|
....*....
gi 1842088001 226 IIELDRGKL 234
Cdd:PRK13548 211 IVLLHQGRL 219
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
286-497 |
3.11e-12 |
|
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: 69.39 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 286 ARINRFNQLESDVKTQHTQDKGELNLAYSRLGKQVYELKNLSKSI-----------------NNKVLFEDVTEIIQSGRR 348
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVeyqdngikfeniplvtpNGDVLIESLSFEVPSGNN 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 349 IGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQ----TEKTLdRDiRVIdYLREESEMAK----EKDGTSI 420
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQrpymTLGTL-RD-QII-YPDSSEDMKRrglsDKDLEQI 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 421 ----SVTQLLERFL-FPSATHGKKVykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTEtltiLEDYI----DDFGGS 491
Cdd:TIGR00954 558 ldnvQLTHILEREGgWSAVQDWMDV--LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD----VEGYMyrlcREFGIT 631
|
....*.
gi 1842088001 492 VITVSH 497
Cdd:TIGR00954 632 LFSVSH 637
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
322-497 |
3.24e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 66.45 E-value: 3.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSK----SINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayFKQTEKTLd 396
Cdd:cd03258 3 ELKNVSKvfgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVdGTDL----TLLSGKEL- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIR-----------------VIDYLREESEMAKEKDGTSIS-VTQLLErflFPSATHGKKVY--KLSGGEQKRLYLLRL 456
Cdd:cd03258 78 RKARrrigmifqhfnllssrtVFENVALPLEIAGVPKAEIEErVLELLE---LVGLEDKADAYpaQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1842088001 457 LVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSH 497
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITH 199
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
322-520 |
3.99e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.82 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkqTEKTL-DRDI 399
Cdd:PRK11432 8 VLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDV-------THRSIqQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RV----------------IDY----LREESEMAKEKDGTSISVTQLL---ERFlfpsathgkkVYKLSGGEQKRLYLLRL 456
Cdd:PRK11432 81 CMvfqsyalfphmslgenVGYglkmLGVPKEERKQRVKEALELVDLAgfeDRY----------VDQISGGQQQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 457 LVHKPNVLLLDEPTNDLDTETLTILEDYIDD----FGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKI 520
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDANLRRSMREKIRElqqqFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQI 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
317-474 |
4.58e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.05 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 317 GKQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------------ 383
Cdd:PRK09452 11 LSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQDIthvpaenrhvnt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 384 ---------------KVAYFKQTEKTLDRDI--RVIDYLReeseMAKekdgtsisvtqlLERFLfpsathGKKVYKLSGG 446
Cdd:PRK09452 91 vfqsyalfphmtvfeNVAFGLRMQKTPAAEItpRVMEALR----MVQ------------LEEFA------QRKPHQLSGG 148
|
170 180
....*....|....*....|....*...
gi 1842088001 447 EQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-234 |
5.41e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 66.63 E-value: 5.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYAD---------KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRYS----- 73
Cdd:PRK10419 6 VSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES--------PSQGNVSWRgepla 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 ----SQKQDLNGHMT-VFEAVLSSDTPTLRIIKKYEEAVnRYALDQSDSNfnKMMEAQEEMDQKDawdynaeiktilskL 148
Cdd:PRK10419 78 klnrAQRKAFRRDIQmVFQDSISAVNPRKTVREIIREPL-RHLLSLDKAE--RLARASEMLRAVD--------------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDRYFLNEVST 224
Cdd:PRK10419 141 DDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDLRLVERFCQ 220
|
250
....*....|
gi 1842088001 225 RIIELDRGKL 234
Cdd:PRK10419 221 RVMVMDNGQI 230
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-229 |
6.35e-12 |
|
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: 65.07 E-value: 6.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 19 EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE----DFTADITHPNQYRIRYSSQKQDLnGHMTVFEAVLSSdt 94
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRpdsgEVRWNGTPLAEQRDEPHENILYL-GHLPGLKPELSA-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 95 ptlriikkyEEAVNRYALDQSDSnfnkmmeaqeemdQKDAWDynaeiktILSKLGIHDTTKKIV-ELSGGQQKRVVLAKT 173
Cdd:TIGR01189 91 ---------LENLHFWAAIHGGA-------------QRTIED-------ALAAVGLTGFEDLPAaQLSAGQQRRLALARL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 174 LIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHT---VLFVTHDRyfLNEVSTRIIEL 229
Cdd:TIGR01189 142 WLSRRPLWILDEPTTALDKAGVALLAGLLRAHLARggiVLLTTHQD--LGLVEARELRL 198
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
23-233 |
7.64e-12 |
|
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: 67.05 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIR------YSSQK---------------QD--L 79
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGL--------ERPDSGRIRlggevlQDSARgiflpphrrrigyvfQEarL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 NGHMTVFEavlssdtptlriikkyeeavN-RYALdqsdsNFNKMMEAQEEMDQkdawdynaeiktILSKLGI-HDTTKKI 157
Cdd:COG4148 89 FPHLSVRG--------------------NlLYGR-----KRAPRAERRISFDE------------VVELLGIgHLLDRRP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHT----VLFVTHDryfLNEV---STRIIELD 230
Cdd:COG4148 132 ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDEldipILYVSHS---LDEVarlADHVVLLE 208
|
...
gi 1842088001 231 RGK 233
Cdd:COG4148 209 QGR 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-256 |
8.50e-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: 64.47 E-value: 8.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftaditHPNqYRIryssqkqdLNGHMTvF 86
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------HPK-YEV--------TEGEIL-F 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPTlriikkYEEAVNRYALdqsdsnfnkmmeaqeemdqkdAWDYNAEI-----KTILSKLGihdttkkiVELS 161
Cdd:cd03217 62 KGEDITDLPP------EERARLGIFL---------------------AFQYPPEIpgvknADFLRYVN--------EGFS 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLNEV-STRIIELDRGKlkty 237
Cdd:cd03217 107 GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVaevINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGR---- 182
|
250
....*....|....*....
gi 1842088001 238 pgnyedyIVMRAENELVEQ 256
Cdd:cd03217 183 -------IVKSGDKELALE 194
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-251 |
8.97e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 65.49 E-value: 8.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYRIRYSSQKQ 77
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVlvdgldvatTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 D--LNGHMTVFEAVlssdtptlriikkyeeAVNRY-----ALDQSDsnfnkmmeaQEEMDQkdAWDYnaeiktilskLGI 150
Cdd:COG4604 83 EnhINSRLTVRELV----------------AFGRFpyskgRLTAED---------REIIDE--AIAY----------LDL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 151 HDTTKK-IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHD-----RYfln 220
Cdd:COG4604 126 EDLADRyLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhsvQMMKLLRRLADELGKTVVIVLHDinfasCY--- 202
|
250 260 270
....*....|....*....|....*....|.
gi 1842088001 221 evSTRIIELDRGKLkTYPGNYEDyiVMRAEN 251
Cdd:COG4604 203 --ADHIVAMKDGRV-VAQGTPEE--IITPEV 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
344-519 |
1.03e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 65.38 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 344 QSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI------------GQtVKVAYFKQTEKTLDRDIRVIDYLREESEM 411
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrdkdGQ-LKVADKNQLRLLRTRLTMVFQHFNLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 AKEKDGTSISVTQL--------------LERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDT-- 475
Cdd:PRK10619 108 TVLENVMEAPIQVLglskqeareravkyLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPel 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1842088001 476 --ETLTILEDYIDDfGGSVITVSHDRYFLNKVVQEYWFIHDGKIEK 519
Cdd:PRK10619 188 vgEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
321-477 |
1.03e-11 |
|
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: 64.92 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 321 YELKNLSKSINN---KVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvkvayfkqTEKTLD- 396
Cdd:cd03245 3 IEFRNVSFSYPNqeiPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT--------DIRQLDp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIR-VIDYLREESEM--AKEKD----GTSISVTQLLER---------FLfpsATH--------GKKVYKLSGGEQKRLY 452
Cdd:cd03245 74 ADLRrNIGYVPQDVTLfyGTLRDnitlGAPLADDERILRaaelagvtdFV---NKHpngldlqiGERGRGLSGGQRQAVA 150
|
170 180
....*....|....*....|....*
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNS 175
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
322-500 |
1.13e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvkvAYFKQTEKTLDRDI-- 399
Cdd:PRK11231 4 RTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK---PISMLSSRQLARRLal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 --------------RVIDYLREE--SEMAKEKDGTSISVTQLLERflfpsaTH-----GKKVYKLSGGEQKRLYLLRLLV 458
Cdd:PRK11231 81 lpqhhltpegitvrELVAYGRSPwlSLWGRLSAEDNARVNQAMEQ------TRinhlaDRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 459 HKPNVLLLDEPTNDLD----TETLTILEDyIDDFGGSVITVSHD-----RY 500
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDinhqVELMRLMRE-LNTQGKTVVTVLHDlnqasRY 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
19-234 |
1.15e-11 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 65.20 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 19 EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedFTAD------------ITHPNQYRIRYSSQKQD---LNGhm 83
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF---YVPEngrvlvdghdlaLADPAWLRRQVGVVLQEnvlFNR-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVLSSDT--PTLRIIkkyeeAVNRYAldqsdsnfnkmmeaqeemdqkDAWDYNAEIK----TILSKLGihdttkki 157
Cdd:cd03252 91 SIRDNIALADPgmSMERVI-----EAAKLA---------------------GAHDFISELPegydTIVGEQG-------- 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQY--PHTVLFVTHdRYFLNEVSTRIIELDRGKL 234
Cdd:cd03252 137 AGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
7-474 |
1.29e-11 |
|
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: 67.16 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE--DFTADITHPNQ----YRIRYSSQK---- 76
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSplkaSNIRDTERAgivi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 --QDLN--GHMTVFEAVLSSDTPTLR-IIKKYEEAVNRyaldqsdsnfnkmmeAQEEMDQkdawdynaeiktilSKLGIH 151
Cdd:TIGR02633 83 ihQELTlvPELSVAENIFLGNEITLPgGRMAYNAMYLR---------------AKNLLRE--------------LQLDAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYV---KQYPHTVLFVTHDryfLNEVS----T 224
Cdd:TIGR02633 134 NVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIrdlKAHGVACVYISHK---LNEVKavcdT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 225 RIIELDRGKLKTYPG---NYEDYIVMRAENELveqkqqekqKALYKQElawmragakarttkqqarinrfnqlesdvktQ 301
Cdd:TIGR02633 211 ICVIRDGQHVATKDMstmSEDDIITMMVGREI---------TSLYPHE-------------------------------P 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 302 HTqdkgelnlaysrLGKQVYELKNLS--KSINNKV-LFEDVTEIIQSGRRIGIVGPNGAGKTTLL-------------NI 365
Cdd:TIGR02633 251 HE------------IGDVILEARNLTcwDVINPHRkRVDDVSFSLRRGEILGVAGLVGAGRTELVqalfgaypgkfegNV 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 366 LSN---------------------EDQDYEG---ELKIGQTVKVAYFKQTEKtldrdIRVIDylreeseMAKEKDGTSIS 421
Cdd:TIGR02633 319 FINgkpvdirnpaqairagiamvpEDRKRHGivpILGVGKNITLSVLKSFCF-----KMRID-------AAAELQIIGSA 386
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 422 VTQLLERFLFPSATHGkkvyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:TIGR02633 387 IQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
322-498 |
1.35e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 64.43 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS---NEDQDYEGELKIGQTV---------KVAYFK 389
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlSPAFSASGEVLLNGRRltalpaeqrRIGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QTE--------------------KTLDRDIRVIDYLrEESEMAKekdgtsisvtqLLERFlfpSAThgkkvykLSGGEQK 449
Cdd:COG4136 83 QDDllfphlsvgenlafalpptiGRAQRRARVEQAL-EEAGLAG-----------FADRD---PAT-------LSGGQRA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTE-TLTILE---DYIDDFGGSVITVSHD 498
Cdd:COG4136 141 RVALLRALLAEPRALLLDEPFSKLDAAlRAQFREfvfEQIRQRGIPALLVTHD 193
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
322-474 |
1.57e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 66.01 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---------KVAYFKQT 391
Cdd:PRK13536 43 DLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlGVPVpararlaraRIGVVPQF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EkTLDRDIRVIDYLREESEMAKEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:PRK13536 123 D-NLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
|
...
gi 1842088001 472 DLD 474
Cdd:PRK13536 202 GLD 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
320-498 |
1.67e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSI----NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELK-IGQTV----------- 383
Cdd:PRK10584 6 IVEVHHLKKSVgqgeHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQPLhqmdeearakl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 384 ---KVAYFKQ------TEKTLDrDIRVIDYLREESEMAKEKDGTsisvtQLLERFLFpsathGKKVY----KLSGGEQKR 450
Cdd:PRK10584 86 rakHVGFVFQsfmlipTLNALE-NVELPALLRGESSRQSRNGAK-----ALLEQLGL-----GKRLDhlpaQLSGGEQQR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 451 LYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHD 498
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHD 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
23-230 |
1.78e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKqdlnGHMTvfeavlssdTPTLRiikk 102
Cdd:cd03223 19 DLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR----PYLP---------LGTLR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 103 yeEAVNrYALDQsdsnfnkmmeaqeemdqkdawdynaeiktilsklgihdttkkivELSGGQQKRVVLAKTLIEQPDLLL 182
Cdd:cd03223 82 --EQLI-YPWDD--------------------------------------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1842088001 183 LDEPTNHLDFESIRWLINYVKQYPHTVLFVTHdRYFLNEVSTRIIELD 230
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLD 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-221 |
2.32e-11 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 64.59 E-value: 2.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDfTA--------DITHPN-----QYRIRYSS---QKQDLNGHMTV 85
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEP-TSgkvlidgqDIAAMSrkelrELRRKKISmvfQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAV---LSsdtptLRIIKKYEeavnRYAldqsdsnfnKMMEAqeemdqkdawdynaeiktiLSKLGIHD-TTKKIVELS 161
Cdd:cd03294 120 LENVafgLE-----VQGVPRAE----REE---------RAAEA-------------------LELVGLEGwEHKYPDELS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESIR-----WLINYVKQYPHTVLFVTHDryfLNE 221
Cdd:cd03294 163 GGMQQRVGLARALAVDPDILLMDEAFSALD-PLIRremqdELLRLQAELQKTIVFITHD---LDE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
320-517 |
2.57e-11 |
|
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: 66.47 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSINNKVLF--EDVTEIIQSGRRIGIVGPNGAGKTTL---LNILSNEDQDYEGELKIGQTVKVAYfkqTEKT 394
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLalaLMGLLPHGGRISGEVLLDGRDLLEL---SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 LDRDIRVI--------DYLREESEMAKEKDGTSIS-------VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVH 459
Cdd:COG1123 81 RGRRIGMVfqdpmtqlNPVTVGDQIAEALENLGLSraeararVLELLEAVGLERRLD-RYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 460 KPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG1123 160 DPDLLIADEPTTALDVttqaEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-234 |
2.87e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIE--HLNKSY----ADKEIfndlNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRYSSQK 76
Cdd:COG3845 1 MMPPALElrGITKRFggvvANDDV----SLTVRPGEIHALLGENGAGKSTLMKILYGL--------YQPDSGEILIDGKP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNG--------------H------MTVFE-AVLSSDTPTLRIIkkyeeavnryaldqsdsnfnkmmeaqeemDQKDAw 135
Cdd:COG3845 69 VRIRSprdaialgigmvhqHfmlvpnLTVAEnIVLGLEPTKGGRL-----------------------------DRKAA- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 136 dyNAEIKTILSKLGIH-DTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLinyVKQyPH 207
Cdd:COG3845 119 --RARIRELSERYGLDvDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTpqeadelFEILRRL---AAE-GK 192
|
250 260 270
....*....|....*....|....*....|
gi 1842088001 208 TVLFVTHDryfLNEV---STRIIELDRGKL 234
Cdd:COG3845 193 SIIFITHK---LREVmaiADRVTVLRRGKV 219
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-191 |
2.96e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 25 NLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTAdiTHPNQYRIRYSSQKQDLNGHMTVFEAVLSSD 93
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFltpasgsltlnGQDHTT--TPPSRRPVSMLFQENNLFSHLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 94 TPTLRiikkyeeavnryaLDQsdsnfnkmmeaqeemDQKDawdynaEIKTILSKLGIHDTTKKI-VELSGGQQKRVVLAK 172
Cdd:PRK10771 97 NPGLK-------------LNA---------------AQRE------KLHAIARQMGIEDLLARLpGQLSGGQRQRVALAR 142
|
170
....*....|....*....
gi 1842088001 173 TLIEQPDLLLLDEPTNHLD 191
Cdd:PRK10771 143 CLVREQPILLLDEPFSALD 161
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-243 |
2.99e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.39 E-value: 2.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVIggldedftadiTH---PNQYRIRyssqkqdLNGH 82
Cdd:PRK11160 341 LNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL-----------TRawdPQQGEIL-------LNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 MtvfeavlssdtptlriIKKYEEAVNRYA---LDQSDSNFNKMMEAQEEMDQKDAWDynAEIKTILSKLGIHdttkKIVE 159
Cdd:PRK11160 403 P----------------IADYSEAALRQAisvVSQRVHLFSATLRDNLLLAAPNASD--EALIEVLQQVGLE----KLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 ---------------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQypH----TVLFVTHDRYFLN 220
Cdd:PRK11160 461 ddkglnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE--HaqnkTVLMITHRLTGLE 538
|
250 260
....*....|....*....|...
gi 1842088001 221 EVStRIIELDRGKLKTYpGNYED 243
Cdd:PRK11160 539 QFD-RICVMDNGQIIEQ-GTHQE 559
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
8-216 |
3.01e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.58 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTAdiTHPNQYR--IRYSS 74
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLisptsgtllfeGEDIST--LKPEIYRqqVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNGHmTVFEAV-----LSSDTPTLriiKKYEEAVNRYALDQsdsnfnkmmeaqeemdqkdawdynaeikTILsklg 149
Cdd:PRK10247 88 QTPTLFGD-TVYDNLifpwqIRNQQPDP---AIFLDDLERFALPD----------------------------TIL---- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 150 ihdtTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDfESIRWLIN-----YVKQYPHTVLFVTHDR 216
Cdd:PRK10247 132 ----TKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD-ESNKHNVNeiihrYVREQNIAVLWVTHDK 198
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
322-498 |
3.45e-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: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINN-KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFK 389
Cdd:cd03295 2 EFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QT-----EKTLDRDIRVIDYLREESEMAKEKdgtsiSVTQLLERFLFPSATHGKKV-YKLSGGEQKRLYLLRLLVHKPNV 463
Cdd:cd03295 82 QQiglfpHMTVEENIALVPKLLKWPKEKIRE-----RADELLALVGLDPAEFADRYpHELSGGQQQRVGVARALAADPPL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 1842088001 464 LLLDEPTNDLDTETLTILEDYI----DDFGGSVITVSHD 498
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFkrlqQELGKTIVFVTHD 195
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
321-498 |
3.53e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 321 YELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTV-----------KVAYFK 389
Cdd:PRK10575 12 FALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 Q----TEKTLDRDIRVID----------YLREESEMAKEkdgtSISVTQLLerflfPSAThgKKVYKLSGGEQKRLYLLR 455
Cdd:PRK10575 92 QqlpaAEGMTVRELVAIGrypwhgalgrFGAADREKVEE----AISLVGLK-----PLAH--RLVDSLSGGERQRAWIAM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 456 LLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK10575 161 LVAQDSRCLLLDEPTSALDiahqVDVLALVHRLSQERGLTVIAVLHD 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
322-517 |
3.63e-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: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVL-FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK----------VAYFK 389
Cdd:cd03254 4 EFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QTEKTLDRDIRV-IDYLREESEMAKEKD-GTSISVTQLLERF---LFPSATHGKKVykLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:cd03254 84 QDTFLFSGTIMEnIRLGRPNATDEEVIEaAKEAGAHDFIMKLpngYDTVLGENGGN--LSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 465 LLDEPTNDLDTETLTILEDYIDDF--GGSVITVSHdRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLmkGRTSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-234 |
3.71e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.47 E-value: 3.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYA-----DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSQKQDL 79
Cdd:PRK13641 2 SIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNAL---------------LKPSSGTITI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 NG-HMTvfeavLSSDTPTLRIIKKYEEAVNRYAldqsdsnfnkmmEAQ--EEMDQKD---------AWDYNAEIKTI--L 145
Cdd:PRK13641 67 AGyHIT-----PETGNKNLKKLRKKVSLVFQFP------------EAQlfENTVLKDvefgpknfgFSEDEAKEKALkwL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 146 SKLGIHDT--TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLN 220
Cdd:PRK13641 130 KKVGLSEDliSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQkagHTVILVTHNMDDVA 209
|
250
....*....|....
gi 1842088001 221 EVSTRIIELDRGKL 234
Cdd:PRK13641 210 EYADDVLVLEHGKL 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
322-499 |
3.91e-11 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 65.12 E-value: 3.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN-EDQDyEGELKI-GQTV-KVAyfkqTEKtldRD 398
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGfETPD-SGRILLdGRDVtGLP----PEK---RN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVI--DY---------------LR----EESEMAKEkdgtsisVTQLLERF-LfpSATHGKKVYKLSGGEQKRLYLLRL 456
Cdd:COG3842 79 VGMVfqDYalfphltvaenvafgLRmrgvPKAEIRAR-------VAELLELVgL--EGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 457 LVHKPNVLLLDEPTNDLD--------TETLTILEdyidDFGGSVITVSHDR 499
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDaklreemrEELRRLQR----ELGITFIYVTHDQ 196
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-229 |
4.11e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.51 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 20 IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQ--YRIRYSSQKQDLN-GHMTVFEAVLSSdtpt 96
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGplDFQRDSIARGLLYlGHAPGIKTTLSV---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 97 lriikkyEEAVNRYALDQSDSnfnkmmeaqeemdqkdawdynaEIKTILSKLGIHDTTKKIV-ELSGGQQKRVVLAKTLI 175
Cdd:cd03231 91 -------LENLRFWHADHSDE----------------------QVEEALARVGLNGFEDRPVaQLSAGQQRRVALARLLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 176 EQPDLLLLDEPTNHLDFESIRWLINYVKQypHT-----VLFVTHDRYFLNEVSTRIIEL 229
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAG--HCarggmVVLTTHQDLGLSEAGARELDL 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
320-477 |
4.24e-11 |
|
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: 62.26 E-value: 4.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSIN----NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN--EDQDYEGELKIGQTVKVAYFKqtek 393
Cdd:cd03232 3 VLTWKNLNYTVPvkggKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQ---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 tldrdiRVIDYLreesemakEKDGTSISVTQLLERFLFPSATHGkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:cd03232 79 ------RSTGYV--------EQQDVHSPNLTVREALRFSALLRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
....
gi 1842088001 474 DTET 477
Cdd:cd03232 140 DSQA 143
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
332-497 |
4.73e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 65.90 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 332 NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQTEKTLDRDIR 400
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdGVPLvqydhhylhrQVALVGQEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 V-IDYLREESEMAkekDGTSISVTQLLERFL--FPSATH---GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:TIGR00958 573 EnIAYGLTDTPDE---EIMAAAKAANAHDFImeFPNGYDtevGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|...
gi 1842088001 475 TETLTILEDYIDDFGGSVITVSH 497
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
17-236 |
4.90e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 63.98 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI-------THPNQYRIRYssqkqdlnghmtvfeav 89
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllTEENVWDIRH----------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 lssdtptlRIIKKYEEAVNRY--ALDQSDSNF---NKMMeAQEEMDQKdawdynaeIKTILSKLGIHD-TTKKIVELSGG 163
Cdd:PRK13650 82 --------KIGMVFQNPDNQFvgATVEDDVAFgleNKGI-PHEEMKER--------VNEALELVGMQDfKEREPARLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 164 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK----QYPHTVLFVTHDryfLNEV--STRIIELDRGKLKT 236
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKgirdDYQMTVISITHD---LDEValSDRVLVMKNGQVES 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
9-234 |
5.51e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 63.47 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 9 EHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL----DEDFTADITHPNQY-------RIRYSSQKQ 77
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLmtpaHGHVWLDGEHIQHYaskevarRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSSDTPT----LRIIKKYEEAVNRyaldqsdsnfnkMMEAQeemdqkdawdynaeiktilsklGIHDT 153
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHqplfTRWRKEDEEAVTK------------AMQAT----------------------GITHL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 TKKIVE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDryfLNEV---STR 225
Cdd:PRK10253 137 ADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHD---LNQAcryASH 213
|
....*....
gi 1842088001 226 IIELDRGKL 234
Cdd:PRK10253 214 LIALREGKI 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
5-234 |
5.67e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 63.47 E-value: 5.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrirYSSQKqdlnGH 82
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL-----------------LKPQS----GE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 MTVFEAVLSSDTptLRIIKK-----YEEAVNRY--ALDQSDSNF---NKMMEaQEEMDQKdawdynaeIKTILSKLGIHD 152
Cdd:PRK13632 66 IKIDGITISKEN--LKEIRKkigiiFQNPDNQFigATVEDDIAFgleNKKVP-PKKMKDI--------IDDLAKKVGMED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 153 TTKKIVE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDryfLNEV--STR 225
Cdd:PRK13632 135 YLDKEPQnLSGGQKQRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD---MDEAilADK 211
|
....*....
gi 1842088001 226 IIELDRGKL 234
Cdd:PRK13632 212 VIVFSEGKL 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
285-497 |
6.94e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 65.21 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 285 QARINRFNQLESDVKTQHTQDKGELNLAYSRlGKQVyELKNLS-KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLL 363
Cdd:COG4178 329 RATVDRLAGFEEALEAADALPEAASRIETSE-DGAL-ALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 364 NILSNEDQDYEGELKIGQTVKVAYFKQT----EKTLdRDirVIDYLREESEMAKEKdgtsisVTQLLERFLFPSATH--- 436
Cdd:COG4178 407 RAIAGLWPYGSGRIARPAGARVLFLPQRpylpLGTL-RE--ALLYPATAEAFSDAE------LREALEAVGLGHLAErld 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 437 -----GKKvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDD--FGGSVITVSH 497
Cdd:COG4178 478 eeadwDQV---LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
325-509 |
7.70e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 61.89 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 325 NLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK---VAYFKQTEKTLDRD-I 399
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlCTYQKQLCFVGHRSgI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDYLREESEMAKEKDGTSISVTQL-----LERFL-FPSAThgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGITELcrlfsLEHLIdYPCGL-------LSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 474 DTETLTILEDYIDDF---GGSVITVSHDRYFLNKV-VQEY 509
Cdd:PRK13540 159 DELSLLTIITKIQEHrakGGAVLLTSHQDLPLNKAdYEEY 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-187 |
7.80e-11 |
|
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: 62.31 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFT-------ADITH--PNQyRIR----YS 73
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSgsirfdgEDITGlpPHR-IARlgigYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 SQKQDLNGHMTVFEavlssdtpTLRIIkkyeeAVNRYALDQSDSNFNKMMEA----QEEMDQKdAWDynaeiktilsklg 149
Cdd:COG0410 84 PEGRRIFPSLTVEE--------NLLLG-----AYARRDRAEVRADLERVYELfprlKERRRQR-AGT------------- 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1842088001 150 ihdttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPT 187
Cdd:COG0410 137 ----------LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-260 |
8.68e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.87 E-value: 8.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG-----------------LDedftadithPNQYR--IRYSS 74
Cdd:PRK11174 359 SPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingielreLD---------PESWRkhLSWVG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QKQDLNgHMTVFEAVLSSDtPTLRiikkyEEAVNRyALDQSD-SNFNKMMEaqeemdqkDAWDYnaEIKTilSKLGihdt 153
Cdd:PRK11174 430 QNPQLP-HGTLRDNVLLGN-PDAS-----DEQLQQ-ALENAWvSEFLPLLP--------QGLDT--PIGD--QAAG---- 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 tkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH--TVLFVTHDRYFLNEVSTrIIELDR 231
Cdd:PRK11174 486 ------LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRrqTTLMVTHQLEDLAQWDQ-IWVMQD 558
|
250 260 270
....*....|....*....|....*....|..
gi 1842088001 232 GKLkTYPGNYEDyiVMRAEN---ELVEQKQQE 260
Cdd:PRK11174 559 GQI-VQQGDYAE--LSQAGGlfaTLLAHRQEE 587
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-214 |
9.24e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 62.62 E-value: 9.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDL--- 79
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARVSGEVYLDGQDIFKMDViel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 80 -NGHMTVFEavLSSDTPTLRIIKKYEEAVNryaldqsdsnFNKMMEAQEEMDQKDAWdynaeiktILSKLGIHDTTKKIV 158
Cdd:PRK14247 81 rRRVQMVFQ--IPNPIPNLSIFENVALGLK----------LNRLVKSKKELQERVRW--------ALEKAQLWDEVKDRL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 159 E-----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQyPHTVLFVTH 214
Cdd:PRK14247 141 DapagkLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENtakIESLFLELKK-DMTIVLVTH 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-474 |
9.97e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 64.48 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 294 LESDVKTQHTQDKgELNlaysrlGKQVYEL--KNLS-KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEd 370
Cdd:PRK11174 328 LETPLAHPQQGEK-ELA------SNDPVTIeaEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 371 QDYEGELKI-GQTVK----------VAY-------FKQTektldrdirvidyLREESEMAKEkDGTSISVTQLLER---- 428
Cdd:PRK11174 400 LPYQGSLKInGIELReldpeswrkhLSWvgqnpqlPHGT-------------LRDNVLLGNP-DASDEQLQQALENawvs 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 429 -FLfPSATHG------KKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK11174 466 eFL-PLLPQGldtpigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-193 |
1.03e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDftaditHPNQYRIRYssQKQDLNGHMTV 85
Cdd:COG2401 31 LEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG------TPVAGCVDV--PDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTPTLRIikkyeEAVNRYALDqsdsnfnkmmeaqeemdqkDAWDYNAEIKtilsklgihdttkkivELSGGQQ 165
Cdd:COG2401 103 IDAIGRKGDFKDAV-----ELLNAVGLS-------------------DAVLWLRRFK----------------ELSTGQK 142
|
170 180
....*....|....*....|....*...
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLDFE 193
Cdd:COG2401 143 FRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-234 |
1.28e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyriRYSSQ-KQDLNGHM-TVFEavlSSDTPTLRI 99
Cdd:PRK13648 26 KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDnFEKLRKHIgIVFQ---NPDNQFVGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 100 IKKYEEAvnrYALDQSDSNFNKMM----EAQEEMDQKDAWDYNAEiktilsklgihdttkkivELSGGQQKRVVLAKTLI 175
Cdd:PRK13648 100 IVKYDVA---FGLENHAVPYDEMHrrvsEALKQVDMLERADYEPN------------------ALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 176 EQPDLLLLDEPTNHLD---FESIRWLINYVKQYPH-TVLFVTHDryfLNEV--STRIIELDRGKL 234
Cdd:PRK13648 159 LNPSVIILDEATSMLDpdaRQNLLDLVRKVKSEHNiTIISITHD---LSEAmeADHVIVMNKGTV 220
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
342-498 |
1.54e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 342 IIQSGRRIGIVGPNGAGKTTLLNILSNEDQ----DYEGELKIGQTVKvaYFKQTE------KTLDRDIRV------IDYL 405
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIpnlgDYEEEPSWDEVLK--RFRGTElqnyfkKLYNGEIKVvhkpqyVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 406 ReesemaKEKDGTsisVTQLLER------------FLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:PRK13409 173 P------KVFKGK---VRELLKKvdergkldevveRLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180
....*....|....*....|....*..
gi 1842088001 474 DTETLTILEDYIDDF--GGSVITVSHD 498
Cdd:PRK13409 244 DIRQRLNVARLIRELaeGKYVLVVEHD 270
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
322-497 |
1.67e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEK------- 393
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIR----RQRDEyhqdlly 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 -----TLDRDIRVIDYLREESEMAKEKDGTSIsvTQLLERF------LFPSAThgkkvykLSGGEQKRLYLLRLLVHKPN 462
Cdd:PRK13538 79 lghqpGIKTELTALENLRFYQRLHGPGDDEAL--WEALAQVglagfeDVPVRQ-------LSAGQQRRVALARLWLTRAP 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1842088001 463 VLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHaeqGGMVILTTH 187
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
7-233 |
1.77e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 62.37 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIF-----NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSQKQDLNG 81
Cdd:PRK13637 4 KIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGL---------------LKPTSGKIIIDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 -HMTVFEAVLSSDTPTLRIIKKY------EEAVNR------YALDQSDSNFNKMMEAQEEMDQKDAWDYNaeiktilskl 148
Cdd:PRK13637 69 vDITDKKVKLSDIRKKVGLVFQYpeyqlfEETIEKdiafgpINLGLSEEEIENRVKRAMNIVGLDYEDYK---------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 gihdtTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLinyVKQYPHTVLFVTHDRYFLNE 221
Cdd:PRK13637 139 -----DKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDpkgrdeiLNKIKEL---HKEYNMTIILVSHSMEDVAK 210
|
250
....*....|..
gi 1842088001 222 VSTRIIELDRGK 233
Cdd:PRK13637 211 LADRIIVMNKGK 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
338-517 |
1.84e-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: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTeiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQtVKVAYFKQTEK---------------TLDRDI--- 399
Cdd:cd03298 18 DLT--FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-VDVTAAPPADRpvsmlfqennlfahlTVEQNVglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVID-YLREESEMAKEKDGTSISVTQLLERFlfPSAthgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD---- 474
Cdd:cd03298 95 LSPGlKLTAEDRQAIEVALARVGLAGLEKRL--PGE--------LSGGERQRVALARVLVRDKPVLLLDEPFAALDpalr 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1842088001 475 TETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:cd03298 165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-56 |
1.98e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 61.64 E-value: 1.98e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1842088001 13 KSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE 56
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILE 77
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-234 |
2.08e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.40 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIG---GLDED---------FTADITHPNQYRI 70
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllELNEEarvegevrlFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSS------QKQDLNGHMTVFEAVlssdtptlRIIKKYeeavnryaldqsdsnfNKMMEAQEEMDQKDAWdynaeiktI 144
Cdd:PRK14267 82 EVRRevgmvfQYPNPFPHLTIYDNV--------AIGVKL----------------NGLVKSKKELDERVEW--------A 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 145 LSKLGIHDTTK-----KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQyPHTVLFVTHDR 216
Cdd:PRK14267 130 LKKAALWDEVKdrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELKK-EYTIVLVTHSP 208
|
250
....*....|....*...
gi 1842088001 217 YFLNEVSTRIIELDRGKL 234
Cdd:PRK14267 209 AQAARVSDYVAFLYLGKL 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
322-517 |
2.59e-10 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 61.16 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLL---NILsnEDQDyEGELKIGqtvkvayfkqtEKTLDRD 398
Cdd:COG1126 3 EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLrciNLL--EEPD-SGTITVD-----------GEDLTDS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVIDYLREESEMakekdgtsisVTQlleRF-LFPSAT----------HGKKVYK------------------------- 442
Cdd:COG1126 69 KKDINKLRRKVGM----------VFQ---QFnLFPHLTvlenvtlapiKVKKMSKaeaeeramellervgladkadaypa 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 443 -LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDfGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:COG1126 136 qLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELvgevLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
322-519 |
2.67e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 62.03 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFE-----DVTEIIQSGRRIGIVGPNGAGKTTL---LNILSNEDQD-----YEGELKIGQTVKVAYF 388
Cdd:PRK13651 4 KVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGtiewiFKDEKNKKKTKEKEKV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 389 KQT---EKTLDRDIRVIDYLRE-------------------------------ESEMAKEKDGTSISVTQLLERFLfpsa 434
Cdd:PRK13651 84 LEKlviQKTRFKKIKKIKEIRRrvgvvfqfaeyqlfeqtiekdiifgpvsmgvSKEEAKKRAAKYIELVGLDESYL---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 435 thGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE-TLTILE--DYIDDFGGSVITVSHDryfLNKVVQeyW- 510
Cdd:PRK13651 160 --QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD---LDNVLE--Wt 232
|
250
....*....|...
gi 1842088001 511 ----FIHDGKIEK 519
Cdd:PRK13651 233 krtiFFKDGKIIK 245
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
343-501 |
2.75e-10 |
|
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: 61.27 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIgQTVKVAYFKQTEKTlDRDIRVIDYLRE-----------ESEM 411
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIKA-DYEGTVRDLLSSitkdfythpyfKTEI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 AKekdgtSISVTQLLERflfpsathgkKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE----TLTILEDYIDD 487
Cdd:cd03237 100 AK-----PLQIEQILDR----------EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAEN 164
|
170
....*....|....
gi 1842088001 488 FGGSVITVSHDRYF 501
Cdd:cd03237 165 NEKTAFVVEHDIIM 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
342-498 |
2.83e-10 |
|
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: 63.26 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 342 IIQSGRRIGIVGPNGAGKTTLLNILSNEDQ----DYEGELKIGQTVKvaYFKQTE------KTLDRDIRV------IDYL 405
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKpnlgDYDEEPSWDEVLK--RFRGTElqdyfkKLANGEIKVahkpqyVDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 406 reesemAKEKDGTsisVTQLLER------------FLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:COG1245 173 ------PKVFKGT---VRELLEKvdergkldelaeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*....
gi 1842088001 474 D-TETLT---ILEDYIDDfGGSVITVSHD 498
Cdd:COG1245 244 DiYQRLNvarLIRELAEE-GKYVLVVEHD 271
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
337-477 |
2.83e-10 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 60.56 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQTEKTLDRDIR-VIDY 404
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPIsqyehkylhsKVSLVGQEPVLFARSLQdNIAY 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 405 -LREES-EMAKEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:cd03248 111 gLQSCSfECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
337-499 |
3.35e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 63.06 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTLDRDIRVI------------D 403
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIR----TVTRASLRRNIAVVfqdaglfnrsieD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 404 YLR--------EESEMAKEKdgtsISVTQLLERFLFPSATH-GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK13657 428 NIRvgrpdatdEEMRAAAER----AQAHDFIERKPDGYDTVvGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
170 180
....*....|....*....|....*
gi 1842088001 475 TETLTILEDYIDdfggsviTVSHDR 499
Cdd:PRK13657 504 VETEAKVKAALD-------ELMKGR 521
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-227 |
3.64e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 61.67 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITHPNQYRIR-------------YSSqkqdLN 80
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRL-EEPTSgeilfdgqDITGLSGRELRplrrrmqmvfqdpYAS----LN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 GHMTVFEAVlssdtptlriikkyEEAvnryaldqsdsnfnkmMEAQEEMDQKDAwdyNAEIKTILSKLGI---------H 151
Cdd:COG4608 110 PRMTVGDII--------------AEP----------------LRIHGLASKAER---RERVAELLELVGLrpehadrypH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 dttkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSIR-----WLINYVKQYPHTVLFVTHD----RYflneV 222
Cdd:COG4608 157 -------EFSGGQRQRIGIARALALNPKLIVCDEPVSALDV-SIQaqvlnLLEDLQDELGLTYLFISHDlsvvRH----I 224
|
....*
gi 1842088001 223 STRII 227
Cdd:COG4608 225 SDRVA 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
343-497 |
3.70e-10 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 60.37 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSN-----------EDQDYE-------------------GELKIGQTVKVAyfkqte 392
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGfltpasgsltlNGQDHTttppsrrpvsmlfqennlfSHLTVAQNIGLG------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 ktLDRDIRVIDYLREE-SEMAKEkdgtsISVTQLLERFlfPSAthgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:PRK10771 96 --LNPGLKLNAAQREKlHAIARQ-----MGIEDLLARL--PGQ--------LSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190
....*....|....*....|....*....|
gi 1842088001 472 DLD----TETLTILEDYIDDFGGSVITVSH 497
Cdd:PRK10771 159 ALDpalrQEMLTLVSQVCQERQLTLLMVSH 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
322-497 |
4.21e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.35 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVA-------------- 386
Cdd:COG3845 7 ELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRsprdaialgigmvh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 387 -YFKQTEkTL-----------DRDIRVIDyLREESEMAKEkdgtsisvtqLLERFLF---PSAthgkKVYKLSGGEQKRL 451
Cdd:COG3845 87 qHFMLVP-NLtvaenivlglePTKGGRLD-RKAARARIRE----------LSERYGLdvdPDA----KVEDLSVGEQQRV 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDL---DTETL-TILEDYIDDfGGSVITVSH 497
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLtpqEADELfEILRRLAAE-GKSIIFITH 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
142-242 |
4.21e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 4.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 142 KTILSKLGIHDT--TKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRW---LINYVKQYPHTVLFVTHDR 216
Cdd:PRK13631 157 KFYLNKMGLDDSylERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEmmqLILDAKANNKTVFVITHTM 236
|
90 100
....*....|....*....|....*.
gi 1842088001 217 YFLNEVSTRIIELDRGKLKTYPGNYE 242
Cdd:PRK13631 237 EHVLEVADEVIVMDKGKILKTGTPYE 262
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
322-470 |
4.28e-10 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 60.14 E-value: 4.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSI-NNKVLFeDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIG----------QTVK--VAYF 388
Cdd:cd03224 2 EVENLNAGYgKSQILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglpphERARagIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 389 KQTEktldrdiRVIDYL--REESEMA---KEKDGTSISVTQLLErfLFP--SATHGKKVYKLSGGEQKRLYLLRLLVHKP 461
Cdd:cd03224 81 PEGR-------RIFPELtvEENLLLGayaRRRAKRKARLERVYE--LFPrlKERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
....*....
gi 1842088001 462 NVLLLDEPT 470
Cdd:cd03224 152 KLLLLDEPS 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
324-498 |
4.41e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 60.29 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 324 KNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQT------------VKVAYFKQt 391
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplhararRGIGYLPQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRDIRVIDYLREESEMAKE--KDGTSISVTQLLERFlfpSATHGKKVY--KLSGGEQKRLYLLRLLVHKPNVLLLD 467
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQIRDDlsAEQREDRANELMEEF---HIEHLRDSMgqSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 1842088001 468 EPTNDLDTETLTILEDYID---DFGGSVITVSHD 498
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEhlrDSGLGVLITDHN 196
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-194 |
6.30e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 62.74 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIR------YSSQKQDLNGHMTVFEAVL 90
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdinlkwWRSKIGVVSQDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 91 SSDTP-TLRIIKKYEEAVNRYALDQSDSNFNKmmEAQEEMDQKDAWDYNAEIKTILSKLGIH--------------DTTK 155
Cdd:PTZ00265 477 KNNIKySLYSLKDLEALSNYYNEDGNDSQENK--NKRNSCRAKCAGDLNDMSNTTDSNELIEmrknyqtikdsevvDVSK 554
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIV---------------------ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 194
Cdd:PTZ00265 555 KVLihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-237 |
6.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrIRYSSQKQDLNG 81
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGI---------------LKPTSGSVLIRG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEavlssdtpTLRIIKKYEEAVNRYALDQ-------SDSNFNKMMEAQEEMDQKDawdynaEIKTILSKLGIHDTT 154
Cdd:PRK13652 66 EPITKE--------NIREVRKFVGLVFQNPDDQifsptveQDIAFGPINLGLDEETVAH------RVSSALHMLGLEELR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 KKIVE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYV----KQYPHTVLFVTHDRYFLNEVSTRIIEL 229
Cdd:PRK13652 132 DRVPHhLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLndlpETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
....*...
gi 1842088001 230 DRGKLKTY 237
Cdd:PRK13652 212 DKGRIVAY 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
318-497 |
6.45e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 6.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS---NEDQDYEGELKI-GQTVkvayfkQTEK 393
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELlGRTV------QREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRDIR--------------------VIDY---------------LREESEMAKEKdgtsisVTQLLERFLFPSATHgK 438
Cdd:PRK09984 76 RLARDIRksrantgyifqqfnlvnrlsVLENvligalgstpfwrtcFSWFTREQKQR------ALQALTRVGMVHFAH-Q 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 439 KVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF----GGSVITVSH 497
Cdd:PRK09984 149 RVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInqndGITVVVTLH 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-259 |
7.18e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 60.49 E-value: 7.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLkviggldEDFTADIThPNQYRIRYSSQKQDLNGHMTVFEAVLSSDT---PTLR 98
Cdd:PRK13651 24 DNVSVEINQGEFIAIIGQTGSGKTTFI-------EHLNALLL-PDTGTIEWIFKDEKNKKKTKEKEKVLEKLViqkTRFK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 99 IIKKYEEAVNR---------YALDQS----DSNFNKM-MEAQEEMDQKDAWDYnaeIKtiLSKLGIHDTTKKIVELSGGQ 164
Cdd:PRK13651 96 KIKKIKEIRRRvgvvfqfaeYQLFEQtiekDIIFGPVsMGVSKEEAKKRAAKY---IE--LVGLDESYLQRSPFELSGGQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKLkTYPGNy 241
Cdd:PRK13651 171 KRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKI-IKDGD- 248
|
250
....*....|....*...
gi 1842088001 242 eDYIVMRAENELVEQKQQ 259
Cdd:PRK13651 249 -TYDILSDNKFLIENNME 265
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-240 |
7.45e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.13 E-value: 7.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyrirYSSQKqdlnGHM 83
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGI-----------------YLPQR----GRV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVLSSDTptlriIKKYEEAVNRYALDQSDSNFN------------KMMEAQEEMDQKdawdynaeIKTILSKLGIH 151
Cdd:PRK13647 63 KVMGREVNAEN-----EKWVRSKVGLVFQDPDDQVFSstvwddvafgpvNMGLDKDEVERR--------VEEALKAVRMW 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTTKKI-VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK13647 130 DFRDKPpYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVI 209
|
250
....*....|...
gi 1842088001 228 ELDRGKLKTYPGN 240
Cdd:PRK13647 210 VLKEGRVLAEGDK 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
337-498 |
1.02e-09 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 59.02 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkqTEKTLDRDIRVIDY-------LREE 408
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQI-------TEPGPDRMVVFQNYsllpwltVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 409 SEMAKEKDGTSIS-------VTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTIL 481
Cdd:TIGR01184 75 IALAVDRVLPDLSkserraiVEEHIALVGLTEAAD-KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180
....*....|....*....|.
gi 1842088001 482 EDYI----DDFGGSVITVSHD 498
Cdd:TIGR01184 154 QEELmqiwEEHRVTVLMVTHD 174
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-194 |
1.04e-09 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 59.09 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVI-------GG---LDEDFTADItHPNQYR--IRYSSQkqdlnghmt 84
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfydptSGeilLDGVDIRDL-NLRWLRsqIGLVSQ--------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 vfEAVLSSDTptlriIKKyeeavN-RYALDqsdsnfnkmmEAQEEMDQKDAWDYNAEiKTILSKLGIHDTT--KKIVELS 161
Cdd:cd03249 85 --EPVLFDGT-----IAE-----NiRYGKP----------DATDEEVEEAAKKANIH-DFIMSLPDGYDTLvgERGSQLS 141
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 194
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
322-469 |
1.05e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 59.27 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-----------VAYFK 389
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 390 QtEKTLDRDIRVIDYLR---EESEMAKEKDgtSISVTQLLERFlfpSATHGKKV--YKLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:COG1137 85 Q-EASIFRKLTVEDNILavlELRKLSKKER--EERLEELLEEF---GITHLRKSkaYSLSGGERRRVEIARALATNPKFI 158
|
....*
gi 1842088001 465 LLDEP 469
Cdd:COG1137 159 LLDEP 163
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-233 |
1.05e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 11 LNKSYADKEIFNDLNLSISEHERIGLVGINGTGKST----LLKVIGGLDEDFTADitHPNQYRIR-----YSSQKQdlng 81
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEIWFDG--QPLHNLNRrqllpVRHRIQ---- 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 hmTVFEAVLSSDTPTLRIIKKYEE--AVNRYALDQsdsnfnkmmeAQEEmdqkdawdynAEIKTILSKLGIHDTTKK--I 157
Cdd:PRK15134 366 --VVFQDPNSSLNPRLNVLQIIEEglRVHQPTLSA----------AQRE----------QQVIAVMEEVGLDPETRHryP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK--QYPHTV--LFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKslQQKHQLayLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-200 |
1.08e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 58.73 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDftADITHPNQyRIRYSSQKQDLNGHMTV 85
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLlppaagtikldGGD--IDDPDVAE-ACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FE------AVLssDTPTLRIikkyEEAVNRYALDqsdsnfnkmmeaqeemdqkdawdynaeiktilsklgiHDTTKKIVE 159
Cdd:PRK13539 91 AEnlefwaAFL--GGEELDI----AAALEAVGLA-------------------------------------PLAHLPFGY 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLIN 200
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
24-234 |
1.19e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 24 LNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---------THPNQYRIRYSSqkqdlnghmtVFeavlsSDt 94
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvtaEQPEDYRKLFSA----------VF-----TD- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 95 ptlriikkyeeavnrYALdqsdsnFNKMMEAQEEMDQKDAWDYNAEIKTILSKLGIHDTTKKIVELSGGQQKRVVLAKTL 174
Cdd:PRK10522 406 ---------------FHL------FDQLLGPEGKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKKRLALLLAL 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 175 IEQPDLLLLDEPTNHLD--FESI--RWLINYVKQYPHTVLFVTH-DRYFlnEVSTRIIELDRGKL 234
Cdd:PRK10522 465 AEERDILLLDEWAADQDphFRREfyQVLLPLLQEMGKTIFAISHdDHYF--IHADRLLEMRNGQL 527
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-186 |
1.25e-09 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 58.89 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKST-------LLKVIGG---LDEDftaDITHPNQYR-----IR 71
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymivgLVKPDSGrifLDGE---DITHLPMHKrarlgIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFE---AVLSsdtpTLRIIKKyeeavnryaldqsdsnfnkmmEAQEEMDQkdawdynaeiktILSKL 148
Cdd:COG1137 82 YLPQEASIFRKLTVEDnilAVLE----LRKLSKK---------------------EREERLEE------------LLEEF 124
|
170 180 190
....*....|....*....|....*....|....*....
gi 1842088001 149 GI-HDTTKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEP 186
Cdd:COG1137 125 GItHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-516 |
1.35e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.18 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEdQDYEGELKIGQT-----------VKVAYFKQTEKTLdRDIRVIDYLREESEM 411
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQpleawsaaelaRHRAYLSQQQTPP-FAMPVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 AKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYL--LRLLVHK---PN--VLLLDEPTNDLDTETLTILEDY 484
Cdd:PRK03695 97 KTRTEAVASALNEVAEALGLDDKLG-RSVNQLSGGEWQRVRLaaVVLQVWPdinPAgqLLLLDEPMNSLDVAQQAALDRL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1842088001 485 IDDF---GGSVITVSHDryfLNKVVQE---YWFIHDGK 516
Cdd:PRK03695 176 LSELcqqGIAVVMSSHD---LNHTLRHadrVWLLKQGK 210
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
327-477 |
1.45e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 58.04 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 327 SKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNedqDYEGELKIGQTVKvaY----FKQTEKTLDRDIRvi 402
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAN---RTEGNVSVEGDIH--YngipYKEFAEKYPGEII-- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 403 dYLREE-SEMAkekdgtSISVTQLLErflFPSATHGKK-VYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:cd03233 87 -YVSEEdVHFP------TLTVRETLD---FALRCKGNEfVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
3-234 |
1.50e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL-----------DEDFTADITHPNQYR-I 70
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISLLPLHARARRgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 71 RYSSQKQDLNGHMTVFEAVLSsdtpTLRIIKKYEEavnryalDQSDSNFNKMMEaqeemdqkdawdyNAEIKTILSKLGi 150
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMA----VLQIRDDLSA-------EQREDRANELME-------------EFHIEHLRDSMG- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 151 hdttkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK10895 136 -------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISvidIKRIIEHLRDSGLGVLITDHNVRETLAVCERAY 208
|
....*..
gi 1842088001 228 ELDRGKL 234
Cdd:PRK10895 209 IVSQGHL 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-230 |
1.53e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRYSSQK---------QDLN--GHMTV 85
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL--------ARPDAGEVLWQGEPirrqrdeyhQDLLylGHQPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSdtptlriikkyEEavnryaldqsdsNFNKMMEAQEEMDQKDAWDynaeiktILSKLGIHDttkkiVE------ 159
Cdd:PRK13538 85 IKTELTA-----------LE------------NLRFYQRLHGPGDDEALWE-------ALAQVGLAG-----FEdvpvrq 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQypHT-----VLFVTHDRYFLNEVSTRIIELD 230
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQ--HAeqggmVILTTHQDLPVASDKVRKLRLG 203
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-237 |
1.59e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 59.89 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 38 GINGTGKSTLLKVIGGLdedftadiTHPNQYRIRyssqkqdLNGHmTVFEAVLSSDTPT-----------LRIIKKYEEA 106
Cdd:PRK11144 31 GRSGAGKTSLINAISGL--------TRPQKGRIV-------LNGR-VLFDAEKGICLPPekrrigyvfqdARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 107 VN-RYALDQSDsnfnkmmeaQEEMDQkdawdynaeiktILSKLGIHDTTKKI-VELSGGQQKRVVLAKTLIEQPDLLLLD 184
Cdd:PRK11144 95 GNlRYGMAKSM---------VAQFDK------------IVALLGIEPLLDRYpGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 185 EPTNHLDFESIRWLINYVKQYPHTV----LFVTHDryfLNEV---STRIIELDRGKLKTY 237
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LDEIlrlADRVVVLEQGKVKAF 210
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-256 |
1.61e-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: 60.47 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftaditHPNQYRIRYssQKQDLNG-----------HM-TVFEAV 89
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL---------IPSEGEIRF--DGQDLDGlsrralrplrrRMqVVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 LSSDTPTLR---IIkkyEE--AVNRYALDQSDSNfNKMMEAQEE--MDQKDAWDYnaeiktilsklgIHdttkkivELSG 162
Cdd:COG4172 372 FGSLSPRMTvgqII---AEglRVHGPGLSAAERR-ARVAEALEEvgLDPAARHRY------------PH-------EFSG 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSIR-----WLINYVKQYPHTVLFVTHD----RYFLNEVstriieldrgk 233
Cdd:COG4172 429 GQRQRIAIARALILEPKLLVLDEPTSALDV-SVQaqildLLRDLQREHGLAYLFISHDlavvRALAHRV----------- 496
|
250 260
....*....|....*....|...
gi 1842088001 234 lktypgnyedyIVMRaENELVEQ 256
Cdd:COG4172 497 -----------MVMK-DGKVVEQ 507
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-237 |
1.62e-09 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 58.27 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD--KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYRIRYSSQ 75
Cdd:cd03244 4 EFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILidgvdiskiGLHDLRSRISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 76 KQDlnghmtvfeAVLSSDTptlriIkkyeeavnRYALD----QSDSnfnKMMEAQEEMDQKDAwdynaeiktILSKLGIH 151
Cdd:cd03244 84 PQD---------PVLFSGT-----I--------RSNLDpfgeYSDE---ELWQALERVGLKEF---------VESLPGGL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTtkKIVE----LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLI-NYVKQypHTVLFVTHdRyfLNEV- 222
Cdd:cd03244 130 DT--VVEEggenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETdalIQKTIrEAFKD--CTVLTIAH-R--LDTIi 202
|
250
....*....|....*.
gi 1842088001 223 -STRIIELDRGKLKTY 237
Cdd:cd03244 203 dSDRILVLDKGRVVEF 218
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
24-251 |
1.64e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 24 LNLSISEHERIGLVGINGTGKSTLLKVIGGL---------DEDFTADITHPNQYRIR-YSSQKQDLNGHMTVFEavlssd 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLlpgsgsiqfAGQPLEAWSAAELARHRaYLSQQQTPPFAMPVFQ------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 94 tptlriikkyeeavnrY-ALDQSDSnfnkmmeAQEEMDQKdAWDYNAEIKTILSKLGIHDTTkkiveLSGGQQKRVVLAK 172
Cdd:PRK03695 89 ----------------YlTLHQPDK-------TRTEAVAS-ALNEVAEALGLDDKLGRSVNQ-----LSGGEWQRVRLAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 173 TLIE-----QPD--LLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDryfLNEV---STRIIELDRGKLKTYpG 239
Cdd:PRK03695 140 VVLQvwpdiNPAgqLLLLDEPMNSLDVAQQAALDRLLSELCQqgiAVVMSSHD---LNHTlrhADRVWLLKQGKLLAS-G 215
|
250
....*....|..
gi 1842088001 240 NYEDyiVMRAEN 251
Cdd:PRK03695 216 RRDE--VLTPEN 225
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
322-470 |
1.66e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYfkQTEKTLDRDIRV 401
Cdd:PRK11614 7 SFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW--QTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 I-DYLREESEMAKEKD----GTSISVTQLLERF-----LFPSaTHGKKVYK---LSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:PRK11614 85 VpEGRRVFSRMTVEENlamgGFFAERDQFQERIkwvyeLFPR-LHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
..
gi 1842088001 469 PT 470
Cdd:PRK11614 164 PS 165
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-256 |
1.80e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.91 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 4 EAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdLNGHM 83
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIK---------------VDGKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVF-EAVLSSDTPTLRiiKKYEEAVNRYALDQSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKLG----IHDT-TKKI 157
Cdd:PRK14246 74 LYFgKDIFQIDAIKLR--KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkeVYDRlNSPA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQyPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK14246 152 SQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
250 260
....*....|....*....|..
gi 1842088001 235 KTYPGNYEdyIVMRAENELVEQ 256
Cdd:PRK14246 231 VEWGSSNE--IFTSPKNELTEK 250
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
332-497 |
2.09e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.98 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 332 NKVLFeDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQTE-KTLDRDIRVIdYLREESE 410
Cdd:PRK13643 19 SRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEiKPVRKKVGVV-FQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 411 MAKE----------------KDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK13643 97 LFEEtvlkdvafgpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180
....*....|....*....|....*..
gi 1842088001 475 ----TETLTILEDyIDDFGGSVITVSH 497
Cdd:PRK13643 177 pkarIEMMQLFES-IHQSGQTVVLVTH 202
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-234 |
2.10e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 58.85 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIryssqkqdlnghmtV 85
Cdd:PRK13644 3 RLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGL--------LRPQKGKV--------------L 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVLSSDTPTLRIIKKYEEAVnryaLDQSDSNF-NKMMEAQEEMDQKDAWDYNAEIKTI----LSKLGI----HDTTKK 156
Cdd:PRK13644 61 VSGIDTGDFSKLQGIRKLVGIV----FQNPETQFvGRTVEEDLAFGPENLCLPPIEIRKRvdraLAEIGLekyrHRSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 iveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLnEVSTRIIELDRGK 233
Cdd:PRK13644 137 ---LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkgkTIVYITHNLEEL-HDADRIIVMDRGK 212
|
.
gi 1842088001 234 L 234
Cdd:PRK13644 213 I 213
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
322-497 |
2.26e-09 |
|
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: 58.01 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSIN-NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTLDRDI 399
Cdd:cd03253 2 EFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIdGQDIR----EVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RV---------------IDYLR-----EESEMAKEK-----------DGTSisvTQLLERFLfpsathgkkvyKLSGGEQ 448
Cdd:cd03253 78 GVvpqdtvlfndtigynIRYGRpdatdEEVIEAAKAaqihdkimrfpDGYD---TIVGERGL-----------KLSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF--GGSVITVSH 497
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-226 |
2.29e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.43 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 24 LNLSISEHERIGLVGINGTGKSTLLKVIGGLDED---FTADithpnqyRIRYSS---------QKQDLNGH--MTVFEAV 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrVTAD-------RMRFDDidllrlsprERRKLVGHnvSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 LSSDTPTLRIIKKYEEAVNRYALdqsdsnfnkmmeaQEEMDQKDAWDYNAEIKtILSKLGIHDTtKKIV-----ELSGGQ 164
Cdd:PRK15093 99 QSCLDPSERVGRQLMQNIPGWTY-------------KGRWWQRFGWRKRRAIE-LLHRVGIKDH-KDAMrsfpyELTEGE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRI 226
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEpttqAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
286-477 |
2.42e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 286 ARINRFNQLESDVKTQHTqdkgELNLAYsRLGkQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNI 365
Cdd:COG2401 2 ARYNPFFVLMRVTKVYSS----VLDLSE-RVA-IVLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 366 LSnedqdyeGELKIGQTVkvAYFKQTEKTLDRDIRVIDYLreesemakEKDGTSISVTQLLERFLFPSATHGKKVYK-LS 444
Cdd:COG2401 76 LA-------GALKGTPVA--GCVDVPDNQFGREASLIDAI--------GRKGDFKDAVELLNAVGLSDAVLWLRRFKeLS 138
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 445 GGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:COG2401 139 TGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-229 |
2.55e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 11 LNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI---THPNQY--RIRYSSQKQDLNGhmtv 85
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidGKTATRgdRSRFMAYLGHLPG---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 feavLSSDTPTLRIIKkYEEAVNRYALDQSDSNfnkmmeaqeemdqkdawdynaeiktILSKLGIHDTTKKIV-ELSGGQ 164
Cdd:PRK13543 93 ----LKADLSTLENLH-FLCGLHGRRAKQMPGS-------------------------ALAIVGLAGYEDTLVrQLSAGQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHT---VLFVTHDRYFLNEVSTRIIEL 229
Cdd:PRK13543 143 KKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGggaALVTTHGAYAAPPVRTRMLTL 210
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-234 |
2.98e-09 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 59.73 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 16 ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVI-------GG---LDEDFTADITHPNQYR-IRYSSQKQDL-NGhm 83
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfyepdSGqilLDGHDLADYTLASLRRqVALVSQDVVLfND-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVLSSDTPTlriikkYEEAVNRYALdqsdsnfnKMMEAQEEMDQKDawdynaeiktilskLGIH-DTTKKIVELSG 162
Cdd:TIGR02203 421 TIANNIAYGRTEQ------ADRAEIERAL--------AAAYAQDFVDKLP--------------LGLDtPIGENGVLLSG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK--QYPHTVLFVTHdRYFLNEVSTRIIELDRGKL 234
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALErlMQGRTTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
322-498 |
3.01e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.24 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGEL-----KIGQTVKVAYFKQTEK--- 393
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlfdgeNIPAMSRSRLYTVRKRmsm 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 -----TLDRDIRVIDY----LREESEMAKEKDGTsiSVTQLLERF-------LFPSathgkkvyKLSGGEQKRLYLLRLL 457
Cdd:PRK11831 89 lfqsgALFTDMNVFDNvaypLREHTQLPAPLLHS--TVMMKLEAVglrgaakLMPS--------ELSGGMARRAALARAI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1842088001 458 VHKPNVLLLDEPTNDLDTETLTILEDYIDD----FGGSVITVSHD 498
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVKLISElnsaLGVTCVVVSHD 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
323-474 |
3.48e-09 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 58.89 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQT-------------------- 382
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmndvppaergvgmvfqsya 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 383 --------------VKVAYFKQTEktldRDIRVidylREESEMakekdgtsISVTQLLERFlfPSAthgkkvykLSGGEQ 448
Cdd:PRK11000 86 lyphlsvaenmsfgLKLAGAKKEE----INQRV----NQVAEV--------LQLAHLLDRK--PKA--------LSGGQR 139
|
170 180
....*....|....*....|....*.
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK11000 140 QRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-187 |
3.62e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNksyaDKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLD---------EDFTADITHPNQ---YRIRYSS 74
Cdd:COG1129 258 EVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADpadsgeirlDGKPVRIRSPRDairAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 ---QKQDLNGHMTVFE----AVLSSDTPTLRIIKKYE-EAVNRYAldqsdsnfnkmmeaqEEMDqkdawdynaeIKTils 146
Cdd:COG1129 334 edrKGEGLVLDLSIREnitlASLDRLSRGGLLDRRRErALAEEYI---------------KRLR----------IKT--- 385
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1842088001 147 klgiHDTTKKIVELSGG-QQKrVVLAKTLIEQPDLLLLDEPT 187
Cdd:COG1129 386 ----PSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPT 422
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
323-525 |
4.20e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFE----DVTEIIQSGRRIG-IVGPNGAGKTTLLN-----ILSNEDQDYEGELKIGQTVKvayfKQTE 392
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalNNTSLTFKKNKVTcVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPANLK----KIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 -KTLDRDIRVIDYLRE--------ESEMA-------KEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRL 456
Cdd:PRK13645 85 vKRLRKEIGLVFQFPEyqlfqetiEKDIAfgpvnlgENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 457 LVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSFE 525
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDpkgeEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFE 237
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-215 |
5.10e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 58.32 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 3 MEAYKIEHLNKSYADK-EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITH--PNQYRIR 71
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERITSgeiwiggrVVNElePADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 72 YSSQKQDLNGHMTVFE----AVLSSDTPTLRIIKKYEEAVnryaldqsdsnfnKMMEAQEEMDQKDAwdynaeiktilsk 147
Cdd:PRK11650 80 MVFQNYALYPHMSVREnmayGLKIRGMPKAEIEERVAEAA-------------RILELEPLLDRKPR------------- 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 148 lgihdttkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD--------FEsIRWLINYVKQyphTVLFVTHD 215
Cdd:PRK11650 134 -----------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDaklrvqmrLE-IQRLHRRLKT---TSLYVTHD 194
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
333-517 |
5.35e-09 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 57.51 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQtEKTLDRDIRVI--------- 402
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrGQDLYQLDRKQ-RRAFRRDVQLVfqdspsavn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 ----------DYLREESEMAKEKDGTSISvtQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTND 472
Cdd:TIGR02769 103 prmtvrqiigEPLRHLTSLDESEQKARIA--ELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1842088001 473 LD----TETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:TIGR02769 181 LDmvlqAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-223 |
6.04e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 57.35 E-value: 6.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 5 AYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdFTADIThpNQYRIRYSSQ---KQDLNG 81
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVR--VEGRVEFFNQniyERRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEAVLSSDTPTLRIIKKYEEAVnrYALD----QSDSNFNKMMEAQeeMDQKDAWDynaEIKtilsklgiHDTTKKI 157
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVA--YGVKivgwRPKLEIDDIVESA--LKDADLWD---EIK--------HKIHKSA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLI-NYVKQYPHTVLFVTHDRYFLNEVS 223
Cdd:PRK14258 149 LDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkVESLIqSLRLRSELTMVIVSHNLHQVSRLS 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-234 |
6.06e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.50 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYAD--KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL---DEDFTADIT-------HPNQY 68
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITvdgitltAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 69 RIRYSSQKQDLNGHMTVFEAVLSSDTPtlriikkyeeavnrYALDQSDSNFNKMMEAqeemdqkdawdynaeIKTILSKL 148
Cdd:PRK13640 81 DIREKVGIVFQNPDNQFVGATVGDDVA--------------FGLENRAVPRPEMIKI---------------VRDVLADV 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 149 GIHDTTK-KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDryfLNEVS 223
Cdd:PRK13640 132 GMLDYIDsEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD---IDEAN 208
|
250
....*....|...
gi 1842088001 224 --TRIIELDRGKL 234
Cdd:PRK13640 209 maDQVLVLDDGKL 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
7-233 |
7.72e-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: 55.94 E-value: 7.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE-----IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG---LDEDFtadITHPNqyRIRYSSQkqd 78
Cdd:cd03250 2 SVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeleKLSGS---VSVPG--SIAYVSQ--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 79 lnghmtvfEAVLSSDTptLR--II-------KKYEEAVNRYALDQsDsnfnkmMEAQEEMDQkdawdynaeikTILSKLG 149
Cdd:cd03250 74 --------EPWIQNGT--IRenILfgkpfdeERYEKVIKACALEP-D------LEILPDGDL-----------TEIGEKG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 150 IHdttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYV----KQYPHTVLFVTHDRYFLNEVStR 225
Cdd:cd03250 126 IN--------LSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCilglLLNNKTRILVTHQLQLLPHAD-Q 196
|
....*...
gi 1842088001 226 IIELDRGK 233
Cdd:cd03250 197 IVVLDNGR 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
324-517 |
7.82e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 7.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 324 KNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTEK--------- 393
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIQHYASKEVARrigllaqna 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRDIRVIDYL--------------REESEMAKEKDGTSISVTQLLerflfpsathGKKVYKLSGGEQKRLYLLRLLVH 459
Cdd:PRK10253 91 TTPGDITVQELVargryphqplftrwRKEDEEAVTKAMQATGITHLA----------DQSVDTLSGGQRQRAWIAMVLAQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 460 KPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD-----RYFLNKVVqeywfIHDGKI 517
Cdd:PRK10253 161 ETAIMLLDEPTTWLDishqIDLLELLSELNREKGYTLAAVLHDlnqacRYASHLIA-----LREGKI 222
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-517 |
9.72e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 325 NLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQD-----YEGELKIGQTVKVAY-----FKQTEKT 394
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrdvleFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 LDR-----DIRVIDYLR---EESEMAKEKDGTSISVTQLLERFLFPSATH--GKKVYKLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:PRK14271 106 LFQrpnpfPMSIMDNVLagvRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrlSDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 465 LLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
14-191 |
1.06e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIggldedfTADitHPNQY--------RIRYSSQK-QDLNGHMT 84
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGD--HPQGYsndltlfgRRRGSGETiWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLSSD---TPTLR--IIKKYEEAVNRYaldQSDSNFNKMMEAQeemdqkdaWdynaeiktiLSKLGIHDTTKK--I 157
Cdd:PRK10938 340 YVSSSLHLDyrvSTSVRnvILSGFFDSIGIY---QAVSDRQQKLAQQ--------W---------LDILGIDKRTADapF 399
|
170 180 190
....*....|....*....|....*....|....
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLD 433
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-517 |
1.17e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.46 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDY-----EGELKI-GQTVkvayFKQTEKTL 395
Cdd:PRK14247 5 EIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLdGQDI----FKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRDIRVIDYLREE----------------SEMAKEKDGTSISVTQLLE----------RFLFPSAthgkkvyKLSGGEQK 449
Cdd:PRK14247 81 RRRVQMVFQIPNPipnlsifenvalglklNRLVKSKKELQERVRWALEkaqlwdevkdRLDAPAG-------KLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
12-214 |
1.24e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 56.67 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 12 NKSYADKEIFnDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRY-------SSQKQDLNGHMT 84
Cdd:PRK13643 14 NSPFASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGL--------LQPTEGKVTVgdivvssTSKQKEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLSSDTPTLriikkYEEAVNRyALDQSDSNFNKMMEAQEEMdqkdawdynAEIKTILSKLGIHDTTKKIVELSGGQ 164
Cdd:PRK13643 85 KVGVVFQFPESQL-----FEETVLK-DVAFGPQNFGIPKEKAEKI---------AAEKLEMVGLADEFWEKSPFELSGGQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 165 QKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYPHTVLFVTH 214
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKArieMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
342-498 |
1.27e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.22 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 342 IIQSGRRIGIVGPNGAGKTTLLNILS-------------------------NEDQDY-----EGELKIgqTVKVAYFKQT 391
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAgklkpnlgkfddppdwdeildefrgSELQNYftkllEGDVKV--IVKPQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 EKTLDRdiRVIDYLREESEM-AKEKDGTSISVTQLLERflfpsathgkKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPT 470
Cdd:cd03236 100 PKAVKG--KVGELLKKKDERgKLDELVDQLELRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|.
gi 1842088001 471 NDLDTE---TLTILEDYIDDFGGSVITVSHD 498
Cdd:cd03236 168 SYLDIKqrlNAARLIRELAEDDNYVLVVEHD 198
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
334-497 |
1.49e-08 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.96 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 334 VLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIG----QTVKVAYFK-------QTEKTLDRDIRVI 402
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlALADPAWLRrqvgvvlQENVLFNRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYL------REESEMAKEKDGTSISVTQLLERFlfpSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:cd03252 96 IALadpgmsMERVIEAAKLAGAHDFISELPEGY---DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170 180
....*....|....*....|...
gi 1842088001 477 TLTILEDYIDDF--GGSVITVSH 497
Cdd:cd03252 173 SEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
326-500 |
1.56e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 326 LSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAyfkqtEKTldrdiRVIDY 404
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRG-----DRS-----RFMAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 405 LreeSEMAKEKDGTSIsvtqlLERFLFPSATHGKK---------------------VYKLSGGEQKRLYLLRLLVHKPNV 463
Cdd:PRK13543 87 L---GHLPGLKADLST-----LENLHFLCGLHGRRakqmpgsalaivglagyedtlVRQLSAGQKKRLALARLWLSPAPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 464 LLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRY 500
Cdd:PRK13543 159 WLLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTHGAY 198
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
8-215 |
1.87e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 55.86 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQYRIRYSSQKQDLNG--HMTV 85
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP--------YQHGSITLDGKPVEGPGaeRGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 F--EAVLSsdtptlriikkYEEAVNRYALDQSDSNFNKmmEAQEEMDQKdawdynaeiktILSKLGIHDTTKK-IVELSG 162
Cdd:PRK11248 76 FqnEGLLP-----------WRNVQDNVAFGLQLAGVEK--MQRLEIAHQ-----------MLKKVGLEGAEKRyIWQLSG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 163 GQQKRVVLAKTLIEQPDLLLLDEPTNHLD-F--ESIRWLINYV-----KQyphtVLFVTHD 215
Cdd:PRK11248 132 GQRQRVGIARALAANPQLLLLDEPFGALDaFtrEQMQTLLLKLwqetgKQ----VLLITHD 188
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-477 |
1.93e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.04 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 331 NNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-------VAYFKQTEKT------LD 396
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPTRqalqknlVAYVPQSEEVdwsfpvLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDYLREESEMAKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRH-RQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
.
gi 1842088001 477 T 477
Cdd:PRK15056 177 T 177
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
338-474 |
2.26e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 55.80 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQT---------------------EKTLD 396
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklkplrkkvgivfqfpehqlfEETVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRV--IDYLREESEmAKEKDGTSISVTQLLERFLFPSAthgkkvYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK13634 105 KDICFgpMNFGVSEED-AKQKAREMIELVGLPEELLARSP------FELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
331-497 |
2.58e-08 |
|
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: 55.24 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 331 NNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILsnedQDY----EGELKI-GQTVK----------VAYFKQtEKTL 395
Cdd:cd03249 15 DVPIL-KGLSLTIPPGKTVALVGSSGCGKSTVVSLL----ERFydptSGEILLdGVDIRdlnlrwlrsqIGLVSQ-EPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 -DRDIRV-IDYLR-----EESEMAKEKDGTSISVTQLLERFlfpsATH-GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLD 467
Cdd:cd03249 89 fDGTIAEnIRYGKpdatdEEVEEAAKKANIHDFIMSLPDGY----DTLvGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190
....*....|....*....|....*....|..
gi 1842088001 468 EPTNDLDTETLTILEDYIDDF--GGSVITVSH 497
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
160-234 |
3.17e-08 |
|
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: 53.59 E-value: 3.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVgakAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
23-214 |
3.37e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.14 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEdftadithPNQyriryssqkqdlnGHMTVFEAVLSSDTPTLRI--I 100
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHV--------PTQ-------------GSVRVDDTLITSTSKNKDIkqI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 101 KKYEEAVNRYALDQ------------SDSNFNKMMEAQEEMdqkdawdynAEIKtiLSKLGIHDT--TKKIVELSGGQQK 166
Cdd:PRK13649 84 RKKVGLVFQFPESQlfeetvlkdvafGPQNFGVSQEEAEAL---------AREK--LALVGISESlfEKNPFELSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTH 214
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsgmTIVLVTH 203
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-215 |
3.40e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 36 LVGINGTGKSTLLKVIGGLDEDFTADIT---HPNQYRIR-----YSSQKQDLNGHMTVF-EAVLS----SDTPTLRIIKK 102
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLASGKISilgQPTRQALQknlvaYVPQSEEVDWSFPVLvEDVVMmgryGHMGWLRRAKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 103 YEEAVNRYALDQSDsnfnkMMEAQEemdqkdawdynaeiktilsklgihdttKKIVELSGGQQKRVVLAKTLIEQPDLLL 182
Cdd:PRK15056 118 RDRQIVTAALARVD-----MVEFRH---------------------------RQIGELSGGQKKRVFLARAIAQQGQVIL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1842088001 183 LDEPTNHLDFES---IRWLINYVKQYPHTVLFVTHD 215
Cdd:PRK15056 166 LDEPFTGVDVKTearIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-227 |
3.82e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 3.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIT---------HPNQYR-IRYSSQK--QD----LNGHMTV 85
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmKDDEWRaVRSDIQMifQDplasLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVlssdTPTLRIikkyeeavnryaldqsdsnFNKMMEAQEEMDqkdawdynaEIKTILSKLGI---------Hdttkk 156
Cdd:PRK15079 118 GEII----AEPLRT-------------------YHPKLSRQEVKD---------RVKAMMLKVGLlpnlinrypH----- 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 157 ivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSIR-WLINYVKQYPH----TVLFVTHDRYFLNEVSTRII 227
Cdd:PRK15079 161 --EFSGGQCQRIGIARALILEPKLIICDEPVSALDV-SIQaQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVL 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
322-497 |
3.89e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.18 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSIN-NKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTEK------ 393
Cdd:COG1129 6 EMRGISKSFGgVKAL-DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVRFRSPRDAQAagiaii 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 ----------------TLDRDIR---VIDY--LREESEMAKEKDGTSISVTQLLERflfpsathgkkvykLSGGEQKRLY 452
Cdd:COG1129 85 hqelnlvpnlsvaeniFLGREPRrggLIDWraMRRRARELLARLGLDIDPDTPVGD--------------LSVAQQQLVE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1842088001 453 LLRLLVHKPNVLLLDEPT---NDLDTETL-TILEDYIDDfGGSVITVSH 497
Cdd:COG1129 151 IARALSRDARVLILDEPTaslTEREVERLfRIIRRLKAQ-GVAIIYISH 198
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-226 |
3.89e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 54.68 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 34 IGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYR--IRY--SSQKQDLnghmtvFEAVLSSDtptLRIIKK--YEEAV 107
Cdd:cd03236 29 LGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeiLDEfrGSELQNY------FTKLLEGD---VKVIVKpqYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 108 NRyaldQSDSNFNKMMEAQEEMDQKDAWDYNAEIKTILSKlgihdttkKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPT 187
Cdd:cd03236 100 PK----AVKGKVGELLKKKDERGKLDELVDQLELRHVLDR--------NIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1842088001 188 NHLDFE---SIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRI 226
Cdd:cd03236 168 SYLDIKqrlNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
308-379 |
3.97e-08 |
|
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: 54.46 E-value: 3.97e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 308 ELNLAYSRLGKQVYELKNLSKSINNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI 379
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWAL-KDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV 81
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
7-191 |
4.35e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGL--DEDFTADI-------THPNQYRIRYSSQKQ 77
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTIlannrkpTKQILKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 78 DLNGHMTVFEAVLSsdTPTLRiikkyeeavnryaLDQSDSNFNKMMEAQeemdqkdawdynaeikTILSKLGIHDTTKKI 157
Cdd:PLN03211 150 ILYPHLTVRETLVF--CSLLR-------------LPKSLTKQEKILVAE----------------SVISELGLTKCENTI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 158 VE------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:PLN03211 199 IGnsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
324-498 |
4.78e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 54.55 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 324 KNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkigqtvkVAYfkqtektLDRDIRVID 403
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGE--------VHY-------RMRDGQLRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 404 -YLREESE----MAKE--------KDGTSISVT-------------------------QLLERFLFPSATHGKKVYKLSG 445
Cdd:PRK11701 75 lYALSEAErrrlLRTEwgfvhqhpRDGLRMQVSaggnigerlmavgarhygdiratagDWLERVEIDAARIDDLPTTFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET----LTILEDYIDDFGGSVITVSHD 498
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVqarlLDLLRGLVRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
7-234 |
4.92e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 54.71 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLN---LSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdLNGHM 83
Cdd:PRK13642 6 EVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVK---------------IDGEL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVFEAVLSSDTptlRIIKKYEEAVNRYALDQSDSNFNKMMEAQ----EEMDQKdawdynaeIKTILSKLGIHD-TTKKIV 158
Cdd:PRK13642 71 LTAENVWNLRR---KIGMVFQNPDNQFVGATVEDDVAFGMENQgiprEEMIKR--------VDEALLAVNMLDfKTREPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDryfLNEV--STRIIELDRG 232
Cdd:PRK13642 140 RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQLTVLSITHD---LDEAasSDRILVMKAG 216
|
..
gi 1842088001 233 KL 234
Cdd:PRK13642 217 EI 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
325-498 |
5.74e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 54.05 E-value: 5.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 325 NLSK-----SINNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTEKTLDRD 398
Cdd:PRK11629 10 NLCKryqegSVQTDVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFnGQPMSKLSSAAKAELRNQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVI--------DYLREES------------EMAKEKDGTSISVTQLLERflfpsATHgkKVYKLSGGEQKRLYLLRLLV 458
Cdd:PRK11629 89 LGFIyqfhhllpDFTALENvamplligkkkpAEINSRALEMLAAVGLEHR-----ANH--RPSELSGGERQRVAIARALV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 459 HKPNVLLLDEPTNDLDTETLTILEDYIDDF----GGSVITVSHD 498
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELnrlqGTAFLVVTHD 205
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
332-498 |
6.32e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 332 NKVLFEdvteiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYfKQTEKTLDRDI----------- 399
Cdd:PRK11308 32 DGVSFT-----LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYqGQDLLKAD-PEAQKLLRQKIqivfqnpygsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 ----RVIDYLREESEMakekdGTSISVTQLLERFLFPSATHGKKV--YK-----LSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:PRK11308 106 nprkKVGQILEEPLLI-----NTSLSAAERREKALAMMAKVGLRPehYDryphmFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190
....*....|....*....|....*....|....
gi 1842088001 469 PTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK11308 181 PVSALDvsvqAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-215 |
6.52e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.73 E-value: 6.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKST-------LLK---VIGGL-----DEDFTADITHPNQYRIRYSSQK-QD----LNG 81
Cdd:PRK09473 33 NDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAangRIGGSatfngREILNLPEKELNKLRAEQISMIfQDpmtsLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 HMTVFEAVLSsdtpTLRIIKK------YEEAVNryALDQSdsnfnKMMEAQEEMdqkdawdynaeiktilsKLGIHdttk 155
Cdd:PRK09473 113 YMRVGEQLME----VLMLHKGmskaeaFEESVR--MLDAV-----KMPEARKRM-----------------KMYPH---- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 156 kivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPHT-VLFVTHD 215
Cdd:PRK09473 161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqAQIMTLLNELKREFNTaIIMITHD 221
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
337-477 |
6.84e-08 |
|
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: 53.77 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQTEKTLDRDIRV-IDY 404
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGLVSQDVFLFNDTVAEnIAY 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 405 LREESEMAKEKDGTSIS-VTQLLERFlfPSATH---GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:cd03251 99 GRPGATREEVEEAARAAnAHEFIMEL--PEGYDtviGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
322-516 |
8.77e-08 |
|
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: 55.22 E-value: 8.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN--EDQDYEGELKI-GQTVKVAYFKQTEK----- 393
Cdd:TIGR02633 3 EMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWsGSPLKASNIRDTERagivi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 -----TLDRDIRVIDYLREESEMA-----KEKDGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNV 463
Cdd:TIGR02633 83 ihqelTLVPELSVAENIFLGNEITlpggrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 464 LLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHDGK 516
Cdd:TIGR02633 163 LILDEPSSSLTEKETEILLDIIRDLkahGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
117-227 |
9.50e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.19 E-value: 9.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 117 SNFNKMMEAQEE-MDQKDAWDynaeIKTILSKlgihdttKKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE-- 193
Cdd:cd03222 39 TTAVKILAGQLIpNGDNDEWD----GITPVYK-------PQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqr 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 1842088001 194 -----SIRWLINYVKQyphTVLFVTHDRYFLNEVSTRII 227
Cdd:cd03222 108 lnaarAIRRLSEEGKK---TALVVEHDLAVLDYLSDRIH 143
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
322-498 |
9.92e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 53.65 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSIN-NKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTEK------ 393
Cdd:PRK13652 5 ETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIREVRKfvglvf 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 ----------TLDRDIRV--IDYLREESEMAKEKDGT--SISVTQLLERflfpsATHgkkvyKLSGGEQKRLYLLRLLVH 459
Cdd:PRK13652 85 qnpddqifspTVEQDIAFgpINLGLDEETVAHRVSSAlhMLGLEELRDR-----VPH-----HLSGGEKKRVAIAGVIAM 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1842088001 460 KPNVLLLDEPTNDLDTETLTILEDYIDDF----GGSVITVSHD 498
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLpetyGMTVIFSTHQ 197
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-237 |
1.00e-07 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 52.80 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADK--EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNqyrIRYSSQK-QDLNGHM 83
Cdd:cd03369 8 EVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDG---IDISTIPlEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 84 TVF--EAVLSSDT--PTLRIIKKYEEAVNRYALDQSDSNFNkmmeaqeemdqkdawdynaeiktilsklgihdttkkive 159
Cdd:cd03369 85 TIIpqDPTLFSGTirSNLDPFDEYSDEEIYGALRVSEGGLN--------------------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES-------IRWLINYVkqyphTVLFVTHDryfLNEVS--TRIIELD 230
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdaliqktIREEFTNS-----TILTIAHR---LRTIIdyDKILVMD 197
|
....*..
gi 1842088001 231 RGKLKTY 237
Cdd:cd03369 198 AGEVKEY 204
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
322-474 |
1.17e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 53.55 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSK-----SINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS-------------NEDQDYEGELK----I 379
Cdd:COG1101 3 ELKNLSKtfnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgslppdsgsilidGKDVTKLPEYKrakyI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 380 GQ-------------TVK----VAYFKQTEKTLDRDIRvidylREESEMAKEKdgtsISVTQL-LERFLfpsathGKKVY 441
Cdd:COG1101 83 GRvfqdpmmgtapsmTIEenlaLAYRRGKRRGLRRGLT-----KKRRELFREL----LATLGLgLENRL------DTKVG 147
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 442 KLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-234 |
1.22e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.56 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 10 HLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTAdithpnqyrIRYSSQKqdLNGHMTVFeav 89
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG---------YRYSGDV--LLGGRSIF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 lssdtpTLRIIKKYEEAV-------NRYALDQSDsNFNKMMEAQEEMDQKDawdYNAEIKTILSKLGIHDTTKKIV---- 158
Cdd:PRK14271 92 ------NYRDVLEFRRRVgmlfqrpNPFPMSIMD-NVLAGVRAHKLVPRKE---FRGVAQARLTEVGLWDAVKDRLsdsp 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 159 -ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH--TVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK14271 162 fRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-233 |
1.26e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 53.07 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQK----------QD--LNGHMTVFEAV 89
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQiarmgvvrtfQHvrLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 90 LSSD--------------TPTLRiikkyeeavnryaldQSDsnfnkmmeaQEEMDQKDAWdynaeiktiLSKLGIHD-TT 154
Cdd:PRK11300 102 LVAQhqqlktglfsgllkTPAFR---------------RAE---------SEALDRAATW---------LERVGLLEhAN 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPT---NHLDFESIRWLINYVK-QYPHTVLFVTHDRYFLNEVSTRIIELD 230
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
...
gi 1842088001 231 RGK 233
Cdd:PRK11300 229 QGT 231
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
323-497 |
1.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFEDVTEIIQSGRRIgIVGPNGAGKTTLLNILSNEDQDYEGEL--KIGQTVKVAYFKQT----EKTLD 396
Cdd:PRK13541 4 LHQLQFNIEQKNLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIyyKNCNINNIAKPYCTyighNLGLK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDYLREESEMAKEKDGTSISVTQL-LERFLfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDT 475
Cdd:PRK13541 83 LEMTVFENLKFWSEIYNSAETLYAAIHYFkLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK 156
|
170 180
....*....|....*....|....*
gi 1842088001 476 ETLTILEDYI---DDFGGSVITVSH 497
Cdd:PRK13541 157 ENRDLLNNLIvmkANSGGIVLLSSH 181
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-497 |
1.43e-07 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 53.12 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS--NEDQD---YEGELKI-GQTVkvayfkqtektL 395
Cdd:COG1117 13 EVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmNDLIPgarVEGEILLdGEDI-----------Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRDIRVIDyLREESEM---------------------------AKEKDGTsisVTQLLER---------FLFPSAThgkk 439
Cdd:COG1117 82 DPDVDVVE-LRRRVGMvfqkpnpfpksiydnvayglrlhgiksKSELDEI---VEESLRKaalwdevkdRLKKSAL---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 440 vyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD-TETLTIlEDYIDDFGG--SVITVSH 497
Cdd:COG1117 154 --GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAKI-EELILELKKdyTIVIVTH 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-214 |
1.48e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.49 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadithpnqyriryssqKQDLNGHMTVFEAVLSSDTPT--LRII 100
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGL---------------------LQPTSGTVTIGERVITAGKKNkkLKPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 101 KK-------------YEEAVnryaldQSDSNFNKMMEAQEEMDQKdawdynAEIKTILSKLGIHDT--TKKIVELSGGQQ 165
Cdd:PRK13634 84 RKkvgivfqfpehqlFEETV------EKDICFGPMNFGVSEEDAK------QKAREMIELVGLPEEllARSPFELSGGQM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEPTNHLD----------FESIRwlinyvKQYPHTVLFVTH 214
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDpkgrkemmemFYKLH------KEKGLTTVLVTH 204
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-243 |
1.56e-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: 52.62 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKE--IFNDLNLSISEHERIGLVGINGTGKSTLLK-------------VIGGLD-EDFTAdithpNQYR-- 69
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNliprfydvdsgriLIDGHDvRDYTL-----ASLRrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 70 IRYSSQKQDL-NGhmTVFEAVLSSDTPTLRiikkyeEAVNRYAldqsdsnfnKMMEAQEEMDQK-DAWDynaeikTILSK 147
Cdd:cd03251 78 IGLVSQDVFLfND--TVAENIAYGRPGATR------EEVEEAA---------RAANAHEFIMELpEGYD------TVIGE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 148 LGihdttkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQyPHTVLFVTHdRYFLNEVST 224
Cdd:cd03251 135 RG--------VKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVqaaLERLMK-NRTTFVIAH-RLSTIENAD 204
|
250
....*....|....*....
gi 1842088001 225 RIIELDRGKLKTYpGNYED 243
Cdd:cd03251 205 RIVVLEDGKIVER-GTHEE 222
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
7-215 |
1.78e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.86 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLD---EDFTADithpnqYRIRYssQKQDLN-GH 82
Cdd:PRK14243 12 RTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdliPGFRVE------GKVTF--HGKNLYaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 83 MTVFEA------VLSSDTPTLRIIKK---YEEAVNRYALDqsdsnfnkMMEAQEE-MDQKDAWDynaEIKTILSKLGIhd 152
Cdd:PRK14243 84 VDPVEVrrrigmVFQKPNPFPKSIYDniaYGARINGYKGD--------MDELVERsLRQAALWD---EVKDKLKQSGL-- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 153 ttkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQyPHTVLFVTHD 215
Cdd:PRK14243 151 ------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPIStlrIEELMHELKE-QYTIIIVTHN 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
317-367 |
1.85e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.39 E-value: 1.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 317 GKQVYELKNLSksinnkvlFEdvteiIQSGRRIGIVGPNGAGKTTLLNILS 367
Cdd:COG1134 36 REEFWALKDVS--------FE-----VERGESVGIIGRNGAGKSTLLKLIA 73
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-215 |
1.85e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 53.54 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADK----EIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdEDFTA--------DITHPNQYRIRYSS 74
Cdd:COG1135 3 ELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLL-ERPTSgsvlvdgvDLTALSERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QK-----QDLN--GHMTVFEAVLSsdtPtLRIIKkyeeaVNRyaldqsdsnfnkmmeaqEEMDQKdawdynaeIKTILSK 147
Cdd:COG1135 82 RKigmifQHFNllSSRTVAENVAL---P-LEIAG-----VPK-----------------AEIRKR--------VAELLEL 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 148 LGIHDttKKIV---ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIrwL-----INyvKQYPHTVLFVTHD 215
Cdd:COG1135 128 VGLSD--KADAypsQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEttrSI--LdllkdIN--RELGLTIVLITHE 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
442-499 |
2.24e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 52.18 E-value: 2.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 442 KLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE----TLTILEDYiDDFGGSVITVSHDR 499
Cdd:PRK10908 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAlsegILRLFEEF-NRVGVTVLMATHDI 197
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-237 |
2.34e-07 |
|
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: 53.89 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 18 KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDedfTADIthpNQY-------RIRYSSQKQDLn 80
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGiwpptsgsvrLD---GADL---KQWdretfgkHIGYLPQDVEL- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 ghmtvFEAVLSSDtptlriIKKYEEAVnryaldqsDSNfnKMMEAQE-----EMDQK--DAWDynaeikTILSKLGIhdt 153
Cdd:TIGR01842 404 -----FPGTVAEN------IARFGENA--------DPE--KIIEAAKlagvhELILRlpDGYD------TVIGPGGA--- 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 154 tkkivELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWLINYVKQYPHTVLFVTHdRYFLNEVSTRIIELD 230
Cdd:TIGR01842 454 -----TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEgeqALANAIKALKARGITVVVITH-RPSLLGCVDKILVLQ 527
|
....*..
gi 1842088001 231 RGKLKTY 237
Cdd:TIGR01842 528 DGRIARF 534
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
317-477 |
2.48e-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: 53.98 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 317 GKQVYELKNLSKSIN-NKVLF---------EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVkva 386
Cdd:TIGR01193 461 KKKRTELNNLNGDIViNDVSYsygygsnilSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS--- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 387 yFKQTEKTLDRdiRVIDYLREESEM----------AKEKDGTSISVTQLLERFL--------FPSATH---GKKVYKLSG 445
Cdd:TIGR01193 538 -LKDIDRHTLR--QFINYLPQEPYIfsgsilenllLGAKENVSQDEIWAACEIAeikddienMPLGYQtelSEEGSSISG 614
|
170 180 190
....*....|....*....|....*....|..
gi 1842088001 446 GEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
160-235 |
2.55e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.40 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQ----YPHTVLFVTHdryFLNEV--STRIIELDRGK 233
Cdd:PRK13633 145 LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnkkYGITIILITH---YMEEAveADRIIVMDSGK 221
|
..
gi 1842088001 234 LK 235
Cdd:PRK13633 222 VV 223
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
21-236 |
2.86e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 53.08 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 21 FNDLNLSISEHERIgLVGINGTGKSTLLKVIggldeDFTADITHPNQYRIRYSSQKQDLNGHMTVFEAVLSSdtPTLRII 100
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEAL-----RLLLGPSSSRKFDEEDFYLGDDPDLPEIEIELTFGS--LLSRLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 101 KKYEEAVNRYALDQS--------DSNFNKMMEAQEEMDQKDAWDYNAEIK-------TILSKLGIH---DTTKKIVELSG 162
Cdd:COG3593 86 RLLLKEEDKEELEEAleelneelKEALKALNELLSEYLKELLDGLDLELElsldeleDLLKSLSLRiedGKELPLDRLGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 163 GQQKRVVLA--KTLIE-----QPDLLLLDEPTNHLDFESIRWLINYVKQY---PHTVLFVTHDRYFLNEVS-TRIIELDR 231
Cdd:COG3593 166 GFQRLILLAllSALAElkrapANPILLIEEPEAHLHPQAQRRLLKLLKELsekPNQVIITTHSPHLLSEVPlENIRRLRR 245
|
....*
gi 1842088001 232 GKLKT 236
Cdd:COG3593 246 DSGGT 250
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
160-235 |
3.03e-07 |
|
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: 53.60 E-value: 3.03e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLNEVStRIIELDRGKLK 235
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALaaaIRALKARGATVVVITHRPSLLAAVD-KLLVLRDGRVQ 545
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
343-498 |
3.27e-07 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.91 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV------KVAYfKQTEKT-----LDRDIRVID------- 403
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLrGQHIeglpghQIAR-MGVVRTfqhvrLFREMTVIEnllvaqh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 404 ----------------YLREESEmAKEKDGTSISVTQLLERFLFPSAThgkkvykLSGGEQKRLYLLRLLVHKPNVLLLD 467
Cdd:PRK11300 107 qqlktglfsgllktpaFRRAESE-ALDRAATWLERVGLLEHANRQAGN-------LAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 1842088001 468 EPT---NDLDTETLTILEDYI-DDFGGSVITVSHD 498
Cdd:PRK11300 179 EPAaglNPKETKELDELIAELrNEHNVTVLLIEHD 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-575 |
4.29e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.38 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEdQDYEGELKIG---------QTVKVAY---------FKQT-EK 393
Cdd:TIGR01271 1232 RAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDgvswnsvtlQTWRKAFgvipqkvfiFSGTfRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLDRDIRVIDylrEESEMAKEKDGTSISVTQLLERFLFPSATHGkkvYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:TIGR01271 1311 NLDPYEQWSD---EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGG---YVLSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 474 DTETLTILEDYIDD-FGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKiigsfedYESFKK-----EHERQAMLSKQ---- 543
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQsFSNCTVILSEHRVEALLECQQFLVIEGSSVKQ-------YDSIQKllnetSLFKQAMSAADrlkl 1457
|
250 260 270
....*....|....*....|....*....|....
gi 1842088001 544 --TEQQNKHKHQPKKKTGlSYKEKLEYETIMTRI 575
Cdd:TIGR01271 1458 fpLHRRNSSKRKPQPKIT-ALREEAEEEVQNTRL 1490
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
338-517 |
4.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLnilsnedQDYEGELK-IGQTVKVAYFKQTEKTLDRDIRVI-------------- 402
Cdd:PRK13646 25 DVNTEFEQGKYYAIVGQTGSGKSTLI-------QNINALLKpTTGTVTVDDITITHKTKDKYIRPVrkrigmvfqfpesq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 ---DYLREESEMAKEKDGTSIS-----VTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK13646 98 lfeDTVEREIIFGPKNFKMNLDevknyAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 475 TET----LTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK13646 178 PQSkrqvMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-234 |
5.00e-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: 51.08 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 9 EHLNKSYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQKQdLNGHMTVF- 86
Cdd:cd03253 4 ENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-DIREVTLDS-LRRAIGVVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 -EAVLSSDTPTLRIikkyeeavnRYA-LDQSDsnfnkmmeaqEEMdqkdawdYNAEIKTIlsklgIHDTTKKI------- 157
Cdd:cd03253 82 qDTVLFNDTIGYNI---------RYGrPDATD----------EEV-------IEAAKAAQ-----IHDKIMRFpdgydti 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 -----VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLINyvkqyPHTVLFVTHDryfLNEVST- 224
Cdd:cd03253 131 vgergLKLSGGEKQRVAIARAILKNPPILLLDEATSALDthtereiQAALRDVSK-----GRTTIVIAHR---LSTIVNa 202
|
250
....*....|.
gi 1842088001 225 -RIIELDRGKL 234
Cdd:cd03253 203 dKIIVLKDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-234 |
6.05e-07 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 51.73 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSY--ADKEI--FNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDfTA--------DITHPNQYRIRYSS 74
Cdd:PRK11153 3 ELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP-TSgrvlvdgqDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 QK-----QDLN--GHMTVFEAV-----LSSdTPTLRIIKKYEEAVNRYALDqsdsnfnkmmeaqeemDQKDAwdYNAEik 142
Cdd:PRK11153 82 RQigmifQHFNllSSRTVFDNValpleLAG-TPKAEIKARVTELLELVGLS----------------DKADR--YPAQ-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 143 tilsklgihdttkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFE---SIRWL---INyvKQYPHTVLFVTHDR 216
Cdd:PRK11153 141 -----------------LSGGQKQRVAIARALASNPKVLLCDEATSALDPAttrSILELlkdIN--RELGLTIVLITHEM 201
|
250
....*....|....*...
gi 1842088001 217 YFLNEVSTRIIELDRGKL 234
Cdd:PRK11153 202 DVVKRICDRVAVIDAGRL 219
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
318-519 |
6.11e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.18 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEdQDY---EGELKigqtvkvayFKQTEKT 394
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PAYkilEGDIL---------FKGESIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 395 -LDRDIRV-------------------IDYLR------EESEMAKEKDGTS--------ISVTQLLERFLFPSATHGkkv 440
Cdd:CHL00131 75 dLEPEERAhlgiflafqypieipgvsnADFLRlaynskRKFQGLPELDPLEfleiinekLKLVGMDPSFLSRNVNEG--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 441 ykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYwfIH---D 514
Cdd:CHL00131 152 --FSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDY--VHvmqN 227
|
....*
gi 1842088001 515 GKIEK 519
Cdd:CHL00131 228 GKIIK 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
322-518 |
7.04e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 51.20 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFE-----DVTEIIQSGRRIGIVGPNGAGKTTLLnilsnedQDYEGELKIGQ-TVKVAYFKQTEKTL 395
Cdd:PRK13637 4 KIENLTHIYMEGTPFEkkaldNVNIEIEDGEFVGLIGHTGSGKSTLI-------QHLNGLLKPTSgKIIIDGVDITDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 D-RDIR-----VIDY----LREE----------SEMAKEKDGTSISVTQLLERFLFPSATHGKKV-YKLSGGEQKRLYLL 454
Cdd:PRK13637 77 KlSDIRkkvglVFQYpeyqLFEEtiekdiafgpINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpFELSGGQKRRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 455 RLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIE 518
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDpkgrDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
351-497 |
7.90e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 351 IVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVayfkQTEKT--LDRDIRVIDYLREESE--------------MAKE 414
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF----DAEKGicLPPEKRRIGYVFQDARlfphykvrgnlrygMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 415 KDGTSISVTQLL--ERFL--FPSAthgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDT----ETLTILEDYID 486
Cdd:PRK11144 105 MVAQFDKIVALLgiEPLLdrYPGS--------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAR 176
|
170
....*....|.
gi 1842088001 487 DFGGSVITVSH 497
Cdd:PRK11144 177 EINIPILYVSH 187
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
322-498 |
8.07e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.85 E-value: 8.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK-------VAYfkQTEK 393
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdGKPVEgpgaergVVF--QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 TLD-RDirVIDYLREESEMAK-EKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:PRK11248 81 LLPwRN--VQDNVAFGLQLAGvEKMQRLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
|
170 180 190
....*....|....*....|....*....|.
gi 1842088001 472 DLDTET----LTILEDYIDDFGGSVITVSHD 498
Cdd:PRK11248 158 ALDAFTreqmQTLLLKLWQETGKQVLLITHD 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-191 |
9.32e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 20 IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNqyRIRYSSQKQ-DLNGhmTVFEAV---LSSDTp 95
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSwIMPG--TIKDNIifgLSYDE- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 tlriiKKYEEAVNRYALDQSDSNFnkmmeaqeemDQKDawdynaeiKTILSKLGIhdttkkivELSGGQQKRVVLAKTLI 175
Cdd:TIGR01271 516 -----YRYTSVIKACQLEEDIALF----------PEKD--------KTVLGEGGI--------TLSGGQRARISLARAVY 564
|
170
....*....|....*.
gi 1842088001 176 EQPDLLLLDEPTNHLD 191
Cdd:TIGR01271 565 KDADLYLLDSPFTHLD 580
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
322-497 |
1.05e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 49.72 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSIN---NKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRD 398
Cdd:cd03369 8 EVENLSVRYApdlPPVL-KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEID---------------GID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 399 IRVIDYLREESEMA-KEKDGT--SISVTQLLERF-------LFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:cd03369 72 ISTIPLEDLRSSLTiIPQDPTlfSGTIRSNLDPFdeysdeeIYGALRVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190
....*....|....*....|....*....|.
gi 1842088001 469 PTNDLDTETLTILEDYI-DDFGGS-VITVSH 497
Cdd:cd03369 152 ATASIDYATDALIQKTIrEEFTNStILTIAH 182
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
311-517 |
1.07e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 50.46 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 311 LAYSRLGKQvYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVKVAYFKQ 390
Cdd:PRK10419 4 LNVSGLSHH-YAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 TEKTLDRDIRVI-------------------DYLREESEMAKEkdGTSISVTQLLERFLFPSATHGKKVYKLSGGEQKRL 451
Cdd:PRK10419 83 QRKAFRRDIQMVfqdsisavnprktvreiirEPLRHLLSLDKA--ERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD----RYFLNKVVqeywFIHDGKI 517
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDlvlqAGVIRLLKKLQQQFGTACLFITHDlrlvERFCQRVM----VMDNGQI 230
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
346-498 |
1.10e-06 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 51.25 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 346 GRRI-GIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTV----KVAYFKQTEKtldrdiRVIDYLREESEM--------- 411
Cdd:COG4148 24 GRGVtALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsARGIFLPPHR------RRIGYVFQEARLfphlsvrgn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 --------AKEKDGTSI-SVTQLL--ERFLfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDT----E 476
Cdd:COG4148 98 llygrkraPRAERRISFdEVVELLgiGHLL------DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLarkaE 171
|
170 180
....*....|....*....|..
gi 1842088001 477 TLTILEDYIDDFGGSVITVSHD 498
Cdd:COG4148 172 ILPYLERLRDELDIPILYVSHS 193
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
322-505 |
1.14e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSN--EDQDYEGELKI-GQTVKVAYFKQTEK----- 393
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFeGEELQASNIRDTERagiai 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 -----TLDRDIRV---------------IDYLREESEMAK--EKDGTSISVTQllerflfpsathgkKVYKLSGGEQKRL 451
Cdd:PRK13549 87 ihqelALVKELSVleniflgneitpggiMDYDAMYLRAQKllAQLKLDINPAT--------------PVGNLGLGQQQLV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDryfLNKV 505
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLkahGIACIYISHK---LNEV 206
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-229 |
1.24e-06 |
|
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: 48.86 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGgldedftadithpnqyrirYSSQKQDLNGHMTVFeavlsSDTPTLRIik 101
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL-------------------YASGKARLISFLPKF-----SRNKLIFI-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 102 kyeeavnryaldqsdsnfnkmmeaqeemDQkdawdynaeIKTiLSKLGIHDTT--KKIVELSGGQQKRVVLAKTLIEQPD 179
Cdd:cd03238 66 ----------------------------DQ---------LQF-LIDVGLGYLTlgQKLSTLSGGELQRVKLASELFSEPP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 180 --LLLLDEPTNHLDFESIRWLINYVK---QYPHTVLFVTHDRYFLNEvSTRIIEL 229
Cdd:cd03238 108 gtLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLSS-ADWIIDF 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
7-214 |
1.42e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftaditHPnQYRIryssqkqdLNGHMTVF 86
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG----------HP-AYKI--------LEGDILFK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSDTPTLR----IIKKYEEAVNRYALDQSD-----SNFNKMMEAQEEMDQKDAWDYnaeIKTILSKLGIHDT--TK 155
Cdd:CHL00131 70 GESILDLEPEERahlgIFLAFQYPIEIPGVSNADflrlaYNSKRKFQGLPELDPLEFLEI---INEKLKLVGMDPSflSR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 156 KIVE-LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTH 214
Cdd:CHL00131 147 NVNEgFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSIILITH 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
345-502 |
1.67e-06 |
|
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: 48.14 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 345 SGRRIGIVGPNGAGKTTLLNILSNedqdyegelkigqtvkvayfkqtektldrdirvidYLREESEMAKEKDGTSISVTQ 424
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALAR-----------------------------------ELGPPGGGVIYIDGEDILEEV 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 425 LLERFLFPSathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---------GGSVITV 495
Cdd:smart00382 46 LDQLLLIIV---GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILT 122
|
....*..
gi 1842088001 496 SHDRYFL 502
Cdd:smart00382 123 TNDEKDL 129
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
9-215 |
1.74e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 9 EHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldeDFTADIThPNQYRIRyssQKQDLNG------- 81
Cdd:PRK13547 5 DHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG---DLTGGGA-PRGARVT---GDVTLNGeplaaid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 82 --HMTVFEAVL----------SSDTPTLriIKKYEEAVNRYALDQSDSNFnkmmeAQEEMDQKDAwdynaeiktilSKLG 149
Cdd:PRK13547 78 apRLARLRAVLpqaaqpafafSAREIVL--LGRYPHARRAGALTHRDGEI-----AWQALALAGA-----------TALV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 150 IHDTTKkiveLSGGQQKRVVLAKTL---------IEQPDLLLLDEPTNHLDFESIRWLINYV----KQYPHTVLFVTHD 215
Cdd:PRK13547 140 GRDVTT----LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrrlaRDWNLGVLAIVHD 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
322-474 |
1.93e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVL-FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTVkVayfkQTEKTLDRDI- 399
Cdd:PRK11650 5 KLQAVRKSYDGKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-V----NELEPADRDIa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 ------------RVIDYL----------REESEMAKEKDGTSISVTQLLERflfpsathgkKVYKLSGGEQKRLYLLRLL 457
Cdd:PRK11650 80 mvfqnyalyphmSVRENMayglkirgmpKAEIEERVAEAARILELEPLLDR----------KPRELSGGQRQRVAMGRAI 149
|
170
....*....|....*..
gi 1842088001 458 VHKPNVLLLDEPTNDLD 474
Cdd:PRK11650 150 VREPAVFLFDEPLSNLD 166
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
343-470 |
2.02e-06 |
|
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: 49.21 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSN-----------EDQDYEG-------ELKIGQ-----------TVK-----VAYF 388
Cdd:COG0410 26 VEEGEIVALLGRNGAGKTTLLKAISGllpprsgsirfDGEDITGlpphriaRLGIGYvpegrrifpslTVEenlllGAYA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 389 KQTEKTLDRDI-RVIDY---LREeseMAKEKDGTsisvtqllerflfpsathgkkvykLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:COG0410 106 RRDRAEVRADLeRVYELfprLKE---RRRQRAGT------------------------LSGGEQQMLAIGRALMSRPKLL 158
|
....*.
gi 1842088001 465 LLDEPT 470
Cdd:COG0410 159 LLDEPS 164
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
323-502 |
2.15e-06 |
|
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: 48.47 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 323 LKNLSKSINNKVLFedvteiiqsgrriGIVGPNGAGKTTLLNilsnedqdyEGELKIGQTVkvaYFKQTEKTLDRDIRVI 402
Cdd:cd03238 11 LQNLDVSIPLNVLV-------------VVTGVSGSGKSTLVN---------EGLYASGKAR---LISFLPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 403 DYLREESEMAKEkdgtsisvtqllerFLfpsaTHGKKVYKLSGGEQKRLYLLRLLV--HKPNVLLLDEPTNDLDTETLTI 480
Cdd:cd03238 66 DQLQFLIDVGLG--------------YL----TLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|....*
gi 1842088001 481 LEDYID---DFGGSVITVSHDRYFL 502
Cdd:cd03238 128 LLEVIKgliDLGNTVILIEHNLDVL 152
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
136-235 |
2.25e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 136 DYNAEIKTI---LSKLGIHDTTK--KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FEsIRWLINYVKQYP 206
Cdd:PRK13549 377 DDAAELKTIlesIQRLKVKTASPelAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDvgakYE-IYKLINQLVQQG 455
|
90 100 110
....*....|....*....|....*....|..
gi 1842088001 207 HTVLFVTHDryfLNEV---STRIIELDRGKLK 235
Cdd:PRK13549 456 VAIIVISSE---LPEVlglSDRVLVMHEGKLK 484
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-222 |
2.30e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGlDEDFT---ADITHPNQYRIRYSSQKQDLNGHMT 84
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG-REDYEvtgGTVEFKGKDLLELSPEDRAGEGIFM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLssDTPTLRiikkyeeavNRYALdQSDSNFNKMMEAQEEMDQKDAWDYnAEIKTILSKLGIHDTTKKI-VELSGG 163
Cdd:PRK09580 83 AFQYPV--EIPGVS---------NQFFL-QTALNAVRSYRGQEPLDRFDFQDL-MEEKIALLKMPEDLLTRSVnVGFSGG 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 164 QQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLNEV 222
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVadgVNSLRDGKRSFIIVTHYQRILDYI 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-191 |
2.43e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 50.43 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 18 KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDE-------DFTAD---ITHPNQYRIRYSSQKQDLN-GHMTVF 86
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPkgvkgsgSVLLNgmpIDAKEMRAISAYVQQDDLFiPTLTVR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAVLSSdtPTLRIIKKYEEAVNRYALDqsdsnfnkmmEAQEEMDQKDAWDynaeiktilSKLGIHDTTKKiveLSGGQQK 166
Cdd:TIGR00955 118 EHLMFQ--AHLRMPRRVTKKEKRERVD----------EVLQALGLRKCAN---------TRIGVPGRVKG---LSGGERK 173
|
170 180
....*....|....*....|....*
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:TIGR00955 174 RLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
336-498 |
2.44e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 49.46 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 336 FEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS-------------NEDQDY--EGELKIGQTVKVAyFKQTEKTLDRDIR 400
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNgilkpssgrilfdGKPIDYsrKGLMKLRESVGMV-FQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VIDYLREESEMAKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TE 476
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKD-KPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSE 179
|
170 180
....*....|....*....|..
gi 1842088001 477 TLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHD 201
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
343-498 |
2.72e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 49.35 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayfKQTEKTL---------DRDIRVIDYLREES--- 409
Cdd:PRK13647 28 IPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVmGREVN----AENEKWVrskvglvfqDPDDQVFSSTVWDDvaf 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 410 ---EMAKEKDGTSISVTQLLERFLFPSATHgKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD---TETLTILED 483
Cdd:PRK13647 104 gpvNMGLDKDEVERRVEEALKAVRMWDFRD-KPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgQETLMEILD 182
|
170
....*....|....*
gi 1842088001 484 YIDDFGGSVITVSHD 498
Cdd:PRK13647 183 RLHNQGKTVIVATHD 197
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
343-554 |
3.06e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 49.31 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTL---LN----------ILSNEDQDYE--GELKIGQTVKVAYFKQTEK----TLDRDIRVid 403
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLflhFNgilkptsgevLIKGEPIKYDkkSLLEVRKTVGIVFQNPDDQlfapTVEEDVAF-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 404 ylrEESEMAKEKDGTSISVTQLLERFLFpSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLT 479
Cdd:PRK13639 103 ---GPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgaSQIMK 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 480 ILEDyIDDFGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKiIGS----FEDYESFKKEHERQAMLSKQTEQQNKHKHQP 554
Cdd:PRK13639 179 LLYD-LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIK-EGTpkevFSDIETIRKANLRLPRVAHLIEILNKEDNLP 255
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
338-477 |
3.15e-06 |
|
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: 50.10 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVK----------VAYFKQTEKTLDRDI------- 399
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqVALVSQDVVLFNDTIanniayg 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 400 RVIDYLREESEMAKEKDGTSISVTQLLERFLFPSathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:TIGR02203 430 RTEQADRAEIERALAAAYAQDFVDKLPLGLDTPI---GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNES 504
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
304-497 |
4.48e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 304 QDKGELNLAYSRLGKQVYELKNLS---KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNIL-------------- 366
Cdd:PTZ00265 1149 RDNGGIRIKNKNDIKGKIEIMDVNfryISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivf 1228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 367 -------SNEDQDYEGELKIGQTVK----------------VAYFKQTEKTLDRDIRVIDY------------------- 404
Cdd:PTZ00265 1229 knehtndMTNEQDYQGDEEQNVGMKnvnefsltkeggsgedSTVFKNSGKILLDGVDICDYnlkdlrnlfsivsqepmlf 1308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 405 -------LREESEMAKEKDGTSISVTQLLERFL--FPS------ATHGKKvykLSGGEQKRLYLLRLLVHKPNVLLLDEP 469
Cdd:PTZ00265 1309 nmsiyenIKFGKEDATREDVKRACKFAAIDEFIesLPNkydtnvGPYGKS---LSGGQKQRIAIARALLREPKILLLDEA 1385
|
250 260 270
....*....|....*....|....*....|..
gi 1842088001 470 TNDLDTETLTILEDYI----DDFGGSVITVSH 497
Cdd:PTZ00265 1386 TSSLDSNSEKLIEKTIvdikDKADKTIITIAH 1417
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-227 |
4.56e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 27 SISEHERIGLVGINGTGKSTLLKVIGGLDeDF----TADITHPNQYRIRYSS--QKQDLNGH--MTVFEAVLSSDTPTLR 98
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVSSLAIMGLI-DYpgrvMAEKLEFNGQDLQRISekERRNLVGAevAMIFQDPMTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 99 IIKKYEEAVnryaldQSDSNFNKMMEAQEEMDqkdawdynaeiktILSKLGIHDTTKKIV----ELSGGQQKRVVLAKTL 174
Cdd:PRK11022 108 VGFQIMEAI------KVHQGGNKKTRRQRAID-------------LLNQVGIPDPASRLDvyphQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 175 IEQPDLLLLDEPTNHLDF----ESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRII 227
Cdd:PRK11022 169 ACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
327-477 |
4.59e-06 |
|
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: 47.85 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 327 SKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvkVAYFKQTEKTLDRDIRviDYLR 406
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--IAYVSQEPWIQNGTIR--ENIL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 407 EESEMAKEKDGTSISVTQLLERF-LFPS--ATH-GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:cd03250 88 FGKPFDEERYEKVIKACALEPDLeILPDgdLTEiGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHV 162
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-535 |
4.96e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.30 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS-----NEDQDYEGELKI-GQTV------------ 383
Cdd:PRK14267 6 ETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrllelNEEARVEGEVRLfGRNIyspdvdpievrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 384 KVAYFKQTEK---------------TLDRDIRVIDYLREESEMAKEKDGTSISVTQLLERFlfPSathgkkvyKLSGGEQ 448
Cdd:PRK14267 86 EVGMVFQYPNpfphltiydnvaigvKLNGLVKSKKELDERVEWALKKAALWDEVKDRLNDY--PS--------NLSGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 449 KRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYI----DDFggSVITVSHDRYFLNKVVQEYWFIHDGKIEKIIGSF 524
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLfelkKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
250
....*....|.
gi 1842088001 525 EDYESfkKEHE 535
Cdd:PRK14267 234 KVFEN--PEHE 242
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
156-191 |
5.01e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 5.01e-06
10 20 30
....*....|....*....|....*....|....*.
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:NF040905 401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
14-234 |
5.92e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 48.15 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYAD-KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGldedftadITHPNqyriryssqkqdlNGHMTVFEAVLSS 92
Cdd:PRK13639 10 SYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNG--------ILKPT-------------SGEVLIKGEPIKY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 93 DTPTLRIIKKYEEAVNRYALDQ-------SDSNFNKM-MEAQEEMDQKdawdynaEIKTILSKLGIHDTTKKIVE-LSGG 163
Cdd:PRK13639 69 DKKSLLEVRKTVGIVFQNPDDQlfaptveEDVAFGPLnLGLSKEEVEK-------RVKEALKAVGMEGFENKPPHhLSGG 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 164 QQKRVVLAKTLIEQPDLLLLDEPTNHLD---FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK13639 142 QKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
322-497 |
6.13e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayFKQTEKTLDRDIR 400
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMR---FASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VID---------------YLRE---------ESEMAKEkdgtsisVTQLLERF---LFPSAthgkKVYKLSGGEQKRLYL 453
Cdd:PRK11288 83 IIYqelhlvpemtvaenlYLGQlphkggivnRRLLNYE-------AREQLEHLgvdIDPDT----PLKYLSIGQRQMVEI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 454 LRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSH 497
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLSAREIEQLFRVIRELraeGRVILYVSH 198
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
157-234 |
6.17e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQYPHTVLFVTHDryfLNEV---STRIIELD 230
Cdd:PRK10762 393 IGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVgakKEIYQLINQFKAEGLSIILVSSE---MPEVlgmSDRILVMH 469
|
....
gi 1842088001 231 RGKL 234
Cdd:PRK10762 470 EGRI 473
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-267 |
6.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 48.47 E-value: 6.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIF-----NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADiTHPNQYRIRYSSQK----QD 78
Cdd:PRK13645 9 LDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQ-TIVGDYAIPANLKKikevKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 79 LNGhmtvfEAVLSSDTPTLRIikkYEEAVNRyaldqsDSNFNKMMEAQeemDQKDAWDYNAEIKTILSkLGIHDTTKKIV 158
Cdd:PRK13645 88 LRK-----EIGLVFQFPEYQL---FQETIEK------DIAFGPVNLGE---NKQEAYKKVPELLKLVQ-LPEDYVKRSPF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYV----KQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK13645 150 ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
250 260 270
....*....|....*....|....*....|...
gi 1842088001 235 KTYPGNYEDYivmrAENELVEQKQQEKQKaLYK 267
Cdd:PRK13645 230 ISIGSPFEIF----SNQELLTKIEIDPPK-LYQ 257
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-194 |
6.69e-06 |
|
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: 47.61 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKE-IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQKQDLNGHMTV 85
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI-DIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 F-EAVLSSDTPTLRIikkyeeavnRYALDqsdsnfnkmmEAQEEmdqkdawdynaEIKTILSKLGIHDTTKKIVE----- 159
Cdd:cd03254 83 LqDTFLFSGTIMENI---------RLGRP----------NATDE-----------EVIEAAKEAGAHDFIMKLPNgydtv 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1842088001 160 -------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 194
Cdd:cd03254 133 lgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
338-556 |
6.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 49.59 E-value: 6.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLNILSnedqdyeGELKIGQTV------KVAYFKQTEKTLDRDIRviDYLREESEM 411
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAML-------GELSHAETSsvvirgSVAYVPQVSWIFNATVR--ENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 AKEKDGTSISVTQLLERF-LFPS---ATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETL-TILEDYID 486
Cdd:PLN03232 706 ESERYWRAIDVTALQHDLdLLPGrdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAhQVFDSCMK 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 487 D--FGGSVITVSHDRYFLnKVVQEYWFIHDGKIeKIIGSFEDY----ESFKKEHERQAMLSKQTEQQNKHKHQPKK 556
Cdd:PLN03232 786 DelKGKTRVLVTNQLHFL-PLMDRIILVSEGMI-KEEGTFAELsksgSLFKKLMENAGKMDATQEVNTNDENILKL 859
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-215 |
7.22e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.84 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDEDFTADITHPNQYRIRYSS--- 74
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqiapdhgeilFDGENIPAMSRSRLYTVRKRMsml 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 75 -QKQDLNGHMTVFEAVlssdTPTLRIIKKYEEAVNRYALdqsdsnfnkMMEaqeemdqkdawdynaeiktiLSKLGIHDT 153
Cdd:PRK11831 90 fQSGALFTDMNVFDNV----AYPLREHTQLPAPLLHSTV---------MMK--------------------LEAVGLRGA 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 154 TK-KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPH----TVLFVTHD 215
Cdd:PRK11831 137 AKlMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalgvTCVVVSHD 203
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
337-474 |
7.97e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.93 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVkvayfkqTEKTLDRDI-----------RVIDY 404
Cdd:COG4525 24 QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdGVPV-------TGPGADRGVvfqkdallpwlNVLDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 405 ----LR-------EESEMAKEKdgtsisvTQL--LERFlfpsatHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTN 471
Cdd:COG4525 97 vafgLRlrgvpkaERRARAEEL-------LALvgLADF------ARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFG 163
|
...
gi 1842088001 472 DLD 474
Cdd:COG4525 164 ALD 166
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-191 |
8.25e-06 |
|
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: 47.93 E-value: 8.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 20 IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNqyRIRYSSQKQDLnghM--TVFEAVL---SSDT 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWI---MpgTIKENIIfgvSYDE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 95 ptlriiKKYEEAVNRYALDQSDSNFnkmmeaqeemDQKDawdynaeiKTILSKLGIhdttkkivELSGGQQKRVVLAKTL 174
Cdd:cd03291 127 ------YRYKSVVKACQLEEDITKF----------PEKD--------NTVLGEGGI--------TLSGGQRARISLARAV 174
|
170
....*....|....*..
gi 1842088001 175 IEQPDLLLLDEPTNHLD 191
Cdd:cd03291 175 YKDADLYLLDSPFGYLD 191
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
334-497 |
8.59e-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: 49.17 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 334 VLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV----------KVAYFKQTEKTLDRDIRV- 401
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIdGLNIakiglhdlrfKITIIPQDPVLFSGSLRMn 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 ID----YLREESEMAKEKDGTSISVTQLLERFLFPSATHGKKvykLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:TIGR00957 1380 LDpfsqYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGEN---LSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
170 180
....*....|....*....|....
gi 1842088001 478 LTILEDYI----DDFggSVITVSH 497
Cdd:TIGR00957 1457 DNLIQSTIrtqfEDC--TVLTIAH 1478
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-231 |
9.27e-06 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 47.69 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 21 FNDLNLSISEHERIG-LVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQDLNGHM--------TVFEAVLS 91
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGEFGDSAKLilyygtsrLLLDGPLK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 92 SDTptlRIIKKYEEAVNRYA-LDQSDSNFNK----MMEAQEEMDQKDAWDYNAEIKTI----------LSKLGIHDTTKK 156
Cdd:COG3950 94 KLE---RLKEEYFSRLDGYDsLLDEDSNLREflewLREYLEDLENKLSDELDEKLEAVrealnkllpdFKDIRIDRDPGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IV------------ELSGGQQKRVVLA--------------KTLIEQPDLLLLDEPTNHLdfeSIRW---LINYVKQ-YP 206
Cdd:COG3950 171 LVildkngeelplnQLSDGERSLLALVgdlarrlaelnpalENPLEGEGIVLIDEIDLHL---HPKWqrrILPDLRKiFP 247
|
250 260
....*....|....*....|....*..
gi 1842088001 207 HT-VLFVTHDRYFLNEVSTR-IIELDR 231
Cdd:COG3950 248 NIqFIVTTHSPLILSSLEDEeVIVLER 274
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
322-481 |
9.56e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQD--YEGELKIGQTVKV--------AYFKQT 391
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKqetfarisGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 392 -----EKTLDRDIRVIDYLREESEMAKEKDGTSI-SVTQLLERFLFPSATHG-KKVYKLSGGEQKRLYLLRLLVHKPNVL 464
Cdd:PLN03140 962 dihspQVTVRESLIYSAFLRLPKEVSKEEKMMFVdEVMELVELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|....*..
gi 1842088001 465 LLDEPTNDLDTETLTIL 481
Cdd:PLN03140 1042 FMDEPTSGLDARAAAIV 1058
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
157-235 |
1.34e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 47.90 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK 233
Cdd:TIGR02633 401 IGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAkyeIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
..
gi 1842088001 234 LK 235
Cdd:TIGR02633 481 LK 482
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-214 |
1.52e-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: 48.21 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQYRIRYSSQKQdlngHMTVfeavlssdtPTLR--I 99
Cdd:TIGR00954 469 ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRP----YMTL---------GTLRdqI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 100 IkkYEEAVnryaldqsdsnfnkmmeaqEEMDQKDAWDynAEIKTILSKLGIHDTTKKIV----------ELSGGQQKRVV 169
Cdd:TIGR00954 536 I--YPDSS-------------------EDMKRRGLSD--KDLEQILDNVQLTHILEREGgwsavqdwmdVLSGGEKQRIA 592
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1842088001 170 LAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYPHTVLFVTH 214
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-517 |
1.64e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 46.92 E-value: 1.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 350 GIVGPNGAGKTTLLNILS-------------NEDQDY--EGELKIGQTVKVAyFKQTEKTL---DRDIRVIDYLRE---- 407
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSgllrpqkgavlwqGKPLDYskRGLLALRQQVATV-FQDPEQQIfytDIDSDIAFSLRNlgvp 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 408 ESEMAKEKDgtsisvtqllERFLFPSATHGKK--VYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTIL 481
Cdd:PRK13638 110 EAEITRRVD----------EALTLVDAQHFRHqpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDpagrTQMIAII 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1842088001 482 EDYIDDfGGSVITVSHDRYFLNKVVQEYWFIHDGKI 517
Cdd:PRK13638 180 RRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
317-498 |
1.84e-05 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 45.50 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 317 GKQVYELKNLSksinNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKvayFKQTEKTL 395
Cdd:cd03215 1 GEPVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVT---RRSPRDAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 396 DRDIRvidYLREEsemaKEKDGtsisvtqllerfLFPSAThgkkVYK-------LSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:cd03215 74 RAGIA---YVPED----RKREG------------LVLDLS----VAEnialsslLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190
....*....|....*....|....*....|....*
gi 1842088001 469 PTNDLDTEtlTILEDY--IDDF---GGSVITVSHD 498
Cdd:cd03215 131 PTRGVDVG--AKAEIYrlIRELadaGKAVLLISSE 163
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
336-498 |
1.93e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.16 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 336 FEDVTEIIQSGRRIGIVGPNGAGKTTLLN--------------------------------ILSNEDQDYEGELKIGQTV 383
Cdd:COG0419 13 YRDTETIDFDDGLNLIVGPNGAGKSTILEairyalygkarsrsklrsdlinvgseeasvelEFEHGGKRYRIERRQGEFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 384 KVAYFKQTEKT--------LDRDIRVIDYLREESEMAKEKDGTSISVTQLLERFLfpSATHGKKVYK-LSGGEQKRLYLL 454
Cdd:COG0419 93 EFLEAKPSERKealkrllgLEIYEELKERLKELEEALESALEELAELQKLKQEIL--AQLSGLDPIEtLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1842088001 455 RLLvhkpnVLLLDepTNDLDTETLTILEDYIDdfggSVITVSHD 498
Cdd:COG0419 171 DLL-----SLILD--FGSLDEERLERLLDALE----ELAIITHV 203
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
332-575 |
1.98e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.77 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 332 NKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEdQDYEGELKIG----QTV--------------KVAYFKQT-E 392
Cdd:cd03289 17 NAVL-ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDgvswNSVplqkwrkafgvipqKVFIFSGTfR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTLDRDIRVIDylrEESEMAKEKDGTSISVTQLLERFLFPSATHGkkvYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTND 472
Cdd:cd03289 95 KNLDPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGG---CVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 473 LDTETLTILEDYIDD-FGGSVITVSHDRYFLNKVVQEYWFIHDGKIEKiigsfedYESFKK-----EHERQAMLSK---- 542
Cdd:cd03289 169 LDPITYQVIRKTLKQaFADCTVILSEHRIEAMLECQRFLVIEENKVRQ-------YDSIQKllnekSHFKQAISPSdrlk 241
|
250 260 270
....*....|....*....|....*....|....*
gi 1842088001 543 --QTEQQNKHKHQPKKKTGlSYKEKLEYETIMTRI 575
Cdd:cd03289 242 lfPRRNSSKSKRKPRPQIQ-ALQEETEEEVQDTRL 275
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-256 |
2.28e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 46.70 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 17 DKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHpNQYRIRYSSQKQDLNGHMTVFEAVLSSDTPT 96
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV-DDITITHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 97 LriikkYEEAVNRyALDQSDSNFNkmmeaqeeMDQKDAWDYNAEIktiLSKLGIHDT--TKKIVELSGGQQKRVVLAKTL 174
Cdd:PRK13646 98 L-----FEDTVER-EIIFGPKNFK--------MNLDEVKNYAHRL---LMDLGFSRDvmSQSPFQMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 175 IEQPDLLLLDEPTNHLDFESIRWLINYVKQYP----HTVLFVTHDryfLNEVStriieldrgklktypgNYEDYIVMRAE 250
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdenKTIILVSHD---MNEVA----------------RYADEVIVMKE 221
|
....*.
gi 1842088001 251 NELVEQ 256
Cdd:PRK13646 222 GSIVSQ 227
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
334-497 |
2.65e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 45.95 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 334 VLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvkvayfkqtektlDRDIRVID--YLReesem 411
Cdd:cd03244 19 VL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILID---------------GVDISKIGlhDLR----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 412 akekdgTSIS-VTQllERFLFP----------------------SATHGKKVYK----------------LSGGEQKRLY 452
Cdd:cd03244 78 ------SRISiIPQ--DPVLFSgtirsnldpfgeysdeelwqalERVGLKEFVEslpggldtvveeggenLSVGQRQLLC 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1842088001 453 LLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF--GGSVITVSH 497
Cdd:cd03244 150 LARALLRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
322-482 |
2.68e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 46.61 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNK-----VLfEDVTEIIQSGRRIGIVGPNGAGKTTLL---NILSN--------EDQDY----EGEL---- 377
Cdd:COG1135 3 ELENLSKTFPTKggpvtAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLERptsgsvlvDGVDLtalsERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 378 -KIG---Q--------TVK--VAYfkqtektldrDIRVIDYLREEsemAKEKdgtsisVTQLLERF-LfpsaTHGKKVY- 441
Cdd:COG1135 82 rKIGmifQhfnllssrTVAenVAL----------PLEIAGVPKAE---IRKR------VAELLELVgL----SDKADAYp 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1842088001 442 -KLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE-TLTILE 482
Cdd:COG1135 139 sQLSGGQKQRVGIARALANNPKVLLCDEATSALDPEtTRSILD 181
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-267 |
3.04e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.94 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEI--FNDLNLSISEHERIGLVGINGTGKSTllkvIGGLDEDFTaDIthpNQYRIRyssqkqdLNGHmT 84
Cdd:PRK11176 343 EFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKST----IANLLTRFY-DI---DEGEIL-------LDGH-D 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 85 VFEAVLSS----------------DTPTLRIIKKYEEAVNRYALDQSdsnfNKM---MEAQEEMDQKdawdynaeIKTIL 145
Cdd:PRK11176 407 LRDYTLASlrnqvalvsqnvhlfnDTIANNIAYARTEQYSREQIEEA----ARMayaMDFINKMDNG--------LDTVI 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 146 SKLGihdttkkiVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK--QYPHTVLFVTHdRYFLNEVS 223
Cdd:PRK11176 475 GENG--------VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDelQKNRTSLVIAH-RLSTIEKA 545
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1842088001 224 TRIIELDRGKLKTYpGNYedyivmraeNELVEQKQQEKQkaLYK 267
Cdd:PRK11176 546 DEILVVEDGEIVER-GTH---------AELLAQNGVYAQ--LHK 577
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-234 |
3.29e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 24 LNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADI------THPNQYRIRYS----SQKQDLNGHMTVFEAVLSsd 93
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVlvggkdIETNLDAVRQSlgmcPQHNILFHHLTVAEHILF-- 1026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 94 tptlriikkyeeavnrYALDQSDSnfnkMMEAQEEMDqkdawdynaeikTILSKLGIHDT-TKKIVELSGGQQKRVVLAK 172
Cdd:TIGR01257 1027 ----------------YAQLKGRS----WEEAQLEME------------AMLEDTGLHHKrNEEAQDLSGGMQRKLSVAI 1074
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 173 TLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP--HTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRsgRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
322-519 |
3.43e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDqDYE---GEL--------------KIGQTVK 384
Cdd:PRK09580 3 SIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRE-DYEvtgGTVefkgkdllelspedRAGEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 385 VAY-------------FKQTEKTLDRDIRVIDYLR--EESEMAKEKdgtsISVTQLLERFLFPSATHGkkvykLSGGEQK 449
Cdd:PRK09580 82 MAFqypveipgvsnqfFLQTALNAVRSYRGQEPLDrfDFQDLMEEK----IALLKMPEDLLTRSVNVG-----FSGGEKK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYID---DFGGSVITVSHDRYFLNKVVQEYWFI-HDGKIEK 519
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNslrDGKRSFIIVTHYQRILDYIKPDYVHVlYQGRIVK 226
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
424-517 |
3.46e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 424 QLLERFLFPSAThGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRY 500
Cdd:NF000106 127 ELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMvrdGATVLLTTQYME 205
|
90
....*....|....*..
gi 1842088001 501 FLNKVVQEYWFIHDGKI 517
Cdd:NF000106 206 EAEQLAHELTVIDRGRV 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
7-234 |
3.52e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLN-KSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDED-------FTADITH--PNQYR---IRYS 73
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPasgsirlDGEDITGlsPRERRrlgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 74 S---QKQDLNGHMTVFE-AVLSS-DTPTLR---IIKKyeEAVNRYAldqsdsnfNKMMEaqeemdqkdawDYNaeIKTIl 145
Cdd:COG3845 339 PedrLGRGLVPDMSVAEnLILGRyRRPPFSrggFLDR--KAIRAFA--------EELIE-----------EFD--VRTP- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 146 sklGIHDTTKKiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLinyvkqypH-----------TVLFVTH 214
Cdd:COG3845 395 ---GPDTPARS---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFI--------HqrllelrdagaAVLLISE 460
|
250 260
....*....|....*....|...
gi 1842088001 215 DryfLNEV---STRIIELDRGKL 234
Cdd:COG3845 461 D---LDEIlalSDRIAVMYEGRI 480
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
338-498 |
3.58e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.78 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTL---LNILSNEDQDyegelkigqTVKVAYFKQTEKTLdRDIR-------------- 400
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLaklLNGLLLPEAG---------TITVGGMVLSEETV-WDVRrqvgmvfqnpdnqf 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 VIDYLREESEMAKEKDGtsISVTQLLER------------FLFPSATHgkkvykLSGGEQKRLYLLRLLVHKPNVLLLDE 468
Cdd:PRK13635 95 VGATVQDDVAFGLENIG--VPREEMVERvdqalrqvgmedFLNREPHR------LSGGQKQRVAIAGVLALQPDIIILDE 166
|
170 180 190
....*....|....*....|....*....|....
gi 1842088001 469 PTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK13635 167 ATSMLDprgrREVLETVRQLKEQKGITVLSITHD 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
405-497 |
3.74e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 405 LREESEMAKEKDGTSISVTQLLERFL--FPSATH---GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLT 479
Cdd:PTZ00265 537 MRKNYQTIKDSEVVDVSKKVLIHDFVsaLPDKYEtlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
90 100
....*....|....*....|..
gi 1842088001 480 ILEDYIDDFGGS----VITVSH 497
Cdd:PTZ00265 617 LVQKTINNLKGNenriTIIIAH 638
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
343-498 |
3.92e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 46.23 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTV----KVAYFKQT-----EKT-LDRDIRVIDYLR------ 406
Cdd:COG4586 45 IEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrRKEFARRIgvvfgQRSqLWWDLPAIDSFRllkaiy 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 407 --EESEMAKEKDgtsiSVTQLLE--RFLfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET-LTI- 480
Cdd:COG4586 125 riPDAEYKKRLD----ELVELLDlgELL------DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkEAIr 194
|
170 180
....*....|....*....|
gi 1842088001 481 --LEDYIDDFGGSVITVSHD 498
Cdd:COG4586 195 efLKEYNRERGTTILLTSHD 214
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-237 |
4.16e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 20 IFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHP--NQYRIRYssqkQDLNGHMTVF--EAVLSSDTp 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDglNIAKIGL----HDLRFKITIIpqDPVLFSGS- 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 96 tLRIikkyeeavnryaldqsdsNFNKMMEAQEEmdqkDAWDYN--AEIKTILSKLGI---HDTTKKIVELSGGQQKRVVL 170
Cdd:TIGR00957 1376 -LRM------------------NLDPFSQYSDE----EVWWALelAHLKTFVSALPDkldHECAEGGENLSVGQRQLVCL 1432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 171 AKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK-QYPH-TVLFVTHDryfLNEVS--TRIIELDRGKLKTY 237
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRtQFEDcTVLTIAHR---LNTIMdyTRVIVLDKGEVAEF 1500
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
343-498 |
4.36e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 45.85 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKVAYFKQTEKTL-----DRDIRVIDYLREE-------- 408
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIgmvfqNPDNQFVGATVEDdvafgmen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 409 -----SEMAKEKDGTSISVTQLLERFLFPSathgkkvyKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLT 479
Cdd:PRK13642 110 qgiprEEMIKRVDEALLAVNMLDFKTREPA--------RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgrQEIMR 181
|
170
....*....|....*....
gi 1842088001 480 ILEDYIDDFGGSVITVSHD 498
Cdd:PRK13642 182 VIHEIKEKYQLTVLSITHD 200
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-187 |
4.81e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 45.26 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 1 MSMEAYKIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADIThpnqyriryssqkqdln 80
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 81 ghmtvFEAVLSSDTPTLRIIKKYEEAV--NRYALDQSDSNFNKMM----EAQEEMDQKDAWDYNaeiktILSKLgIHDTT 154
Cdd:PRK11614 64 -----FDGKDITDWQTAKIMREAVAIVpeGRRVFSRMTVEENLAMggffAERDQFQERIKWVYE-----LFPRL-HERRI 132
|
170 180 190
....*....|....*....|....*....|...
gi 1842088001 155 KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPT 187
Cdd:PRK11614 133 QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
161-215 |
5.20e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 45.73 E-value: 5.20e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 161 SGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFeSIR-----WLINYVKQYPHTVLFVTHD 215
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDV-SVQaqvlnLMMDLQQELGLSYVFISHD 214
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
160-234 |
6.33e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.81 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES---IRWLINYVKQYPHTVLFVTHDryfLNEV---STRIIELDRGK 233
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSArndIYQLIRSIAAQNVAVLFISSD---LEEIeqmADRVLVMHQGE 480
|
.
gi 1842088001 234 L 234
Cdd:PRK15439 481 I 481
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
338-477 |
7.18e-05 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 45.97 E-value: 7.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEIIQSGRRIGIVGPNGAGKTTLLNILsnedqdY------EGELKI-GQTVKvayfKQTEKTLDRDIRV--------- 401
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLL------FrfydvtSGRILIdGQDIR----DVTQASLRAAIGIvpqdtvlfn 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 402 ------IDYLR-----EESEMAKE-----------KDGTSisvTQLLERFLfpsathgkkvyKLSGGEQKRLYLLRLLVH 459
Cdd:COG5265 446 dtiaynIAYGRpdaseEEVEAAARaaqihdfieslPDGYD---TRVGERGL-----------KLSGGEKQRVAIARTLLK 511
|
170
....*....|....*...
gi 1842088001 460 KPNVLLLDEPTNDLDTET 477
Cdd:COG5265 512 NPPILIFDEATSALDSRT 529
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
322-498 |
7.38e-05 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 45.04 E-value: 7.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS--INNKVLF--EDVTEIIQSGRRIGIVGPNGAGKTTL----LNILSNEDQDyEGELKI-GQTVkvayFKQTE 392
Cdd:COG0444 3 EVRNLKVYfpTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGIT-SGEILFdGEDL----LKLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 393 KTLdRDIR--------------------VIDYLRE--------ESEMAKEKdgtsisVTQLLERFLFPSAthgKKVYK-- 442
Cdd:COG0444 78 KEL-RKIRgreiqmifqdpmtslnpvmtVGDQIAEplrihgglSKAEARER------AIELLERVGLPDP---ERRLDry 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 443 ---LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:COG0444 148 pheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqAQILNLLKDLQRELGLAILFITHD 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
333-474 |
7.87e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 7.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 333 KVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGQTvkVAYFKQTEKTLDRDIRV-IDYLREESEm 411
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--IAYVPQQAWIMNATVRGnILFFDEEDA- 749
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 412 AKEKDGTSIS-----VTQL---LERFLfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PTZ00243 750 ARLADAVRVSqleadLAQLgggLETEI------GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-194 |
8.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 8.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 20 IFNDLNLSISEHERIGLVGINGTGKSTLLKVIggldedftadithpnqyrIRYSSQKQDlngHMTVFEAVLSSDTPTLRI 99
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLL------------------MRFYDLKND---HHIVFKNEHTNDMTNEQD 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 100 IKKYEEA------VNRYALD------QSDSNFNKMMEAQeeMDQKDAWDYN-AEIKTILS-----------------KLG 149
Cdd:PTZ00265 1242 YQGDEEQnvgmknVNEFSLTkeggsgEDSTVFKNSGKIL--LDGVDICDYNlKDLRNLFSivsqepmlfnmsiyeniKFG 1319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 150 IHDTTKKIVE-----------------------------LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFES 194
Cdd:PTZ00265 1320 KEDATREDVKrackfaaidefieslpnkydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
317-534 |
8.31e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 317 GKQVYELKNLS-----KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLN-----------------ILSNEDQDYE 374
Cdd:PRK13631 18 DDIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiqvgdIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 375 GELKIGQTVKVAYFKQTEKTLDRDIRVIDY-----------------LREESEMAKEKDGTSISVTQLLERFLFPSAthg 437
Cdd:PRK13631 98 ELITNPYSKKIKNFKELRRRVSMVFQFPEYqlfkdtiekdimfgpvaLGVKKSEAKKLAKFYLNKMGLDDSYLERSP--- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 438 kkvYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKVVQEYWFIHD 514
Cdd:PRK13631 175 ---FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkanNKTVFVITHTMEHVLEVADEVIVMDK 251
|
250 260
....*....|....*....|
gi 1842088001 515 GKIEKiigSFEDYESFKKEH 534
Cdd:PRK13631 252 GKILK---TGTPYEIFTDQH 268
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-215 |
9.07e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 9.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 7 KIEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLdedftadiTHPNQYRIRYSSQKQDLNGHMTVF 86
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSAR--------LAPDAGEVHYRMRDGQLRDLYALS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAvlssdtpTLRIIKKYEEA-VNRYALD------QSDSNFNKMMEAQEE------MDQKDAWDYNAEIKtiLSKLGIHDT 153
Cdd:PRK11701 80 EA-------ERRRLLRTEWGfVHQHPRDglrmqvSAGGNIGERLMAVGArhygdiRATAGDWLERVEID--AARIDDLPT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1842088001 154 TkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLinyVKQYPHTVLFVTHD 215
Cdd:PRK11701 151 T-----FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsvqarlLDLLRGL---VRELGLAVVIVTHD 211
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
156-191 |
1.45e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.90 E-value: 1.45e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:PRK11288 393 LIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID 428
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
147-214 |
1.49e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1842088001 147 KLGIHDTTkkiveLSGGQQKRVVLAKTLIEQ---PDLLLLDEPTNHLDFESIRWLINYVKQY---PHTVLFVTH 214
Cdd:TIGR00630 822 RLGQPATT-----LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLvdkGNTVVVIEH 890
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-219 |
1.60e-04 |
|
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: 43.47 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 21 FNDLNLSISEHERIGLVGINGTGKSTLLKVIGG---------------LDEDFTADITHPNQYRIRYSSQKQDLNgHMTV 85
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqtlegkvhwsnknESEPSFEATRSRNRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 86 FEAVlSSDTPTLRiiKKYEEAVNRYALdqsdsnfnkmmeaQEEMDQKDAWDynaeiKTILSKLGIHdttkkiveLSGGQQ 165
Cdd:cd03290 96 EENI-TFGSPFNK--QRYKAVTDACSL-------------QPDIDLLPFGD-----QTEIGERGIN--------LSGGQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 166 KRVVLAKTLIEQPDLLLLDEP--------TNHLDFESIrwlINYVKQYPHTVLFVTHDRYFL 219
Cdd:cd03290 147 QRICVARALYQNTNIVFLDDPfsaldihlSDHLMQEGI---LKFLQDDKRTLVLVTHKLQYL 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
157-215 |
1.68e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 1.68e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 157 IVELSGGQQKRVVLAKTLIEQP----DLLLLDEPTNHLDFESIRWLINYVK-QYPH--TVLFVTHD 215
Cdd:cd03227 75 RLQLSGGEKELSALALILALASlkprPLYILDEIDRGLDPRDGQALAEAILeHLVKgaQVIVITHL 140
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-213 |
1.69e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 43.02 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 18 KEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHpnqyrIRYssqkqdlNGHmtvfeavlssdtptl 97
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGD-----IHY-------NGI--------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 98 riikKYEEAVNRYaldQSDSNFNkmmeaqEEMDQKDAWDYNAE-IKTILSKLGiHDTTKKIvelSGGQQKRVVLAKTLIE 176
Cdd:cd03233 73 ----PYKEFAEKY---PGEIIYV------SEEDVHFPTLTVREtLDFALRCKG-NEFVRGI---SGGERKRVSIAEALVS 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1842088001 177 QPDLLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVT 213
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEILKCIRTMADvlkTTTFVS 175
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
443-509 |
1.92e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.61 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 443 LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD-------TETLTIL-EDYiddfggSVITVSH---------DR--YFLN 503
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDpisagkiEETLLGLkDDY------TMLLVTRsmqqasrisDRtgFFLD 222
|
....*.
gi 1842088001 504 KVVQEY 509
Cdd:PRK14239 223 GDLIEY 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-234 |
1.94e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.25 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 23 DLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDF---------------TADITHPNQYRIRYSSQKQDLNGHMTVfe 87
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTrgqvlidgvdiakisDAELREVRRKKIAMVFQSFALMPHMTV-- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 88 avlssdtptlriikkyeeavnryaLDQSDSNFNKMMEAQEEMDQKdAWDynaeiktILSKLGIHDTTKKIV-ELSGGQQK 166
Cdd:PRK10070 124 ------------------------LDNTAFGMELAGINAEERREK-ALD-------ALRQVGLENYAHSYPdELSGGMRQ 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 167 RVVLAKTLIEQPDLLLLDEPTNHLD----FESIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:PRK10070 172 RVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
438-498 |
2.17e-04 |
|
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: 43.40 E-value: 2.17e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1842088001 438 KKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirREMQDELLRLQAELQKTIVFITHD 220
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
306-505 |
2.32e-04 |
|
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: 43.97 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 306 KGEL---NLAYSRLGKQVYELKNLSksinnkvlFEdvteiIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQ 381
Cdd:COG4618 328 KGRLsveNLTVVPPGSKRPILRGVS--------FS-----LEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdGA 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 382 TVKvayfkqtekTLDRDI--RVIDYLREESEMAkekDGT---SISvtqlleRFlfPSAThGKKVYK-------------- 442
Cdd:COG4618 395 DLS---------QWDREElgRHIGYLPQDVELF---DGTiaeNIA------RF--GDAD-PEKVVAaaklagvhemilrl 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 443 --------------LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDF---GGSVITVSHDRYFLNKV 505
Cdd:COG4618 454 pdgydtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHRPSLLAAV 533
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
322-497 |
2.36e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.58 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKSINNKVLFE-----DVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGElkigqtVKVAYFKQTEKTLD 396
Cdd:PRK13649 4 NLQNVSYTYQAGTPFEgralfDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGS------VRVDDTLITSTSKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVID------YLREESEMAKE---KD--------GTSISVTQLLER----------FLFpsathGKKVYKLSGGEQK 449
Cdd:PRK13649 78 KDIKQIRkkvglvFQFPESQLFEEtvlKDvafgpqnfGVSQEEAEALAReklalvgiseSLF-----EKNPFELSGGQMR 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 450 RLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDfGGSVITVSH 497
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDpkgrKELMTLFKKLHQS-GMTIVLVTH 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
8-230 |
2.55e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.94 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSY-ADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGG----------LDEDFTADITHpnqyrirySSQK 76
Cdd:PRK10790 343 IDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypltegeirLDGRPLSSLSH--------SVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 77 QDLNghMTVFEAVLSSDT----PTL-RIIKkyEEAVNRyALDQSdsnfnKMMEAQEEMDQKdawdynaeiktILSKLGIH 151
Cdd:PRK10790 415 QGVA--MVQQDPVVLADTflanVTLgRDIS--EEQVWQ-ALETV-----QLAELARSLPDG-----------LYTPLGEQ 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 152 DTTkkiveLSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDF---ESIRWLINYVKQypHTVLFVTHDRyflneVSTrIIE 228
Cdd:PRK10790 474 GNN-----LSVGQKQLLALARVLVQTPQILILDEATANIDSgteQAIQQALAAVRE--HTTLVVIAHR-----LST-IVE 540
|
..
gi 1842088001 229 LD 230
Cdd:PRK10790 541 AD 542
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
343-498 |
2.57e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 43.28 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLnilsnedQDYEGELKIGQ-TVKVAYFKQTEKTLDRDIRVI------------DYLREES 409
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLM-------QHFNALLKPSSgTITIAGYHITPETGNKNLKKLrkkvslvfqfpeAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 410 ----------------EMAKEKdgtsisVTQLLERFLFPSATHGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL 473
Cdd:PRK13641 103 vlkdvefgpknfgfseDEAKEK------ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180
....*....|....*....|....*....
gi 1842088001 474 D----TETLTILEDYiDDFGGSVITVSHD 498
Cdd:PRK13641 177 DpegrKEMMQLFKDY-QKAGHTVILVTHN 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
160-220 |
3.00e-04 |
|
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: 42.21 E-value: 3.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1842088001 160 LSGGQQK------RVVLAKTLIEQPDLLLLDEPTNHLDFESIRW----LINYVKQYPH-TVLFVTHDRYFLN 220
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEEslaeIIEERKSQKNfQLIVITHDEELVD 187
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
8-474 |
3.18e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 8 IEHLNKSYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyRIRYSSQKQDL-NGHMTVF 86
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGK-EIDFKSSKEALeNGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 87 EAvlssdtptLRIIKKYEEAVN----RYALDQSDSNFNKMmeaqeemdqkdawdYNaEIKTILSKLGIH-DTTKKIVELS 161
Cdd:PRK10982 80 QE--------LNLVLQRSVMDNmwlgRYPTKGMFVDQDKM--------------YR-DTKAIFDELDIDiDPRAKVATLS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 162 GGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLNEVSTRIIELDRGK-LKTY 237
Cdd:PRK10982 137 VSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLftiIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQwIATQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 238 P--GNYEDYIV-MRAENELveqkqqekqkalykqelawmragakarttkqqarinrfnqlesdvkTQHTQDKGelnlayS 314
Cdd:PRK10982 217 PlaGLTMDKIIaMMVGRSL----------------------------------------------TQRFPDKE------N 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 315 RLGKQVYELKNLSkSINNKVLfEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTVKV-------- 385
Cdd:PRK10982 245 KPGEVILEVRNLT-SLRQPSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLhGKKINNhnaneain 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 386 -AYFKQTEKTldRDIRVIDYLREE-----SEMAKEKDGTSI-------SVTQ-LLERFLFPSATHGKKVYKLSGGEQKRL 451
Cdd:PRK10982 323 hGFALVTEER--RSTGIYAYLDIGfnsliSNIRNYKNKVGLldnsrmkSDTQwVIDSMRVKTPGHRTQIGSLSGGNQQKV 400
|
490 500
....*....|....*....|...
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLD 474
Cdd:PRK10982 401 IIGRWLLTQPEILMLDEPTRGID 423
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
138-232 |
3.22e-04 |
|
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: 41.59 E-value: 3.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 138 NAEIKTILSKLGIHDTTKKIVELSGGQQKRVVLAKTLIEQ--PDLLLLDEPTNHLD---------FESIRWLINYVKQYP 206
Cdd:smart00382 37 DGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKlkPDVLILDEITSLLDaeqeallllLEELRLLLLLKSEKN 116
|
90 100 110
....*....|....*....|....*....|.
gi 1842088001 207 HTVLFVTHDRYFLNE-----VSTRIIELDRG 232
Cdd:smart00382 117 LTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
338-498 |
3.36e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 43.17 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 338 DVTEI------IQSGRRIGIVGPNGAGKT----TLLNILSNE-----DQDYEG---------ELKIGQTVKVAYFKQTEK 393
Cdd:PRK09473 28 DVTAVndlnfsLRAGETLGIVGESGSGKSqtafALMGLLAANgriggSATFNGreilnlpekELNKLRAEQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 394 T-LDRDIRVIDYLRE----ESEMAKeKDGTSISVtQLLERFLFPSATHGKKVY--KLSGGEQKRLYLLRLLVHKPNVLLL 466
Cdd:PRK09473 108 TsLNPYMRVGEQLMEvlmlHKGMSK-AEAFEESV-RMLDAVKMPEARKRMKMYphEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 1842088001 467 DEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK09473 186 DEPTTALDvtvqAQIMTLLNELKREFNTAIIMITHD 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
343-580 |
3.73e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.96 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLN-ILSNEDQDYEGELKIGQTVkvAYFKQTEKTLDRDIRviDYLREESEMAKEKDGTSIS 421
Cdd:PLN03130 640 VPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTV--AYVPQVSWIFNATVR--DNILFGSPFDPERYERAID 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 422 VTQL---LErfLFPSATH---GKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET-LTILEDYI-DDFGGSV- 492
Cdd:PLN03130 716 VTALqhdLD--LLPGGDLteiGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgRQVFDKCIkDELRGKTr 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 493 ITVSHDRYFLNKvVQEYWFIHDGKI------EKII-------------GSFEDYESFKKEHERQAMLSKQTEQQNKHKhq 553
Cdd:PLN03130 794 VLVTNQLHFLSQ-VDRIILVHEGMIkeegtyEELSnngplfqklmenaGKMEEYVEENGEEEDDQTSSKPVANGNANN-- 870
|
250 260
....*....|....*....|....*..
gi 1842088001 554 pKKKTGLSYKEKLEYETIMTRIEMTET 580
Cdd:PLN03130 871 -LKKDSSSKKKSKEGKSVLIKQEERET 896
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
335-477 |
5.11e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 43.36 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 335 LFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGelKIGQTVKVAYFKQTEKTLDRDIR-------------- 400
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--KIKHSGRISFSPQTSWIMPGTIKdniifglsydeyry 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 --VIDYLREESEMAK--EKDGTSIsvtqllerflfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:TIGR01271 519 tsVIKACQLEEDIALfpEKDKTVL----------------GEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
.
gi 1842088001 477 T 477
Cdd:TIGR01271 583 T 583
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
156-234 |
5.57e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 156 KIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD----FEsIRWLINYVKQYPHTVLFVTHDRYFLNEVSTRIIELDR 231
Cdd:PRK10982 388 QIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgakFE-IYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSN 466
|
...
gi 1842088001 232 GKL 234
Cdd:PRK10982 467 GLV 469
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
157-220 |
5.77e-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: 42.38 E-value: 5.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 157 IVELSGGQQK---RVVLAKTLIEQPDLLLLDEPTNHLDFESIRWL---INYVKQYPHTVLFVTHDRYFLN 220
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLlelLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
320-498 |
6.27e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.08 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 320 VYELKNLSKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKIGqtvKVAYFKQTekTLDRDI 399
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEG---KVTFHGKN--LYAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 400 RVIDyLREESEMAKEK------------------DGTSISVTQLLERFLFPSATHGKKVYKL-------SGGEQKRLYLL 454
Cdd:PRK14243 85 DPVE-VRRRIGMVFQKpnpfpksiydniaygariNGYKGDMDELVERSLRQAALWDEVKDKLkqsglslSGGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1842088001 455 RLLVHKPNVLLLDEPTNDLDTETLTILEDYIDDFGG--SVITVSHD 498
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEqyTIIIVTHN 209
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-498 |
6.28e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 42.03 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 351 IVGPNGAGKTTLLNILSNEDQDYEGElkigqtvkvAYFKQTEKT----------------------------------LD 396
Cdd:COG4674 41 IIGPNGAGKTTLMDVITGKTRPDSGS---------VLFGGTDLTgldeheiarlgigrkfqkptvfeeltvfenlelaLK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 397 RDIRVIDYLReesemAKEKDGTSISVTQLLER-FLFPSAthGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDL-D 474
Cdd:COG4674 112 GDRGVFASLF-----ARLTAEERDRIEEVLETiGLTDKA--DRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMtD 184
|
170 180 190
....*....|....*....|....*....|.
gi 1842088001 475 TET-------LTILEDYiddfggSVITVSHD 498
Cdd:COG4674 185 AETertaellKSLAGKH------SVVVVEHD 209
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
147-215 |
6.51e-04 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 41.83 E-value: 6.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 147 KLGIHDTTkkiveLSGGQQKRVVLAKTLIEQ---PDLLLLDEPTNHLDFESIRWLIN----YVKQyPHTVLFVTHD 215
Cdd:cd03271 162 KLGQPATT-----LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEvlqrLVDK-GNTVVVIEHN 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
22-270 |
6.76e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 22 NDLNLSISEHERIGLVGINGTGKSTLLKVIGGLDEDFTADITHPNQyrIRYSSQKQDLNGHMTVFEAVlssdtptlriik 101
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--VSVIAISAGLSGQLTGIENI------------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 102 kyeeAVNRYALDQSDSNFNKMMEAQEEmdqkdawdynaeiktiLSKLG--IHDTTKKiveLSGGQQKRVVLAKTLIEQPD 179
Cdd:PRK13546 107 ----EFKMLCMGFKRKEIKAMTPKIIE----------------FSELGefIYQPVKK---YSSGMRAKLGFSINITVNPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 180 LLLLDEPTNHLDFESIRWLINYVKQYPH---TVLFVTHDRYFLNEVSTRIIELDRGKLKTYpGNYEDyiVMRAENELV-- 254
Cdd:PRK13546 164 ILVIDEALSVGDQTFAQKCLDKIYEFKEqnkTIFFVSHNLGQVRQFCTKIAWIEGGKLKDY-GELDD--VLPKYEAFLnd 240
|
250
....*....|....*..
gi 1842088001 255 -EQKQQEKQKAlYKQEL 270
Cdd:PRK13546 241 fKKKSKAEQKE-FRNKL 256
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-243 |
6.80e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.04 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 14 SYADKEIFNDLNLSISEHERIGLVGINGTGKSTLLK-VIGGLD--EDFTADIthpnQYRIRYSSQKQDLNgHMTVFEAVL 90
Cdd:PLN03232 626 SKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELShaETSSVVI----RGSVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 91 -SSDTPTLRiikkYEEAVNRYALdqsdsnfnkmmeaQEEMDQKDAWDynaeiktiLSKLGihdttKKIVELSGGQQKRVV 169
Cdd:PLN03232 701 fGSDFESER----YWRAIDVTAL-------------QHDLDLLPGRD--------LTEIG-----ERGVNISGGQKQRVS 750
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1842088001 170 LAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP---HTVLFVTHDRYFLNEVStRIIELDRGKLKTyPGNYED 243
Cdd:PLN03232 751 MARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDElkgKTRVLVTNQLHFLPLMD-RIILVSEGMIKE-EGTFAE 825
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
159-203 |
8.64e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 40.69 E-value: 8.64e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1842088001 159 ELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVK 203
Cdd:cd03232 108 GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
343-501 |
9.03e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 42.27 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 343 IQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQTV---KVAYFKQTEKTLDRDIRVIDYLRE-ESEMAKEKDg 417
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLdGKPVtaeQPEDYRKLFSAVFTDFHLFDQLLGpEGKPANPAL- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 418 tsisVTQLLERFLFPSATH--GKKV--YKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFG 489
Cdd:PRK10522 425 ----VEKWLERLKMAHKLEleDGRIsnLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrREFYQVLLPLLQEMG 500
|
170
....*....|...
gi 1842088001 490 GSVITVSH-DRYF 501
Cdd:PRK10522 501 KTIFAISHdDHYF 513
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
155-234 |
1.19e-03 |
|
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: 42.24 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 155 KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD-------FESIRWLINYVKQypHTVLFVTHDRYFLNEVSTrII 227
Cdd:TIGR00957 756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDahvgkhiFEHVIGPEGVLKN--KTRILVTHGISYLPQVDV-II 832
|
....*..
gi 1842088001 228 ELDRGKL 234
Cdd:TIGR00957 833 VMSGGKI 839
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
337-470 |
1.20e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 337 EDVTEIIQSGRRIGIVGPNGAGKTTLLNILSnedqdyeGELKIGQ-TVKV------------------AYFKQ------- 390
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIA-------GARKIQQgRVEVlggdmadarhrravcpriAYMPQglgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 391 ----TEKTLD------------RDIRVIDYLReesemakekdgtSISVTQLLERflfPSAthgkkvyKLSGG-EQKrLYL 453
Cdd:NF033858 91 ptlsVFENLDffgrlfgqdaaeRRRRIDELLR------------ATGLAPFADR---PAG-------KLSGGmKQK-LGL 147
|
170
....*....|....*..
gi 1842088001 454 LRLLVHKPNVLLLDEPT 470
Cdd:NF033858 148 CCALIHDPDLLILDEPT 164
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
306-477 |
1.31e-03 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 41.93 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 306 KGEL---NLAYSRLGKQVYELKNLSKSInnkvlfedvteiiQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGELKI-GQ 381
Cdd:PRK11176 339 KGDIefrNVTFTYPGKEVPALRNINFKI-------------PAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLdGH 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 382 TVK----------VAYFKQT----EKTLDRDI---RVIDYLREESEMA-----------KEKDG--TSIsvtqllerflf 431
Cdd:PRK11176 406 DLRdytlaslrnqVALVSQNvhlfNDTIANNIayaRTEQYSREQIEEAarmayamdfinKMDNGldTVI----------- 474
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1842088001 432 psathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTET 477
Cdd:PRK11176 475 -----GENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
347-373 |
1.48e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 39.40 E-value: 1.48e-03
10 20
....*....|....*....|....*..
gi 1842088001 347 RRIGIVGPNGAGKTTLLNILSNEDQDY 373
Cdd:COG4917 2 KRIMLIGRSGAGKTTLTQALNGEELEY 28
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
128-234 |
2.16e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 40.87 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 128 EMDQKDAwdyNAEIKTILSKLGIHDTT-KKIVELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINYVKQYP 206
Cdd:NF000106 115 DLSRKDA---RARADELLERFSLTEAAgRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV 191
|
90 100 110
....*....|....*....|....*....|.
gi 1842088001 207 H---TVLFVTHDRYFLNEVSTRIIELDRGKL 234
Cdd:NF000106 192 RdgaTVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
160-229 |
2.57e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 2.57e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1842088001 160 LSGGQQKRVVLAKTLI---EQPDLLLLDEPTNHLDFESIRWLINYVK---QYPHTVLFVTHDRYFLnEVSTRIIEL 229
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQsltHQGHTVVIIEHNMHVV-KVADYVLEL 884
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
321-541 |
2.77e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 40.41 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 321 YELKNLsKSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLL------------------------------------- 363
Cdd:COG1106 5 FSIENF-RSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLealyflrnlvlnssqpgdklvepflldsesknepsef 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 364 -NILSNEDQDYEGELKIGQ---------------TVKVAYFKQTEKTLDRDIRVIDYLREESEMAKEKDGTSISVTQLLE 427
Cdd:COG1106 84 eILFLLDGVRYEYGFELDKeriisewlyflstaaQLNVPLLSPLYDWFDNNISLDTSSDGLTLLLKEDESLKEELLELLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 428 RFLF-------------------PSATHGKKVYKL-----SGGEQKRLYLLRLLV---HKPNVLLLDEPTNDLDTETL-T 479
Cdd:COG1106 164 IADPgiedieveeeeiedlverkLIFKHKGGNVPLplseeSDGTKRLLALAGALLdalAKGGVLLIDEIEASLHPSLLrK 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1842088001 480 ILEDYID---DFGGSVITVSHDRYFLNKVVQ-----EYWFIH---DGKIEKIigSFEDYESFKKEHERQAMLS 541
Cdd:COG1106 244 LLKLFLDlanKNNAQLIFTTHSTELLDAFLEllrrdQIWFVEkdkDGASELY--SLEDFKVRKDENLEKGYLQ 314
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
160-191 |
3.15e-03 |
|
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: 40.57 E-value: 3.15e-03
10 20 30
....*....|....*....|....*....|..
gi 1842088001 160 LSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLD 191
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
341-369 |
3.24e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 39.06 E-value: 3.24e-03
10 20
....*....|....*....|....*....
gi 1842088001 341 EIIQSGRRIGIVGPNGAGKTTLLNILSNE 369
Cdd:cd01130 7 LAVRARKNILISGGTGSGKTTLLNALLSF 35
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
340-369 |
4.12e-03 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 39.76 E-value: 4.12e-03
10 20 30
....*....|....*....|....*....|
gi 1842088001 340 TEIIQSGRRIGIVGPNGAGKTTLLNILSNE 369
Cdd:COG4962 176 RAAVRARLNILVSGGTGSGKTTLLNALSGF 205
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
318-498 |
4.23e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.33 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 318 KQVYELKNLS---KSINNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILS-----------------NEDQDYEGEL 377
Cdd:PRK13650 2 SNIIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDglleaesgqiiidgdllTEENVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 378 KIGQTVKVAYFKQTEKTLDRDI------RVIDYlreeSEMaKEKdgtsisVTQLLErFLFPSATHGKKVYKLSGGEQKRL 451
Cdd:PRK13650 82 KIGMVFQNPDNQFVGATVEDDVafglenKGIPH----EEM-KER------VNEALE-LVGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1842088001 452 YLLRLLVHKPNVLLLDEPTNDLDT----ETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPegrlELIKTIKGIRDDYQMTVISITHD 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
322-482 |
4.43e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 39.78 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 322 ELKNLSKS----INNKVLFEDVTEIIQSGRRIGIVGPNGAGKTTLL---NILSN--------EDQDY----EGEL----- 377
Cdd:PRK11153 3 ELKNISKVfpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLLERptsgrvlvDGQDLtalsEKELrkarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 378 KIG-----------QTV--KVAYFKQTEKTLDRDIRvidylreesemAKekdgtsisVTQLLERFlfpSATHGKKVY--K 442
Cdd:PRK11153 83 QIGmifqhfnllssRTVfdNVALPLELAGTPKAEIK-----------AR--------VTELLELV---GLSDKADRYpaQ 140
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1842088001 443 LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTETL-TILE 482
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTrSILE 181
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
443-498 |
4.87e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 39.40 E-value: 4.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 443 LSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLD----TETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK13640 144 LSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQILKLIRKLKKKNNLTVISITHD 203
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
335-477 |
6.73e-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: 39.07 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 335 LFEDVTEIIQSGRRIGIVGPNGAGKTTLLNILSNEDQDYEGelKIGQTVKVAYFKQTEKTLDRDIR-------------- 400
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHSGRISFSSQFSWIMPGTIKeniifgvsydeyry 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 401 --VIDYLREESEMAK--EKDGTSIsvtqllerflfpsathGKKVYKLSGGEQKRLYLLRLLVHKPNVLLLDEPTNDLDTE 476
Cdd:cd03291 130 ksVVKACQLEEDITKfpEKDNTVL----------------GEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
.
gi 1842088001 477 T 477
Cdd:cd03291 194 T 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
158-269 |
7.21e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1842088001 158 VELSGGQQKRVVLAKTLIEQPDLLLLDEPTNHLDFESIRWLINY-----VKQypHTVLFVTHDRYFLNEVStRIIELDRG 232
Cdd:PLN03130 739 VNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKcikdeLRG--KTRVLVTNQLHFLSQVD-RIILVHEG 815
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1842088001 233 KLKTyPGNYEDYI--------VMRAENELVEQKQQEKQKALYKQE 269
Cdd:PLN03130 816 MIKE-EGTYEELSnngplfqkLMENAGKMEEYVEENGEEEDDQTS 859
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
437-498 |
8.53e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.43 E-value: 8.53e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1842088001 437 GKKVYKLSGGEQKRL---YLLRLLVHKPNVLLLDEPTNDL---DTETLTILEDYIDDFGGSVITVSHD 498
Cdd:PRK00635 804 GRPLSSLSGGEIQRLklaYELLAPSKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQGHTVVIIEHN 871
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